Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P00504
|
AATC_CHICK
|
MAASIFAAVPRAPPVAVFKLTADFREDGDSRKVNLGVGAYRTDEGQPWVLPVVRKVEQLIAGDGSLNHEYLPILGLPEFRANASRIALGDDSPAIAQKRVGSVQGLGGTGALRIGAEFLRRWYNGNNNTATPVYVSSPTWENHNSVFMDAGFKDIRTYRYWDAAKRGLDLQGLLDDMEKAPEFSIFILHACAHNPTGTDPTPDEWKQIAAVMKRRCLFPFFDSAYQGFASGSLDKDAWAVRYFVSEGFELFCAQSFSKNFGLYNERVGNLSVVGKDEDNVQRVLSQMEKIVRTTWSNPPSQGARIVATTLTSPQLFAEWKDNVKTMADRVLLMRSELRSRLESLGTPGTWNHITDQIGMFSFTGLNPKQVEYMIKEKHIYLMASGRINMCGLTTKNLDYVAKSIHEAVTKIQ
|
2.6.1.1; 2.6.1.3
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:7897655};
|
2-oxoglutarate metabolic process [GO:0006103]; aspartate biosynthetic process [GO:0006532]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; cellular response to insulin stimulus [GO:0032869]; fatty acid homeostasis [GO:0055089]; gluconeogenesis [GO:0006094]; glutamate catabolic process to 2-oxoglutarate [GO:0019551]; glutamate catabolic process to aspartate [GO:0019550]; glutamate metabolic process [GO:0006536]; glycerol biosynthetic process [GO:0006114]; Notch signaling pathway [GO:0007219]; oxaloacetate metabolic process [GO:0006107]; response to glucocorticoid [GO:0051384]
|
cytosol [GO:0005829]
|
L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-cysteine transaminase activity [GO:0047801]; phosphatidylserine decarboxylase activity [GO:0004609]; pyridoxal phosphate binding [GO:0030170]
|
PF00155;
|
3.90.1150.10;3.40.640.10;
|
Class-I pyridoxal-phosphate-dependent aminotransferase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000250|UniProtKB:P13221}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21825; Evidence={ECO:0000250|UniProtKB:P13221}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-cysteine = 2-oxo-3-sulfanylpropanoate + L-glutamate; Xref=Rhea:RHEA:17441, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35235, ChEBI:CHEBI:57678; EC=2.6.1.3; Evidence={ECO:0000250|UniProtKB:P13221}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17442; Evidence={ECO:0000250|UniProtKB:P13221}; CATALYTIC ACTIVITY: Reaction=(2S)-2-aminobutanoate + 2-oxoglutarate = 2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:70223, ChEBI:CHEBI:16763, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:74359; Evidence={ECO:0000250|UniProtKB:P17174}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70225; Evidence={ECO:0000250|UniProtKB:P17174}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-sulfino-L-alanine = 3-sulfinopyruvate + L-glutamate; Xref=Rhea:RHEA:70295, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:61085, ChEBI:CHEBI:140699; Evidence={ECO:0000250|UniProtKB:P13221}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70297; Evidence={ECO:0000250|UniProtKB:P13221};
| null | null | null | null |
FUNCTION: Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain. {ECO:0000250|UniProtKB:P13221}.
|
Gallus gallus (Chicken)
|
P00505
|
AATM_HUMAN
|
MALLHSGRVLPGIAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEVLKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFTGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCKDADEAKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKVMADRIIGMRTQLVSNLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGYLAHAIHQVTK
|
2.6.1.1; 2.6.1.7
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
|
2-oxoglutarate metabolic process [GO:0006103]; 4-hydroxyproline catabolic process [GO:0019470]; aspartate biosynthetic process [GO:0006532]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; fatty acid transport [GO:0015908]; glutamate catabolic process to 2-oxoglutarate [GO:0019551]; glutamate catabolic process to aspartate [GO:0019550]; glutamate metabolic process [GO:0006536]; oxaloacetate metabolic process [GO:0006107]; response to ethanol [GO:0045471]
|
extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
kynurenine-oxoglutarate transaminase activity [GO:0016212]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; pyridoxal phosphate binding [GO:0030170]; RNA binding [GO:0003723]
|
PF00155;
|
3.90.1150.10;3.40.640.10;
|
Class-I pyridoxal-phosphate-dependent aminotransferase family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:9537447}. Cell membrane {ECO:0000269|PubMed:9537447}. Note=Exposure to alcohol promotes translocation to the cell membrane. {ECO:0000269|PubMed:9537447}.
|
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000269|PubMed:26902786, ECO:0000269|PubMed:31422819}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.7; Evidence={ECO:0000250|UniProtKB:P00507};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:26902786};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 47.5 degrees Celsius. {ECO:0000269|PubMed:26902786};
|
FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolism. Facilitates cellular uptake of long-chain free fatty acids. {ECO:0000269|PubMed:31422819, ECO:0000269|PubMed:9537447}.
|
Homo sapiens (Human)
|
P00506
|
AATM_PIG
|
MALLHSGRVLSGVASAFHPGLAAAASARASSWWAHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENNEVLKSGRYVTVQTISGTGALRIGANFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLHSYRYYDPKTCGFDFTGALEDISKIPAQSVILLHACAHNPTGVDPRPEQWKEMATLVKKNNLFAFFDMAYQGFASGDGNKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPMYSNPPVNGARIASTILTSPDLRQQWLQEVKGMADRIISMRTQLVSNLKKEGSSHNWQHIVDQIGMFCFTGIKPEQVERLTKEFSIYMTKDGRISVAGVTSGNVGYLAHAIHQVTK
|
2.6.1.1; 2.6.1.7
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
|
2-oxoglutarate metabolic process [GO:0006103]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; glutamate metabolic process [GO:0006536]; L-phenylalanine biosynthetic process from chorismate via phenylpyruvate [GO:0033585]; lipid transport [GO:0006869]
|
cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]; kynurenine-oxoglutarate transaminase activity [GO:0016212]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-tyrosine:2-oxoglutarate aminotransferase activity [GO:0004838]; pyridoxal phosphate binding [GO:0030170]
|
PF00155;
|
3.90.1150.10;3.40.640.10;
|
Class-I pyridoxal-phosphate-dependent aminotransferase family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix. Cell membrane {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000250|UniProtKB:P00507}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.7; Evidence={ECO:0000250|UniProtKB:P00507};
| null | null | null | null |
FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolism. Facilitates cellular uptake of long-chain free fatty acids. {ECO:0000250|UniProtKB:P00505}.
|
Sus scrofa (Pig)
|
P00507
|
AATM_RAT
|
MALLHSGRVLSGMAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAGKNLDKEYLPIGGLADFCKASAELALGENSEVLKSGRFVTVQTISGTGALRVGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFSGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEMAAVVKKKNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPLYSNPPLNGARIAATILTSPDLRKQWLQEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSVYMTKDGRISVAGVTSGNVGYLAHAIHQVTK
|
2.6.1.1; 2.6.1.7
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
|
2-oxoglutarate metabolic process [GO:0006103]; amino acid metabolic process [GO:0006520]; aspartate biosynthetic process [GO:0006532]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; dicarboxylic acid metabolic process [GO:0043648]; fatty acid transport [GO:0015908]; female pregnancy [GO:0007565]; glutamate catabolic process to 2-oxoglutarate [GO:0019551]; glutamate catabolic process to aspartate [GO:0019550]; glutamate metabolic process [GO:0006536]; L-phenylalanine biosynthetic process from chorismate via phenylpyruvate [GO:0033585]; lactation [GO:0007595]; oxaloacetate metabolic process [GO:0006107]; response to ethanol [GO:0045471]; response to insulin [GO:0032868]; response to muscle activity [GO:0014850]
|
cell surface [GO:0009986]; cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; sarcolemma [GO:0042383]; T-tubule [GO:0030315]
|
amino acid binding [GO:0016597]; carboxylic acid binding [GO:0031406]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; kynurenine-oxoglutarate transaminase activity [GO:0016212]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-tyrosine:2-oxoglutarate aminotransferase activity [GO:0004838]; phospholipid binding [GO:0005543]; pyridoxal phosphate binding [GO:0030170]
|
PF00155;
|
3.90.1150.10;3.40.640.10;
|
Class-I pyridoxal-phosphate-dependent aminotransferase family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:11962739}. Cell membrane {ECO:0000269|PubMed:11962739}. Note=Located in the mitochondria of liver, pancreas, spleen, heart, pituitary gland and submandibular gland cells. In kidney, located in the mitochondria, on the cell surface of regions with protrusions in distal tubules, on the apical cell surface of protrusions along the microvilli in cortical collecting ducts, in condensing vacuoles, on the cell surface at cell boundaries of adjoining kidney cells and on the cell surface of endothelial cells lining capillaries in the glomerulus. Also located at the cell surface of endothelial cells lining arterioles and on the cell surface of lymphocytes.
|
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000269|PubMed:17442055}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.7; Evidence={ECO:0000269|PubMed:17442055};
| null | null | null | null |
FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolism. Facilitates cellular uptake of long-chain free fatty acids (By similarity). {ECO:0000250, ECO:0000269|PubMed:17442055}.
|
Rattus norvegicus (Rat)
|
P00508
|
AATM_CHICK
|
MALLQSRLLLSAPRRAAATARASSWWSHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKSYVLNCVRKAEAMIAAKKMDKEYLPIAGLADFTRASAELALGENSEAFKSGRYVTVQGISGTGSLRVGANFLQRFFKFSRDVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSLDFTGAMEDISKIPEKSIILLHACAHNPTGVDPRQEQWKELASVVKKRNLLAYFDMAYQGFASGDINRDAWALRHFIEQGIDVVLSQSYAKNMGLYGERAGAFTVICRDAEEAKRVESQLKILIRPMYSNPPMNGARIASLILNTPELRKEWLVEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSIYMTKDGRISVAGVASSNVGYLAHAIHQVTK
|
2.6.1.1; 2.6.1.7
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:1593633, ECO:0000269|PubMed:7903048, ECO:0000269|PubMed:8665890, ECO:0000269|PubMed:8952476};
|
2-oxoglutarate metabolic process [GO:0006103]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; glutamate metabolic process [GO:0006536]; L-phenylalanine biosynthetic process from chorismate via phenylpyruvate [GO:0033585]
|
cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
kynurenine-oxoglutarate transaminase activity [GO:0016212]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-tyrosine:2-oxoglutarate aminotransferase activity [GO:0004838]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]
|
PF00155;
|
3.90.1150.10;3.40.640.10;
|
Class-I pyridoxal-phosphate-dependent aminotransferase family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:8665890}.
|
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000250|UniProtKB:P00507}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.7;
| null | null | null | null |
FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolism. {ECO:0000250|UniProtKB:P00505}.
|
Gallus gallus (Chicken)
|
P00509
|
AAT_ECOLI
|
MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
|
2.6.1.1
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:11148029};
|
aspartate catabolic process [GO:0006533]; L-phenylalanine biosynthetic process [GO:0009094]; L-phenylalanine biosynthetic process from chorismate via phenylpyruvate [GO:0033585]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
identical protein binding [GO:0042802]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-tyrosine:2-oxoglutarate aminotransferase activity [GO:0004838]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]
|
PF00155;
|
3.90.1150.10;3.40.640.10;
|
Class-I pyridoxal-phosphate-dependent aminotransferase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000269|PubMed:10556573};
| null | null | null | null | null |
Escherichia coli (strain K12)
|
P00511
|
PFKAM_RABIT
|
MTHEEHHAARTLGVGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVDGGDHIREATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLSDLQKAGKITAEEATRSSYLNIVGLVGSIDNDFCGTDMTIGTDSALHRITEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDNWEDHLCRRLSETRTRGSRLNIIIVAEGAIDRNGKPITSEGVKDLVVRRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTKAMDEKRFDEAMKLRGRSFMNNWEVYKLLAHIRPPAPKSGSYTVAVMNVGAPAAGMNAAVRSTVRIGLIQGNRVLVVHDGFEGPAKGQIEEAGWSYVGGWTGQGGSKLGSKRTLPKKSFEQISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSVGADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNWMAGKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVTELQNQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSEHAHLEHISRKRSGEATV
|
2.7.1.11
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
|
canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]
|
6-phosphofructokinase complex [GO:0005945]; membrane [GO:0016020]
|
6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029]
|
PF00365;
|
3.40.50.450;3.40.50.460;
|
Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Eukaryotic two domain clade 'E' sub-subfamily
|
PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
|
CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
| null |
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03184}.
| null | null |
FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184}.
|
Oryctolagus cuniculus (Rabbit)
|
P00512
|
PFKA_GEOSE
|
MKRIGVLTSGGDSPGMNAAIRSVVRKAIYHGVEVYGVYHGYAGLIAGNIKKLEVGDVGDIIHRGGTILYTARCPEFKTEEGQKKGIEQLKKHGIEGLVVIGGDGSYQGAKKLTEHGFPCVGVPGTIDNDIPGTDFTIGFDTALNTVIDAIDKIRDTATSHERTYVIEVMGRHAGDIALWSGLAGGAETILIPEADYDMNDVIARLKRGHERGKKHSIIIVAEGVGSGVDFGRQIQEATGFETRVTVLGHVQRGGSPTAFDRVLASRLGARAVELLLEGKGGRCVGIQNNQLVDHDIAEALANKHTIDQRMYALSKELSI
|
2.7.1.11
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:6115424};
|
canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]
|
6-phosphofructokinase complex [GO:0005945]; membrane [GO:0016020]
|
6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029]
|
PF00365;
|
3.40.50.450;3.40.50.460;
|
Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Prokaryotic clade 'B1' sub-subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339}.
|
CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:8136379};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.07 mM for ATP {ECO:0000269|PubMed:8136379}; KM=0.033 mM for fructose 6-phosphate {ECO:0000269|PubMed:8136379};
|
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00339}.
| null | null |
FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:8136379}.
|
Geobacillus stearothermophilus (Bacillus stearothermophilus)
|
P00514
|
KAP0_BOVIN
|
MASGTTASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFEKLEKEEAKQIQNLQKAGSRADSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cardiac muscle cell proliferation [GO:0060038]; cellular response to glucagon stimulus [GO:0071377]; mesoderm formation [GO:0001707]; negative regulation of activated T cell proliferation [GO:0046007]; negative regulation of gene expression [GO:0010629]; positive regulation of insulin secretion [GO:0032024]; regulation of protein phosphorylation [GO:0001932]; sarcomere organization [GO:0045214]
|
axoneme [GO:0005930]; cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; immunological synapse [GO:0001772]; multivesicular body [GO:0005771]; neuromuscular junction [GO:0031594]; nucleotide-activated protein kinase complex [GO:0031588]; plasma membrane raft [GO:0044853]; sperm connecting piece [GO:0097224]
|
cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; identical protein binding [GO:0042802]; protein domain specific binding [GO:0019904]; protein kinase A catalytic subunit binding [GO:0034236]; ubiquitin protein ligase binding [GO:0031625]
|
PF00027;PF02197;
|
1.20.890.10;2.60.120.10;
|
CAMP-dependent kinase regulatory chain family
|
PTM: The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity. The physiological significance of the in vitro phosphorylation of a proximal serine is unclear.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.
|
Bos taurus (Bovine)
|
P00515
|
KAP2_BOVIN
|
MSHIQIPPGLTELLQGYTVEVLRQRPPDLVDFAVDYFTRLREARSRASTPPAAPPSGSQDFDPGAGLVADAVADSESEDEEDLDVPIPGRFDRRVSVCAETYNPDEEEEDTDPRVIHPKTDQQRCRLQEACKDILLFKNLDPEQLSQVLDAMFERTVKVDEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNHGSFGELALMYNTPRAATIVATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLLKSLEVSERMKIVDVIGEKVYKDGERIITQGEKADSFYIIESGEVSILIKSKTKVNKDGENQEVEIARCHKGQYFGELALVTNKPRAASAYAVGDVKCLVMDVQAFERLLGPCMDIMKRNISHYEEQLVKMFGSSMDLIDPGQ
| null | null |
regulation of protein phosphorylation [GO:0001932]
|
axoneme [GO:0005930]; cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; cytosol [GO:0005829]; nucleotide-activated protein kinase complex [GO:0031588]; plasma membrane raft [GO:0044853]
|
cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; protein domain specific binding [GO:0019904]; protein kinase A catalytic subunit binding [GO:0034236]; ubiquitin protein ligase binding [GO:0031625]
|
PF00027;PF02197;
|
1.20.890.10;2.60.120.10;
|
CAMP-dependent kinase regulatory chain family
|
PTM: A second phosphorylation site has not been located. {ECO:0000269|PubMed:1654846}.; PTM: Phosphorylation of Thr-212 by PDPK1 seems to attenuate the activity of PKA, perhaps by strengthening interaction between the regulatory and the catalytic subunits. {ECO:0000269|PubMed:1654846}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and the cell membrane. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
P00516
|
KGP1_BOVIN
|
MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFRKFTKSERSKDLIKEAILDNDFMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEGVKLCTMGPGKVFGELAILYNCTRTATVKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEYMEFLKSVPTFQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGKVNVTREDSPNEDPVFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAEAKAKYEAEAAFFANLKLSDFNIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDFIVRLYRTFKDSKYLYMLMEACLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGIIYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEIILNKGHDISADYWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPSERLGNLKNGVKDIQKHKWFEGFNWEGLRKGTLTPPIIPSVASPTDTSNFDSFPEDNDEPPPDDNSGWDIDF
|
2.7.11.12
| null |
cGMP-mediated signaling [GO:0019934]; collateral sprouting [GO:0048668]; dendrite development [GO:0016358]; forebrain development [GO:0030900]; negative regulation of platelet aggregation [GO:0090331]; negative regulation of vascular associated smooth muscle cell migration [GO:1904753]; negative regulation of vascular associated smooth muscle cell proliferation [GO:1904706]; neuron migration [GO:0001764]; phosphorylation [GO:0016310]; regulation of GTPase activity [GO:0043087]; relaxation of vascular associated smooth muscle [GO:0060087]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; calcium channel regulator activity [GO:0005246]; cGMP binding [GO:0030553]; cGMP-dependent protein kinase activity [GO:0004692]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]
|
PF00027;PF16808;PF00069;
|
2.60.120.10;1.20.5.490;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, cGMP subfamily
|
PTM: Autophosphorylation increases kinase activity. {ECO:0000250}.; PTM: 65 kDa monomer is produced by proteolytic cleavage.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalized with TRPC7 in the plasma membrane. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.12; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.12;
| null | null | null | null |
FUNCTION: Serine/threonine protein kinase that acts as a key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates IRAG1 and inhibits IP3-induced Ca(2+) release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca(2+) levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
P00517
|
KAPCA_BOVIN
|
MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLVKHMETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
|
2.7.11.11
| null |
cellular response to heat [GO:0034605]; mesoderm formation [GO:0001707]; negative regulation of TORC1 signaling [GO:1904262]; peptidyl-serine phosphorylation [GO:0018105]; protein kinase A signaling [GO:0010737]; protein phosphorylation [GO:0006468]
|
acrosomal vesicle [GO:0001669]; cAMP-dependent protein kinase complex [GO:0005952]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; neuromuscular junction [GO:0031594]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; sperm flagellum [GO:0036126]
|
AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; protein domain specific binding [GO:0019904]; protein kinase A regulatory subunit binding [GO:0034237]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily
|
PTM: Autophosphorylated. Phosphorylation is enhanced by vitamin K(2). Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity (By similarity). Phosphorylated at Tyr-331 by activated receptor tyrosine kinases EGFR and PDGFR; this increases catalytic efficiency (By similarity). {ECO:0000250|UniProtKB:P05132, ECO:0000250|UniProtKB:P17612}.; PTM: Asn-3 is deaminated to Asp in more than 25% of the proteins, giving rise to 2 major isoelectric variants, called CB and CA respectively (0.4 pH unit change). Deamidation proceeds via the so-called beta-aspartyl shift mechanism and yields either 'D-Asp-3' (major) or 'D-isoAsp-2' (minor), in addition to L-isomers. Deamidation occurs after the addition of myristate. The Asn-3 form reaches a significantly larger nuclear/cytoplasmic ratio than the 'Asp-2' form. {ECO:0000269|PubMed:10684253, ECO:0000269|PubMed:11152138, ECO:0000269|PubMed:6262777, ECO:0000269|PubMed:9521123}.; PTM: When myristoylated, Ser-11 is autophosphorylated probably in conjunction with deamidation of Asn-3. {ECO:0000250|UniProtKB:P05132}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10684253}. Cell membrane {ECO:0000250|UniProtKB:P17612}. Membrane {ECO:0000250|UniProtKB:P17612}; Lipid-anchor {ECO:0000250|UniProtKB:P17612}. Nucleus {ECO:0000269|PubMed:10684253}. Mitochondrion {ECO:0000250|UniProtKB:P05132}. Note=Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm. Distributed throughout the cytoplasm in meiotically incompetent oocytes. Associated to mitochondrion as meiotic competence is acquired. Aggregates around the germinal vesicles (GV) at the immature GV stage oocytes (By similarity). Colocalizes with HSF1 in nuclear stress bodies (nSBs) upon heat shock (By similarity). Recruited to the cell membrane through interaction with SMO (By similarity). {ECO:0000250|UniProtKB:P05132, ECO:0000250|UniProtKB:P17612}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.11;
| null | null | null | null |
FUNCTION: Phosphorylates a large number of substrates in the cytoplasm and the nucleus (By similarity). Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA, SOX9 and VASP (By similarity). Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts (By similarity). Involved in chondrogenesis by mediating phosphorylation of SOX9 (By similarity). Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Required for phosphorylation of GLI transcription factors which inhibits them and prevents transcriptional activation of Hedgehog signaling pathway target genes (By similarity). GLI transcription factor phosphorylation is inhibited by interaction of PRKACA with SMO which sequesters PRKACA at the cell membrane (By similarity). Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis most probably through the regulation of OFD1 in ciliogenesis (By similarity). Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation (By similarity). May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT) (By similarity). Phosphorylates APOBEC3G and AICDA. Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock (By similarity). Acts as a negative regulator of mTORC1 by mediating phosphorylation of RPTOR (By similarity). {ECO:0000250|UniProtKB:P05132, ECO:0000250|UniProtKB:P17612, ECO:0000250|UniProtKB:P27791}.
|
Bos taurus (Bovine)
|
P00518
|
PHKG1_RABIT
|
MTRDAALPGSHSTHGFYENYEPKEILGRGVSSVVRRCIHKPTCKEYAVKIIDVTGGGSFSAEEVQELREATLKEVDILRKVSGHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPGEKLREVCGTPSYLAPEIIECSMNDNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEWDDYSDTVKDLVSRFLVVQPQKRYTAEEALAHPFFQQYVVEEVRHFSPRGKFKVICLTVLASVRIYYQYRRVKPVTREIVIRDPYALRPLRRLIDAYAFRIYGHWVKKGQQQNRAALFENTPKAVLFSLAEDDY
|
2.7.11.1; 2.7.11.19; 2.7.11.26
| null |
glycogen biosynthetic process [GO:0005978]; phosphorylation [GO:0016310]
|
phosphorylase kinase complex [GO:0005964]; skeletal muscle myofibril [GO:0098723]
|
ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; phosphorylase kinase activity [GO:0004689]; protein serine kinase activity [GO:0106310]; tau-protein kinase activity [GO:0050321]
|
PF12330;PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family
| null | null |
CATALYTIC ACTIVITY: Reaction=2 ATP + phosphorylase b = 2 ADP + phosphorylase a.; EC=2.7.11.19; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703, Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.26; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3. {ECO:0000269|PubMed:8454596, ECO:0000269|PubMed:8999860}.
|
Oryctolagus cuniculus (Rabbit)
|
P00519
|
ABL1_HUMAN
|
MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR
|
2.7.10.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00520};
|
actin cytoskeleton organization [GO:0030036]; actin filament polymerization [GO:0030041]; activated T cell proliferation [GO:0050798]; activation of protein kinase C activity [GO:1990051]; alpha-beta T cell differentiation [GO:0046632]; associative learning [GO:0008306]; autophagy [GO:0006914]; B cell proliferation involved in immune response [GO:0002322]; B cell receptor signaling pathway [GO:0050853]; B-1 B cell homeostasis [GO:0001922]; Bergmann glial cell differentiation [GO:0060020]; BMP signaling pathway [GO:0030509]; canonical NF-kappaB signal transduction [GO:0007249]; cardiac muscle cell proliferation [GO:0060038]; cell-cell adhesion [GO:0098609]; cellular response to dopamine [GO:1903351]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to oxidative stress [GO:0034599]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular senescence [GO:0090398]; cerebellum morphogenesis [GO:0021587]; DN4 thymocyte differentiation [GO:1904157]; DNA conformation change [GO:0071103]; DNA damage response [GO:0006974]; endothelial cell migration [GO:0043542]; epidermal growth factor receptor signaling pathway [GO:0007173]; ERK1 and ERK2 cascade [GO:0070371]; establishment of localization in cell [GO:0051649]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; integrin-mediated signaling pathway [GO:0007229]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; microspike assembly [GO:0030035]; mismatch repair [GO:0006298]; mitochondrial depolarization [GO:0051882]; mitotic cell cycle [GO:0000278]; myoblast proliferation [GO:0051450]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of cellular senescence [GO:2000773]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of long-term synaptic potentiation [GO:1900272]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of phospholipase C activity [GO:1900275]; negative regulation of protein serine/threonine kinase activity [GO:0071901]; negative regulation of ubiquitin-protein transferase activity [GO:0051444]; neural tube closure [GO:0001843]; neuroepithelial cell differentiation [GO:0060563]; neuromuscular process controlling balance [GO:0050885]; neuron apoptotic process [GO:0051402]; neuron differentiation [GO:0030182]; neuropilin signaling pathway [GO:0038189]; peptidyl-tyrosine autophosphorylation [GO:0038083]; peptidyl-tyrosine phosphorylation [GO:0018108]; platelet-derived growth factor receptor-beta signaling pathway [GO:0035791]; podocyte apoptotic process [GO:1903210]; positive regulation of actin filament binding [GO:1904531]; positive regulation of apoptotic process [GO:0043065]; positive regulation of blood vessel branching [GO:1905555]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of dendrite development [GO:1900006]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of extracellular matrix organization [GO:1903055]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of microtubule binding [GO:1904528]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of osteoblast proliferation [GO:0033690]; positive regulation of oxidoreductase activity [GO:0051353]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of T cell migration [GO:2000406]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of type II interferon production [GO:0032729]; positive regulation of vasoconstriction [GO:0045907]; positive regulation of Wnt signaling pathway, planar cell polarity pathway [GO:2000096]; post-embryonic development [GO:0009791]; protein autophosphorylation [GO:0046777]; protein localization to cytoplasmic microtubule plus-end [GO:1904518]; protein modification process [GO:0036211]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of autophagy [GO:0010506]; regulation of axon extension [GO:0030516]; regulation of Cdc42 protein signal transduction [GO:0032489]; regulation of cell adhesion [GO:0030155]; regulation of cell cycle [GO:0051726]; regulation of cell motility [GO:2000145]; regulation of DNA-templated transcription [GO:0006355]; regulation of endocytosis [GO:0030100]; regulation of hematopoietic stem cell differentiation [GO:1902036]; regulation of microtubule polymerization [GO:0031113]; regulation of modification of synaptic structure [GO:1905244]; regulation of T cell differentiation [GO:0045580]; response to endoplasmic reticulum stress [GO:0034976]; response to epinephrine [GO:0071871]; response to oxidative stress [GO:0006979]; response to xenobiotic stimulus [GO:0009410]; signal transduction in response to DNA damage [GO:0042770]; spleen development [GO:0048536]; substrate adhesion-dependent cell spreading [GO:0034446]; T cell receptor signaling pathway [GO:0050852]; thymus development [GO:0048538]; transitional one stage B cell differentiation [GO:0002333]
|
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; growth cone [GO:0030426]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nuclear body [GO:0016604]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; postsynapse [GO:0098794]; protein-containing complex [GO:0032991]; ruffle [GO:0001726]
|
actin filament binding [GO:0051015]; actin monomer binding [GO:0003785]; ATP binding [GO:0005524]; bubble DNA binding [GO:0000405]; delta-catenin binding [GO:0070097]; DNA binding [GO:0003677]; ephrin receptor binding [GO:0046875]; four-way junction DNA binding [GO:0000400]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; mitogen-activated protein kinase binding [GO:0051019]; neuropilin binding [GO:0038191]; nicotinate-nucleotide adenylyltransferase activity [GO:0004515]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphotyrosine residue binding [GO:0001784]; proline-rich region binding [GO:0070064]; protein kinase activity [GO:0004672]; protein kinase C binding [GO:0005080]; protein self-association [GO:0043621]; protein tyrosine kinase activity [GO:0004713]; sequence-specific double-stranded DNA binding [GO:1990837]; SH2 domain binding [GO:0042169]; SH3 domain binding [GO:0017124]; syntaxin binding [GO:0019905]; transcription coactivator activity [GO:0003713]
|
PF08919;PF07714;PF00017;PF00018;
|
1.20.120.330;3.30.505.10;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, ABL subfamily
|
PTM: Acetylated at Lys-711 by EP300 which promotes the cytoplasmic translocation. {ECO:0000269|PubMed:16648821}.; PTM: Phosphorylation at Tyr-70 by members of the SRC family of kinases disrupts SH3 domain-based autoinhibitory interactions and intermolecular associations, such as that with ABI1, and also enhances kinase activity. Phosphorylation at Tyr-226 and Tyr-393 correlate with increased activity. DNA damage-induced activation of ABL1 requires the function of ATM and Ser-446 phosphorylation (By similarity). Phosphorylation at Ser-569 has been attributed to a CDC2-associated kinase and is coupled to cell division (By similarity). Phosphorylation at Ser-618 and Ser-619 by PAK2 increases binding to CRK and reduces binding to ABI1. Phosphorylation on Thr-735 is required for binding 14-3-3 proteins for cytoplasmic translocation. Phosphorylated by PRKDC (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated. Polyubiquitination of ABL1 leads to degradation. {ECO:0000269|PubMed:12475393}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Mitochondrion {ECO:0000250}. Note=Shuttles between the nucleus and cytoplasm depending on environmental signals. Sequestered into the cytoplasm through interaction with 14-3-3 proteins. Localizes to mitochondria in response to oxidative stress (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform IB]: Nucleus membrane; Lipid-anchor. Note=The myristoylated c-ABL protein is reported to be nuclear.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:20357770, ECO:0000269|PubMed:28428613};
| null | null | null | null |
FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9 (PubMed:22810897). Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717' (PubMed:28428613). ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 acts also as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Regulates T-cell differentiation in a TBX21-dependent manner (By similarity). Positively regulates chemokine-mediated T-cell migration, polarization, and homing to lymph nodes and immune-challenged tissues, potentially via activation of NEDD9/HEF1 and RAP1 (By similarity). Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity (By similarity). {ECO:0000250|UniProtKB:P00520, ECO:0000269|PubMed:10391250, ECO:0000269|PubMed:11971963, ECO:0000269|PubMed:12379650, ECO:0000269|PubMed:12531427, ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:15556646, ECO:0000269|PubMed:15657060, ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:16424036, ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:16943190, ECO:0000269|PubMed:17306540, ECO:0000269|PubMed:17623672, ECO:0000269|PubMed:18328268, ECO:0000269|PubMed:18945674, ECO:0000269|PubMed:19891780, ECO:0000269|PubMed:20357770, ECO:0000269|PubMed:20417104, ECO:0000269|PubMed:22810897, ECO:0000269|PubMed:28428613, ECO:0000269|PubMed:9037071, ECO:0000269|PubMed:9144171, ECO:0000269|PubMed:9461559}.
|
Homo sapiens (Human)
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P00520
|
ABL1_MOUSE
|
MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTIYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVSAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKRGTRGGAGSMLQAPELPTKTRTCRRAAEQKDAPDTPELLHTKGLGESDALDSEPAVSPLLPRKERGPPDGSLNEDERLLPRDRKTNLFSALIKKKKKMAPTPPKRSSSFREMDGQPDRRGASEDDSRELCNGPPALTSDAAEPTKSPKASNGAGVPNGAFREPGNSGFRSPHMWKKSSTLTGSRLAAAEEESGMSSSKRFLRSCSASCMPHGARDTEWRSVTLPRDLPSAGKQFDSSTFGGHKSEKPALPRKRTSESRSEQVAKSTAMPPPRLVKKNEEAAEEGFKDTESSPGSSPPSLTPKLLRRQVTASPSSGLSHKEEATKGSASGMGTPATAEPAPPSNKVGLSKASSEEMRVRRHKHSSESPGRDKGRLAKLKPAPPPPPACTGKAGKPAQSPSQEAGEAGGPTKTKCTSLAMDAVNTDPTKAGPPGEGLRKPVPPSVPKPQSTAKPPGTPTSPVSTPSTAPAPSPLAGDQQPSSAAFIPLISTRVSLRKTRQPPERIASGTITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLESNLRELQICPATASSGPAATQDFSKLLSSVKEISDIVRR
|
2.7.10.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12748290}; Note=Mg(2+) and Mn(2+) were both present in the kinase buffer but Mg(2+) is likely to be the in vivo cofactor. {ECO:0000305};
|
actin cytoskeleton organization [GO:0030036]; actin filament polymerization [GO:0030041]; activated T cell proliferation [GO:0050798]; alpha-beta T cell differentiation [GO:0046632]; associative learning [GO:0008306]; autophagy [GO:0006914]; B cell proliferation [GO:0042100]; B cell proliferation involved in immune response [GO:0002322]; B cell receptor signaling pathway [GO:0050853]; B-1 B cell homeostasis [GO:0001922]; Bergmann glial cell differentiation [GO:0060020]; BMP signaling pathway [GO:0030509]; canonical NF-kappaB signal transduction [GO:0007249]; cardiac muscle cell proliferation [GO:0060038]; cell-cell adhesion [GO:0098609]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular senescence [GO:0090398]; cerebellum morphogenesis [GO:0021587]; circulatory system development [GO:0072359]; DN4 thymocyte differentiation [GO:1904157]; DNA conformation change [GO:0071103]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; endothelial cell migration [GO:0043542]; epidermal growth factor receptor signaling pathway [GO:0007173]; ERK1 and ERK2 cascade [GO:0070371]; establishment of localization in cell [GO:0051649]; integrin-mediated signaling pathway [GO:0007229]; learning or memory [GO:0007611]; microspike assembly [GO:0030035]; myoblast proliferation [GO:0051450]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of cellular senescence [GO:2000773]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of long-term synaptic potentiation [GO:1900272]; negative regulation of mitotic cell cycle [GO:0045930]; neural tube closure [GO:0001843]; neuroepithelial cell differentiation [GO:0060563]; neuromuscular process controlling balance [GO:0050885]; neuron apoptotic process [GO:0051402]; neuron differentiation [GO:0030182]; neuropilin signaling pathway [GO:0038189]; peptidyl-tyrosine phosphorylation [GO:0018108]; phagocytosis [GO:0006909]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; platelet-derived growth factor receptor-beta signaling pathway [GO:0035791]; podocyte apoptotic process [GO:1903210]; positive regulation of apoptotic process [GO:0043065]; positive regulation of blood vessel branching [GO:1905555]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of dendrite development [GO:1900006]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of extracellular matrix organization [GO:1903055]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of osteoblast proliferation [GO:0033690]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of T cell migration [GO:2000406]; positive regulation of type II interferon production [GO:0032729]; positive regulation of vasoconstriction [GO:0045907]; positive regulation of Wnt signaling pathway, planar cell polarity pathway [GO:2000096]; post-embryonic development [GO:0009791]; protein localization to cytoplasmic microtubule plus-end [GO:1904518]; protein phosphorylation [GO:0006468]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of axon extension [GO:0030516]; regulation of Cdc42 protein signal transduction [GO:0032489]; regulation of cell cycle [GO:0051726]; regulation of cell population proliferation [GO:0042127]; regulation of cellular senescence [GO:2000772]; regulation of extracellular matrix organization [GO:1903053]; regulation of microtubule polymerization [GO:0031113]; regulation of modification of synaptic structure [GO:1905244]; regulation of T cell differentiation [GO:0045580]; response to endoplasmic reticulum stress [GO:0034976]; response to epinephrine [GO:0071871]; response to oxidative stress [GO:0006979]; response to xenobiotic stimulus [GO:0009410]; signal transduction in response to DNA damage [GO:0042770]; spleen development [GO:0048536]; substrate adhesion-dependent cell spreading [GO:0034446]; T cell receptor signaling pathway [GO:0050852]; thymus development [GO:0048538]; transitional one stage B cell differentiation [GO:0002333]
|
actin cytoskeleton [GO:0015629]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; growth cone [GO:0030426]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nuclear body [GO:0016604]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]; ruffle [GO:0001726]
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actin filament binding [GO:0051015]; ATP binding [GO:0005524]; bubble DNA binding [GO:0000405]; delta-catenin binding [GO:0070097]; ephrin receptor binding [GO:0046875]; four-way junction DNA binding [GO:0000400]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; mitogen-activated protein kinase binding [GO:0051019]; neuropilin binding [GO:0038191]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphotyrosine residue binding [GO:0001784]; proline-rich region binding [GO:0070064]; protein domain specific binding [GO:0019904]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein kinase C binding [GO:0005080]; protein self-association [GO:0043621]; protein tyrosine kinase activity [GO:0004713]; sequence-specific double-stranded DNA binding [GO:1990837]; SH2 domain binding [GO:0042169]; SH3 domain binding [GO:0017124]; syntaxin binding [GO:0019905]
|
PF08919;PF07714;PF00017;PF00018;
|
1.20.120.330;3.30.505.10;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, ABL subfamily
|
PTM: Acetylated at Lys-710 by EP300 which promotes the cytoplasmic translocation. {ECO:0000250}.; PTM: Phosphorylation at Tyr-70 by members of the SRC family of kinases disrupts SH3 domain-based autoinhibitory interactions and intermolecular associations, such as that with ABI1, and also enhances kinase activity (By similarity). Phosphorylation at Tyr-226 and Tyr-393 correlate with increased activity (By similarity). DNA damage-induced activation of ABL1 requires the function of ATM and Ser-446 phosphorylation. Phosphorylation at Thr-547 and Ser-569 has been attributed to a CDC2-associated kinase and is coupled to cell division. Phosphorylation at Ser-618 and Ser-619 by PAK2 increases binding to CRK and reduces binding to ABI1 (By similarity). Phosphorylation on Thr-734 is required for binding 14-3-3 proteins for cytoplasmic translocation (By similarity). Phosphorylated by PDGFRB and PRKDC. {ECO:0000250, ECO:0000269|PubMed:10988075, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293, ECO:0000269|PubMed:1566087, ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:2183353, ECO:0000269|PubMed:9109492}.; PTM: Polyubiquitinated. Polyubiquitination of ABL1 leads to degradation (By similarity). {ECO:0000250}.; PTM: Isoform IV is myristoylated on Gly-2. {ECO:0000269|PubMed:12654251}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Mitochondrion. Note=The myristoylated c-ABL protein is reported to be nuclear. Sequestered into the cytoplasm through interaction with 14-3-3 proteins (By similarity). Localizes to mitochondria in response to oxidative stress. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:10988075, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:19878872, ECO:0000269|PubMed:20072125};
| null | null | null | null |
FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717' (By similarity). ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-191' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. Regulates T-cell differentiation in a TBX21-dependent manner (PubMed:21690296). Positively regulates chemokine-mediated T-cell migration, polarization, and homing to lymph nodes and immune-challenged tissues, potentially via activation of NEDD9/HEF1 and RAP1 (PubMed:22810897). Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity (PubMed:21690296). {ECO:0000250|UniProtKB:P00519, ECO:0000269|PubMed:11279004, ECO:0000269|PubMed:11279131, ECO:0000269|PubMed:11350980, ECO:0000269|PubMed:12107171, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293, ECO:0000269|PubMed:19878872, ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:21690296, ECO:0000269|PubMed:22810897, ECO:0000269|PubMed:7780740, ECO:0000269|PubMed:8194526, ECO:0000269|PubMed:9109492}.
|
Mus musculus (Mouse)
|
P00522
|
ABL_DROME
|
MGAQQGKDRGAHSGGGGSGAPVSCIGLSSSPVASVSPHCISSSSGVSSAPLGGGSTLRGSRIKSSSSGVASGSGSGGGGGGSGSGLSQRSGGHKDARCNPTVGLNIFTEHNEALLQSRPLPHIPAGSTAASLLADAAELQQHQQDSGGLGLQGSSLGGGHSSTTSVFESAHRWTSKENLLAPGPEEDDPQLFVALYDFQAGGENQLSLKKGEQVRILSYNKSGEWCEAHSDSGNVGWVPSNYVTPLNSLEKHSWYHGPISRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRISEDPDGKVFVTQEAKFNTLAELVHHHSVPHEGHGLITPLLYPAPKQNKPTVFPLSPEPDEWEICRTDIMMKHKLGGGQYGEVYEAVWKRYGNTVAVKTLKEDTMALKDFLEEAAIMKEMKHPNLVQLIGVCTREPPFYIITEFMSHGNLLDFLRSAGRETLDAVALLYMATQIASGMSYLESRNYIHRDLAARNCLVGDNKLVKVADFGLARLMRDDTYTAHAGAKFPIKWTAPEGLAYNKFSTKSDVWAFGVLLWEIATYGMSPYPAIDLTDVYHKLDKGYRMERPPGCPPEVYDLMRQCWQWDATDRPTFKSIHHALEHMFQESSITEAVEKQLNANATSASSSAPSTSGVATGGGATTTTAASGCASSSSATASLSLTPQMVKKGLPGGQALTPNAHHNDPHQQQASTPMSETGSTSTKLSTFSSQGKGNVQMRRTTNKQGKQAPAPPKRTSLLSSSRDSTYREEDPANARCNFIDDLSTNGLARDINSLTQRYDSETDPAADPDTDATGDSLEQSLSQVIAAPVTNKMQHSLHSGGGGGGIGPRSSQQHSSFKRPTGTPVMGNRGLETRQSKRSQLHSQAPGPGPPSTQPHHGNNGVVTSAHPITVGALDVMNVKQVVNRYGTLPKGARIGAYLDSLEDSSEAAPALPATAPSLPPANGHATPPAARLNPKASPIPPQQMIRSNSSGGVTMQNNAAASLNKLQRHRTTTEGTMMTFSSFRAGGSSSSPKRSASGVASGVQPALANLEFPPPPLDLPPPPEEFEGGPPPPPPAPESAVQAIQQHLHAQLPNNGNISNGNGTNNNDSSHNDVSNIAPSVEEASSRFGVSLRKREPSTDSCSSLGSPPEDLKEKLITEIKAAGKDTAPASHLANGSGIAVVDPVSLLVTELAESMNLPKPPPQQQQKLTNGNSTGSGFKAQLKKVEPKKMSAPMPKAEPANTIIDFKAHLRRVDKEKEPATPAPAPATVAVANNANCNTTGTLNRKEDGSKKFSQAMQKTEIKIDVTNSNVEADAGAAGEGDLGKRRSTGSINSLKKLWEQQPPAPDYATSTILQQQPSVVNGGGTPNAQLSPKYGMKSGAINTVGTLPAKLGNKQPPAAPPPPPPNCTTSNSSTTSISTSSRDCTSRQQASSTIKTSHSTQLFTDDEEQSHTEGLGSGGQGSADMTQSLYEQKPQIQQKPAVPHKPTKLTIYATPIAKLTEPASSASSTQISRESILELVGLLEGSLKHPVNAIAGSQWLQLSDKLNILHNSCVIFAENGAMPPHSKFQFRELVTRVEAQSQHLRSAGSKNVQDNERLVAEVGQSLRQISNALNR
|
2.7.10.2
| null |
axis elongation [GO:0003401]; axon guidance [GO:0007411]; axon midline choice point recognition [GO:0016199]; axonogenesis [GO:0007409]; branchiomotor neuron axon guidance [GO:0021785]; central nervous system development [GO:0007417]; chemical synaptic transmission [GO:0007268]; compound eye development [GO:0048749]; dendrite morphogenesis [GO:0048813]; dorsal closure [GO:0007391]; epithelial cell morphogenesis [GO:0003382]; learning or memory [GO:0007611]; motor neuron axon guidance [GO:0008045]; negative regulation of neuron projection development [GO:0010977]; negative regulation of synaptic assembly at neuromuscular junction [GO:0045886]; neuron migration [GO:0001764]; ommatidial rotation [GO:0016318]; ovarian nurse cell to oocyte transport [GO:0007300]; peptidyl-tyrosine phosphorylation [GO:0018108]; photoreceptor cell axon guidance [GO:0072499]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of protein export from nucleus [GO:0046827]; protein autophosphorylation [GO:0046777]; regulation of actin polymerization or depolymerization [GO:0008064]; regulation of adherens junction organization [GO:1903391]; regulation of apoptotic process [GO:0042981]; regulation of cell shape [GO:0008360]; regulation of protein localization [GO:0032880]; regulation of protein stability [GO:0031647]; ventral cord development [GO:0007419]; ventral furrow formation [GO:0007370]
|
apical cortex [GO:0045179]; axon [GO:0030424]; cell cortex [GO:0005938]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; synapse [GO:0045202]
|
ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]
|
PF08919;PF07714;PF00017;PF00018;
|
1.20.120.330;3.30.505.10;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, ABL subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:2832740};
| null | null | null | null |
FUNCTION: Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis; critical for embryonic epithelial morphogenesis regulating cell shape changes and cell migration (PubMed:11756472, PubMed:12973825, PubMed:9635189). Plays a critical role in transducing embryonic midline repulsive cues; may regulate cytoskeletal dynamics underlying a growth cone's response to midline cues (PubMed:12973825). The ability of pCC/MP2 axons to correctly interpret midline repulsive cues and stay on the ipsilateral side is dependent on the strength of both Slit/robo and Abl-dependent signaling pathways (PubMed:12973825). Function in neurons is essential for adult survival, and is important for climbing behavior and activity (PubMed:37041188). {ECO:0000269|PubMed:11756472, ECO:0000269|PubMed:12973825, ECO:0000269|PubMed:37041188, ECO:0000269|PubMed:9635189}.
|
Drosophila melanogaster (Fruit fly)
|
P00523
|
SRC_CHICK
|
MGSSKSKPKDPSQRRRSLEPPDSTHHGGFPASQTPNKTAAPDTHRTPSRSFGTVATEPKLFGGFNTSDTVTSPQRAGALAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRLTNVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKDPEERPTFEYLQAFLEDYFTSTEPQYQPGENL
|
2.7.10.2
| null |
bone resorption [GO:0045453]; cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; epidermal growth factor receptor signaling pathway [GO:0007173]; innate immune response [GO:0045087]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; osteoclast development [GO:0036035]; phosphorylation [GO:0016310]; progesterone receptor signaling pathway [GO:0050847]; regulation of cell cycle [GO:0051726]
|
cell junction [GO:0030054]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal adhesion [GO:0005925]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
ATP binding [GO:0005524]; connexin binding [GO:0071253]; heme binding [GO:0020037]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein phosphatase binding [GO:0019903]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102]
|
PF07714;PF00017;PF00018;
|
3.30.505.10;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, SRC subfamily
|
PTM: Myristoylated at Gly-2, and this is essential for targeting to membranes. {ECO:0000250}.; PTM: Dephosphorylated at Tyr-527 by PTPRJ. Phosphorylated on Tyr-527 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-416. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-527, the SH3 domain engaged with the SH2-kinase linker, and Tyr-416 dephosphorylated. Dephosphorylation of Tyr-527 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-527, Tyr-416 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-527 by CSK allows this interaction to reform, resulting in SRC inactivation (By similarity). {ECO:0000250}.; PTM: S-nitrosylation is important for activation of its kinase activity. {ECO:0000269|PubMed:19948721}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1378446, ECO:0000269|PubMed:8325872}; Lipid-anchor {ECO:0000250|UniProtKB:P05480}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P05480}. Endosome membrane {ECO:0000269|PubMed:1378446}; Peripheral membrane protein {ECO:0000269|PubMed:1378446}. Nucleus {ECO:0000269|PubMed:8550628}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8325872}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P05480}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P12931}. Note=Localizes to focal adhesion sites following integrin engagement (By similarity). Localization to focal adhesion sites requires myristoylation and the SH3 domain. {ECO:0000250|UniProtKB:P05480, ECO:0000250|UniProtKB:P12931}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates involved in this process (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (By similarity). Also active at the sites of cell-cell contact adherens junctions and at gap junctions. Implicated in the regulation of pre-mRNA-processing (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus (PubMed:1717492, PubMed:8550628). Involved in anchorage-independent cell growth (PubMed:19307596). {ECO:0000250|UniProtKB:P12931, ECO:0000269|PubMed:1717492, ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:8550628, ECO:0000305|PubMed:11964124, ECO:0000305|PubMed:8672527, ECO:0000305|PubMed:9442882}.
|
Gallus gallus (Chicken)
|
P00524
|
SRC_RSVSA
|
MGSSKSKPKDPSQRRRSLEPPDSTHHGGFPASQTPNKTAAPDTHRTPSRSFGTVATEPKLFGGFNTSDTVTSPQRAGALAGGVTTFVALYDYESWIETDLSFKKGERLQIVNNTEGNWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRLTNVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVIEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMGNGEVLDRVERGYRMPCPPECPESLHDLMCQCWRRDPEERPTFEYLQAQLLPACVLEVAE
|
2.7.10.2
| null |
bone resorption [GO:0045453]; cell adhesion [GO:0007155]; epidermal growth factor receptor signaling pathway [GO:0007173]; innate immune response [GO:0045087]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; osteoclast development [GO:0036035]; phosphorylation [GO:0016310]; progesterone receptor signaling pathway [GO:0050847]
|
extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]
|
ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102]
|
PF07714;PF00017;PF00018;
|
3.30.505.10;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, SRC subfamily
|
PTM: The phosphorylated form is termed pp60v-src. {ECO:0000269|PubMed:6264320}.
| null |
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro. Causes mitotic slippage in addition to cytokinesis failure in the host cell (PubMed:30135207). Phosphorylates and attenuates the activity of host CDK1, possibly causing the mitotic slippage (PubMed:30135207). {ECO:0000269|PubMed:30135207}.
|
Rous sarcoma virus subgroup A (strain Schmidt-Ruppin) (RSV-SR-A)
|
P00525
|
SRC_AVISR
|
MGSSKSKPKDPSQRRCSLEPPDSTHHGGFPASQTPNKTAAPDTHRTPSRSFGTVATEPKLFGGFNTSDTVTSPQRAGALAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRLTNVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMGNGEVLDRVERGYRMPCPPECPESLHDLMCQCWRRDPEERPTFEYLQAQLLPACVLEVAE
|
2.7.10.2
| null |
bone resorption [GO:0045453]; cell adhesion [GO:0007155]; epidermal growth factor receptor signaling pathway [GO:0007173]; innate immune response [GO:0045087]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; osteoclast development [GO:0036035]; phosphorylation [GO:0016310]; progesterone receptor signaling pathway [GO:0050847]
|
extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]
|
ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102]
|
PF07714;PF00017;PF00018;
|
3.30.505.10;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, SRC subfamily
|
PTM: The phosphorylated form is termed pp60v-src. {ECO:0000250|UniProtKB:P00524}.
| null |
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro.
|
Avian sarcoma virus (strain rASV1441)
|
P00526
|
SRC_RSVP
|
MGSSKSKPKDPSQRRHSLEPPDSTHHGGFPASQTPDETAAPDAHRNPSRSFGTVATEPKLFWGFNTSDTVTSPQRAGALAGGVTTFVALYDYESWTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRKSETAKGAYCLSVSDFDNAKGPNVKHYKIYKLYSGGFYITSRTQFGSLQQLVAYYSKHADGLCHRLANVCPTSKPQTQGLAKDAWEIPRESLRLEAKLGQGCFGEVWMGTWNDTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVIEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKDPEERPTFKYLQAQLLPACVLEVAE
|
2.7.10.2
| null |
bone resorption [GO:0045453]; cell adhesion [GO:0007155]; epidermal growth factor receptor signaling pathway [GO:0007173]; innate immune response [GO:0045087]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; osteoclast development [GO:0036035]; phosphorylation [GO:0016310]; progesterone receptor signaling pathway [GO:0050847]
|
extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]
|
ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102]
|
PF07714;PF00017;PF00018;
|
3.30.505.10;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, SRC subfamily
|
PTM: The phosphorylated form is termed pp60v-src. {ECO:0000269|PubMed:6264320}.
| null |
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro.
|
Rous sarcoma virus subgroup C (strain Prague) (RSV-Pr-C)
|
P00528
|
SRC64_DROME
|
MGNKCCSKRQDQELALAYPTGGYKKSDYTFGQTHINSSGGGNMGGVLGQKHNNGGSLDSRYTPDPNHRGPLKIGGKGGVDIIRPRTTPTGVPGVVLKRVVVALYDYKSRDESDLSFMKGDRMEVIDDTESDWWRVVNLTTRQEGLIPLNFVAEERSVNSEDWFFENVLRKEADKLLLAEENPRGTFLVRPSEHNPNGYSLSVKDWEDGRGYHVKHYRIKPLDNGGYYIATNQTFPSLQALVMAYSKNALGLCHILSRPCPKPQPQMWDLGPELRDKYEIPRSEIQLLRKLGRGNFGEVFYGKWRNSIDVAVKTLREGTMSTAAFLQEAAIMKKFRHNRLVALYAVCSQEEPIYIVQEYMSKGSLLDFLREGDGRYLHFEDLIYIATQVASGMEYLESKQLIHRDLAARNVLIGENNVAKICDFGLARVIADDEYCPKQGSRFPVKWTAPEAIIYGKFSIKSDVWSYGILLMELFTYGQVPYPGMHSREVIENIERGFRMPKPTNHYFPDNIYQLLLQCWDAVPEKRPTFEFLNHYFESFSVTSEVPYREVQD
|
2.7.10.2
| null |
actin cytoskeleton organization [GO:0030036]; adherens junction organization [GO:0034332]; axon guidance [GO:0007411]; cell differentiation [GO:0030154]; cellularization [GO:0007349]; epithelial cell-cell adhesion [GO:0090136]; female germline ring canal formation [GO:0007301]; female germline ring canal formation, actin assembly [GO:0008302]; female germline ring canal stabilization [GO:0008335]; filtration diaphragm assembly [GO:0036058]; germarium-derived egg chamber formation [GO:0007293]; germarium-derived female germ-line cyst encapsulation [GO:0030708]; innate immune response [GO:0045087]; long-term memory [GO:0007616]; mushroom body development [GO:0016319]; negative regulation of hippo signaling [GO:0035331]; negative regulation of synaptic assembly at neuromuscular junction [GO:0045886]; oocyte karyosome formation [GO:0030717]; oogenesis [GO:0048477]; open tracheal system development [GO:0007424]; ovarian fusome organization [GO:0030723]; ovarian nurse cell to oocyte transport [GO:0007300]; parallel actin filament bundle assembly [GO:0030046]; phosphorylation [GO:0016310]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of fibroblast growth factor receptor signaling pathway [GO:0045743]; positive regulation of sevenless signaling pathway [GO:0045874]; positive regulation of torso signaling pathway [GO:0120176]; regulation of actin polymerization or depolymerization [GO:0008064]; regulation of synaptic plasticity [GO:0048167]; salivary gland morphogenesis [GO:0007435]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; germline ring canal [GO:0045172]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102]
|
PF07714;PF00017;PF00018;
|
3.30.505.10;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, SRC subfamily
|
PTM: Phosphorylated. {ECO:0000269|PubMed:31491385}.
| null |
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Tyrosine-protein kinase that may play a role in the development of neural tissue and smooth muscle (PubMed:2996778). May contribute to tyrosine phosphorylation of Dscam1, a cell surface receptor involved in targeting of growing axons during eye morphogenesis (PubMed:12014990). {ECO:0000269|PubMed:12014990, ECO:0000269|PubMed:2996778}.
|
Drosophila melanogaster (Fruit fly)
|
P00533
|
EGFR_HUMAN
|
MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA
|
2.7.10.1
| null |
activation of phospholipase C activity [GO:0007202]; astrocyte activation [GO:0048143]; cell surface receptor signaling pathway [GO:0007166]; cell-cell adhesion [GO:0098609]; cellular response to amino acid stimulus [GO:0071230]; cellular response to cadmium ion [GO:0071276]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to estradiol stimulus [GO:0071392]; cellular response to mechanical stimulus [GO:0071260]; cellular response to reactive oxygen species [GO:0034614]; cellular response to xenobiotic stimulus [GO:0071466]; cerebral cortex cell migration [GO:0021795]; circadian rhythm [GO:0007623]; digestive tract morphogenesis [GO:0048546]; diterpenoid metabolic process [GO:0016101]; embryonic placenta development [GO:0001892]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell proliferation [GO:0050673]; ERBB2-EGFR signaling pathway [GO:0038134]; eyelid development in camera-type eye [GO:0061029]; hair follicle development [GO:0001942]; hydrogen peroxide metabolic process [GO:0042743]; learning or memory [GO:0007611]; liver regeneration [GO:0097421]; lung development [GO:0030324]; midgut development [GO:0007494]; morphogenesis of an epithelial fold [GO:0060571]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cardiocyte differentiation [GO:1905208]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of protein catabolic process [GO:0042177]; neurogenesis [GO:0022008]; neuron projection morphogenesis [GO:0048812]; ossification [GO:0001503]; ovulation cycle [GO:0042698]; peptidyl-tyrosine autophosphorylation [GO:0038083]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of bone resorption [GO:0045780]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell growth [GO:0030307]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045737]; positive regulation of DNA repair [GO:0045739]; positive regulation of DNA replication [GO:0045740]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of mucus secretion [GO:0070257]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of phosphorylation [GO:0042327]; positive regulation of prolactin secretion [GO:1902722]; positive regulation of protein kinase C activity [GO:1900020]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of superoxide anion generation [GO:0032930]; positive regulation of synaptic transmission, glutamatergic [GO:0051968]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vasoconstriction [GO:0045907]; protein autophosphorylation [GO:0046777]; protein insertion into membrane [GO:0051205]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of JNK cascade [GO:0046328]; regulation of peptidyl-tyrosine phosphorylation [GO:0050730]; regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051896]; response to calcium ion [GO:0051592]; response to cobalamin [GO:0033590]; response to hydroxyisoflavone [GO:0033594]; response to UV-A [GO:0070141]; salivary gland morphogenesis [GO:0007435]; signal transduction [GO:0007165]; tongue development [GO:0043586]; translation [GO:0006412]; vasodilation [GO:0042311]
|
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cell junction [GO:0030054]; cell surface [GO:0009986]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; Golgi membrane [GO:0000139]; intracellular vesicle [GO:0097708]; membrane [GO:0016020]; membrane raft [GO:0045121]; multivesicular body, internal vesicle lumen [GO:0097489]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; receptor complex [GO:0043235]; ruffle membrane [GO:0032587]; Shc-EGFR complex [GO:0070435]
|
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; ATPase binding [GO:0051117]; cadherin binding [GO:0045296]; calmodulin binding [GO:0005516]; chromatin binding [GO:0003682]; double-stranded DNA binding [GO:0003690]; enzyme binding [GO:0019899]; epidermal growth factor binding [GO:0048408]; epidermal growth factor receptor activity [GO:0005006]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; kinase binding [GO:0019900]; MAP kinase kinase kinase activity [GO:0004709]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]; protein tyrosine kinase activator activity [GO:0030296]; protein tyrosine kinase activity [GO:0004713]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; transmembrane signaling receptor activity [GO:0004888]; ubiquitin protein ligase binding [GO:0031625]; virus receptor activity [GO:0001618]
|
PF00757;PF14843;PF07714;PF01030;PF21314;
|
1.20.5.420;3.80.20.20;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, EGF receptor subfamily
|
PTM: Phosphorylated on Tyr residues in response to EGF (PubMed:20462955, PubMed:27153536). Phosphorylation at Ser-695 is partial and occurs only if Thr-693 is phosphorylated. Phosphorylation at Thr-678 and Thr-693 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation. Dephosphorylation by PTPRJ prevents endocytosis and stabilizes the receptor at the plasma membrane. Autophosphorylation at Tyr-1197 is stimulated by methylation at Arg-1199 and enhances interaction with PTPN6. Autophosphorylation at Tyr-1092 and/or Tyr-1110 recruits STAT3. Dephosphorylated by PTPN1 and PTPN2. {ECO:0000269|PubMed:10523301, ECO:0000269|PubMed:12873986, ECO:0000269|PubMed:16083266, ECO:0000269|PubMed:19563760, ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:2543678, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:3138233}.; PTM: Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting (PubMed:27153536). Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs. Deubiquitination by OTUD7B prevents degradation. Ubiquitinated by RNF115 and RNF126 (By similarity). Ubiquitinated by ZNRF1 or CBL at different lysines in response to EGF stimulation; leading to recruitment of the ESCRT machinery and subsequent degradation in the lysosomes (PubMed:33996800). Deubiquitinated by UCHL1 leading to the inhibition of its degradation (By similarity). {ECO:0000250|UniProtKB:Q01279, ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:22179831, ECO:0000269|PubMed:22298428, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:33996800}.; PTM: Palmitoylated on Cys residues by ZDHHC20. Palmitoylation inhibits internalization after ligand binding, and increases the persistence of tyrosine-phosphorylated EGFR at the cell membrane. Palmitoylation increases the amplitude and duration of EGFR signaling. {ECO:0000269|PubMed:27153536}.; PTM: Methylated. Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197. {ECO:0000269|PubMed:19563760, ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:21258366}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:23589287, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:2790960, ECO:0000269|PubMed:35538033}; Single-pass type I membrane protein {ECO:0000269|PubMed:27153536}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:27153536}; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Nucleus membrane; Single-pass type I membrane protein. Endosome {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:27153536}. Endosome membrane. Nucleus {ECO:0000269|PubMed:17115032, ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:20551055, ECO:0000269|PubMed:20674546}. Note=In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER (PubMed:17909029, PubMed:20674546). Endocytosed upon activation by ligand (PubMed:17182860, PubMed:17909029, PubMed:27153536, PubMed:2790960). Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) (PubMed:20551055). {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:20674546, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:2790960}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:15374980, ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:18046415, ECO:0000269|PubMed:18227510, ECO:0000269|PubMed:19560417, ECO:0000269|PubMed:19563760};
| null | null | null | null |
FUNCTION: Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:10805725, PubMed:27153536, PubMed:2790960, PubMed:35538033). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF (PubMed:12297049, PubMed:15611079, PubMed:17909029, PubMed:20837704, PubMed:27153536, PubMed:2790960, PubMed:7679104, PubMed:8144591, PubMed:9419975). Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (PubMed:27153536). May also activate the NF-kappa-B signaling cascade (PubMed:11116146). Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling (PubMed:11602604). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589). Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration (PubMed:20462955). Plays a role in enhancing learning and memory performance (By similarity). Plays a role in mammalian pain signaling (long-lasting hypersensitivity) (By similarity). {ECO:0000250|UniProtKB:Q01279, ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11116146, ECO:0000269|PubMed:11483589, ECO:0000269|PubMed:11602604, ECO:0000269|PubMed:12297049, ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:12873986, ECO:0000269|PubMed:15374980, ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:15611079, ECO:0000269|PubMed:17115032, ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:19560417, ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:20837704, ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:2790960, ECO:0000269|PubMed:35538033, ECO:0000269|PubMed:7679104, ECO:0000269|PubMed:8144591, ECO:0000269|PubMed:9419975}.; FUNCTION: Isoform 2 may act as an antagonist of EGF action.; FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins. {ECO:0000269|PubMed:21516087}.
|
Homo sapiens (Human)
|
P00536
|
MOS_MOUSE
|
MPSPLSLCRYLPRELSPSVDSRSCSIPLVAPRKAGKLFLGTTPPRAPGLPRRLAWFSIDWEQVCLMHRLGSGGFGSVYKATYHGVPVAIKQVNKCTKDLRASQRSFWAELNIARLRHDNIVRVVAASTRTPEDSNSLGTIIMEFGGNVTLHQVIYGATRSPEPLSCREQLSLGKCLKYSLDVVNGLLFLHSQSILHLDLKPANILISEQDVCKISDFGCSQKLQDLRCRQASPHHIGGTYTHQAPEILKGEIATPKADIYSFGITLWQMTTREVPYSGEPQYVQYAVVAYNLRPSLAGAVFTASLTGKTLQNIIQSCWEARALQRPGAELLQRDLKAFRGALG
|
2.7.11.1
| null |
chromatin organization [GO:0006325]; establishment of meiotic spindle orientation [GO:0051296]; MAPK cascade [GO:0000165]; meiotic spindle organization [GO:0000212]; negative regulation of metaphase/anaphase transition of meiotic cell cycle [GO:1902103]; oocyte maturation [GO:0001556]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of MAPK cascade [GO:0043410]; protein autophosphorylation [GO:0046777]; regulation of meiotic nuclear division [GO:0040020]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00540}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Serine/threonine kinase involved in the regulation of MAPK signaling. Is an activator of the ERK1/2 signaling cascade playing an essential role in the stimulation of oocyte maturation. {ECO:0000250|UniProtKB:P00540}.
|
Mus musculus (Mouse)
|
P00539
|
MOS_RAT
|
MPSPLILCRYLPRELSPTVDSRSCSSPLVASRAGKFLGATPPRAPRLSRRLAWCFIDWGQVCLLHRLGSGGFGSVYKATYHGVPVAIKQVNKCTRTLRASQRNFWAELNIARLHHDNIIRVVAASTRTPEGSNSLGTIIMEFGGNVTLHQVIYGATRSPEPLSCREQLSLGKCLKYSLDIVNGLLFLHSQSILHLDLKPANILISEKDVCKISDFGCSQKLQDLRCRPSLHHIGGTYTHQAPELLKGEIATPKADIYSFGITLWQMTTREVPYSGEPQYVQYAVVAYNLRPHWQAVFTASLTGKTLQNNVQSCWEARALQRPGAELLQKDLKAFRGALG
|
2.7.11.1
| null |
chromatin organization [GO:0006325]; establishment of meiotic spindle orientation [GO:0051296]; intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; meiotic spindle organization [GO:0000212]; negative regulation of metaphase/anaphase transition of meiotic cell cycle [GO:1902103]; oocyte maturation [GO:0001556]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of MAPK cascade [GO:0043410]; protein autophosphorylation [GO:0046777]; regulation of meiotic nuclear division [GO:0040020]; signal transduction [GO:0007165]; spermatogenesis [GO:0007283]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00540}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Serine/threonine kinase involved in the regulation of MAPK signaling. Is an activator of the ERK1/2 signaling cascade playing an essential role in the stimulation of oocyte maturation. {ECO:0000250|UniProtKB:P00540}.
|
Rattus norvegicus (Rat)
|
P00540
|
MOS_HUMAN
|
MPSPLALRPYLRSEFSPSVDARPCSSPSELPAKLLLGATLPRAPRLPRRLAWCSIDWEQVCLLQRLGAGGFGSVYKATYRGVPVAIKQVNKCTKNRLASRRSFWAELNVARLRHDNIVRVVAASTRTPAGSNSLGTIIMEFGGNVTLHQVIYGAAGHPEGDAGEPHCRTGGQLSLGKCLKYSLDVVNGLLFLHSQSIVHLDLKPANILISEQDVCKISDFGCSEKLEDLLCFQTPSYPLGGTYTHRAPELLKGEGVTPKADIYSFAITLWQMTTKQAPYSGERQHILYAVVAYDLRPSLSAAVFEDSLPGQRLGDVIQRCWRPSAAQRPSARLLLVDLTSLKAELG
|
2.7.11.1
| null |
chromatin organization [GO:0006325]; establishment of meiotic spindle orientation [GO:0051296]; MAPK cascade [GO:0000165]; meiotic spindle organization [GO:0000212]; negative regulation of metaphase/anaphase transition of meiotic cell cycle [GO:1902103]; oocyte maturation [GO:0001556]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of MAPK cascade [GO:0043410]; protein autophosphorylation [GO:0046777]; regulation of meiotic nuclear division [GO:0040020]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:35670744}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Serine/threonine kinase involved in the regulation of MAPK signaling. Is an activator of the ERK1/2 signaling cascade playing an essential role in the stimulation of oocyte maturation. {ECO:0000269|PubMed:34779126, ECO:0000269|PubMed:34997960, ECO:0000269|PubMed:35670744}.
|
Homo sapiens (Human)
|
P00545
|
KFMS_FSVMD
|
RMPSGPGHYGASAETPGPRPPLCPASSCCLPTEAMGPRALLVLLMATAWHAQGVPVIQPSGPELVVEPGTTVTLRCVGNGSVEWDGPISPHWNLDLDPPSSILTTNNATFQNTGTYHCTEPGNPRGGNATIHLYVKDPARPWKVLAQEVTVLEGQDALLPCLLTDPALEAGVSLVRVRGRPVLRQTNYSFSPWHGFTIHKAKFIENHVYQCSARVDGRTVTSMGIWLKVQKDISGPATLTLEPAELVRIQGEAAQIVCSASNIDVNFDVSLRHGDTKLTISQQSDFHDNRYQKVLTLNLDHVSFQDAGNYSCTATNAWGNHSASMVFRVVESAYSNLTSEQSLLQEVTVGEKVDLQVKVEAYPGLESFNWTYLGPFSDYQDKLDFVTIKDTYRYTSTLSLPRLKRSESGRYSFLARNAGGQNALTFELTLRYPPEVRVTMTLINGSDTLLCEASGYPQPSVTWVQCRSHTDRCDESAGLVLEDSHSEVLSQVPFYEVIVHSLLAIGTLEHNRTYECRAFNSVGNSSQTFWPISIGAHTPLPDELLFTPVLLTCMSIMALLLLLLLLLLYKYKQKPKYQVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGTGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRQAEAMLGPSLSVGQDPEAGAGYKNIHLEKKYVRRDSGFSSQGVDTYVEMRPVSTSSSNDSFSEEDLGKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTSGRVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTRRPTFQQICSLLQKQAQEDRRVPNYTNLPSSSSSRLLRPWQRTPPVAR
|
2.7.10.1
| null |
osteoclast differentiation [GO:0030316]; phosphorylation [GO:0016310]; positive regulation of cell migration [GO:0030335]; regulation of MAPK cascade [GO:0043408]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
CSF1-CSF1R complex [GO:1990682]; membrane [GO:0016020]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; macrophage colony-stimulating factor receptor activity [GO:0005011]
|
PF00047;PF07714;
|
2.60.40.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Truncated version of the receptor for colony-stimulating factor 1 (CSF-1).
|
Feline sarcoma virus (strain McDonough)
|
P00546
|
CDK1_YEAST
|
MSGELANYKRLEKVGEGTYGVVYKALDLRPGQGQRVVALKKIRLESEDEGVPSTAIREISLLKELKDDNIVRLYDIVHSDAHKLYLVFEFLDLDLKRYMEGIPKDQPLGADIVKKFMMQLCKGIAYCHSHRILHRDLKPQNLLINKDGNLKLGDFGLARAFGVPLRAYTHEIVTLWYRAPEVLLGGKQYSTGVDTWSIGCIFAEMCNRKPIFSGDSEIDQIFKIFRVLGTPNEAIWPDIVYLPDFKPSFPQWRRKDLSQVVPSLDPRGIDLLDKLLAYDPINRISARRAAIHPYFQES
|
2.7.11.22
| null |
7-methylguanosine mRNA capping [GO:0006370]; cell division [GO:0051301]; DNA damage response [GO:0006974]; DNA double-strand break processing [GO:0000729]; double-strand break repair via nonhomologous end joining [GO:0006303]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; meiotic DNA double-strand break processing [GO:0000706]; mitotic sister chromatid biorientation [GO:1990758]; mitotic spindle assembly [GO:0090307]; negative regulation of DNA replication origin binding [GO:1902596]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of double-strand break repair via nonhomologous end joining [GO:2001033]; negative regulation of meiotic cell cycle [GO:0051447]; negative regulation of mitotic actomyosin contractile ring assembly [GO:1903500]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of sister chromatid cohesion [GO:0045875]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of glycogen catabolic process [GO:0045819]; positive regulation of meiotic cell cycle [GO:0051446]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of mitotic DNA damage checkpoint [GO:1904291]; positive regulation of mitotic spindle pole body separation [GO:0010696]; positive regulation of nuclear cell cycle DNA replication [GO:0010571]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of trehalose catabolic process [GO:1901319]; positive regulation of triglyceride catabolic process [GO:0010898]; post-Golgi vesicle-mediated transport [GO:0006892]; protein catabolic process [GO:0030163]; protein localization to nuclear periphery [GO:1990139]; protein localization to nucleus [GO:0034504]; protein localization to spindle microtubule [GO:1902889]; protein phosphorylation [GO:0006468]; regulation of budding cell apical bud growth [GO:0010568]; regulation of cell cycle G1/S phase transition [GO:1902806]; regulation of chromatin organization [GO:1902275]; regulation of DNA-templated transcription [GO:0006355]; regulation of filamentous growth [GO:0010570]; regulation of G2/M transition of mitotic cell cycle [GO:0010389]; regulation of gene expression [GO:0010468]; regulation of protein localization [GO:0032880]; regulation of protein localization to chromatin [GO:1905634]; regulation of spindle assembly [GO:0090169]; regulation of telomere maintenance via telomerase [GO:0032210]; response to organic substance [GO:0010033]; signal transduction [GO:0007165]; synaptonemal complex assembly [GO:0007130]
|
cellular bud neck [GO:0005935]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; histone binding [GO:0042393]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II complex binding [GO:0000993]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000250|UniProtKB:P24941}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000250|UniProtKB:P04551};
| null | null | null | null |
FUNCTION: Cyclin-dependent kinase that acts as a master regulator of the mitotic and meiotic cell cycles (By similarity). Required to drive the G1-S transition (PubMed:2664468). More than 200 substrates have been identified (PubMed:14574415). Substrate specificity is in part regulated by the bound cyclin protein (By similarity). Phosphorylates YTA7 during S-phase to promote transcription of histones (PubMed:22156209). {ECO:0000250|UniProtKB:P04551, ECO:0000269|PubMed:14574415, ECO:0000269|PubMed:22156209, ECO:0000269|PubMed:2664468}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00549
|
KPYK1_YEAST
|
MSRLERLTSLNVVAGSDLRRTSIIGTIGPKTNNPETLVALRKAGLNIVRMNFSHGSYEYHKSVIDNARKSEELYPGRPLAIALDTKGPEIRTGTTTNDVDYPIPPNHEMIFTTDDKYAKACDDKIMYVDYKNITKVISAGRIIYVDDGVLSFQVLEVVDDKTLKVKALNAGKICSHKGVNLPGTDVDLPALSEKDKEDLRFGVKNGVHMVFASFIRTANDVLTIREVLGEQGKDVKIIVKIENQQGVNNFDEILKVTDGVMVARGDLGIEIPAPEVLAVQKKLIAKSNLAGKPVICATQMLESMTYNPRPTRAEVSDVGNAILDGADCVMLSGETAKGNYPINAVTTMAETAVIAEQAIAYLPNYDDMRNCTPKPTSTTETVAASAVAAVFEQKAKAIIVLSTSGTTPRLVSKYRPNCPIILVTRCPRAARFSHLYRGVFPFVFEKEPVSDWTDDVEARINFGIEKAKEFGILKKGDTYVSIQGFKAGAGHSNTLQVSTV
|
2.7.1.40
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10413488}; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000305|PubMed:9519410};
|
cellular response to insulin stimulus [GO:0032869]; glycolytic process [GO:0006096]; phosphorylation [GO:0016310]; pyruvate metabolic process [GO:0006090]
|
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; potassium ion binding [GO:0030955]; pyruvate kinase activity [GO:0004743]
|
PF00224;PF02887;
|
3.20.20.60;2.40.33.10;3.40.1380.20;
|
Pyruvate kinase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; EC=2.7.1.40; Evidence={ECO:0000269|PubMed:10413488};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.31 mM for phosphoenolpyruvate (with magnesium as divalent cation) {ECO:0000269|PubMed:10413488}; KM=0.021 mM for phosphoenolpyruvate (with manganese as divalent cation) {ECO:0000269|PubMed:10413488}; KM=1.1 mM for ADP (with magnesium as divalent cation) {ECO:0000269|PubMed:10413488}; KM=0.24 mM for ADP (with manganese as divalent cation) {ECO:0000269|PubMed:10413488};
|
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:10413488};
| null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00550
|
PTM3C_ECOLI
|
MSSDIKIKVQSFGRFLSNMVMPNIGAFIAWGIITALFIPTGWLPNETLAKLVGPMITYLLPLLIGYTGGKLVGGERGGVVGAITTMGVIVGADMPMFLGSMIAGPLGGWCIKHFDRWVDGKIKSGFEMLVNNFSAGIIGMILAILAFLGIGPIVEALSKMLAAGVNFMVVHDMLPLASIFVEPAKILFLNNAINHGIFSPLGIQQSHELGKSIFFLIEANPGPGMGVLLAYMFFGRGSAKQSAGGAAIIHFLGGIHEIYFPYVLMNPRLILAVILGGMTGVFTLTILGGGLVSPASPGSILAVLAMTPKGAYFANIAGVCAAMAVSFVVSAILLKTSKVKEEDDIEAATRRMQDMKAESKGASPLSAGDVTNDLSHVRKIIVACDAGMGSSAMGAGVLRKKIQDAGLSQISVTNSAINNLPPDVDLVITHRDLTERAMRQVPQAQHISLTNFLDSGLYTSLTERLVAAQRHTANEEKVKDSLKDSFDDSSANLFKLGAENIFLGRKAATKEEAIRFAGEQLVKGGYVEPEYVQAMLDREKLTPTYLGESIAVPHGTVEAKDRVLKTGVVFCQYPEGVRFGEEEDDIARLVIGIAARNNEHIQVITSLTNALDDESVIERLAHTTSVDEVLELLAGRK
|
2.7.1.197
| null |
mannitol transmembrane transport [GO:0015797]; phosphoenolpyruvate-dependent sugar phosphotransferase system [GO:0009401]; phosphorylation [GO:0016310]
|
plasma membrane [GO:0005886]
|
kinase activity [GO:0016301]; protein-N(PI)-phosphohistidine-mannitol phosphotransferase system transmembrane transporter activity [GO:0022872]; protein-phosphocysteine-mannitol phosphotransferase system transporter activity [GO:0090565]; protein-phosphocysteine-sugar phosphotransferase activity [GO:0090563]
|
PF00359;PF02378;PF02302;
|
3.40.50.2300;
| null |
PTM: An intramolecular phosphotransfer takes places between His-554 and Cys-384. {ECO:0000305|PubMed:16443929}.
|
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000269|PubMed:15919996, ECO:0000305|PubMed:6309813}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000269|PubMed:15919996, ECO:0000305|PubMed:368051}.
|
CATALYTIC ACTIVITY: Reaction=D-mannitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-mannitol 1-phosphate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:33363, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:16899, ChEBI:CHEBI:29979, ChEBI:CHEBI:61381, ChEBI:CHEBI:64837; EC=2.7.1.197; Evidence={ECO:0000269|PubMed:2123863, ECO:0000305|PubMed:368051};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=66 uM for mannitol phosphorylation {ECO:0000269|PubMed:2123863}; Vmax=21.7 nmol/min/mg enzyme toward mannitol {ECO:0000269|PubMed:2123863};
| null | null | null |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in D-mannitol transport (PubMed:2123863, PubMed:368051, PubMed:6427236). Also able to use D-mannonic acid (PubMed:6427236). {ECO:0000269|PubMed:2123863, ECO:0000269|PubMed:368051, ECO:0000269|PubMed:6427236}.
|
Escherichia coli (strain K12)
|
P00558
|
PGK1_HUMAN
|
MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGVPMPDKYSLEPVAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLENLRFHVEEEGKGKDASGNKVKAEPAKIEAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGPESSKKYAEAVTRAKQIVWNGPVGVFEWEAFARGTKALMDEVVKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKVLPGVDALSNI
|
2.7.2.3
| null |
canonical glycolysis [GO:0061621]; cellular response to hypoxia [GO:0071456]; epithelial cell differentiation [GO:0030855]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; negative regulation of angiogenesis [GO:0016525]; phosphorylation [GO:0016310]; plasminogen activation [GO:0031639]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; membrane raft [GO:0045121]
|
ADP binding [GO:0043531]; ATP binding [GO:0005524]; phosphoglycerate kinase activity [GO:0004618]; protein-disulfide reductase (NAD(P)) activity [GO:0047134]
|
PF00162;
|
3.40.50.1260;
|
Phosphoglycerate kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616, ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3; Evidence={ECO:0000269|PubMed:30323285, ECO:0000269|PubMed:7391028};
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. {ECO:0000269|PubMed:30323285, ECO:0000269|PubMed:7391028}.
| null | null |
FUNCTION: Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate (PubMed:30323285, PubMed:7391028). In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein) (PubMed:2324090). May play a role in sperm motility (PubMed:26677959). {ECO:0000269|PubMed:2324090, ECO:0000269|PubMed:26677959, ECO:0000269|PubMed:30323285, ECO:0000269|PubMed:7391028}.
|
Homo sapiens (Human)
|
P00560
|
PGK_YEAST
|
MSLSSKLSVQDLDLKDKRVFIRVDFNVPLDGKKITSNQRIVAALPTIKYVLEHHPRYVVLASHLGRPNGERNEKYSLAPVAKELQSLLGKDVTFLNDCVGPEVEAAVKASAPGSVILLENLRYHIEEEGSRKVDGQKVKASKEDVQKFRHELSSLADVYINDAFGTAHRAHSSMVGFDLPQRAAGFLLEKELKYFGKALENPTRPFLAILGGAKVADKIQLIDNLLDKVDSIIIGGGMAFTFKKVLENTEIGDSIFDKAGAEIVPKLMEKAKAKGVEVVLPVDFIIADAFSADANTKTVTDKEGIPAGWQGLDNGPESRKLFAATVAKAKTIVWNGPPGVFEFEKFAAGTKALLDEVVKSSAAGNTVIIGGGDTATVAKKYGVTDKISHVSTGGGASLELLEGKELPGVAFLSEKK
|
2.7.2.3
| null |
gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
ADP binding [GO:0043531]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; phosphoglycerate kinase activity [GO:0004618]
|
PF00162;
|
3.40.50.1260;
|
Phosphoglycerate kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11502169}. Mitochondrion {ECO:0000269|PubMed:16823961}.
|
CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616, ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
| null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00561
|
AK1H_ECOLI
|
MRVLKFGGTSVANAERFLRVADILESNARQGQVATVLSAPAKITNHLVAMIEKTISGQDALPNISDAERIFAELLTGLAAAQPGFPLAQLKTFVDQEFAQIKHVLHGISLLGQCPDSINAALICRGEKMSIAIMAGVLEARGHNVTVIDPVEKLLAVGHYLESTVDIAESTRRIAASRIPADHMVLMAGFTAGNEKGELVVLGRNGSDYSAAVLAACLRADCCEIWTDVDGVYTCDPRQVPDARLLKSMSYQEAMELSYFGAKVLHPRTITPIAQFQIPCLIKNTGNPQAPGTLIGASRDEDELPVKGISNLNNMAMFSVSGPGMKGMVGMAARVFAAMSRARISVVLITQSSSEYSISFCVPQSDCVRAERAMQEEFYLELKEGLLEPLAVTERLAIISVVGDGMRTLRGISAKFFAALARANINIVAIAQGSSERSISVVVNNDDATTGVRVTHQMLFNTDQVIEVFVIGVGGVGGALLEQLKRQQSWLKNKHIDLRVCGVANSKALLTNVHGLNLENWQEELAQAKEPFNLGRLIRLVKEYHLLNPVIVDCTSSQAVADQYADFLREGFHVVTPNKKANTSSMDYYHQLRYAAEKSRRKFLYDTNVGAGLPVIENLQNLLNAGDELMKFSGILSGSLSYIFGKLDEGMSFSEATTLAREMGYTEPDPRDDLSGMDVARKLLILARETGRELELADIEIEPVLPAEFNAEGDVAAFMANLSQLDDLFAARVAKARDEGKVLRYVGNIDEDGVCRVKIAEVDGNDPLFKVKNGENALAFYSHYYQPLPLVLRGYGAGNDVTAAGVFADLLRTLSWKLGV
|
1.1.1.3; 2.7.2.4
| null |
homoserine biosynthetic process [GO:0009090]; lysine biosynthetic process via diaminopimelate [GO:0009089]; phosphorylation [GO:0016310]; protein homotetramerization [GO:0051289]; threonine biosynthetic process [GO:0009088]
| null |
aspartate kinase activity [GO:0004072]; ATP binding [GO:0005524]; homoserine dehydrogenase activity [GO:0004412]; identical protein binding [GO:0042802]; NADP binding [GO:0050661]
|
PF00696;PF13840;PF00742;PF03447;
|
3.40.1160.10;3.40.50.720;3.30.2130.10;
|
Aspartokinase family; Homoserine dehydrogenase family
| null | null |
CATALYTIC ACTIVITY: Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde + NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3; CATALYTIC ACTIVITY: Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH; Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3; CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP; Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4;
| null |
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.; PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.; PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5.
| null | null | null |
Escherichia coli (strain K12)
|
P00562
|
AK2H_ECOLI
|
MSVIAQAGAKGRQLHKFGGSSLADVKCYLRVAGIMAEYSQPDDMMVVSAAGSTTNQLINWLKLSQTDRLSAHQVQQTLRRYQCDLISGLLPAEEADSLISAFVSDLERLAALLDSGINDAVYAEVVGHGEVWSARLMSAVLNQQGLPAAWLDAREFLRAERAAQPQVDEGLSYPLLQQLLVQHPGKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSEIDLQLRCSYTPDQGSTRIERVLASGTGARIVTSHDDVCLIEFQVPASQDFKLAHKEIDQILKRAQVRPLAVGVHNDRQLLQFCYTSEVADSALKILDEAGLPGELRLRQGLALVAMVGAGVTRNPLHCHRFWQQLKGQPVEFTWQSDDGISLVAVLRTGPTESLIQGLHQSVFRAEKRIGLVLFGKGNIGSRWLELFAREQSTLSARTGFEFVLAGVVDSRRSLLSYDGLDASRALAFFNDEAVEQDEESLFLWMRAHPYDDLVVLDVTASQQLADQYLDFASHGFHVISANKLAGASDSNKYRQIHDAFEKTGRHWLYNATVGAGLPINHTVRDLIDSGDTILSISGIFSGTLSWLFLQFDGSVPFTELVDQAWQQGLTEPDPRDDLSGKDVMRKLVILAREAGYNIEPDQVRVESLVPAHCEGGSIDHFFENGDELNEQMVQRLEAAREMGLVLRYVARFDANGKARVGVEAVREDHPLASLLPCDNVFAIESRWYRDNPLVIRGPGAGRDVTAGAIQSDINRLAQLL
|
1.1.1.3; 2.7.2.4
| null |
homoserine biosynthetic process [GO:0009090]; lysine biosynthetic process via diaminopimelate [GO:0009089]; methionine biosynthetic process [GO:0009086]; phosphorylation [GO:0016310]; threonine biosynthetic process [GO:0009088]
|
cytosol [GO:0005829]
|
aspartate kinase activity [GO:0004072]; ATP binding [GO:0005524]; homoserine dehydrogenase activity [GO:0004412]; NADP binding [GO:0050661]
|
PF00696;PF00742;PF03447;
|
3.40.1160.10;1.20.120.1320;3.40.50.720;
|
Aspartokinase family; Homoserine dehydrogenase family
| null | null |
CATALYTIC ACTIVITY: Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde + NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3; CATALYTIC ACTIVITY: Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH; Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3; CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP; Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4;
| null |
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.; PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.; PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5.
| null | null | null |
Escherichia coli (strain K12)
|
P00568
|
KAD1_HUMAN
|
MEEKLKKTKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRSEVSSGSARGKKLSEIMEKGQLVPLETVLDMLRDAMVAKVNTSKGFLIDGYPREVQQGEEFERRIGQPTLLLYVDAGPETMTQRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDSVFSQVCTHLDALK
|
2.7.4.10; 2.7.4.3; 2.7.4.6
| null |
ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleoside triphosphate biosynthetic process [GO:0009142]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; outer dense fiber [GO:0001520]
|
adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; nucleoside diphosphate kinase activity [GO:0004550]; nucleoside triphosphate adenylate kinase activity [GO:0046899]
|
PF00406;
|
3.40.50.300;
|
Adenylate kinase family, AK1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P05081}.
|
CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:2542324}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:23416111}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:23416111}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-diphosphate + ADP; Xref=Rhea:RHEA:13749, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.10; Evidence={ECO:0000269|PubMed:2542324}; CATALYTIC ACTIVITY: Reaction=ATP + GDP = ADP + GTP; Xref=Rhea:RHEA:27686, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000269|PubMed:23416111}; CATALYTIC ACTIVITY: Reaction=ATP + UDP = ADP + UTP; Xref=Rhea:RHEA:25098, ChEBI:CHEBI:30616, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000269|PubMed:23416111}; CATALYTIC ACTIVITY: Reaction=ATP + dGDP = ADP + dGTP; Xref=Rhea:RHEA:27690, ChEBI:CHEBI:30616, ChEBI:CHEBI:58595, ChEBI:CHEBI:61429, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000269|PubMed:23416111}; CATALYTIC ACTIVITY: Reaction=ATP + dTDP = ADP + dTTP; Xref=Rhea:RHEA:27682, ChEBI:CHEBI:30616, ChEBI:CHEBI:37568, ChEBI:CHEBI:58369, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000269|PubMed:23416111}; CATALYTIC ACTIVITY: Reaction=ADP + thiamine diphosphate = AMP + thiamine triphosphate; Xref=Rhea:RHEA:69180, ChEBI:CHEBI:58937, ChEBI:CHEBI:58938, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P05081};
| null | null | null | null |
FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP (PubMed:2542324). Exhibits nucleoside diphosphate kinase activity, catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donor (PubMed:23416111). Also catalyzes at a very low rate the synthesis of thiamine triphosphate (ThTP) from thiamine diphosphate (ThDP) and ADP (By similarity). {ECO:0000250|UniProtKB:P05081, ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:23416111, ECO:0000269|PubMed:2542324}.
|
Homo sapiens (Human)
|
P00569
|
KAD1_RABIT
|
MEEKLKKAKIIFVVGGPGSGKGTQCEKIVHKYGYTHLSTGDLLRAEVSSGSARGKKLSEIMEKGQLVPLETVLDMLRDAMVAKADTSKGFLIDGYPRQVQQGEEFERRIAQPTLLLYVDAGPETMQKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDNVFSQVCTHLDALK
|
2.7.4.10; 2.7.4.3; 2.7.4.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P05081};
|
ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; nucleoside triphosphate biosynthetic process [GO:0009142]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]
|
adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; nucleoside diphosphate kinase activity [GO:0004550]; nucleoside triphosphate adenylate kinase activity [GO:0046899]
|
PF00406;
|
3.40.50.300;
|
Adenylate kinase family, AK1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P05081}.
|
CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_03171}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-Rule:MF_03171}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-Rule:MF_03171}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-diphosphate + ADP; Xref=Rhea:RHEA:13749, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.10; Evidence={ECO:0000250|UniProtKB:P00568}; CATALYTIC ACTIVITY: Reaction=ATP + GDP = ADP + GTP; Xref=Rhea:RHEA:27686, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000250|UniProtKB:P00568}; CATALYTIC ACTIVITY: Reaction=ATP + UDP = ADP + UTP; Xref=Rhea:RHEA:25098, ChEBI:CHEBI:30616, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000250|UniProtKB:P00568}; CATALYTIC ACTIVITY: Reaction=ATP + dGDP = ADP + dGTP; Xref=Rhea:RHEA:27690, ChEBI:CHEBI:30616, ChEBI:CHEBI:58595, ChEBI:CHEBI:61429, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000250|UniProtKB:P00568}; CATALYTIC ACTIVITY: Reaction=ATP + dTDP = ADP + dTTP; Xref=Rhea:RHEA:27682, ChEBI:CHEBI:30616, ChEBI:CHEBI:37568, ChEBI:CHEBI:58369, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000250|UniProtKB:P00568}; CATALYTIC ACTIVITY: Reaction=ADP + thiamine diphosphate = AMP + thiamine triphosphate; Xref=Rhea:RHEA:69180, ChEBI:CHEBI:58937, ChEBI:CHEBI:58938, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P05081};
| null | null | null | null |
FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP (By similarity). Exhibits nucleoside diphosphate kinase activity, catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donor (By similarity). Also catalyzes at a very low rate the synthesis of thiamine triphosphate (ThTP) from thiamine diphosphate (ThDP) and ADP (By similarity). {ECO:0000250|UniProtKB:P00568, ECO:0000250|UniProtKB:P05081}.
|
Oryctolagus cuniculus (Rabbit)
|
P00570
|
KAD1_BOVIN
|
MEEKLKKTKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRAEVSSGSARGKMLSEIMEKGQLVPLETVLDMLRDAMVAKVDTSKGFLIDGYPREVQQGEEFERRIAQPTLLLYVDAGPETMTKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDNVFSQVCTHLDALK
|
2.7.4.10; 2.7.4.3; 2.7.4.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P05081};
|
ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; nucleoside triphosphate biosynthetic process [GO:0009142]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; outer dense fiber [GO:0001520]
|
adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; nucleoside diphosphate kinase activity [GO:0004550]; nucleoside triphosphate adenylate kinase activity [GO:0046899]
|
PF00406;
|
3.40.50.300;
|
Adenylate kinase family, AK1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P05081}.
|
CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_03171}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-Rule:MF_03171}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-Rule:MF_03171}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-diphosphate + ADP; Xref=Rhea:RHEA:13749, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.10; Evidence={ECO:0000250|UniProtKB:P00568}; CATALYTIC ACTIVITY: Reaction=ATP + GDP = ADP + GTP; Xref=Rhea:RHEA:27686, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000250|UniProtKB:P00568}; CATALYTIC ACTIVITY: Reaction=ATP + UDP = ADP + UTP; Xref=Rhea:RHEA:25098, ChEBI:CHEBI:30616, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000250|UniProtKB:P00568}; CATALYTIC ACTIVITY: Reaction=ATP + dGDP = ADP + dGTP; Xref=Rhea:RHEA:27690, ChEBI:CHEBI:30616, ChEBI:CHEBI:58595, ChEBI:CHEBI:61429, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000250|UniProtKB:P00568}; CATALYTIC ACTIVITY: Reaction=ATP + dTDP = ADP + dTTP; Xref=Rhea:RHEA:27682, ChEBI:CHEBI:30616, ChEBI:CHEBI:37568, ChEBI:CHEBI:58369, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000250|UniProtKB:P00568}; CATALYTIC ACTIVITY: Reaction=ADP + thiamine diphosphate = AMP + thiamine triphosphate; Xref=Rhea:RHEA:69180, ChEBI:CHEBI:58937, ChEBI:CHEBI:58938, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P05081};
| null | null | null | null |
FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP (By similarity). Exhibits nucleoside diphosphate kinase activity, catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donor (By similarity). Also catalyzes at a very low rate the synthesis of thiamine triphosphate (ThTP) from thiamine diphosphate (ThDP) and ADP (By similarity). {ECO:0000250|UniProtKB:P00568, ECO:0000250|UniProtKB:P05081, ECO:0000255|HAMAP-Rule:MF_03171}.
|
Bos taurus (Bovine)
|
P00571
|
KAD1_PIG
|
MEEKLKKSKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRAEVSSGSARGKMLSEIMEKGQLVPLETVLDMLRDAMVAKVDTSKGFLIDGYPREVKQGEEFERKIGQPTLLLYVDAGPETMTKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDDVFSQVCTHLDTLK
|
2.7.4.10; 2.7.4.3; 2.7.4.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:2551297, ECO:0000305|PubMed:2551298};
|
ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; nucleoside triphosphate biosynthetic process [GO:0009142]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; nucleoside diphosphate kinase activity [GO:0004550]; nucleoside triphosphate adenylate kinase activity [GO:0046899]
|
PF00406;
|
3.40.50.300;
|
Adenylate kinase family, AK1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03171}.
|
CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:2551297}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-Rule:MF_03171}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-Rule:MF_03171}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-diphosphate + ADP; Xref=Rhea:RHEA:13749, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.10; Evidence={ECO:0000269|PubMed:2551297}; CATALYTIC ACTIVITY: Reaction=ATP + GDP = ADP + GTP; Xref=Rhea:RHEA:27686, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000250|UniProtKB:P00568}; CATALYTIC ACTIVITY: Reaction=ATP + UDP = ADP + UTP; Xref=Rhea:RHEA:25098, ChEBI:CHEBI:30616, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000250|UniProtKB:P00568}; CATALYTIC ACTIVITY: Reaction=ATP + dGDP = ADP + dGTP; Xref=Rhea:RHEA:27690, ChEBI:CHEBI:30616, ChEBI:CHEBI:58595, ChEBI:CHEBI:61429, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000250|UniProtKB:P00568}; CATALYTIC ACTIVITY: Reaction=ATP + dTDP = ADP + dTTP; Xref=Rhea:RHEA:27682, ChEBI:CHEBI:30616, ChEBI:CHEBI:37568, ChEBI:CHEBI:58369, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000250|UniProtKB:P00568}; CATALYTIC ACTIVITY: Reaction=ADP + thiamine diphosphate = AMP + thiamine triphosphate; Xref=Rhea:RHEA:69180, ChEBI:CHEBI:58937, ChEBI:CHEBI:58938, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:2551297, ECO:0000269|PubMed:2551298};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.83 mM for ThDP {ECO:0000269|PubMed:2551298}; KM=43 mM for ADP {ECO:0000269|PubMed:2551298};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10.0 for ThTP synthesis. {ECO:0000269|PubMed:2551298};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius for ThTP synthesis. {ECO:0000269|PubMed:2551298};
|
FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP (PubMed:2551297). Exhibits nucleoside diphosphate kinase activity, catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donor (By similarity). Also catalyzes at a very low rate the synthesis of thiamine triphosphate (ThTP) from thiamine diphosphate (ThDP) and ADP (PubMed:2551297, PubMed:2551298). {ECO:0000250|UniProtKB:P00568, ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:2551297, ECO:0000269|PubMed:2551298}.
|
Sus scrofa (Pig)
|
P00572
|
KTHY_YEAST
|
MMGRGKLILIEGLDRTGKTTQCNILYKKLQPNCKLLKFPERSTRIGGLINEYLTDDSFQLSDQAIHLLFSANRWEIVDKIKKDLLEGKNIVMDRYVYSGVAYSAAKGTNGMDLDWCLQPDVGLLKPDLTLFLSTQDVDNNAEKSGFGDERYETVKFQEKVKQTFMKLLDKEIRKGDESITIVDVTNKGIQEVEALIWQIVEPVLSTHIDHDKFSFF
|
2.7.4.9
| null |
dTDP biosynthetic process [GO:0006233]; dTTP biosynthetic process [GO:0006235]; dUDP biosynthetic process [GO:0006227]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; nucleoside diphosphate kinase activity [GO:0004550]; thymidylate kinase activity [GO:0004798]; UMP/dUMP kinase activity [GO:0009041]
|
PF02223;
|
3.40.50.300;
|
Thymidylate kinase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000269|PubMed:6088527}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13518; Evidence={ECO:0000269|PubMed:6088527};
| null |
PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000305|PubMed:6088527}.
| null | null |
FUNCTION: Catalyzes the conversion of dTMP to dTDP. {ECO:0000269|PubMed:6088527}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00573
|
RPOL_BPT7
|
MNTINIAKNDFSDIELAAIPFNTLADHYGERLAREQLALEHESYEMGEARFRKMFERQLKAGEVADNAAAKPLITTLLPKMIARINDWFEEVKAKRGKRPTAFQFLQEIKPEAVAYITIKTTLACLTSADNTTVQAVASAIGRAIEDEARFGRIRDLEAKHFKKNVEEQLNKRVGHVYKKAFMQVVEADMLSKGLLGGEAWSSWHKEDSIHVGVRCIEMLIESTGMVSLHRQNAGVVGQDSETIELAPEYAEAIATRAGALAGISPMFQPCVVPPKPWTGITGGGYWANGRRPLALVRTHSKKALMRYEDVYMPEVYKAINIAQNTAWKINKKVLAVANVITKWKHCPVEDIPAIEREELPMKPEDIDMNPEALTAWKRAAAAVYRKDKARKSRRISLEFMLEQANKFANHKAIWFPYNMDWRGRVYAVSMFNPQGNDMTKGLLTLAKGKPIGKEGYYWLKIHGANCAGVDKVPFPERIKFIEENHENIMACAKSPLENTWWAEQDSPFCFLAFCFEYAGVQHHGLSYNCSLPLAFDGSCSGIQHFSAMLRDEVGGRAVNLLPSETVQDIYGIVAKKVNEILQADAINGTDNEVVTVTDENTGEISEKVKLGTKALAGQWLAYGVTRSVTKRSVMTLAYGSKEFGFRQQVLEDTIQPAIDSGKGLMFTQPNQAAGYMAKLIWESVSVTVVAAVEAMNWLKSAAKLLAAEVKDKKTGEILRKRCAVHWVTPDGFPVWQEYKKPIQTRLNLMFLGQFRLQPTINTNKDSEIDAHKQESGIAPNFVHSQDGSHLRKTVVWAHEKYGIESFALIHDSFGTIPADAANLFKAVRETMVDTYESCDVLADFYDQFADQLHESQLDKMPALPAKGNLNLRDILESDFAFA
|
2.7.7.6
| null |
DNA-templated transcription [GO:0006351]; DNA-templated viral transcription [GO:0039695]
|
DNA-directed RNA polymerase complex [GO:0000428]
|
DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; mitochondrial promoter sequence-specific DNA binding [GO:0001018]
|
PF00940;PF14700;
|
1.10.287.260;1.10.287.280;1.10.150.20;1.10.1320.10;
|
Phage and mitochondrial RNA polymerase family
| null | null |
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10031, ECO:0000255|PROSITE-ProRule:PRU10032, ECO:0000269|PubMed:8133519};
| null | null | null | null |
FUNCTION: Highly processive DNA-dependent RNA polymerase that catalyzes the transcription of class II and class III viral genes. Recognizes a specific promoter sequence and enters first into an 'abortive phase' where very short transcripts are synthesized and released before proceeding to the processive transcription of long RNA chains. Unwinds the double-stranded DNA to expose the coding strand for templating. Participates in the initiation of viral DNA replication presumably by making primers accessible to the DNA polymerase, thus facilitating the DNA opening. Also plays a role in viral DNA packaging, probably by pausing the transcription at the right end of concatemer junction to allow packaging complex recruitment and beginning of the packaging process. {ECO:0000269|PubMed:15223315, ECO:0000269|PubMed:3415967, ECO:0000269|PubMed:6945573, ECO:0000269|PubMed:7373707, ECO:0000269|PubMed:9192997}.
|
Escherichia phage T7 (Bacteriophage T7)
|
P00579
|
RPOD_ECOLI
|
MEQNPQSQLKLLVTRGKEQGYLTYAEVNDHLPEDIVDSDQIEDIIQMINDMGIQVMEEAPDADDLMLAENTADEDAAEAAAQVLSSVESEIGRTTDPVRMYMREMGTVELLTREGEIDIAKRIEDGINQVQCSVAEYPEAITYLLEQYDRVEAEEARLSDLITGFVDPNAEEDLAPTATHVGSELSQEDLDDDEDEDEEDGDDDSADDDNSIDPELAREKFAELRAQYVVTRDTIKAKGRSHATAQEEILKLSEVFKQFRLVPKQFDYLVNSMRVMMDRVRTQERLIMKLCVEQCKMPKKNFITLFTGNETSDTWFNAAIAMNKPWSEKLHDVSEEVHRALQKLQQIEEETGLTIEQVKDINRRMSIGEAKARRAKKEMVEANLRLVISIAKKYTNRGLQFLDLIQEGNIGLMKAVDKFEYRRGYKFSTYATWWIRQAITRSIADQARTIRIPVHMIETINKLNRISRQMLQEMGREPTPEELAERMLMPEDKIRKVLKIAKEPISMETPIGDDEDSHLGDFIEDTTLELPLDSATTESLRAATHDVLAGLTAREAKVLRMRFGIDMNTDYTLEEVGKQFDVTRERIRQIEAKALRKLRHPSRSEVLRSFLDD
| null | null |
DNA-templated transcription initiation [GO:0006352]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of DNA-templated transcription initiation [GO:2000142]; response to heat [GO:0009408]
|
cytosol [GO:0005829]; cytosolic DNA-directed RNA polymerase complex [GO:0000345]; sigma factor antagonist complex [GO:1903865]
|
DNA binding [GO:0003677]; sigma factor activity [GO:0016987]
|
PF04546;PF03979;PF00140;PF04542;PF04539;PF04545;
|
1.10.601.10;1.10.220.120;1.10.10.10;
|
Sigma-70 factor family, RpoD/SigA subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00963}.
| null | null | null | null | null |
FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. Preferentially transcribes genes associated with fast growth, such as ribosomal operons, other protein-synthesis related genes, rRNA- and tRNA-encoding genes and prfB. {ECO:0000255|HAMAP-Rule:MF_00963, ECO:0000269|PubMed:1643661, ECO:0000269|PubMed:1745227, ECO:0000269|PubMed:21398637, ECO:0000269|PubMed:24843001, ECO:0000269|PubMed:3543015, ECO:0000269|PubMed:8289270, ECO:0000269|PubMed:8808934}.
|
Escherichia coli (strain K12)
|
P00581
|
DPOL_BPT7
|
MIVSDIEANALLESVTKFHCGVIYDYSTAEYVSYRPSDFGAYLDALEAEVARGGLIVFHNGHKYDVPALTKLAKLQLNREFHLPRENCIDTLVLSRLIHSNLKDTDMGLLRSGKLPGKRFGSHALEAWGYRLGEMKGEYKDDFKRMLEEQGEEYVDGMEWWNFNEEMMDYNVQDVVVTKALLEKLLSDKHYFPPEIDFTDVGYTTFWSESLEAVDIEHRAAWLLAKQERNGFPFDTKAIEELYVELAARRSELLRKLTETFGSWYQPKGGTEMFCHPRTGKPLPKYPRIKTPKVGGIFKKPKNKAQREGREPCELDTREYVAGAPYTPVEHVVFNPSSRDHIQKKLQEAGWVPTKYTDKGAPVVDDEVLEGVRVDDPEKQAAIDLIKEYLMIQKRIGQSAEGDKAWLRYVAEDGKIHGSVNPNGAVTGRATHAFPNLAQIPGVRSPYGEQCRAAFGAEHHLDGITGKPWVQAGIDASGLELRCLAHFMARFDNGEYAHEILNGDIHTKNQIAAELPTRDNAKTFIYGFLYGAGDEKIGQIVGAGKERGKELKKKFLENTPAIAALRESIQQTLVESSQWVAGEQQVKWKRRWIKGLDGRKVHVRSPHAALNTLLQSAGALICKLWIIKTEEMLVEKGLKHGWDGDFAYMAWVHDEIQVGCRTEEIAQVVIETAQEAMRWVGDHWNFRCLLDTEGKMGPNWAICH
|
2.7.7.7; 3.1.11.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04101, ECO:0000305|PubMed:9440688};
|
DNA synthesis involved in DNA replication [GO:0090592]; DNA-templated DNA replication [GO:0006261]; double-strand break repair via alternative nonhomologous end joining [GO:0097681]; viral DNA genome replication [GO:0039693]
| null |
3'-5' exonuclease activity [GO:0008408]; DNA binding [GO:0003677]; DNA exonuclease activity [GO:0004529]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]
|
PF00476;
|
3.30.70.370;3.30.420.10;
|
DNA polymerase type-A family
| null | null |
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|HAMAP-Rule:MF_04101, ECO:0000269|PubMed:24591606};
| null | null | null | null |
FUNCTION: Replicates viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'-5' direction (By similarity). Non-processive DNA polymerase that achieves processivity by binding to host thioredoxin (TrxA). This interaction increases the rate of dNTP incorporation to yield a processivity of approximately 800 nucleotides (nt) per binding event. Interacts with DNA helicase gp4 to coordinate nucleotide polymerization with unwinding of the DNA. The leading strand is synthesized continuously while synthesis of the lagging strand requires the synthesis of oligoribonucleotides by the primase domain of gp4. {ECO:0000255|HAMAP-Rule:MF_04101, ECO:0000269|PubMed:15292168, ECO:0000269|PubMed:21606333, ECO:0000269|PubMed:2703498, ECO:0000269|PubMed:9218486}.
|
Escherichia phage T7 (Bacteriophage T7)
|
P00582
|
DPO1_ECOLI
|
MVQIPQNPLILVDGSSYLYRAYHAFPPLTNSAGEPTGAMYGVLNMLRSLIMQYKPTHAAVVFDAKGKTFRDELFEHYKSHRPPMPDDLRAQIEPLHAMVKAMGLPLLAVSGVEADDVIGTLAREAEKAGRPVLISTGDKDMAQLVTPNITLINTMTNTILGPEEVVNKYGVPPELIIDFLALMGDSSDNIPGVPGVGEKTAQALLQGLGGLDTLYAEPEKIAGLSFRGAKTMAAKLEQNKEVAYLSYQLATIKTDVELELTCEQLEVQQPAAEELLGLFKKYEFKRWTADVEAGKWLQAKGAKPAAKPQETSVADEAPEVTATVISYDNYVTILDEETLKAWIAKLEKAPVFAFDTETDSLDNISANLVGLSFAIEPGVAAYIPVAHDYLDAPDQISRERALELLKPLLEDEKALKVGQNLKYDRGILANYGIELRGIAFDTMLESYILNSVAGRHDMDSLAERWLKHKTITFEEIAGKGKNQLTFNQIALEEAGRYAAEDADVTLQLHLKMWPDLQKHKGPLNVFENIEMPLVPVLSRIERNGVKIDPKVLHNHSEELTLRLAELEKKAHEIAGEEFNLSSTKQLQTILFEKQGIKPLKKTPGGAPSTSEEVLEELALDYPLPKVILEYRGLAKLKSTYTDKLPLMINPKTGRVHTSYHQAVTATGRLSSTDPNLQNIPVRNEEGRRIRQAFIAPEDYVIVSADYSQIELRIMAHLSRDKGLLTAFAEGKDIHRATAAEVFGLPLETVTSEQRRSAKAINFGLIYGMSAFGLARQLNIPRKEAQKYMDLYFERYPGVLEYMERTRAQAKEQGYVETLDGRRLYLPDIKSSNGARRAAAERAAINAPMQGTAADIIKRAMIAVDAWLQAEQPRVRMIMQVHDELVFEVHKDDVDAVAKQIHQLMENCTRLDVPLLVEVGSGENWDQAH
|
2.7.7.7
| null |
base-excision repair [GO:0006284]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA-templated DNA replication [GO:0006261]; double-strand break repair [GO:0006302]; double-strand break repair via alternative nonhomologous end joining [GO:0097681]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
3'-5' exonuclease activity [GO:0008408]; 5'-3' exonuclease activity [GO:0008409]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]
|
PF01367;PF02739;PF00476;PF01612;
|
3.30.70.370;1.10.150.20;3.40.50.1010;3.30.420.10;
|
DNA polymerase type-A family
| null | null |
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7;
| null | null | null | null |
FUNCTION: In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. It is able to utilize nicked circular duplex DNA as a template and can unwind the parental DNA strand from its template.
|
Escherichia coli (strain K12)
|
P00586
|
THTR_BOVIN
|
MVHQVLYRALVSTKWLAESVRAGKVGPGLRVLDASWYSPGTREARKEYLERHVPGASFFDIEECRDKASPYEVMLPSEAGFADYVGSLGISNDTHVVVYDGDDLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAIFKATLNRSLLKTYEQVLENLESKRFQLVDSRAQGRYLGTQPEPDAVGLDSGHIRGSVNMPFMNFLTEDGFEKSPEELRAMFEAKKVDLTKPLIATCRKGVTACHIALAAYLCGKPDVAIYDGSWFEWFHRAPPETWVSQGKGGKA
|
2.8.1.1
| null |
rRNA import into mitochondrion [GO:0035928]; rRNA transport [GO:0051029]
|
mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
3-mercaptopyruvate sulfurtransferase activity [GO:0016784]; 5S rRNA binding [GO:0008097]; thiosulfate sulfurtransferase activity [GO:0004792]
|
PF00581;
|
3.40.250.10;
| null | null |
SUBCELLULAR LOCATION: Mitochondrion matrix.
|
CATALYTIC ACTIVITY: Reaction=hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate; Xref=Rhea:RHEA:16881, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:18022, ChEBI:CHEBI:18407, ChEBI:CHEBI:33542; EC=2.8.1.1; Evidence={ECO:0000269|PubMed:711738};
| null | null | null | null |
FUNCTION: Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA (By similarity). Formation of iron-sulfur complexes and cyanide detoxification. Binds molecular oxygen and sulfur. {ECO:0000250}.
|
Bos taurus (Bovine)
|
P00588
|
DTX_CORBE
|
MLVRGYVVSRKLFASILIGALLGIGAPPSAHAGADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGVVKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALSVELEINFETRGKRGQDAMYEYMAQACAGNRVRRSVGSSLSCINLDWDVIRDKTKTKIESLKEHGPIKNKMSESPNKTVSEEKAKQYLEEFHQTALEHPELSELKTVTGTNPVFAGANYAAWAVNVAQVIDSETADNLEKTTAALSILPGIGSVMGIADGAVHHNTEEIVAQSIALSSLMVAQAIPLVGELVDIGFAAYNFVESIINLFQVVHNSYNRPAYSPGHKTQPFLHDGYAVSWNTVEDSIIRTGFQGESGHDIKITAENTPLPIAGVLLPTIPGKLDVNKSKTHISVNGRKIRMRCRAIDGDVTFCRPKSPVYVGNGVHANLHVAFHRSSSEKIHSNEISSDSIGVLGYQKTVDHTKVNSKLSLFFEIKS
|
2.4.2.36
| null | null |
extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]; NAD+-diphthamide ADP-ribosyltransferase activity [GO:0047286]; nucleotidyltransferase activity [GO:0016779]; protein transmembrane transporter activity [GO:0008320]; toxin activity [GO:0090729]
|
PF02763;PF01324;PF02764;
|
3.90.175.10;2.60.40.700;1.10.490.40;
| null |
PTM: Proteolytic activation by host furin cleaves the protein in two parts, Diphtheria toxin fragment A and Diphtheria toxin fragment B; which remain associated via a disulfide bond. {ECO:0000269|PubMed:8253774}.
| null |
CATALYTIC ACTIVITY: Reaction=diphthamide-[translation elongation factor 2] + NAD(+) = H(+) + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2] + nicotinamide; Xref=Rhea:RHEA:11820, Rhea:RHEA-COMP:10174, Rhea:RHEA-COMP:10175, ChEBI:CHEBI:15378, ChEBI:CHEBI:16692, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:82697; EC=2.4.2.36;
| null | null | null | null |
FUNCTION: Diphtheria toxin, produced by a phage infecting Corynebacterium diphtheriae, is a proenzyme that, after activation, catalyzes the covalent attachment of the ADP ribose moiety of NAD to eukaryotic elongation factor 2 (eEF-2). Fragment A is the catalytic portion responsible for enzymatic ADP-ribosylation of elongation factor 2, while fragment B is responsible for binding of toxin to cell receptors and entry of fragment A. {ECO:0000269|PubMed:18276581, ECO:0000269|PubMed:19793133}.
|
Corynephage beta
|
P00590
|
CUTI1_FUSVN
|
MKFFALTTLLAATASALPTSNPAQELEARQLGRTTRDDLINGNSASCRDVIFIYARGSTETGNLGTLGPSIASNLESAFGKDGVWIQGVGGAYRATLGDNALPRGTSSAAIREMLGLFQQANTKCPDATLIAGGYSQGAALAAASIEDLDSAIRDKIAGTVLFGYTKNLQNRGRIPNYPADRTKVFCNTGDLVCTGSLIVAAPHLAYGPDARGPAPEFLIEKVRAVRGSA
|
3.1.1.74
| null | null |
extracellular region [GO:0005576]
|
cutinase activity [GO:0050525]
|
PF01083;
|
3.40.50.1820;
|
Cutinase family
|
PTM: The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme. {ECO:0000250|UniProtKB:P11373}.; PTM: O-glycosylated; contains one mole each of mannose, arabinose, N-acetylglucosamine, and glucuronic acid. {ECO:0000269|PubMed:7398618}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}.
|
CATALYTIC ACTIVITY: Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109, ECO:0000269|PubMed:18658138, ECO:0000305|PubMed:19810726, ECO:0000305|PubMed:8286366, ECO:0000305|PubMed:8555209};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.67 uM for p-nitrophenyl acetate (at pH 7.5) {ECO:0000269|PubMed:19810726}; KM=1.26 uM for p-nitrophenyl butyrate (at pH 7.5) {ECO:0000269|PubMed:19810726}; KM=0.68 mM for p-nitrophenyl butyrate (at pH 9 and 30 degrees Celsius) {ECO:0000269|PubMed:8555209}; KM=1.48 uM for p-nitrophenyl valerate (at pH 7.5) {ECO:0000269|PubMed:19810726}; KM=1.5 uM for p-nitrophenyl hexanoate (at pH 7.5) {ECO:0000269|PubMed:19810726}; Note=kcat is 1800 sec(-1) with p-nitrophenyl butyrate as substrate (at pH 9 and 30 degrees Celsius). {ECO:0000269|PubMed:8555209};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:18658138};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is below 30 degrees Celsius (PubMed:19810726). Optimum temperature is 30-40 degrees Celsius (PubMed:18658138). {ECO:0000269|PubMed:18658138, ECO:0000269|PubMed:19810726};
|
FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:18658138, PubMed:19810726, PubMed:8286366, PubMed:8555209). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:18658138, PubMed:19810726, PubMed:8286366, PubMed:8555209). Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (Ref.4). {ECO:0000269|PubMed:18658138, ECO:0000269|PubMed:19810726, ECO:0000269|PubMed:8286366, ECO:0000269|PubMed:8555209, ECO:0000269|Ref.4}.
|
Fusarium vanettenii (Neocosmospora pisi)
|
P00591
|
LIPP_PIG
|
SEVCFPRLGCFSDDAPWAGIVQRPLKILPWSPKDVDTRFLLYTNQNQNNYQELVADPSTITNSNFRMDRKTRFIIHGFIDKGEEDWLSNICKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEVLKSSLGYSPSNVHVIGHSLGSHAAGEAGRRTNGTIERITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDAAPIIPNLGFGMSQTVGHLDFFPNGGKQMPGCQKNILSQIVDIDGIWEGTRDFVACNHLRSYKYYADSILNPDGFAGFPCDSYNVFTANKCFPCPSEGCPQMGHYADRFPGKTNGVSQVFYLNTGDASNFARWRYKVSVTLSGKKVTGHILVSLFGNEGNSRQYEIYKGTLQPDNTHSDEFDSDVEVGDLQKVKFIWYNNNVINPTLPRVGASKITVERNDGKVYDFCSQETVREEVLLTLNPC
|
3.1.1.3
| null |
lipid catabolic process [GO:0016042]
|
extracellular space [GO:0005615]
|
all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity [GO:0047376]; metal ion binding [GO:0046872]; triglyceride lipase activity [GO:0004806]
|
PF00151;PF01477;
|
3.40.50.1820;2.60.60.20;
|
AB hydrolase superfamily, Lipase family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P16233}.
|
CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000250|UniProtKB:P16233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000250|UniProtKB:P16233}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000250|UniProtKB:P16233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000250|UniProtKB:P16233}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000250|UniProtKB:P16233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000250|UniProtKB:P16233}; CATALYTIC ACTIVITY: Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616; Evidence={ECO:0000250|UniProtKB:P16233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934; Evidence={ECO:0000250|UniProtKB:P16233}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38455, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52323, ChEBI:CHEBI:75937; Evidence={ECO:0000250|UniProtKB:P16233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38456; Evidence={ECO:0000250|UniProtKB:P16233};
| null | null | null | null |
FUNCTION: Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones. {ECO:0000250|UniProtKB:P16233}.
|
Sus scrofa (Pig)
|
P00592
|
PA21B_PIG
|
MKFLVLAVLLTVGAAQEGISSRALWQFRSMIKCAIPGSHPLMDFNNYGCYCGLGGSGTPVDELDRCCETHDNCYRDAKNLDSCKFLVDNPYTESYSYSCSNTEITCNSKNNACEAFICNCDRNAAICFSKAPYNKEHKNLDTKKYC
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P00593}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00593};
|
cellular response to insulin stimulus [GO:0032869]; fatty acid biosynthetic process [GO:0006633]; intracellular signal transduction [GO:0035556]; leukotriene biosynthetic process [GO:0019370]; lipid catabolic process [GO:0016042]; neutrophil chemotaxis [GO:0030593]; neutrophil mediated immunity [GO:0002446]; phosphatidylcholine metabolic process [GO:0046470]; phosphatidylglycerol metabolic process [GO:0046471]; phospholipid metabolic process [GO:0006644]; positive regulation of calcium ion transport into cytosol [GO:0010524]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of immune response [GO:0050778]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of podocyte apoptotic process [GO:1904635]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of glucose import [GO:0046324]
|
cell surface [GO:0009986]; extracellular region [GO:0005576]
|
bile acid binding [GO:0032052]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family
|
PTM: Acylation causes dimerization. {ECO:0000269|PubMed:2498336}.; PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. {ECO:0000250|UniProtKB:P04054}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}. Note=Secreted from pancreatic acinar cells in its inactive form. {ECO:0000250|UniProtKB:P04054}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036, ECO:0000269|PubMed:17603006}; CATALYTIC ACTIVITY: Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 2-tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate; Xref=Rhea:RHEA:54404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:131738; Evidence={ECO:0000269|PubMed:17603006}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:P04054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000250|UniProtKB:P04054}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; Evidence={ECO:0000250|UniProtKB:P04054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; Evidence={ECO:0000250|UniProtKB:P04054}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = (9Z,12Z)-octadecadienoate + H(+) + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:56424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:85334, ChEBI:CHEBI:85335; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56425; Evidence={ECO:0000250|UniProtKB:P04055};
| null | null | null | null |
FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract (PubMed:17603006). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (By similarity). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity). May act in an autocrine and paracrine manner (By similarity). Has anti-helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity (By similarity). {ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055, ECO:0000250|UniProtKB:Q9Z0Y2, ECO:0000269|PubMed:17603006}.
|
Sus scrofa (Pig)
|
P00593
|
PA21B_BOVIN
|
MRLLVLAALLTVGAGQAGLNSRALWQFNGMIKCKIPSSEPLLDFNNYGCYCGLGGSGTPVDDLDRCCQTHDNCYKQAKKLDSCKVLVDNPYTNNYSYSCSNNEITCSSENNACEAFICNCDRNAAICFSKVPYNKEHKNLDKKNC
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:10089353, ECO:0000305|PubMed:7265241, ECO:0000305|PubMed:9115986}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305|PubMed:10089353, ECO:0000305|PubMed:7265241, ECO:0000305|PubMed:9115986};
|
antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; arachidonic acid secretion [GO:0050482]; defense response to Gram-positive bacterium [GO:0050830]; fatty acid biosynthetic process [GO:0006633]; innate immune response in mucosa [GO:0002227]; lipid catabolic process [GO:0016042]; phosphatidylcholine metabolic process [GO:0046470]; phosphatidylglycerol metabolic process [GO:0046471]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of podocyte apoptotic process [GO:1904635]
|
cell surface [GO:0009986]; extracellular space [GO:0005615]
|
bile acid binding [GO:0032052]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family
|
PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. {ECO:0000250|UniProtKB:P04054}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}. Note=Secreted from pancreatic acinar cells in its inactive form. {ECO:0000250|UniProtKB:P04054}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055, ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}; CATALYTIC ACTIVITY: Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate; Xref=Rhea:RHEA:54456, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:64489; Evidence={ECO:0000250|UniProtKB:P04054}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:P04054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000250|UniProtKB:P04054}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; Evidence={ECO:0000250|UniProtKB:P04054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; Evidence={ECO:0000250|UniProtKB:P04054}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = (9Z,12Z)-octadecadienoate + H(+) + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:56424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:85334, ChEBI:CHEBI:85335; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56425; Evidence={ECO:0000250|UniProtKB:P04055};
| null | null | null | null |
FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity). May act in an autocrine and paracrine manner (By similarity). Has anti-helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity (By similarity). {ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055, ECO:0000250|UniProtKB:Q9Z0Y2}.
|
Bos taurus (Bovine)
|
P00594
|
PA21B_HORSE
|
ENGISPRAVWQFRSMIQCTIPNSKPYLEFNDYGCYCGLGGSGTPVDELDACCQVHDNCYTQAKELSSCRFLVDNPYTESYKFSCSGTEVTCSDKNNACEAFICNCDRNAAICFSKAPYNPENKNLDSKRKCA
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P00593}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00593};
|
arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phosphatidylglycerol metabolic process [GO:0046471]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of podocyte apoptotic process [GO:1904635]
|
extracellular region [GO:0005576]
|
bile acid binding [GO:0032052]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family
|
PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. {ECO:0000250|UniProtKB:P04054}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}. Note=Secreted from pancreatic acinar cells in its inactive form. {ECO:0000250|UniProtKB:P04054}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055, ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}; CATALYTIC ACTIVITY: Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate; Xref=Rhea:RHEA:54456, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:64489; Evidence={ECO:0000250|UniProtKB:P04054}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:P04054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000250|UniProtKB:P04054}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; Evidence={ECO:0000250|UniProtKB:P04054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; Evidence={ECO:0000250|UniProtKB:P04054}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = (9Z,12Z)-octadecadienoate + H(+) + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:56424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:85334, ChEBI:CHEBI:85335; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56425; Evidence={ECO:0000250|UniProtKB:P04055};
| null | null | null | null |
FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity). May act in an autocrine and paracrine manner (By similarity). Has anti-helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity (By similarity). {ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055, ECO:0000250|UniProtKB:Q9Z0Y2}.
|
Equus caballus (Horse)
|
P00596
|
PA2A1_NAJKA
|
MNPAHLLILAAVCVSPLGAFSNRPMPLNLYQFKNMIQCTVPNRSWWDFADYGCYCGRGGSGTPVDDLDRCCQVHDNCYNEAEKISRCWPYFKTYSYECSQGTLTCKGDNDACAAAVCDCDRLAAICFAGAPYNNNNYNIDLKARCQ
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250};
|
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]
|
extracellular region [GO:0005576]
|
acetylcholine receptor inhibitor activity [GO:0030550]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group I subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7460933}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=165 umol/min/mg enzyme {ECO:0000269|PubMed:19622365};
| null | null | null |
FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (Probable). Is able to suppress the acetylcholine (ACh)-evoked current mediated by alpha-7 (CHRNA7)-similar nAChRs in L.stagnalis neurons (IC(50)=37 nM) and to compete with alpha-bungarotoxin for binding to muscle- and alpha-7 neuronal nAChR types, as well as to AChBPs (PubMed:25522251). In inhibition of alpha-bungarotoxin binding, this toxin is similarly active against T.californica nAChR (IC(50)=1.2 uM), human alpha-7 nAChR (IC(50)=3.2 uM), and L.stagnalis AChBP (IC(50)=1.0 uM), whereas it is not active against A.californica AChBP (IC(50)>100 uM) (PubMed:25522251). {ECO:0000269|PubMed:25522251, ECO:0000305}.
|
Naja kaouthia (Monocled cobra) (Naja siamensis)
|
P00597
|
PA2A2_NAJKA
|
MNPAHLLILAAVCVSSLGASSNRPMPLNLYQFKNMIQCTVPSRSWWDFADYGCYCGRGGSGTPVDDLDRCCQVHDNCYNEAEKISGCWPYFKTYSYECSQGTLTCKGGNNACAAAVCDCDRLAAICFAGAPYNNNNYNIDLKARCQ
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250};
|
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group I subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
| null | null | null | null |
FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
Naja kaouthia (Monocled cobra) (Naja siamensis)
|
P00598
|
PA2A1_NAJAT
|
MTPAHLLILAAVCVSPLGASSNRPMPLNLYQFKNMIQCTVPSRSWWDFADYGCYCGRGGSGTPVDDLDRCCQVHDNCYNEAEKISGCWPYFKTYSYECSQGTLTCKGGNNACAAAVCDCDRLAAICFAGAPYNNNNYNIDLKARCQ
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:2274785, ECO:0000305|PubMed:2274787}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305|PubMed:2274785, ECO:0000305|PubMed:2274787};
|
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group I subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
| null | null | null | null |
FUNCTION: Snake venom phospholipase A2 (PLA2) that has high affinity for muscarinic acetylcholine receptors mAChRs (CHRM) and has the ability to activate them. In guinea-pig ileum, produces an onset and dose-dependent contraction. Has also weak anticoagulant activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:18281071, ECO:0000269|PubMed:3117784}.
|
Naja atra (Chinese cobra)
|
P00608
|
PA2B_NOTSC
|
NLVQFSYLIQCANHGKRPTWHYMDYGCYCGAGGSGTPVDELDRCCKIHDDCYDEAGKKGCFPKMSAYDYYCGENGPYCRNIKKKCLRFVCDCDVEAAFCFAKAPYNNANWNIDTKKRCQ
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P60043}; Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P60043};
|
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group I subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
| null | null | null | null |
FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. Is directly toxic to skeletal muscle upon local application in vivo (dystrophic effect). Also has direct nephrotoxicity in experimental mice; a single subcutaneous dose (1.38 ug/kg) produces renal tubular and glomerular damage within 24 hours (PubMed:7580101). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
|
P00611
|
PA2A1_LATSE
|
MYPAHLLVLLAVCVSLLGATAIPPLPLNLVQFSNLIQCVNKGSRASYHYADYGCYCGAGGSGTPVDELDRCCKIHDDCYGEAEKMGCYPKWTLYTYDCSTEEPNCSTKTGCQGFVCACDLEAAKCFARSPYNNKNYNIDTSKRCK
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250};
|
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group I subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
| null | null | null | null |
FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000250}.
|
Laticauda semifasciata (Black-banded sea krait) (Pseudolaticauda semifasciata)
|
P00614
|
PA2TA_OXYSC
|
NLLQFGFMIRCANRRSRPVWHYMDYGCYCGKGGSGTPVDDLDRCCQVHDECYGEAVRRFGCAPYWTLYSWKCYGKAPTCNTKTRCQRFVCRCDAKAAECFARSPYQNSNWNINTKARCR
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250};
|
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group I subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036, ECO:0000269|PubMed:22776098};
| null | null | null | null |
FUNCTION: Heterotrimer: Snake venom phospholipase A2 (PLA2) heterotrimer that acts as a potent presynaptic neurotoxin by blocking synaptic transmission and synaptic vesicle recycling. May act by binding in a calcium-dependent fashion to neurotonal pentraxin-1 (NPTX1) and neurotonal pentraxin-2 (NPTX2), but not to neuronal pentraxin receptor (NPTXR). Also binds to taipoxin-associated calcium binding protein 49 (RCN2), a protein localized in the lumen of endoplasmic reticulum.; FUNCTION: Monomer (alpha chain): Snake venom phospholipase A2 (PLA2) alpha chain that possesses the same high enzymatic activity as the heterotrimer. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
|
P00615
|
PA2HB_OXYSC
|
MHPAHLLVLLAVCVSLLGASDIPPLPLNLVQFGKMIECAIRNRRPALDFMNYGCYCGKGGSGTPVDDLDRCCQVHDECYAEAEKHGCYPSLTTYTWECRQVGPYCNSKTQCEVFVCACDFAAAKCFAQEDYNPAHSNINTGERCK
| null | null |
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group I subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Heterotrimer: Snake venom phospholipase A2 (PLA2) heterotrimer that acts as a potent presynaptic neurotoxin by blocking synaptic transmission and synaptic vesicle recycling. May act by binding in a calcium-dependent fashion to neurotonal pentraxin-1 (NPTX1) and neurotonal pentraxin-2 (NPTX2), but not to neuronal pentraxin receptor (NPTXR). Also binds to taipoxin-associated calcium binding protein 49 (RCN2), a protein localized in the lumen of endoplasmic reticulum.; FUNCTION: Monomer (beta chain): Snake venom phospholipase A2 homolog that is neither toxic nor enzymatically active. Does not bind calcium.
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
|
P00616
|
PA2HG_OXYSC
|
MHPAHLLVLLAVCVSLLGSSEIPQPSLDFEQFSNMIQCTIPCGESCLAYMDYGCYCGPGGSGTPIDDLDRCCKTHDECYAEAGKLSACKSVLSEPNNDTYSYECNEGQLTCNDDNDECKAFICNCDRTAVTCFAGAPYNDLNYNIGMIEHCK
| null | null |
arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group I subfamily, D49 sub-subfamily
|
PTM: Contains 0.9% fucose, 2.2% mannose, 4.2% N-acetyl-D-glucosamine, 3.5% galactose, and 3.8% N-acetyl-neuraminic acid (sialic acid). {ECO:0000269|PubMed:976268}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Heterotrimer: Snake venom phospholipase A2 (PLA2) heterotrimer that acts as a potent presynaptic neurotoxin by blocking synaptic transmission and synaptic vesicle recycling. May act by binding in a calcium-dependent fashion to neurotonal pentraxin-1 (NPTX1) and neurotonal pentraxin-2 (NPTX2), but not to neuronal pentraxin receptor (NPTXR). Also binds to taipoxin-associated calcium binding protein 49 (RCN2), a protein localized in the lumen of endoplasmic reticulum.; FUNCTION: Monomer (gamma chain): Snake venom phospholipase A2 homolog that is neither toxic nor enzymatically active. Does not bind calcium (PubMed:22776098). {ECO:0000269|PubMed:10748068, ECO:0000269|PubMed:22776098, ECO:0000269|PubMed:7722520, ECO:0000269|PubMed:976268}.
|
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
|
P00617
|
PA2B1_BUNMU
|
MNPAHLLVLSAVCVSLLGAANIPPHPLNLINFMEMIRYTIPCEKTWGEYADYGCYCGAGGSGRPIDALDRCCYVHDNCYGDAEKKHKCNPKTQSYSYKLTKRTIICYGAAGTCGRIVCDCDRTAALCFGNSEYIEGHKNIDTARFCQ
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:8590005}; Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:8590005};
|
arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group I subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:624701, ECO:0000269|PubMed:7096304}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
| null | null | null | null |
FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
Bungarus multicinctus (Many-banded krait)
|
P00618
|
PA2B2_BUNMU
|
MLIFLWCGAVCVSLLGAANIPPHPLNLINFMEMIRYTIPCEKTWGEYADYGCYCGAGGSGRPIDALDRCCYVHDNCYGDAEKKHKCNPKTQSYSYKLTKRTIICYGAAGTCARIVCDCDRTAALCFGNSEYIERHKNIDTKRHCR
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250};
|
arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group I subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
| null | null | null | null |
FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
Bungarus multicinctus (Many-banded krait)
|
P00619
|
PA2A3_BUNMU
|
MYPAHLLVLSAVCVSLLGAANIPPHPLNLINFMEMIRYTIPCEKTWGEYTNYGCYCGAGGSGRPIDALDRCCYVHDNCYGDAANIRDCNPKTQSYSYKLTKRTIICYGAAGTCARVVCDCDRTAALCFGDSEYIEGHKNIDTARFCQ
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250};
|
arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group I subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
| null | null | null | null |
FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
Bungarus multicinctus (Many-banded krait)
|
P00623
|
PA2A_CROAD
|
MRTLWIVAVLLLGVEGSLVQFETLIMKVAKRSGLLWYSAYGCYCGWGGHGRPQDATDRCCFVHDCCYGKATDCNPKTVSYTYSEENGEIVCGGDDPCGTQICECDKAAAICFRDNIPSYDNKYWLFPPKNCREEPEPC
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
|
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group II subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
| null | null | null | null |
FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
Crotalus adamanteus (Eastern diamondback rattlesnake)
|
P00624
|
PA2A_CROAT
|
MRTLWIVAVLLLGVEGSLVQFETLIMKIAGRSGLLWYSAYGCYCGWGGHGLPQDATDRCCFVHDCCYGKATDCNPKTVSYTYSEENGEIICGGDDPCGTQICECDKAAAICFRDNIPSYDNKYWLFPPKNCREEPEPC
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q8AXY1}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8AXY1};
|
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group II subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
| null | null | null | null |
FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
Crotalus atrox (Western diamondback rattlesnake)
|
P00625
|
PA2A1_OVOOK
|
MRTLWIMAVLLLGVEGHLMQFETLIMKIAGRSGVWWYGSYGCYCGAGGQGRPQDPSDRCCFVHDCCYGKVTGCNTKDEFYTYSEENGAITCGGENPCLKEVCECDLAAAICFRDNLDTYNSKKYWMFPAKNCLEESEPC
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250};
|
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644]
|
extracellular region [GO:0005576]; host extracellular space [GO:0043655]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group II subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
| null | null | null | null |
FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits the ADP- and collagen-induced human platelet aggregation (By similarity). Exhibits high hydrolytic activities and preferred the anionic micelles to the zwitterionic micelles. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000250, ECO:0000269|PubMed:22115990}.
|
Ovophis okinavensis (Ryukyu Island pit viper) (Trimeresurus okinavensis)
|
P00626
|
PA2BA_VIPAA
|
MRTLWIVAVCLIGVEGSLLEFGMMILGETGKNPLTSYSFYGCYCGVGGKGTPKDATDRCCFVHDCCYGNLPDCSPKTDRYKYHRENGAIVCGKGTSCENRICECDRAAAICFRKNLKTYNYIYRNYPDFLCKKESEKC
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:16156665}; Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:16156665};
|
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group II subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18261469}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:18261469}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036, ECO:0000269|PubMed:11027615, ECO:0000269|PubMed:11931665, ECO:0000269|PubMed:15488774, ECO:0000269|PubMed:16156665};
| null | null | null | null |
FUNCTION: Snake venom phospholipase A2 (PLA2) that acts as a presynaptic neurotoxin, an inhibitor of blood coagulation, and has been found to bind with high affinity to intracellular proteins. The response of indirectly stimulated neuromuscular preparations to ammodytoxin (Atx) is triphasic. The first phase, the transient inhibition of the acetylcholine (ACh) release, starts soon after the addition of Atx and lasts for several minutes. This phase is probably independent of Atx enzymatic activity. The effect may be due to the specific binding of the toxin to presynaptic receptors. These receptors, called N-type receptors, are still unidentified. It is noteworthy that a neuronal isoform of the M-type PLA2 receptor (R180) has been identified as a high-affinity receptor for Atx in neuronal plasma membranes. It was demonstrated however that this receptor is not essential for expression of neurotoxicity by Atx. The second phase corresponds to an augmentation of neurotransmitter release. A peak is reached 10-20 minutes after exposure of the preparation to Atx and is followed by a gradual reduction. In this phase, the enzymatic activity of Atx of the mammalian is not significant. It is speculated that the increased release of neurotransmitter in this phase is induced by the interference of Atx with voltage-gated potassium channels. Measurements of ionic currents showed however that voltage-gated potassium channels are not affected by Atx. The third phase of the response of neuromuscular preparations to Atx, which corresponds to a complete and irreversible paralysis, is clearly dependent on the hydrolytic activity of the toxin. In addition to its presynaptic neurotoxicity, Atx shows an anticoagulant activity by binding with high affinity to activated coagulation factor X (F10) thus inhibiting the formation of the prothrombinase complex (FX/FV) and its activity (IC(50) is 20 nM). Surprisingly, Atx was discovered to bind intracellular proteins such as calmodulin (CaM) (IC(50) is 6 nM), 14-3-3 proteins gamma (YWHAG) and epsilon (YWHAE) (by similarity with AtxC), as well as R25 (by similarity with AtxC), a mitochondrial integral membrane protein found in cerebral cortex. These findings raised a doubt about the dogma of the exclusively extracellular action of PLA2s, defended by the potential instability of these molecules in the reducing environment of the eukaryotic cytosol coupled with their possible inability to act as enzymes in this cellular compartment, due to too low concentration of calcium ions. This hypothesis was challenged efficiently by demonstrating the internalization of AtxA into a culture cells, but still remains to be directly demonstrated in vivo. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:11600150, ECO:0000269|PubMed:15485650, ECO:0000269|PubMed:16039772, ECO:0000269|PubMed:16815622, ECO:0000269|PubMed:3986212}.
|
Vipera ammodytes ammodytes (Western sand viper)
|
P00627
|
PA2B6_BUNFA
|
AVCVSLLGAANIPPQSLNLYQFKNMIECAGTRTWLAYVKYGCYCGPGGTGTPLDELDRCCQTHDHCYDNAKKFGNCIPYLKTYVYTCNKPDITCTGAKGSCGRNVCDCDRAAAICFAAAPYNLANFGIDKEKHCQ
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250};
|
arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group I subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17166178, ECO:0000269|PubMed:700923}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
| null | null | null | null |
FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Very weakly suppress the acetylcholine (ACh)-evoked current mediated by alpha-7-similar nAChRs in L.stagnalis neurons. {ECO:0000269|PubMed:25522251}.
|
Bungarus fasciatus (Banded krait) (Pseudoboa fasciata)
|
P00628
|
PA2BV_BUNFA
|
AVCVSLLGAANIPPQPLNLLQFKNMIQCAGSRLWVAYVKYGCYCGPGGTGTPLDQLDRCCQTHDHCYDNAKKFGNCIPYFKSYEYTCNKPDLTCTDAKGSCARNVCDCDRAAAICFAAAPYNLANFGINKETHCQ
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250};
|
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group I subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
| null | null | null | null |
FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
Bungarus fasciatus (Banded krait) (Pseudoboa fasciata)
|
P00629
|
PA2B3_BUNFA
|
AVCVSLLGAANIPPQPLNLLQFKNMIQCAGSRLWVAYVKYGCYCGPGGTGTPLDQLDRCCQTHDHCYDNAKKFGNCIPYFKTYEYTCNKPDITCTDAKGSCGRTVCDCDRAAAICFAAAPYNLANFGIDKEKHCQ
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250};
|
arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]; toxin activity [GO:0090729]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family, Group I subfamily, D49 sub-subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
| null | null | null | null |
FUNCTION: Snake venom phospholipase A2 (PLA2) that has only a weak enzymatic activity. Inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
Bungarus fasciatus (Banded krait) (Pseudoboa fasciata)
|
P00630
|
PA2_APIME
|
MQVVLGSLFLLLLSTSHGWQIRDRIGDNELEERIIYPGTLWCGHGNKSSGPNELGRFKHTDACCRTHDMCPDVMSAGESKHGLTNTASHTRLSCDCDDKFYDCLKNSADTISSYFVGKMYFNLIDTKCYKLEHPVTGCGERTEGRCLHYTVDKSKPKVYQWFDLRKY
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:2274788}; Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:2274788};
|
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]
|
PF05826;
|
1.20.90.10;
|
Phospholipase A2 family, Group III subfamily
|
PTM: N-glycosylated; contains mannose, N-acetylglucosamine and fucose alphal-6 and/or alphal-3 linked to the innermost N-acetylglucosamine. {ECO:0000269|PubMed:8504812}.
|
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035};
| null | null | null | null |
FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
Apis mellifera (Honeybee)
|
P00634
|
PPB_ECOLI
|
MKQSTIALALLPLLFTPVTKARTPEMPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQDATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVTLGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLAQMTDKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQRALEFAKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYGNSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLK
|
3.1.3.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion.; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions.;
|
dephosphorylation [GO:0016311]; protein dephosphorylation [GO:0006470]
|
outer membrane-bounded periplasmic space [GO:0030288]; periplasmic space [GO:0042597]
|
alkaline phosphatase activity [GO:0004035]; hydrogenase (acceptor) activity [GO:0033748]; magnesium ion binding [GO:0000287]; oxidoreductase activity, acting on phosphorus or arsenic in donors [GO:0030613]; phosphoprotein phosphatase activity [GO:0004721]; zinc ion binding [GO:0008270]
|
PF00245;
|
3.40.720.10;
|
Alkaline phosphatase family
| null |
SUBCELLULAR LOCATION: Periplasm.
|
CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};
| null | null | null | null | null |
Escherichia coli (strain K12)
|
P00635
|
PPA5_YEAST
|
MFKSVVYSILAASLANAGTIPLGKLADVDKIGTQKDIFPFLGGAGPYYSFPGDYGISRDLPEGCEMKQLQMVGRHGERYPTVSLAKTIKSTWYKLSNYTRQFNGSLSFLNDDYEFFIRDDDDLEMETTFANSDDVLNPYTGEMNAKRHARDFLAQYGYMVENQTSFAVFTSNSKRCHDTAQYFIDGLGDQFNITLQTVSEAESAGANTLSACNSCPAWDYDANDDIVNEYDTTYLDDIAKRLNKENKGLNLTSTDASTLFSWCAFEVNAKGYSDVCDIFTKDELVHYSYYQDLHTYYHEGPGYDIIKSVGSNLFNASVKLLKQSEIQDQKVWLSFTHDTDILNFLTTAGIIDDKNNLTAEYVPFMGNTFHRSWYVPQGARVYTEKFQCSNDTYVRYVINDAVVPIETCSTGPGFSCEINDFYDYAEKRVAGTDFLKVCNVSSVSNSTELTFYWDWNTTHYNASLLRQ
|
3.1.3.2
| null |
cellular response to phosphate starvation [GO:0016036]; phosphate-containing compound metabolic process [GO:0006796]; regulation of cell size [GO:0008361]
|
cell periphery [GO:0071944]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]
|
acid phosphatase activity [GO:0003993]; nucleoside triphosphate diphosphatase activity [GO:0047429]; ribonucleoside triphosphate phosphatase activity [GO:0017111]
|
PF00328;
|
3.40.50.1240;
|
Histidine acid phosphatase family
|
PTM: Glycosylated during secretion across the membrane.
|
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; Evidence={ECO:0000269|PubMed:3537710, ECO:0000269|PubMed:6300772};
| null | null | null | null |
FUNCTION: Partially mediates extracellular nucleotide derived phosphate hydrolysis along with NPP1 and NPP2. {ECO:0000269|PubMed:16278456}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00636
|
F16P1_PIG
|
MTDQAAFDTNIVTLTRFVMEEGRKARGTGEMTQLLNSLCTAVKAISTAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVINVLKSSFATCVLVSEEDKNAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKNSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMVNGVNCFMLDPAIGEFILVDRDVKIKKKGSIYSINEGYAKEFDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFMYPANKKSPKGKLRLLYECNPMAYVMEKAGGLATTGKEAVLDIVPTDIHQRAPIILGSPEDVTELLEIYQKHAAK
|
3.1.3.11
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:9708979}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:9708979};
|
cellular response to magnesium ion [GO:0071286]; cellular response to xenobiotic stimulus [GO:0071466]; dephosphorylation [GO:0016311]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; fructose metabolic process [GO:0006000]; gluconeogenesis [GO:0006094]; negative regulation of cell growth [GO:0030308]; negative regulation of glycolytic process [GO:0045820]; negative regulation of Ras protein signal transduction [GO:0046580]; regulation of gluconeogenesis [GO:0006111]; sucrose biosynthetic process [GO:0005986]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
AMP binding [GO:0016208]; fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029]
|
PF00316;PF18913;
|
3.40.190.80;3.30.540.10;
|
FBPase class 1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000269|PubMed:15767255, ECO:0000305|PubMed:1313579};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 uM for fructose-1,6-diphosphate {ECO:0000269|PubMed:15767255};
|
PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
| null | null |
FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain. {ECO:0000250|UniProtKB:P09467}.
|
Sus scrofa (Pig)
|
P00637
|
F16P1_RABIT
|
MADKAPFDTDISTMTRFVMEEGRKAGGTGEMTQLLNSLCTAVKAISTAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKNAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKKSTDEPSTKDALQPGRNLVAAGYALYGSATMLVLAGGSGVNSFMLDPAIGEFILVDKNVKIKKKGNIYSLNEGYAKDFDPAVTEYIQKKKFPPDNSSPYGARYVGSMVADVHRTLVYGGIFLYPANKKSPDGKLRLLYECNPMAFIMEKAGGMATTGKEAILDIVPTDIHQRAPVILGSPDDVQEFLEIYKKHAVK
|
3.1.3.11
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00636}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P00636};
|
cellular response to magnesium ion [GO:0071286]; cellular response to xenobiotic stimulus [GO:0071466]; dephosphorylation [GO:0016311]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; fructose metabolic process [GO:0006000]; gluconeogenesis [GO:0006094]; negative regulation of cell growth [GO:0030308]; negative regulation of glycolytic process [GO:0045820]; negative regulation of Ras protein signal transduction [GO:0046580]; regulation of gluconeogenesis [GO:0006111]; sucrose biosynthetic process [GO:0005986]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
AMP binding [GO:0016208]; fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029]
|
PF00316;PF18913;
|
3.40.190.80;3.30.540.10;
|
FBPase class 1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000269|PubMed:202200};
| null |
PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
| null | null |
FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain. {ECO:0000250|UniProtKB:P09467}.
|
Oryctolagus cuniculus (Rabbit)
|
P00639
|
DNAS1_BOVIN
|
MRGTRLMGLLLALAGLLQLGLSLKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYDDGCESCGNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYGLSNEMALAISDHYPVEVTLT
|
3.1.21.1
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:3352748, ECO:0000269|PubMed:4976790, ECO:0000269|PubMed:5166750}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:3352748, ECO:0000269|PubMed:4976790, ECO:0000269|PubMed:5166750}; Note=Divalent metal cations. Prefers Ca(2+) or Mg(2+). {ECO:0000269|PubMed:3352748, ECO:0000269|PubMed:4976790, ECO:0000269|PubMed:5166750};
|
apoptotic process [GO:0006915]; DNA catabolic process [GO:0006308]; neutrophil activation involved in immune response [GO:0002283]; regulation of acute inflammatory response [GO:0002673]; regulation of neutrophil mediated cytotoxicity [GO:0070948]
|
extracellular region [GO:0005576]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; zymogen granule [GO:0042588]
|
actin binding [GO:0003779]; deoxyribonuclease I activity [GO:0004530]; DNA binding [GO:0003677]
|
PF03372;
|
3.60.10.10;
|
DNase I family
|
PTM: The only differences between the A and B forms and the C and D forms are in the compositions of the carbohydrate bound to Asn-40. {ECO:0000269|PubMed:1748997}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4734471}. Zymogen granule {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}.
|
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.; EC=3.1.21.1; Evidence={ECO:0000269|PubMed:3352748, ECO:0000269|PubMed:4976790, ECO:0000269|PubMed:5166750};
| null | null | null | null |
FUNCTION: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:2395459, PubMed:3352748, PubMed:4976790, PubMed:5166750). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis (PubMed:2395459). Binds specifically to G-actin and blocks actin polymerization (PubMed:2395459). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity). {ECO:0000250|UniProtKB:P21704, ECO:0000250|UniProtKB:P49183, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:3352748, ECO:0000269|PubMed:4976790, ECO:0000269|PubMed:5166750}.
|
Bos taurus (Bovine)
|
P00642
|
T2E1_ECOLX
|
MSNKKQSNRLTEQHKLSQGVIGIFGDYAKAHDLAVGEVSKLVKKALSNEYPQLSFRYRDSIKKTEINEALKKIDPDLGGTLFVSNSSIKPDGGIVEVKDDYGEWRVVLVAEAKHQGKDIINIRNGLLVGKRGDQDLMAAGNAIERSHKNISEIANFMLSESHFPYVLFLEGSNFLTENISITRPDGRVVNLEYNSGILNRLDRLTAANYGMPINSNLCINKFVNHKDKSIMLQAASIYTQGDGREWDSKIMFEIMFDISTTSLRVLGRDLFEQLTSK
|
3.1.21.4
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 magnesium ions per subunit.;
|
DNA restriction-modification system [GO:0009307]
| null |
DNA binding [GO:0003677]; magnesium ion binding [GO:0000287]; type II site-specific deoxyribonuclease activity [GO:0009036]
|
PF02963;
|
3.40.580.10;
|
EcoRI type II restriction endonuclease family
| null | null |
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4; Evidence={ECO:0000269|PubMed:3024321};
| null | null | null | null |
FUNCTION: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GAATTC-3' and cleaves after G-1. {ECO:0000269|PubMed:3024321, ECO:0000303|PubMed:12654995}.
|
Escherichia coli
|
P00644
|
NUC_STAAU
|
MLVMTEYLLSAGICMAIVSILLIGMAISNVSKGQYAKRFFFFATSCLVLTLVVVSSLSSSANASQTDNGVNRSGSEDPTVYSATSTKKLHKEPATLIKAIDGDTVKLMYKGQPMTFRLLLVDTPETKHPKKGVEKYGPEASAFTKKMVENAKKIEVEFDKGQRTDKYGRGLAYIYADGKMVNEALVRQGLAKVAYVYKPNNTHEQHLRKSEAQAKKEKLNIWSEDNADSGQ
|
3.1.31.1
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit.;
| null |
extracellular region [GO:0005576]; membrane [GO:0016020]
|
endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters [GO:0016894]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]
|
PF00565;
|
2.40.50.90;
|
Thermonuclease family
| null |
SUBCELLULAR LOCATION: [Nuclease A]: Secreted {ECO:0000269|PubMed:893427, ECO:0000305|PubMed:4324890}.; SUBCELLULAR LOCATION: [Nuclease B]: Membrane.
|
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.; EC=3.1.31.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10048, ECO:0000255|PROSITE-ProRule:PRU10049};
| null | null | null | null |
FUNCTION: Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond.
|
Staphylococcus aureus
|
P00646
|
CEA3_ECOLX
|
MSGGDGRGHNTGAHSTSGNINGGPTGLGVGGGASDGSGWSSENNPWGGGSGSGIHWGGGSGHGNGGGNGNSGGGSGTGGNLSAVAAPVAFGFPALSTPGAGGLAVSISAGALSAAIADIMAALKGPFKFGLWGVALYGVLPSQIAKDDPNMMSKIVTSLPADDITESPVSSLPLDKATVNVNVRVVDDVKDERQNISVVSGVPMSVPVVDAKPTERPGVFTASIPGAPVLNISVNNSTPAVQTLSPGVTNNTDKDVRPAGFTQGGNTRDAVIRFPKDSGHNAVYVSVSDVLSPDQVKQRQDEENRRQQEWDATHPVEAAERNYERARAELNQANEDVARNQERQAKAVQVYNSRKSELDAANKTLADAIAEIKQFNRFAHDPMAGGHRMWQMAGLKAQRAQTDVNNKQAAFDAAAKEKSDADAALSSAMESRKKKEDKKRSAENNLNDEKNKPRKGFKDYGHDYHPAPKTENIKGLGDLKPGIPKTPKQNGGGKRKRWTGDKGRKIYEWDSQHGELEGYRASDGQHLGSFDPKTGNQLKGPDPKRNIKKYL
|
4.6.1.-
| null |
defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640]; negative regulation of ion transmembrane transporter activity [GO:0032413]
|
extracellular region [GO:0005576]; extrachromosomal circular DNA [GO:0005727]
|
endonuclease activity [GO:0004519]; lyase activity [GO:0016829]; ribosome binding [GO:0043022]; rRNA binding [GO:0019843]; transmembrane transporter binding [GO:0044325]; tRNA binding [GO:0000049]
|
PF03515;PF09000;PF11570;
|
3.10.380.10;1.10.287.620;1.20.5.740;
|
Cloacin colicin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4944624}.
| null | null | null | null | null |
FUNCTION: Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria (PubMed:3889348, PubMed:4930243, PubMed:4930244, PubMed:6295812). Cleaves 16S rRNA between adenosine-1492 and guanosine-1493 (E.coli 16S rRNA numbering), releasing a 49 nucleotide (nt) 'colicin' fragment (PubMed:20852642). Inactivates 70S ribosomes or 30S subunits by endonucleolytically cleaving 16S RNA at a specific site about 50 nt from its C-terminus (PubMed:4930243, PubMed:4930244, PubMed:782524). Produces 5'-OH-guanosine and a 2',3'-cyclic phosphate adenosine (PubMed:20852642, PubMed:4930244). Mixing a susceptible (e.g. strain K12 / A19) and colicin E3 producing strain results in total protein translation inhibition within 11 minutes (PubMed:4930243). Its activity is inhibited by cognate immunity protein Im3 (PubMed:10986462, PubMed:11741540, PubMed:336615, PubMed:6295812). {ECO:0000269|PubMed:10986462, ECO:0000269|PubMed:11741540, ECO:0000269|PubMed:20852642, ECO:0000269|PubMed:336615, ECO:0000269|PubMed:3889348, ECO:0000269|PubMed:4930243, ECO:0000269|PubMed:4930244, ECO:0000269|PubMed:6295812, ECO:0000269|PubMed:782524}.; FUNCTION: Uses BtuB, the vitamin B transporter, as a receptor on the outer membrane; binds via the receptor (R) domain (PubMed:14528295, PubMed:4579869). Then the translocation domain (T) probably 'fishes' for its outer membrane translocon protein, OmpF (Probable) (PubMed:16922495, PubMed:18636093). The N-terminal 83 residues (T83) can bind to and occlude OmpF channels. A complex of the cytotoxic C-terminal 96 residues (C96) plus the immunity protein does not occlude OmpF; upon complex separation from the immunity protein C96 becomes disordered and is able to bind OmpF (PubMed:16922495). The N-terminus probably binds TolB and then reinserts into an empty pore of trimeric OmpF; the rest of the protein is pulled through OmpF and crosses the inner membrane, where the cytotoxic fragment is probably released by protease FtsH (Probable) (PubMed:30541793). {ECO:0000269|PubMed:14528295, ECO:0000269|PubMed:16922495, ECO:0000269|PubMed:4579869, ECO:0000305|PubMed:16922495, ECO:0000305|PubMed:18636093, ECO:0000305|PubMed:30541793}.
|
Escherichia coli
|
P00655
|
RNAS_ASPGI
|
MVAIKNLVLVALTAVTALAVPSPLEARAVTWTCLNDQKNPKTNKYETKRLLYNQNKAESNSHHAPLSDGKTGSSYPHWFTNGYDGDGKLPKGRTPIKFGKSDCDRPPKHSKDGNGKTDHYLLEFPTFPDGHDYKFDSKKPKENPGPARVIYTYPNKVFCGIIAHTKENQGELKLCSH
|
4.6.1.23
| null |
negative regulation of cytoplasmic translation [GO:2000766]
|
extracellular region [GO:0005576]
|
lyase activity [GO:0016829]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521]; rRNA endonuclease activity [GO:0033902]
| null |
3.10.450.30;
|
Ribonuclease U2 family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=a 28S rRNA containing guanosine-adenosine pair + H2O = an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment].; EC=4.6.1.23; Evidence={ECO:0000305};
| null | null | null | null |
FUNCTION: Alpha-sarcin is specific for purines in both single- and double-stranded RNA. Its toxic action on eukaryotic cells is the result of cleavage of a single phosphodiester bond in the 60S subunit of ribosomes (By similarity). Inhibits both the EFl (elongation factor 1)-dependent binding of aminoacyl-tRNA and the GTP-dependent binding of EF2 (elongation factor 2) to ribosomes (PubMed:2930482). {ECO:0000250|UniProtKB:P0CL70, ECO:0000269|PubMed:2930482}.
|
Aspergillus giganteus
|
P00657
|
RNAS1_BUBBU
|
KETAAAKFQRQHMDSSTSSASSSNYCNQMMKSRNMTSDRCKPVNTFVHESLADVQAVCSQENVACKNGQTNCYQSYSTMSITDCRETGSSKYPNCAYKTTQANKHIIVACEGNPYVPVHYDASV
|
4.6.1.18
| null |
defense response to Gram-positive bacterium [GO:0050830]
|
extracellular region [GO:0005576]
|
lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522]
|
PF00074;
|
3.10.130.10;
|
Pancreatic ribonuclease family
|
PTM: Swamp breed ribonuclease do not bind carbohydrate, but there is evidence of a polymorphic form that does.
|
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
| null | null | null | null |
FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). {ECO:0000250}.
|
Bubalus bubalis (Domestic water buffalo)
|
P00659
|
RNAS1_DAMKO
|
KESAAAKFZRZHMBSSTSSASSSBYCBZMMKSRNLTQDRCKPVBTFVHZSLABVZAVCSZKBVACKBGZTBCYZSYSTMSITBCRZTGSSKYPBCAYKTTQAKKHIIVACZGBPYVPVHFBASV
|
4.6.1.18
| null |
defense response to Gram-positive bacterium [GO:0050830]
|
extracellular region [GO:0005576]
|
lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522]
|
PF00074;
|
3.10.130.10;
|
Pancreatic ribonuclease family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
| null | null | null | null |
FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). {ECO:0000250}.
|
Damaliscus korrigum (Topi) (Damaliscus lunatus korrigum)
|
P00660
|
RNAS1_CONTA
|
KESAAAKFERQHMDSSTSSASSSNYCNQMMKSRNLTQDRCKPVNTFVHEPLADVQAVCSQKNVACKNGQTNCYQSYSTMSITDCRETGSSKYPNCAYKATQAKKHIIVACEGNPYVPVHFDASV
|
4.6.1.18
| null |
defense response to Gram-positive bacterium [GO:0050830]
|
extracellular region [GO:0005576]
|
lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522]
|
PF00074;
|
3.10.130.10;
|
Pancreatic ribonuclease family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
| null | null | null | null |
FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). {ECO:0000250}.
|
Connochaetes taurinus (Blue wildebeest)
|
P00669
|
RNS_BOVIN
|
MALKSLVVLPLLVLVLLLVRVQPSLGKESAAAKFERQHMDSGNSPSSSSNYCNLMMCCRKMTQGKCKPVNTFVHESLADVKAVCSQKKVTCKNGQTNCYQSKSTMRITDCRETGSSKYPNCAYKTTQVEKHIIVACGGKPSVPVHFDASV
|
4.6.1.18
| null |
defense response to Gram-positive bacterium [GO:0050830]; metabolic process [GO:0008152]
|
extracellular region [GO:0005576]
|
identical protein binding [GO:0042802]; lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522]; RNA nuclease activity [GO:0004540]
|
PF00074;
|
3.10.130.10;
|
Pancreatic ribonuclease family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; Evidence={ECO:0000269|PubMed:4664228}; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; Evidence={ECO:0000269|PubMed:4664228};
| null | null | null | null |
FUNCTION: This enzyme hydrolyzes both single- and double-stranded RNA.
|
Bos taurus (Bovine)
|
P00684
|
RNS1B_RAT
|
MGLEKSLFLFSLLVLVLGWVQPSLGGESRESSADKFKRQHMDTEGPSKSSPTYCNQMMKRQGMTKGSCKPVNTFVHEPLEDVQAICSQGQVTCKNGRNNCHKSSSTLRITDCRLKGSSKYPNCDYTTTDSQKHIIIACDGNPYVPVHFDASV
|
4.6.1.18
| null |
defense response to Gram-positive bacterium [GO:0050830]; response to bacterium [GO:0009617]
|
cytosol [GO:0005829]; extracellular region [GO:0005576]; lysosomal lumen [GO:0043202]
|
lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522]; RNA nuclease activity [GO:0004540]
|
PF00074;
|
3.10.130.10;
|
Pancreatic ribonuclease family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
| null | null | null | null |
FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
P00687
|
AMY1_MOUSE
|
MKFFLLLSLIGFCWAQYDPHTQYGRTAIVHLFEWRWVDIAKECERYLAPNGFAGVQVSPPNENIVVHSPSRPWWERYQPISYKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHMCGVGAQAGQSSTCGSYFNPNNRDFPGVPYSGFDFNDGKCRTASGGIENYQDAAQVRDCRLSGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNTKWFSQGSRPFIFQEVIDLGGEAVSSNEYFGNGRVTEFKYGAKLGKVMRKWDGEKMSYLKNWGEGWGLMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYYWPRNFQNGKDVNDWVGPPNNNGKTKEVSINPDSTCGNDWICEHRWRQIRNMVAFRNVVNGQPFANWWDNDSNQVAFGRGNKGFIVFNNDDWALSETLQTGLPAGTYCDVISGDKVDGNCTGIKVYVGNDGKAHFSISNSAEDPFIAIHAESKI
|
3.2.1.1
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P04746}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P04746}; COFACTOR: Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P04746}; Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P04746};
|
carbohydrate metabolic process [GO:0005975]; response to bacterium [GO:0009617]
|
extracellular space [GO:0005615]
|
alpha-amylase activity [GO:0004556]; amylase activity [GO:0016160]; metal ion binding [GO:0046872]
|
PF00128;PF02806;
|
3.20.20.80;2.60.40.1180;
|
Glycosyl hydrolase 13 family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P04746};
| null | null | null | null | null |
Mus musculus (Mouse)
|
P00688
|
AM2A5_MOUSE
|
MKFVLLLSLIGFCWAQYDPHTSDGRTAIVHLFEWRWVDIAKECERYLAPKGFGGVQVSPPNENVVVHNPSRPWWERYQPISYKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHMCGAGNPAGTSSTCGSYLNPNNREFPAVPYSAWDFNDNKCNGEIDNYNDAYQVRNCRLTGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDAAKHMWPGDIKAVLDKLHNLNTKWFSQGSRPFIFQEVIDLGGEAIKGSEYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGLVPSDRALVFVDNHDNQRGHGAGGSSILTFWDARMYKMAVGFMLAHPYGFTRVMSSYRWNRNFQNGKDQNDWIGPPNNNGVTKEVTINADTTCGNDWVCEHRWRQIRNMVAFRNVVNGQPFSNWWDNNSNQVAFSRGNRGFIVFNNDDWALSATLQTGLPAGTYCDVISGDKVDGNCTGLRVNVGSDGKAHFSISNSAEDPFIAIHADSKL
|
3.2.1.1
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P04746}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P04746}; COFACTOR: Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P04746}; Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P04746};
|
carbohydrate catabolic process [GO:0016052]; carbohydrate metabolic process [GO:0005975]
|
extracellular space [GO:0005615]
|
alpha-amylase activity [GO:0004556]; amylase activity [GO:0016160]; calcium ion binding [GO:0005509]; chloride ion binding [GO:0031404]
|
PF00128;PF02806;
|
3.20.20.80;2.60.40.1180;
|
Glycosyl hydrolase 13 family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space.
|
CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P04746};
| null | null | null | null | null |
Mus musculus (Mouse)
|
P00690
|
AMYP_PIG
|
MKLFLLLSAFGFCWAQYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENIVVTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVINHMCGSGAAAGTGTTCGSYCNPGNREFPAVPYSAWDFNDGKCKTASGGIESYNDPYQVRDCQLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASKHMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGEAIQSSEYFGNGRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKVAVGFMLAHPYGFTRVMSSYRWARNFVNGQDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWRQIRNMVWFRNVVDGQPFANWWANGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYCDVISGDKVGNSCTGIKVYVSSDGTAQFSISNSAEDPFIAIHAESKL
|
3.2.1.1
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:3502087, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, ECO:0000269|PubMed:9385631}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:3502087, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, ECO:0000269|PubMed:9385631}; COFACTOR: Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:3502087, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:9385631}; Note=Binds 1 Cl(-) ion per subunit. {ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:3502087, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:9385631};
|
carbohydrate catabolic process [GO:0016052]; carbohydrate metabolic process [GO:0005975]
|
extracellular space [GO:0005615]
|
alpha-amylase activity [GO:0004556]; calcium ion binding [GO:0005509]; chloride ion binding [GO:0031404]
|
PF00128;PF02806;
|
3.20.20.80;2.60.40.1180;
|
Glycosyl hydrolase 13 family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space.
|
CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P04746};
| null | null | null | null | null |
Sus scrofa (Pig)
|
P00693
|
AMY1_HORVU
|
MGKNGSLCCFSLLLLLLLAGLASGHQVLFQGFNWESWKQSGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNEGYMPGRLYDIDASKYGNAAELKSLIGALHGKGVQAIADIVINHRCADYKDSRGIYCIFEGGTSDGRLDWGPHMICRDDTKYSDGTANLDTGADFAAAPDIDHLNDRVQRELKEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPSLAVAEVWDNMATGGDGKPNYDQDAHRQNLVNWVDKVGGAASAGMVFDFTTKGILNAAVEGELWRLIDPQGKAPGVMGWWPAKAATFVDNHDTGSTQAMWPFPSDKVMQGYAYILTHPGIPCIFYDHFFNWGFKDQIAALVAIRKRNGITATSALKILMHEGDAYVAEIDGKVVVKIGSRYDVGAVIPAGFVTSAHGNDYAVWEKNGAAATLQRS
|
3.2.1.1
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886}; Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886};
|
starch catabolic process [GO:0005983]
|
extracellular region [GO:0005576]
|
alpha-amylase activity [GO:0004556]; calcium ion binding [GO:0005509]
|
PF07821;PF00128;
|
3.20.20.80;2.60.40.1180;
|
Glycosyl hydrolase 13 family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space.
|
CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:18588886, ECO:0000269|PubMed:24089528, ECO:0000269|PubMed:7901200};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5 with p-nitrophenyl maltoheptaoside or amylopectin as substrate. {ECO:0000269|PubMed:24089528};
| null |
FUNCTION: Alpha-amylase displaying a robust amylolytic activity toward p-nitrophenyl maltoheptaoside (BPNP-G7), amylopectin and beta-limit dextrin (PubMed:24089528). {ECO:0000269|PubMed:24089528}.
|
Hordeum vulgare (Barley)
|
P00697
|
LYSC1_RAT
|
MKALLVLGFLLLSASVQAKIYERCQFARTLKRNGMSGYYGVSLADWVCLAQHESNYNTQARNYNPGDQSTDYGIFQINSRYWCNDGKTPRAKNACGIPCSALLQDDITQAIQCAKRVVRDPQGIRAWVAWQRHCKNRDLSGYIRNCGV
|
3.2.1.17
| null |
defense response to bacterium [GO:0042742]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]; metabolic process [GO:0008152]
|
endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]; Golgi cis cisterna [GO:0000137]; Golgi stack [GO:0005795]; microvillus [GO:0005902]; rough endoplasmic reticulum lumen [GO:0048237]; secretory granule [GO:0030141]; trans-Golgi network transport vesicle [GO:0030140]
|
hydrolase activity, acting on glycosyl bonds [GO:0016798]; identical protein binding [GO:0042802]; lysozyme activity [GO:0003796]
|
PF00062;
|
1.10.530.10;
|
Glycosyl hydrolase 22 family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17;
| null | null | null | null |
FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. In the intestine they may also have a digestive function.
|
Rattus norvegicus (Rat)
|
P00698
|
LYSC_CHICK
|
MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
|
3.2.1.17
| null |
cell wall macromolecule catabolic process [GO:0016998]; defense response to bacterium [GO:0042742]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]
|
cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]
|
beta-N-acetylglucosaminidase activity [GO:0016231]; identical protein binding [GO:0042802]; lysozyme activity [GO:0003796]
|
PF00062;
|
1.10.530.10;
|
Glycosyl hydrolase 22 family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17;
| null | null | null | null |
FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus. {ECO:0000255|PROSITE-ProRule:PRU00680, ECO:0000269|PubMed:22044478}.
|
Gallus gallus (Chicken)
|
P00701
|
LYSC_COTJA
|
MRSLLVLVLCFLPLAALGKVYGRCELAAAMKRHGLDKYQGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDVHGMNAWVAWRNRCKGTDVNAWIRGCRL
|
3.2.1.17
| null |
defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]; metabolic process [GO:0008152]
|
extracellular region [GO:0005576]
|
lysozyme activity [GO:0003796]
|
PF00062;
|
1.10.530.10;
|
Glycosyl hydrolase 22 family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; Evidence={ECO:0000269|Ref.3};
| null | null | null | null |
FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
|
Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
|
P00702
|
LYSC_PHACO
|
MRSLLILVLCFLPLAAPGKVYGRCELAAAMKRMGLDNYRGYSLGNWVCAAKFESNFNTGATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCHIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRKHCKGTDVNVWIRGCRL
|
3.2.1.17
| null |
defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]; metabolic process [GO:0008152]
|
extracellular region [GO:0005576]
|
lysozyme activity [GO:0003796]
|
PF00062;
|
1.10.530.10;
|
Glycosyl hydrolase 22 family
|
PTM: By an evolutionary shift in the site of proteolytic cleavage of prelysozyme, Gly-18 became the N-terminal residue of the mature protein instead of being the C-terminal residue of the signal sequence as in other birds.
|
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17;
| null | null | null | null |
FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
|
Phasianus colchicus colchicus (Black-necked pheasant)
|
P00703
|
LYSC_MELGA
|
MRSLLILVLCFLPLAALGKVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCNIPCSALLSSDITASVNCAKKIASGGNGMNAWVAWRNRCKGTDVHAWIRGCRL
|
3.2.1.17
| null |
cell wall macromolecule catabolic process [GO:0016998]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]
|
glycosaminoglycan binding [GO:0005539]; identical protein binding [GO:0042802]; lysozyme activity [GO:0003796]
|
PF00062;
|
1.10.530.10;
|
Glycosyl hydrolase 22 family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17;
| null | null | null | null |
FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
|
Meleagris gallopavo (Wild turkey)
|
P00709
|
LALBA_HUMAN
|
MRFFVPLFLVGILFPAILAKQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAIVENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGIDYWLAHKALCTEKLEQWLCEKL
| null | null |
apoptotic process [GO:0006915]; cell-cell signaling [GO:0007267]; defense response to bacterium [GO:0042742]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; lactose biosynthetic process [GO:0005989]; signal transduction [GO:0007165]
|
extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]; protein-containing complex [GO:0032991]
|
calcium ion binding [GO:0005509]; lactose synthase activity [GO:0004461]; lysozyme activity [GO:0003796]
|
PF00062;
|
1.10.530.10;
|
Glycosyl hydrolase 22 family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
|
Homo sapiens (Human)
|
P00711
|
LALBA_BOVIN
|
MMSFVSLLLVGILFHATQAEQLTKCEVFRELKDLKGYGGVSLPEWVCTTFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSSNICNISCDKFLDDDLTDDIMCVKKILDKVGINYWLAHKALCSEKLDQWLCEKL
| null | null |
defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; lactose biosynthetic process [GO:0005989]; response to 11-deoxycorticosterone [GO:1903496]; response to dehydroepiandrosterone [GO:1903494]; response to estradiol [GO:0032355]; response to progesterone [GO:0032570]
|
extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; lactose synthase activity [GO:0004461]; lysozyme activity [GO:0003796]
|
PF00062;
|
1.10.530.10;
|
Glycosyl hydrolase 22 family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
|
Bos taurus (Bovine)
|
P00712
|
LALBA_CAPHI
|
MMSFVSLLLVGILFHATQAEQLTKCEVFQKLKDLKDYGGVSLPEWVCTAFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSRNICNISCDKFLDDDLTDDIVCAKKILDKVGINYWLAHKALCSEKLDQWLCEKL
| null | null |
defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; lactose biosynthetic process [GO:0005989]
|
extracellular region [GO:0005576]; protein-containing complex [GO:0032991]
|
calcium ion binding [GO:0005509]; lactose synthase activity [GO:0004461]; lysozyme activity [GO:0003796]
|
PF00062;
|
1.10.530.10;
|
Glycosyl hydrolase 22 family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
|
Capra hircus (Goat)
|
P00713
|
LALBA_CAVPO
|
MMSFFPLLLVGILFPAVQAKQLTKCALSHELNDLAGYRDITLPEWLCIIFHISGYDTQAIVKNSDHKEYGLFQINDKDFCESSTTVQSRNICDISCDKLLDDDLTDDIMCVKKILDIKGIDYWLAHKPLCSDKLEQWYCEAQ
| null | null |
defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; lactose biosynthetic process [GO:0005989]
|
extracellular region [GO:0005576]; protein-containing complex [GO:0032991]
|
calcium ion binding [GO:0005509]; lactose synthase activity [GO:0004461]; lysozyme activity [GO:0003796]
|
PF00062;
|
1.10.530.10;
|
Glycosyl hydrolase 22 family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
|
Cavia porcellus (Guinea pig)
|
P00714
|
LALBA_RAT
|
MMRFVPLFLACISLPAFQATEFTKCEVSHAIEDMDGYQGISLLEWTCVLFHTSGYDSQAIVKNNGSTEYGLFQISNRNWCKSSEFPESENICDISCDKFLDDELADDIVCAKKIVAIKGIDYWKAHKPMCSEKLEQWRCEKPGAPALVVPALNSETPVP
| null | null |
defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; lactose biosynthetic process [GO:0005989]
|
extracellular region [GO:0005576]; protein-containing complex [GO:0032991]
|
calcium ion binding [GO:0005509]; lactose synthase activity [GO:0004461]; lysozyme activity [GO:0003796]
|
PF00062;
|
1.10.530.10;
|
Glycosyl hydrolase 22 family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
|
Rattus norvegicus (Rat)
|
P00716
|
LALBA_RABIT
|
MMPLVPLLLVSIVFPGIQATQLTRCELTEKLKELDGYRDISMSEWICTLFHTSGLDTKITVNNNGSTEYGIFQISDKLWCVSKQNPQSKNICDTPCENFLDDNLTDDVKCAMKILDKEGIDHWLAHKPLCSENLEQWVCKK
| null | null |
defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; lactose biosynthetic process [GO:0005989]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; lactose synthase activity [GO:0004461]; lysozyme activity [GO:0003796]
|
PF00062;
|
1.10.530.10;
|
Glycosyl hydrolase 22 family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
|
Oryctolagus cuniculus (Rabbit)
|
P00720
|
ENLYS_BPT4
|
MNIFEMLRIDERLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSIWYNQTPNRAKRVITTFRTGTWDAYKNL
|
3.2.1.17
| null |
cell wall macromolecule catabolic process [GO:0016998]; defense response to bacterium [GO:0042742]; peptidoglycan catabolic process [GO:0009253]; viral release from host cell by cytolysis [GO:0044659]
|
host cell cytoplasm [GO:0030430]
|
lysozyme activity [GO:0003796]
|
PF00959;
|
1.10.530.40;
|
Glycosyl hydrolase 24 family
| null |
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04110}. Note=The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane. {ECO:0000255|HAMAP-Rule:MF_04110}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:4865643};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.3. {ECO:0000269|PubMed:4865643};
| null |
FUNCTION: Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer. {ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:22389108}.
|
Enterobacteria phage T4 (Bacteriophage T4)
|
P00722
|
BGAL_ECOLI
|
MTMITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWRFAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDMWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWSAEIPNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEHHPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFCMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALDGKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRIDPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGPQENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNISRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQLSAGRYHYQLVWCQK
|
3.2.1.23
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 2 magnesium ions per monomer. Can also use manganese.; COFACTOR: Name=Na(+); Xref=ChEBI:CHEBI:29101; Note=Binds 1 sodium ion per monomer.;
|
lactose catabolic process [GO:0005990]
|
beta-galactosidase complex [GO:0009341]
|
alkali metal ion binding [GO:0031420]; beta-galactosidase activity [GO:0004565]; carbohydrate binding [GO:0030246]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]
|
PF02929;PF00703;PF02836;PF02837;PF16353;
|
2.70.98.10;2.60.120.260;3.20.20.80;2.60.40.10;
|
Glycosyl hydrolase 2 family
| null | null |
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.; EC=3.2.1.23;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.04 mM for p-nitrophenyl beta-D-galactoside {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715}; KM=0.12 mM for o-nitrophenyl beta-D-galactoside {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715}; KM=0.15 mM for 2,3-dinitrophenyl beta-D-galactopyranoside {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715}; KM=0.41 mM for 2,5-dinitrophenyl beta-D-galactopyranoside {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715}; KM=11.6 mM for p-nitrophenol-alpha-L-arabinopyranoside {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715}; KM=16.9 mM for p-nitrophenol-beta-D-fucopyranoside {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715}; KM=34 uM for p-nitrophenyl beta-D-galactoside (with magnesium as cofactor and 30 degrees Celsius) {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715}; KM=140 uM for o-nitrophenyl beta-D-galactoside (with magnesium as cofactor and 30 degrees Celsius) {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715}; KM=940 uM for allolactose (with magnesium as cofactor and 30 degrees Celsius) {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715}; KM=1350 uM for lactose (with magnesium as cofactor and 30 degrees Celsius) {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715}; Vmax=30.9 umol/min/mg enzyme with lactose as substrate (with magnesium as cofactor and 30 degrees Celsius) {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715}; Vmax=49.7 umol/min/mg enzyme with allolactose as substrate (with magnesium as cofactor and 30 degrees Celsius) {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715}; Vmax=59.7 umol/min/mg enzyme with p-nitrophenyl beta-D-galactoside as substrate (with magnesium as cofactor and 30 degrees Celsius) {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715}; Vmax=360 umol/min/mg enzyme with o-nitrophenyl beta-D-galactoside as substrate (with magnesium as cofactor and 30 degrees Celsius) {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715}; Note=The values for the enzymatic assays using manganese as cofactor are very close.;
| null | null | null | null |
Escherichia coli (strain K12)
|
P00724
|
INV2_YEAST
|
MLLQAFLFLLAGFAAKISASMTNETSDRPLVHFTPNKGWMNDPNGLWYDEKDAKWHLYFQYNPNDTVWGTPLFWGHATSDDLTNWEDQPIAIAPKRNDSGAFSGSMVVDYNNTSGFFNDTIDPRQRCVAIWTYNTPESEEQYISYSLDGGYTFTEYQKNPVLAANSTQFRDPKVFWYEPSQKWIMTAAKSQDYKIEIYSSDDLKSWKLESAFANEGFLGYQYECPGLIEVPTEQDPSKSYWVMFISINPGAPAGGSFNQYFVGSFNGTHFEAFDNQSRVVDFGKDYYALQTFFNTDPTYGSALGIAWASNWEYSAFVPTNPWRSSMSLVRKFSLNTEYQANPETELINLKAEPILNISNAGPWSRFATNTTLTKANSYNVDLSNSTGTLEFELVYAVNTTQTISKSVFADLSLWFKGLEDPEEYLRMGFEVSASSFFLDRGNSKVKFVKENPYFTNRMSVNNQPFKSENDLSYYKVYGLLDQNILELYFNDGDVVSTNTYFMTTGNALGSVNMTTGVDNLFYIDKFQVREVK
|
3.2.1.26
| null |
fructan catabolic process [GO:0010147]; inulin catabolic process [GO:1902927]; raffinose catabolic process [GO:0034484]; sucrose catabolic process [GO:0005987]
|
cell periphery [GO:0071944]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; fungal-type vacuole [GO:0000324]; mitochondrion [GO:0005739]
|
beta-fructofuranosidase activity [GO:0004564]; inulinase activity [GO:0051670]; sucrose alpha-glucosidase activity [GO:0004575]
|
PF08244;PF00251;
| null |
Glycosyl hydrolase 32 family
|
PTM: Isoform Secreted is glycosylated. Isoform Intracellular is not glycosylated. {ECO:0000269|PubMed:3284881}.
|
SUBCELLULAR LOCATION: [Isoform Intracellular]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform Secreted]: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.; EC=3.2.1.26; Evidence={ECO:0000255|PROSITE-ProRule:PRU10067};
| null | null | null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
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