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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P0CZ17 | ASP21_YEAST | MRSLNTLLLSLFVAMSSGAPLLKIREEKNSSLPSIKIFGTGGTIASKGSTSATTAGYSVGLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPLYHGISEALASDDYAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSLGRGTMITLNDRIASGFWTTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQFFDISNLTDPSEIPEVIILYSYQGLNPELIVKAVKDLGAKGIVLAGSGAGSWTATGSIVNEQLYEEYGIPIVHSRRTADGTVPPDDA... | 3.5.1.1 | null | asparagine catabolic process [GO:0006530]; cellular response to nitrogen starvation [GO:0006995] | cell wall-bounded periplasmic space [GO:0030287]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; nuclear envelope [GO:0005635]; periplasmic space [GO:0042597] | asparaginase activity [GO:0004067] | PF00710;PF17763; | 3.40.50.40;3.40.50.1170; | Asparaginase 1 family | null | SUBCELLULAR LOCATION: Secreted. Periplasm. | CATALYTIC ACTIVITY: Reaction=H2O + L-asparagine = L-aspartate + NH4(+); Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.27 mM for L-asparagine {ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375}; KM=0.27 mM for D-asparagine {ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375}; KM=0.27 mM for N-acetyl-L-asparagine {ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375}; KM=0... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8. Active from pH 5.5 to pH 7.5. Stable from pH 3.5 to pH 10.5. {ECO:0000269|PubMed:342521, ECO:0000269|PubMed:6986375}; | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0CZ23 | ACOX3_ARATH | MSDNRALRRAHVLANHILQSNPPSSNPSLSRELCLQYSPPELNESYGFDVKEMRKLLDGHNVVDRDWIYGLMMQSNLFNRKERGGKIFVSPDYNQTMEQQREITMKRIWYLLENGVFKGWLTETGPEAELRKLALLEVCGIYDHSVSIKVGVHFFLWGNAVKFFGTKRHHEKWLKNTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLHINGTNQGVHAFIAQIRDQDGSICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNAVADVSSDGKYVSSIKD... | 1.3.3.6 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; | fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; lipid homeostasis [GO:0055088]; medium-chain fatty acid metabolic process [GO:0051791] | extracellular region [GO:0005576]; peroxisome [GO:0005777] | acyl-CoA oxidase activity [GO:0003997]; FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; pristanoyl-CoA oxidase activity [GO:0016402] | PF01756;PF00441;PF02770; | 2.40.110.10;1.20.140.10; | Acyl-CoA oxidase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10918060}. | CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2; Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.7 uM for lauroyl-CoA; | PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9.0.; | null | FUNCTION: Catalyzes the desaturation of medium-chain acyl-CoAs to 2-trans-enoyl-CoAs. Active on C8:0- to C14:0-CoA with a maximal activity on C12:0-CoA. | Arabidopsis thaliana (Mouse-ear cress) |
P0DD38 | SPEB_STRP3 | MNKKKLGIRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRSDFSKQDWEAQID... | 3.4.22.10 | null | evasion of host immune response [GO:0042783]; proteolysis [GO:0006508]; symbiont-induced defense-related programmed cell death [GO:0034050]; symbiont-mediated suppression of host autophagy [GO:0140321] | extracellular region [GO:0005576]; host cell cytosol [GO:0044164]; host extracellular space [GO:0043655] | cysteine-type endopeptidase activity [GO:0004197]; toxin activity [GO:0090729] | PF13734;PF01640; | 3.90.70.50; | Peptidase C10 family | PTM: The mature protease is derived from the precursor sequence by cleavage, either in cis via an autocatalytic mechanism, or in trans by mature SpeB or host proteases (trypsin, plasmin or subtilisin). Maturation can involve a number of protein cleavage intermediates. Mature SpeB probably plays the most important role ... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7516997}. Host extracellular space {ECO:0000269|PubMed:7516997}. Host cytoplasm {ECO:0000250|UniProtKB:P0C0J0}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage with hydrophobic residues at P2, P1 and P1'.; EC=3.4.22.10; Evidence={ECO:0000250|UniProtKB:P0C0J1}; | null | null | null | null | FUNCTION: Cysteine protease that acts as a key streptococcal virulence factor by cleaving host proteins involved in immune response (PubMed:7516997). Triggers inflammation by mediating cleavage of host proteins, which can both promote host pathogenesis by triggering sterile inflammation and/or restrict streptococcal in... | Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315) |
P0DH74 | PYRDB_ENTFA | MMKNPLAVSIPGLTLKNPIIPASGCFGFGEEYANYYDLDQLGSIMIKATTPQARYGNPTPRVAETPSGMLNAIGLQNPGLEVVMQEKLPKLEKYPNLPIIANVAGACEEDYVAVCAKIGQAPNVKAIELNISCPNVKHGGIAFGTDPEVAFQLTQAVKKVASVPIYVKLSPNVTDIVPIAQAIEAGGADGFSMINTLLGMRIDLKTRKPILANQTGGLSGPAIKPVAIRLIRQVASVSQLPIIGMGGVQTVDDVLEMFMAGASAVGVGTANFTDPYICPKLIDGLPKRMEELGIESLEQLIKEVREGQQNAR | 1.3.1.14 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:10529184}; Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:10529184}; | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205] | cytoplasm [GO:0005737] | dihydroorotate dehydrogenase (NADH) activity [GO:0004589] | PF01180; | 3.20.20.70; | Dihydroorotate dehydrogenase family, Type 1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate; Xref=Rhea:RHEA:13513, ChEBI:CHEBI:15378, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.14; Evidence={ECO:0000269|PubMed:10529184}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=36.4 uM for orotate {ECO:0000269|PubMed:10529184}; KM=33.2 uM for dihydroorotate {ECO:0000269|PubMed:10529184}; KM=135 uM for NAD(+) {ECO:0000269|PubMed:10529184}; KM=27 uM for NADH {ECO:0000269|PubMed:10529184}; | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-8. {ECO:0000269|PubMed:10529184}; | null | FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor. | Enterococcus faecalis (strain ATCC 700802 / V583) |
P0DH86 | SRK_ARATH | MRGELPNKHHSYTFFVFLFFFLILFPDLSISVNTLSATESLTISSNKTIVSPGGVFELGFFRILGDSWYLGIWYKKISQRTYVWVANRDTPLSNPIGILKISNANLVILDNSDTHVWSTNLTGAVRSSVVAELLDNGNFVLRGSKINESDEFLWQSFDFPTDTLLPQMKLGRDHKRGLNRFVTSWKSSFDPSSGSFMFKLETLGLPEFFGFTSFLEVYRSGPWDGLRFSGILEMQQWDDIIYNFTENREEVAYTFRVTDHNSYSRLTINTVGRLEGFMWEPTQQEWNMFWFMPKDTCDLYGICGPYAYCDMSTSPTCNCI... | 2.7.11.1 | null | defense response to bacterium [GO:0042742]; protein autophosphorylation [GO:0046777]; recognition of pollen [GO:0048544] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; carbohydrate binding [GO:0030246]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; ubiquitin protein ligase binding [GO:0031625] | PF01453;PF11883;PF12398;PF08276;PF07714;PF00954; | 2.90.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {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=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Female specificity determinant of self-incompatibility. {ECO:0000269|PubMed:15505209, ECO:0000269|PubMed:17237349, ECO:0000269|PubMed:17656687, ECO:0000269|PubMed:20400945}. | Arabidopsis thaliana (Mouse-ear cress) |
P0DH91 | ARF2B_ARATH | MGLSFAKLFSRLFAKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWLSNNIAGKA | null | null | intracellular protein transport [GO:0006886]; vesicle-mediated transport [GO:0016192] | Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; mRNA binding [GO:0003729]; phospholipase activator activity [GO:0016004] | PF00025; | 3.40.50.300; | Small GTPase superfamily, Arf family | null | SUBCELLULAR LOCATION: Golgi apparatus. | null | null | null | null | null | FUNCTION: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. | Arabidopsis thaliana (Mouse-ear cress) |
P0DH96 | CALM4_ARATH | MADQLTDEQISEFKEAFSLFDKDGDGCITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLNLMAKKMKDTDSEEELKEAFRVFDKDQNGFISAAELRHVMTNLGEKLTDEEVEEMIREADVDGDGQINYEEFVKIMMAK | null | null | null | null | calcium ion binding [GO:0005509] | PF13499; | 1.10.238.10; | Calmodulin family | null | null | null | null | null | null | null | FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Activates MPK8 through direct binding and in an calcium-dependent manner. {ECO:0000269|... | Arabidopsis thaliana (Mouse-ear cress) |
P0DI10 | PER1_ARATH | MAIKNILALVVLLSVVGVSVAIPQLLDLDYYRSKCPKAEEIVRGVTVQYVSRQKTLAAKLLRMHFHDCFVRGCDGSVLLKSAKNDAERDAVPNLTLKGYEVVDAAKTALERKCPNLISCADVLALVARDAVAVIGGPWWPVPLGRRDGRISKLNDALLNLPSPFADIKTLKKNFANKGLNAKDLVVLSGGHTIGISSCALVNSRLYNFTGKGDSDPSMNPSYVRELKRKCPPTDFRTSLNMDPGSALTFDTHYFKVVAQKKGLFTSDSTLLDDIETKNYVQTQAILPPVFSSFNKDFSDSMVKLGFVQILTGKNGEIRKR... | 1.11.1.7 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00297}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000255|PROSITE-ProRule:PRU00297}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00297}; Note=Binds 2 calcium... | hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979] | extracellular region [GO:0005576]; plant-type cell wall [GO:0009505]; plasmodesma [GO:0009506] | heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872] | PF00141; | 1.10.520.10;1.10.420.10; | Peroxidase family, Classical plant (class III) peroxidase subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}. | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; | null | null | null | null | FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. | Arabidopsis thaliana (Mouse-ear cress) |
P0DI81 | TPC2A_HUMAN | MSGSFYFVIVGHHDNPVFEMEFLPAGKAESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGHMRFIMLHDIRQEDGIKNFFTDVYDLYIKFSMNPFYEPNSPIRSSAFDRKVQFLGKKHLLS | null | null | COPII vesicle coating [GO:0048208]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; skeletal system development [GO:0001501]; vesicle coating [GO:0006901]; vesicle tethering [GO:0099022] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; TRAPP complex [GO:0030... | transmembrane transporter binding [GO:0044325] | PF04628; | 3.30.450.70; | TRAPP small subunits family, Sedlin subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11031107}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:11031107}. Nucleus {ECO:0000269|PubMed:20498720, ECO:0000269|PubMed:25918224}. Cytoplasm {ECO:0000269|PubMed:20498720}. Note=Localized in perinuclear granular struc... | null | null | null | null | null | FUNCTION: Prevents transcriptional repression and induction of cell death by ENO1 (By similarity). May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}. | Homo sapiens (Human) |
P0DI82 | TPC2B_HUMAN | MSGSFYFVIVGHHDNPVFEMEFLPAGKAESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGHMRFIMLHDIRQEDGIKNFFTDVYDLYIKFSMNPFYEPNSPIRSSAFDRKVQFLGKKHLLS | null | null | COPII vesicle coating [GO:0048208]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; positive regulation of gene expression [GO:0010628]; vesicle coating [GO:0006901]; vesicle tethering [GO:0099022] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; intracellular membrane-bounded organelle [GO:0043231]; nuclear outer membrane [GO:0005640]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; TRAPP c... | transcription corepressor binding [GO:0001222]; transcription regulator inhibitor activity [GO:0140416] | PF04628; | 3.30.450.70; | TRAPP small subunits family, Sedlin subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11134351}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm {ECO:0000250|UniProtKB:P0DI81}. Note=Localized in perinuclear granular structures. {ECO:0000250|UniPro... | null | null | null | null | null | FUNCTION: Prevents transcriptional repression and induction of cell death by ENO1. May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000269|PubMed:11134351}. | Homo sapiens (Human) |
P0DI83 | NARR_HUMAN | MVGQPQPRDDVGSPRPRVIVGTIRPRVIVGTIRPRVIVGSARARPPPDGTPRPQLAAEESPRPRVIFGTPRARVILGSPRPRVIVSSPWPAVVVASPRPRTPVGSPWPRVVVGTPRPRVIVGSPRARVADADPASAPSQGALQGRRQDEHSGTRAEGSRPGGAAPVPEEGGRFARAQRLPPPRHLRLPGAPDRHRGQI | null | null | null | nucleolus [GO:0005730] | null | null | null | null | PTM: Phosphorylated during M-phase. {ECO:0000269|PubMed:21586586}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21586586}. Nucleus, nucleolus {ECO:0000269|PubMed:21586586}. Note=Colocalizes with rDNA clusters. | null | null | null | null | null | null | Homo sapiens (Human) |
P0DI84 | OXLA_VIPAA | DRNPLEECFRETDYEEFLEIARNGLKKTSNPKHVVVVGAGMSGLSAAYVLAGAGHKVTVLEASERAGGRVRTHRNSKEGWYANLGPMRIPEKHRIVREYIRKFGLNLNEFSQENDNAWYFIKNIRKRVGEVNKDPGLLKYPVKPSEEGKSAGQLYEESLGSAVKDLKRTNCSYILNKYDTYSTKEYLIKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDQLPTSMYRAIEEKVKFNARVIKIQQNANQVTVTYQTPEKDTSSNTADYVIVCTTSRAARRIQFEPPLPPKKQHALRSVHYR... | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:20938508}; | amino acid catabolic process [GO:0009063]; apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | L-amino-acid oxidase activity [GO:0001716]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family, FIG1 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18931435}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000250|UniProtKB:P81382}; | null | null | null | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or... | Vipera ammodytes ammodytes (Western sand viper) |
P0DI88 | OXLA_BOTJA | ADDKNPLEECFRETDYEEFLEIARNGLKATSNPKRVV | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P81382}; | apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | L-phenylalaine oxidase activity [GO:0106329]; toxin activity [GO:0090729] | null | 3.90.660.10; | Flavin monoamine oxidase family, FIG1 subfamily | PTM: N-Glycosylated. {ECO:0000269|PubMed:19101583}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18346051, ECO:0000269|PubMed:19101583}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:18346051, ECO:0000269|PubMed:19101583}; CAT... | null | null | null | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:18346051). Is highly active on L-Leu, L-Met, moderately active on L-Arg, L-Trp, L-Phe, L-Val, L-His, and L-Ile, a... | Bothrops jararaca (Jararaca) (Bothrops jajaraca) |
P0DI89 | OXLA_BOTLC | ADDRNPLEECFRETDYEEFLEIAKNGLSTT | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P81382}; | apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | L-phenylalaine oxidase activity [GO:0106329]; toxin activity [GO:0090729] | null | 3.90.660.10; | Flavin monoamine oxidase family, FIG1 subfamily | PTM: N-glycosylated. {ECO:0000269|PubMed:21539897}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21539897}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:21539897}; CATALYTIC ACTIVITY: Reaction=H2O... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.8 for L-Leu. {ECO:0000269|PubMed:21539897}; | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:21539897). Is highly active against L-Met, L-Leu, L-norleucine (L-2-aminohexanoate), L-Trp, L-Phe, moderately act... | Bothrops leucurus (Whitetail lancehead) |
P0DI90 | OXLA2_DABRR | ADDKNPLEECFCEDDDYCEG | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:18384385}; | apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | L-phenylalaine oxidase activity [GO:0106329]; toxin activity [GO:0090729] | null | null | Flavin monoamine oxidase family, FIG1 subfamily | PTM: N-glycosylated. {ECO:0000305|PubMed:18384385}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18384385}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:18384385}; CATALYTIC ACTIVITY: Reaction=H2O... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.89 mM for L-Ile {ECO:0000269|PubMed:18384385}; KM=599.7 uM for L-Leu {ECO:0000269|PubMed:18384385}; KM=222.8 uM for L-Met {ECO:0000269|PubMed:18384385}; KM=49.3 uM for L-Phe {ECO:0000269|PubMed:18384385}; KM=235.1 uM for L-Trp {ECO:0000269|PubMed:18384385}; KM=53... | null | null | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:18384385). Is active on L-Ile, L-Leu, L-Met, L-Phe, L-Trp, and L-Tyr (PubMed:18384385). Exhibits diverse biologic... | Daboia russelii (Russel's viper) (Vipera russelii) |
P0DI91 | OXLA_NAJOX | DDRRSPLEECFQQNDYEEFLEIARNSQLYQESLREDSSYHLSFIESLKSDALFSYEKKFWEADGIHGGKVINDLSLIHDLPKREIQALCYPSIKK | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P81382}; | apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | L-phenylalaine oxidase activity [GO:0106329]; toxin activity [GO:0090729] | null | 3.90.660.10; | Flavin monoamine oxidase family, FIG1 subfamily | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18294891}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:18294891}; CATALYTIC ACTIVITY: Reaction=H2O... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.885 mM for L-Met {ECO:0000269|PubMed:18294891}; KM=0.75 mM for L-Leu {ECO:0000269|PubMed:18294891}; KM=0.147 mM for L-Trp {ECO:0000269|PubMed:18294891}; KM=0.051 mM for L-Phe {ECO:0000269|PubMed:18294891}; | null | null | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:18294891). Is highly active on L-Met, L-Leu, L-Phe, L-Trp, and L-Arg, and no weakly or no active on L-His, L-Tyr,... | Naja oxiana (Central Asian cobra) (Oxus cobra) |
P0DI97 | NRX1B_MOUSE | MYQRMLRCGADLGSPGGGSGGGAGGRLALIWIVPLTLSGLLGVAWGASSLGAHHIHHFHGSSKHHSVPIAIYRSPASLRGGHAGTTYIFSKGGGQITYKWPPNDRPSTRADRLAIGFSTVQKEAVLVRVDSSSGLGDYLELHIHQGKIGVKFNVGTDDIAIEESNAIINDGKYHVVRFTRSGGNATLQVDSWPVIERYPAGNNDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQATIIIGGKEQGQPFQGQLSGLYYNGLKVLNMAAENDANIAIVGNVRLVGEVPSSMTTESTATAMQSEMSTSIMETTTTLA... | null | null | angiogenesis [GO:0001525]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell-cell adhesion involved in synapse maturation [GO:0090125]; cellular response to calcium ion [GO:0071277]; cerebellar granule cell differentiation [GO:0021707]; chemical synaptic transmission [G... | axonal growth cone [GO:0044295]; cell surface [GO:0009986]; endocytic vesicle [GO:0030139]; endoplasmic reticulum [GO:0005783]; excitatory synapse [GO:0060076]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; inhibitory synapse [GO:0060077]; neuromuscular junction [GO:0031594]; neuron to neuron syn... | acetylcholine receptor binding [GO:0033130]; calcium channel regulator activity [GO:0005246]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; cell adhesion molecule binding [GO:0050839]; neuroligin family protein binding [GO:0097109]; protein-containing complex binding [GO:0044877]; si... | PF02210;PF01034; | 2.60.120.200; | Neurexin family | PTM: O-glycosylated; contains heparan sulfate. Heparan sulfate attachment is required for synapse development by mediating interactions with neuroligins. {ECO:0000269|PubMed:30100184}. | SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q63373}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q63373}. | null | null | null | null | null | FUNCTION: Neuronal cell surface protein involved in cell recognition and cell adhesion by forming intracellular junctions through binding to neuroligins (By similarity). Plays a role in formation of synaptic junctions (PubMed:30100184). {ECO:0000250|UniProtKB:Q63373, ECO:0000269|PubMed:30100184}. | Mus musculus (Mouse) |
P0DJ06 | CARP2_CANAL | MFLKNIFIALAIALLVDATPTTTKRSAGFVALDFSVVKTPKAFPVTNGQEGKTSKRQAVPVTLHNEQVTYAADITVGSNNQKLNVIVDTGSSDLWVPDVNVDCQVTYSDQTADFCKQKGTYDPSGSSASQDLNTPFKIGYGDGSSSQGTLYKDTVGFGGVSIKNQVLADVDSTSIDQGILGVGYKTNEAGGSYDNVPVTLKKQGVIAKNAYSLYLNSPDAATGQIIFGGVDNAKYSGSLIALPVTSDRELRISLGSVEVSGKTINTDNVDVLVDSGTTITYLQQDLADQIIKAFNGKLTQDSNGNSFYEVDCNLSGDVVF... | 3.4.23.24 | null | adhesion of symbiont to host [GO:0044406]; fungal-type cell wall organization [GO:0031505]; induction by symbiont of defense-related host calcium ion flux [GO:0052391]; induction by symbiont of host defense response [GO:0044416]; protein catabolic process [GO:0030163]; protein metabolic process [GO:0019538]; proteolysi... | extracellular region [GO:0005576]; extracellular vesicle [GO:1903561]; fungal-type cell wall [GO:0009277] | aspartic-type endopeptidase activity [GO:0004190]; metal ion binding [GO:0046872] | PF00026; | 2.40.70.10; | Peptidase A1 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1447155, ECO:0000269|PubMed:8478090, ECO:0000269|PubMed:9841840}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin.; EC=3.4.23.24; Evidence={ECO:0000269|PubMed:21646240, ECO:0000269|PubMed:27390786, ECO:... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0 using BSA or casein-resorufin as substrates, and 6.0-7.0, the pH of the saliva, for cleavage of Hst 5. {ECO:0000269|PubMed:21646240, ECO:0000269|PubMed:27390786, ECO:0000269|PubMed:9043112}; | null | FUNCTION: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors (PubMed:11478679, PubMed:12761103, PubMed:15820985, PubMed:15845479, PubMed:19880183, PubMed:20713630, PubMed:22302440, PubMed:23927842). These enzymes supply the fungus with nutrient amino acids as we... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
P0DJ26 | COFA_DICDI | MSSGIALAPNCVSTFNDLKLGRKYGGIIYRISDDSKEIIVDSTLPAGCSFDEFTKCLPENECRYVVLDYQYKEEGAQKSKICFVAWCPDTANIKKKMMATSSKDSLRKACVGIQVEIQGTDASEVKDSCFYEKCTKI | null | null | actin filament bundle assembly [GO:0051017]; actin filament depolymerization [GO:0030042]; actin filament fragmentation [GO:0030043]; actin filament severing [GO:0051014]; cell motility [GO:0048870]; hyperosmotic response [GO:0006972]; response to bacterium [GO:0009617] | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; intranuclear rod [GO:0061836]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]; phagocytic vesicle [GO:0045335]; ruffle [GO:0001726] | actin filament binding [GO:0051015]; actin monomer binding [GO:0003785] | PF00241; | 3.40.20.10; | Actin-binding proteins ADF family | null | SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. | null | null | null | null | null | FUNCTION: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods (By similarity). {ECO:0000250}. | Dictyostelium discoideum (Social amoeba) |
P0DJ31 | KA231_VAEMS | AAAISCVGSPECPPKCRAQGCKNGKCMNRKCECYYC | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; toxin activity [GO:0090729] | PF00451; | 3.30.30.10; | Short scorpion toxin superfamily, Potassium channel inhibitor family, Alpha-KTx 23 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22540187, ECO:0000269|PubMed:22622363, ECO:0000269|Ref.1}. | null | null | null | null | null | FUNCTION: Voltage-gated potassium channel inhibitor. Selectively and irreversibly binds (K(d)=2.9 pM) and blocks hKv1.3/KCNA3 potassium channels of human T-lymphocytes. Weakly blocks hKCa3.1/KCNN4, mKv1.1/KCNA1, and hKv1.2/KCNA2 channels. In vivo, high doses (200 ug) produce no symptoms of intoxication when injected in... | Vaejovis mexicanus smithi (Mexican scorpion) (Vaejovis smithi) |
P0DJ41 | KKX51_HETLA | MKLLPLLFVILIVCAILPDEASCDQSELERKEENFKDESREIVKRSCKKECSGSRRTKKCMQKCNREHGHGR | null | null | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792] | acetylcholine receptor inhibitor activity [GO:0030550]; potassium channel regulator activity [GO:0015459]; toxin activity [GO:0090729] | null | null | Short scorpion toxin superfamily, Potassium channel inhibitor kappa-KTx family, Kappa-KTx 5 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22305749}. | null | null | null | null | null | FUNCTION: Weak blocker of potassium channels Kv1.1/KCNA1 (IC(50)=578.5 nM-9.9 uM) and Kv1.6/KCNA6 (~60% block at 30 uM of toxin) (PubMed:22305749, PubMed:26724500). Acts by binding to the pore and occluding it (PubMed:22305749). Has a voltage-dependent mode of action, which can be explained by a high content of basic r... | Heterometrus laoticus (Thai giant scorpion) |
P0DJ42 | VM1CR_CROAT | LLRRKSHDHAQNHDGDKCLRGASLGYYQSFLNQYKPQCILNKP | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | envenomation resulting in fibrinogenolysis in another organism [GO:0044485]; envenomation resulting in hemorrhagic damage in another organism [GO:0044358]; envenomation resulting in negative regulation of platelet aggregation in another organism [GO:0044477]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; host extracellular space [GO:0043655] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | null | null | Venom metalloproteinase (M12B) family, P-I subfamily | PTM: This protein autoproteolytically degrades to 10 kDa and 14 kDa fragments in the presence of SDS. Interestingly, the two fragments, as well as reduced crotalin are able to bind vWF, indicating that the binding activity does not require a specific protein conformation. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom zinc metalloproteinase that inhibits ristocin-induced platelet aggregation by abolishing the binding of von Willebrand factor (vWF) to platelet glycoprotein Ib alpha (GPIBA) through the cleavage of both GP1BA and vWF. Also has fibrinogenolytic activities by degrading the alpha- (FGA) and beta-chai... | Crotalus atrox (Western diamondback rattlesnake) |
P0DJ43 | VM3_MICIK | TNTPEQDRYLQVKKYLEYVVVDNNMYRNYGNAGPCVMSAEISFEPLQEFSSCDIQEPLSQDIVQPAVCGNYYVEVGGECDCGSPKPCRSACCNAATCKLQREHQCDSGECCEKKDDCDLPEICTGRSAKCSCVISQGDLGYGMVEPGTKCTDGMVCSNEQCVDVQTAAK | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | induction of blood coagulation in another organism [GO:0035807]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; host extracellular space [GO:0043655]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; peptidase activator activity [GO:0016504]; toxin activity [GO:0090729] | null | 4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom zinc metalloproteinase that calcium-independently catalyzes the conversion of prothrombin (F2) to alpha-thrombin through the formation of a thrombin intermediate. {ECO:0000269|PubMed:12485606}. | Micropechis ikaheca (New Guinean small-eyed snake) |
P0DJ44 | VM3_VIPAA | MVTKYSSIFMSPILSNPPILYFSDCSREXYQKXLTN | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | envenomation resulting in fibrinogenolysis in another organism [GO:0044485]; envenomation resulting in hemorrhagic damage in another organism [GO:0044358]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; host extracellular space [GO:0043655] | metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]; toxin activity [GO:0090729] | null | null | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily | PTM: The N-terminus is blocked.; PTM: Glycosylated. | SUBCELLULAR LOCATION: Secreted. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:11602279}; | null | FUNCTION: Snake venom zinc metalloprotease that exhibits strong hemorrhagic activity. It also degrades alpha-chain of fibrinogen (FGA), but not the beta- and the gamma-chains. Possesses potent azocaseinolytic activity and cleaves insulin B-chain, hydrolyzing it at positions Ala(14)-Leu(15), followed by Tyr(16)-Leu(17) ... | Vipera ammodytes ammodytes (Western sand viper) |
P0DJ46 | VKT21_LYCMC | MKSFLLIALVLFFLFVSYASAKKKCQLPSDVGKGKASFTRYYYNEESGKCETFIYGGVGGNSNNFLTKEDCCRECAQGSC | null | null | envenomation resulting in negative regulation of voltage-gated potassium channel activity in another organism [GO:0044562] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; host cell membrane [GO:0033644] | potassium channel regulator activity [GO:0015459]; serine-type endopeptidase inhibitor activity [GO:0004867]; toxin activity [GO:0090729] | PF00014; | 4.10.410.10; | Venom Kunitz-type family, Scorpion delta-Ktx subfamily, Delta-Ktx 2 sub-subfamily | PTM: Lacks the conserved CysII-CysIV disulfide bond but contains 2 cysteine residues at the C-terminus that generate a new disulfide bond. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Dual-function toxin that completely inhibits trypsin activity at a molar ratio of 1:1 (Ki=140 nM) and that inhibits mKv1.3/KCNA3 potassium channel currents (1 uM inhibits 50% of currents) (IC(50)=1.58 uM). Shows also weak inhibition on Kv1.1/KCNA1 (1 uM inhibits 25% of currents) and Kv1.2/KCNA2 (1 uM inhibits... | Lychas mucronatus (Chinese swimming scorpion) |
P0DJ86 | VSPL_BOTLC | VIGGDECDINEHPFLAFMYYSPRYFCGMTLINQEWVLTAAHCNRRFMRIXXXXHAGSVANYDEVVRXXXXXFICPNKKKNVITDKDIMLIRLDRPVKNSEHIAPLSLPSNPPSVGSVCRIMGWGAITTSEDTYPDVPHCANINLFNNTVCREAYNGLPAKTLCAGVLQGGIDTCGGDSGGPLICNGQFQGILSWGSDPCAEPRKPAFYTKVFDYLPWIQSIIAGNKTATCP | 3.4.21.74 | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: Glycosylated. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16481207}. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme.; EC=3.4.21.74; Evidence={ECO:0000269|PubMed:16481207}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.9 uM for H-D-Val-Leu-Arg-pNA (S-2266) {ECO:0000269|PubMed:16481207}; KM=7.9 uM for H-D-Pro-Phe-Arg-pNA (S-2302) {ECO:0000269|PubMed:16481207}; KM=2.7 uM for Bz-Phe-Val-Arg-pNA (S-2160) {ECO:0000269|PubMed:16481207}; KM=5.7 uM for H-D-Val-Leu-Lys-pNA (S-2251) {ECO... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-8.5. {ECO:0000269|PubMed:16481207}; | null | FUNCTION: Thrombin-like snake venom serine protease that cleaves Arg-Gly bonds in alpha-chain of fibrinogen (FGA). Induces temporary episodes of opisthotonos and rapid rolling around the long axis of the animal (gyroxin-like effect), when injected into the tail veins of mice (0.143 ug/g mouse). {ECO:0000269|PubMed:1648... | Bothrops leucurus (Whitetail lancehead) |
P0DJA3 | LSC_ZYMMO | MLNKAGIAEPSLWTRADAMKVHTDDPTATMPTIDYDFPVMTDKYWVWDTWPLRDINGQVVSFQGWSVIFALVADRTKYGWHNRNDGARIGYFYSRGGSNWIFGGHLLKDGANPRSWEWSGCTIMAPGTANSVEVFFTSVNDTPSESVPAQCKGYIYADDKSVWFDGFDKVTDLFQADGLYYADYAENNFWDFRDPHVFINPEDGKTYALFEGNVAMERGTVAVGEEEIGPVPPKTETPDGARYCAAAIGIAQALNEARTEWKLLPPLVTAFGVNDQTERPHVVFQNGLTYLFTISHHSTYADGLSGPDGVYGFVSENGIF... | 2.4.1.10 | null | carbohydrate utilization [GO:0009758] | extracellular region [GO:0005576] | levansucrase activity [GO:0050053] | PF02435; | null | Glycosyl hydrolase 68 family | PTM: Does not seem to be N-terminally processed. {ECO:0000305|PubMed:7766026}. | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:7766026}. | CATALYTIC ACTIVITY: Reaction=[6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside + sucrose = [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D-glucopyranoside + D-glucose; Xref=Rhea:RHEA:13653, Rhea:RHEA-COMP:13093, Rhea:RHEA-COMP:13094, ChEBI:CHEBI:4167, ChEBI:CHEBI:17992, ChEBI:CHEBI:134464; EC=2.4.1.10; Evidence... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=125 mM for sucrose {ECO:0000269|PubMed:12359071}; Note=kcat is 1700 min(-1) for sucrose hydrolase activity. {ECO:0000269|PubMed:12359071}; | null | null | null | FUNCTION: Catalyzes the synthesis of levan, a fructose polymer, by transferring the fructosyl moiety from sucrose to a growing acceptor molecule (PubMed:12359071). Can also cleave raffinose and stachyose, but does not cleave 1-kestose, nystose, levan and inulin (PubMed:12359071). Also displays sucrose hydrolase activit... | Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) |
P0DJD2 | APOA2_PONAB | MKLLAATVLLLTICSLEGALVRRQAKEPCVESPVSQYFQTVTDYGKDLMEKVKSPELQAEAKSYFEKSKEQLTPLIKKAGTELVNFLNYFLEL | null | null | cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle remodeling [GO:0034375]; lipoprotein metabolic process [GO:0042157]; low-density lipoprotein particle remodelin... | blood microparticle [GO:0072562]; chylomicron [GO:0042627]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | apolipoprotein receptor binding [GO:0034190]; cholesterol binding [GO:0015485]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; lipase inhibitor activity [GO:0055102]; phosphatidylcholine binding [GO:0031210] | PF04711; | 6.10.250.100; | Apolipoprotein A2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}. | null | null | null | null | null | FUNCTION: May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism. | Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
P0DJD3 | RBY1A_HUMAN | MVEADHPGKLFIGGLNRETNEKMLKAVFGKHGPISEVLLIKDRTSKSRGFAFITFENPADAKNAAKDMNGKSLHGKAIKVEQAKKPSFQSGGRRRPPASSRNRSPSGSLRSARGSRGGTRGWLPSHEGHLDDGGYTPDLKMSYSRGLIPVKRGPSSRSGGPPPKKSAPSAVARSNSWMGSQGPMSQRRENYGVPPRRATISSWRNDRMSTRHDGYATNDGNHPSCQETRDYAPPSRGYAYRDNGHSNRDEHSSRGYRNHRSSRETRDYAPPSRGHAYRDYGHSRRDESYSRGYRNRRSSRETREYAPPSRGHGYRDYGHS... | null | null | mRNA processing [GO:0006397]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; RNA splicing [GO:0008380] | nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681] | mRNA binding [GO:0003729]; RNA binding [GO:0003723] | PF08081;PF00076; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9108067}. | null | null | null | null | null | FUNCTION: RNA-binding protein involved in pre-mRNA splicing. Required for sperm development. Acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN. Binds non-specifically to mRNAs. {ECO:0000269|PubMed:12165565, ECO:0000269|PubMed:8269511}. | Homo sapiens (Human) |
P0DJD4 | RBY1C_HUMAN | MVEADHPGKLFIGGLNRETNEKMLKAVFGKHGPISEVLLIKDRTSKSRGFAFITFENPADAKNAAKDMNGKSLHGKAIKVEQAQKPSFQSGGRRRPPASSRNRSPSGSLRSARGSRGGTRGWLPSHEGHLDDGGYTPDLKMSYSRGLIPVKRGPSSRSGGPPPKKSAPSAVARSNSWMGSQGPMSQRRENYGVPPRRATISSWRNDRMSTRHDGYATNDGNHPSCQETRDYAPPSRGYAYRDNGHSNRDEHSSRGYRNHRSSRETRDYAPPSRGHAYRDYGHSRRDESYSRGYRNRRSSRETREYAPPSRGHGYRDYGHS... | null | null | mRNA processing [GO:0006397]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; regulation of RNA splicing [GO:0043484]; RNA splicing [GO:0008380] | nucleus [GO:0005634]; protein-containing complex [GO:0032991]; spliceosomal complex [GO:0005681] | identical protein binding [GO:0042802]; RNA binding [GO:0003723] | PF08081;PF00076; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9108067}. | null | null | null | null | null | FUNCTION: RNA-binding protein involved in pre-mRNA splicing. Required for sperm development. Acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN. Binds non-specifically to mRNAs. | Homo sapiens (Human) |
P0DJD7 | PEPA4_HUMAN | MKWLLLLGLVALSECIMYKVPLIRKKSLRRTLSERGLLKDFLKKHNLNPARKYFPQWEAPTLVDEQPLENYLDMEYFGTIGIGTPAQDFTVVFDTGSSNLWVPSVYCSSLACTNHNRFNPEDSSTYQSTSETVSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWNQGLVSQDLFSVYLSADDQSGSVVIFGGIDSSYYTGSLNWVPVTVEGYWQITVDSITMNGEAIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGDMVVSCSAISSLPDI... | 3.4.23.1 | null | digestion [GO:0007586]; proteolysis [GO:0006508] | extracellular exosome [GO:0070062]; multivesicular body lumen [GO:0097486] | aspartic-type endopeptidase activity [GO:0004190] | PF07966;PF00026; | 6.10.140.60;2.40.70.10; | Peptidase A1 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.; EC=3.4.... | null | null | null | null | FUNCTION: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent. | Homo sapiens (Human) |
P0DJD8 | PEPA3_HUMAN | MKWLLLLGLVALSECIMYKVPLIRKKSLRRTLSERGLLKDFLKKHNLNPARKYFPQWKAPTLVDEQPLENYLDMEYFGTIGIGTPAQDFTVVFDTGSSNLWVPSVYCSSLACTNHNRFNPEDSSTYQSTSETVSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWNQGLVSQDLFSVYLSADDQSGSVVIFGGIDSSYYTGSLNWVPVTVEGYWQITVDSITMNGEAIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGDMVVSCSAISSLPDI... | 3.4.23.1 | null | digestion [GO:0007586]; proteolysis [GO:0006508] | extracellular exosome [GO:0070062]; multivesicular body lumen [GO:0097486] | aspartic-type endopeptidase activity [GO:0004190] | PF07966;PF00026; | 6.10.140.60;2.40.70.10; | Peptidase A1 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.; EC=3.4.... | null | null | null | null | FUNCTION: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent. | Homo sapiens (Human) |
P0DJD9 | PEPA5_HUMAN | MKWLLLLGLVALSECIMYKVPLIRKKSLRRTLSERGLLKDFLKKHNLNPARKYFPQWEAPTLVDEQPLENYLDMEYFGTIGIGTPAQDFTVVFDTGSSNLWVPSVYCSSLACTNHNRFNPEDSSTYQSTSETVSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWNQGLVSQDLFSVYLSADDKSGSVVIFGGIDSSYYTGSLNWVPVTVEGYWQITVDSITMNGETIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGDMVVSCSAISSLPDI... | 3.4.23.1 | null | digestion [GO:0007586]; proteolysis [GO:0006508] | extracellular exosome [GO:0070062]; multivesicular body lumen [GO:0097486] | aspartic-type endopeptidase activity [GO:0004190] | PF07966;PF00026; | 6.10.140.60;2.40.70.10; | Peptidase A1 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.; EC=3.4.... | null | null | null | null | FUNCTION: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent. | Homo sapiens (Human) |
P0DJE1 | VM1B1_BOTAT | YIELAVVADHGIFTKYNSNLNTIR | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]; toxin activity [GO:0090729] | null | null | Venom metalloproteinase (M12B) family, P-I subfamily | PTM: The N-terminus is blocked.; PTM: Contains 3 disulfide bonds. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Zinc metalloproteinase that exhits a weak hemorrhagic activity. Degrades preferentially the Aalpha- (FGA) and Bbeta-chains (FGB) of fibrinogen, and partially degrades gamma-chain (FGG) at higher concentration. Induces a mild myotoxicity, but lacks coagulant activity on human plasma or bovin fibrinogen and def... | Bothrops atrox (Barba amarilla) (Fer-de-lance) |
P0DJE2 | VM3A_VIPAA | KSAAXVTLDLFGDWRAKRHDNAQLLTGINLNGQTLGIAFMSKXSVGLIQDYXKSYLLVASVMAHELGHNLGMEHDDGNCICPAKCIDNKPLRTDIVSPAVCGNYFVELTPGSQCADGVCCDQCRKAGVTVAPDLCFDYNQLGTEDKFTHSPDDPDYGMVDLGTKCADGKVCNSNRQCVDVNTAY | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF01421; | 3.40.390.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIc sub-subfamily | PTM: The N-terminus is blocked.; PTM: N-glycosylated. {ECO:0000269|PubMed:21933678}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom zinc metalloprotease that has fibrinogenolytic and hemorrhagic activities in mouse and rats. Hydrolyzes the Aalpha-chain (FGA) and more slowly the Bbeta-chain of fibrinogen (FGB), without affecting the gamma-chain. Its hemorrhagic activity results of its involvement in cleavage of basal membrane c... | Vipera ammodytes ammodytes (Western sand viper) |
P0DJE9 | VSP1_BOTMA | VIGGDECNINESPFLAFLYSQLLSSRRYFCGMTLINQEWVLTAAHCNLYPDRKDMNWWLLIKLGKHSGSTRRWVANYDEQVRYWPKEKFIWWYCPNKKKDVINNYVWVWWDKDILLWELWMLIRLNRPVKYSEHIAPLSLPSSPPSAKWWHVGSVCRIMGWGQITETWWNSEDTLPDVPRCANINLFNYEVCRAYNQRWWRGLPAKTLCAGDLEGIIRGGWDTCVGDSGGPLICDGQYQGIAYWGSKPCAEPDEPAAYSKVFDHLDWSQSVIAGGTWWRGDDTCP | 3.4.21.- | null | envenomation resulting in fibrinogenolysis in another organism [GO:0044485]; envenomation resulting in positive regulation of platelet aggregation in another organism [GO:0044478]; regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638] | extracellular region [GO:0005576]; secretory granule [GO:0030141] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: Homologous thrombin-like enzymes are N-glycosylated. This enzyme does not contain the consensus glycosylation sites, suggesting it is not glycosylated. | SUBCELLULAR LOCATION: Secreted. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 M for N-alpha-benzoyl-DL-arginine-p-nitroanilide {ECO:0000269|PubMed:19931298}; Vmax=0.052 nmol/min/mg enzyme toward N-alpha-benzoyl-DL-arginine-p-nitroanilide {ECO:0000269|PubMed:19931298}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:19931298}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 38-40 degrees Celsius. {ECO:0000269|PubMed:19931298}; | FUNCTION: Thrombin-like enzyme that induces the formation of fibrin clot. Cleaves the Aalpha-chain of fibrinogen (FGA) with higher activity than the Bbeta-chain (FGB). Induces platelet aggregation in both platelet-rich plasma and in washed platelet preparations. This aggregation is strongly inhibited by preincubation o... | Bothrops marajoensis (Marajo lancehead) |
P0DJF0 | VSP48_BOTJR | VVGGDCIPQVPFLAFLYSEYFC | 3.4.21.- | null | proteolysis [GO:0006508] | extracellular region [GO:0005576] | serine-type peptidase activity [GO:0008236]; toxin activity [GO:0090729] | null | null | Peptidase S1 family, Snake venom subfamily | PTM: Glycosylated; required for activity. Highly glycosylated with 42% of N-linked carbohydrates composed of Fuc(1):GalN(4):GlcN(5):Gal(1):Man(2) and a high content of sialic acid residues (8-12%). {ECO:0000269|PubMed:17433397}. | SUBCELLULAR LOCATION: Secreted. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.83 mM for BApNA {ECO:0000269|PubMed:17433397}; KM=0.4 mM for BAME {ECO:0000269|PubMed:17433397}; KM=0.6 mM for TAME {ECO:0000269|PubMed:17433397}; KM=0.3 mM for Nalpha-Tos-Gly-Pro-ME {ECO:0000269|PubMed:17433397}; KM=0.36 mM for Nalpha-Tos-Gly-Pro-Arg-pNA {ECO:00... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:17433397}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:17433397}; | FUNCTION: Thrombin-like serine protease which cleaves specifically the Aalpha chain of human fibrinogen (FGA) to release fibrinopeptide A. Also cleaves rapidly the Bbeta chain of human fibrinogen (FGB). Is selective for Arg over Lys at position 1 of the tripeptide substrates. {ECO:0000269|PubMed:17433397}. | Bothrops jararacussu (Jararacussu) |
P0DJG0 | APOA1_PANTR | MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ | null | null | acylglycerol homeostasis [GO:0055090]; cholesterol efflux [GO:0033344]; cholesterol metabolic process [GO:0008203]; lipoprotein metabolic process [GO:0042157]; phosphatidylcholine metabolic process [GO:0046470]; phospholipid efflux [GO:0033700]; positive regulation of cholesterol efflux [GO:0010875]; positive regulatio... | chylomicron [GO:0042627]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; very-low-density lipoprotein particle [GO:0034361] | cholesterol transfer activity [GO:0120020]; high-density lipoprotein particle receptor binding [GO:0070653]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803] | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility (By similarity). {ECO:0000250}. | Pan troglodytes (Chimpanzee) |
P0DJG1 | APOA1_PONAB | MKAAVLTLAVLFLTGSQARHFWQQDEPPQTPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSMTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELHEKLSPLGEEMRDRARAHVDALRTHLAPYTDELRQRLAARLEALKENGGARLAEYHAKASEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ | null | null | adrenal gland development [GO:0030325]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; endothelial cell proliferation [GO:0001935]; G protein-coupled receptor sig... | endocytic vesicle [GO:0030139]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:000... | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility (By similarity). {ECO:0000250}. | Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
P0DJG2 | APOA2_GORGO | MKLLAATVLLLTICSLEGALVRRQAKEPCVESLVSQYFQTVTDYGKDLMEKVKSPELQAEAKSYFEKSKEQLTPLIKKAGTELVNFLSYFVELGTQPATQ | null | null | cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle remodeling [GO:0034375]; lipoprotein metabolic process [GO:0042157]; low-density lipoprotein particle remodelin... | blood microparticle [GO:0072562]; chylomicron [GO:0042627]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | apolipoprotein receptor binding [GO:0034190]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; lipase inhibitor activity [GO:0055102]; phosphatidylcholine binding [GO:003... | PF04711; | 6.10.250.100; | Apolipoprotein A2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}. | null | null | null | null | null | FUNCTION: May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism. | Gorilla gorilla gorilla (Western lowland gorilla) |
P0DJG3 | VSP1_BOTAN | VIGGDECNINEHPFLVALYYSTFFCGMTLINQEWVLTAAHESEKFPKEKYFIFCPNNKDIMLIRLDKPVSNSEHIAPLSLPSSPPSVGSVCRKPALYTKVFDYLLWIQSIIAGNTATCP | 3.4.21.- | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: Contains both N-linked carbohydrates and sialic acid. {ECO:0000269|PubMed:22155303}. | SUBCELLULAR LOCATION: Secreted. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.79 M for N-alpha-benzoyl-DL-Arg-p-nitroanilide (DL-BApNA) {ECO:0000269|PubMed:22155303}; Vmax=0.54 nmol/min/mg enzyme with N-alpha-benzoyl-DL-Arg-p-nitroanilide (DL-BApNA) as substrate {ECO:0000269|PubMed:22155303}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:22155303}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:22155303}; | FUNCTION: Thrombin-like snake venom serine protease, with high clotting activity in vitro. Has also fibrinogenolytic ability, showing a fast degradation of fibrinogen Aalpha chain (FGA), a slow degradation of Bbeta chain (FGB) and no degradation of gamma chain. Also causes platelet aggregation in platelet rich plasma (... | Bothrocophias andianus (Andean lancehead) (Bothrops andianus) |
P0DJG7 | VSP2_DEIAC | VIGGVECDINEHRFL | 3.4.21.- | null | proteolysis [GO:0006508] | extracellular region [GO:0005576] | serine-type peptidase activity [GO:0008236]; toxin activity [GO:0090729] | null | null | Peptidase S1 family, Snake venom subfamily | PTM: Seems to be only O-glycosylated (is not affected by PNGase F which only removes N-linked glycans, but is affected by TFMS that removes both O- and N-linked glycans). | SUBCELLULAR LOCATION: Secreted. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=403 uM for BAEE (at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:18643779}; KM=68.5 nM for DL-BAPA (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:18643779}; Vmax=1560 nmol/sec/mg enzyme (at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:18643779};... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 (at 25 degrees Celsius). {ECO:0000269|PubMed:18643779}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25-50 degrees Celsius (at pH 7.0). {ECO:0000269|PubMed:18643779}; | FUNCTION: Thrombin-like snake venom serine protease that has high fibrinogen-clotting activity (2025 NIH units/mg) on human fibrinogen. Shows esterase and amidase activities. {ECO:0000269|PubMed:17904430}. | Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus) |
P0DJH3 | VMP3A_DEIAC | DVVSPPVCGN | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]; toxin activity [GO:0090729] | null | null | Venom metalloproteinase (M12B) family, P-III subfamily | PTM: N-glycosylated. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Zinc metalloprotease-disintegrin AAV1: snake venom zinc metalloprotease that binds to the platelet collagen receptor glycoprotein VI (GP6) thus inhibiting collagen- and convulxin- (a GP6 agonist) induced platelet aggregation and the tyrosine phosphorylation of intracellular signaling proteins (LAT, SYK, p76SL... | Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus) |
P0DJH5 | VM3DM_DABSI | VATSEPNRYFNPYSYVELIITVDHS | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]; toxin activity [GO:0090729] | null | null | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily | PTM: N-glycosylated.; PTM: Contains 16 disulfide bonds. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7 uM for NFF-2 (fluorogenic substrates with cleavage at Ala-Nva); | null | null | null | FUNCTION: Snake venom zinc metalloprotease that possesses high hemorrhagic activity (minimum hemorrhagic dose, MHD=0.86 ug) when subcutaneously injected into mice. Has potent fibrinogenolytic activity on alpha-chain of fibrinogen (FGA). Hydrolyzes model substrate (beta-chain of insulin) at Ala(14)-Leu(15) and Tyr(16)-L... | Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis) |
P0DJH6 | CENPW_CHICK | MRRTVPRGTLRKIIKKHKPHLRLAANTDLLVHLSFLLFLHRLAEEARTNAFENKSKIIKPEHTIAAAKVILKKSRG | null | null | cell division [GO:0051301]; chromosome segregation [GO:0007059]; kinetochore assembly [GO:0051382]; mitotic cell cycle [GO:0000278] | kinetochore [GO:0000776]; nucleoplasm [GO:0005654] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982] | PF15510; | 1.10.20.10; | CENP-W/WIP1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19070575}. Chromosome, centromere {ECO:0000269|PubMed:19070575}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19070575}. Note=Constitutively localizes to centromeres throughout the cell cycle, and to kinetochores during mitosis (PubMed:19070575). Localizes to... | null | null | null | null | null | FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation (By similarity). The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of ... | Gallus gallus (Chicken) |
P0DJI6 | FCOR_MOUSE | MGGPTRRHQEEGSAECLGGPSTRAAPGPGLRDFHFTTAGPSKADRLGDAAQIHRERMRPVQCGDGSGERVFLQSPGSIGTLYIRLDLNSQRSTCCCLLNAGTKGMC | 2.3.1.- | null | cellular response to cold [GO:0070417]; cellular response to starvation [GO:0009267]; energy homeostasis [GO:0097009]; fat cell differentiation [GO:0045444]; intracellular glucose homeostasis [GO:0001678]; negative regulation of DNA-templated transcription [GO:0045892]; protein acetylation [GO:0006473]; temperature hom... | cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | acetyltransferase activity [GO:0016407]; chromatin binding [GO:0003682] | null | null | null | PTM: Phosphorylated at Thr-93 by PKA, leading to import into the nucleus. {ECO:0000269|PubMed:22510882}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22510882}. Nucleus {ECO:0000269|PubMed:22510882}. Note=Imported into the nucleus following phosphorylation at Thr-93 upon treatment of cells with forskolin. Probably shuttles between the nucleus and the cytoplasm. | null | null | null | null | null | FUNCTION: Regulator of adipocytes that acts by repressing FOXO1 transcriptional activity. Acts by promoting acetylation of FOXO1, both by preventing the interaction between FOXO1 and SIRT1 deacetylase, and by mediating acetyltransferase activity in vitro. Regulates insulin sensitivity and energy metabolism. {ECO:000026... | Mus musculus (Mouse) |
P0DJI8 | SAA1_HUMAN | MKLLTGLVFCSLVLGVSSRSFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGAWAAEVITDARENIQRFFGHGAEDSLADQAANEWGRSGKDPNHFRPAGLPEKY | null | null | acute-phase response [GO:0006953]; lymphocyte chemotaxis [GO:0048247]; macrophage chemotaxis [GO:0048246]; negative regulation of inflammatory response [GO:0050728]; neutrophil chemotaxis [GO:0030593]; platelet activation [GO:0030168]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cytokine p... | cytoplasmic microtubule [GO:0005881]; endocytic vesicle lumen [GO:0071682]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; high-density lipoprotein particle [GO:0034364] | G protein-coupled receptor binding [GO:0001664]; heparin binding [GO:0008201] | PF00277; | 1.10.132.110; | SAA family | PTM: This protein is the precursor of amyloid protein A, which is formed by the removal of approximately 24 residues from the C-terminal end. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7115671}. | null | null | null | null | null | FUNCTION: Major acute phase protein. | Homo sapiens (Human) |
P0DJI9 | SAA2_HUMAN | MKLLTGLVFCSLVLSVSSRSFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGAWAAEVISNARENIQRLTGRGAEDSLADQAANKWGRSGRDPNHFRPAGLPEKY | null | null | acute-phase response [GO:0006953] | extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364] | null | PF00277; | 1.10.132.110; | SAA family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DJI8}. | null | null | null | null | null | FUNCTION: Major acute phase reactant. {ECO:0000250|UniProtKB:P05366}. | Homo sapiens (Human) |
P0DJJ0 | SRG2C_HUMAN | MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAEHFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKWESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPCSPDSTANVRIEEKHVRRSSVKKIEKMKEKHQAKYTENKLKAIKAQNEYLLALEATNASVFKYYIHDLSDLIDQCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENL... | null | null | cerebral cortex development [GO:0021987]; excitatory synapse assembly [GO:1904861]; extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration [GO:0021816]; inhibitory synapse assembly [GO:1904862]; negative regulation of cell migration [GO:0030336]; negative regulation of ... | cytoplasm [GO:0005737] | protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF00611; | 1.20.1270.60; | null | null | null | null | null | null | null | null | FUNCTION: Human-specific protein that acts as a key modifier of cortical connectivity in the human brain (PubMed:22559944, PubMed:27373832, PubMed:34707291). Acts by inhibiting the functions of ancestral paralog SRGAP2/SRGAP2A, a postsynaptic protein that regulates excitatory and inhibitory synapse maturation and densi... | Homo sapiens (Human) |
P0DJJ3 | SGIP1_RAT | MMEGLKKRTRKAFGIRKKEKDTDSTGSPDRDGMQPSPHEPPYHSKAECAREGGKKASKKSNGAPNGFYAEIDWERYNSPELDEEGYSIRPEEPGSTKGKHFYSSSESEEEEESHKKFNIKIKPLQSKDVLKNAATVDELKASIGNIALSPSPVRKSPRRSPGAIKRNLSSEEVARPRRSTPTPELTSKKPLDDTLALAPLFGPPLESAFDEQKTEVLLDQPEIWGSGQPINPSMESPKLARPFPTGTPPPLPPKAVPATPPRTGSPLTVATGNDQAATEAKIEKLPSISDLDSIFGPVLSPKSVAVNTEEKWVHFSDASP... | null | null | actin filament polymerization [GO:0030041]; clathrin-dependent endocytosis [GO:0072583]; energy homeostasis [GO:0097009]; positive regulation of eating behavior [GO:1904000]; positive regulation of feeding behavior [GO:2000253]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of r... | actin filament [GO:0005884]; AP-2 adaptor complex [GO:0030122]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; terminal bouton [GO:0043195] | actin filament binding [GO:0051015]; microtubule binding [GO:0008017]; phospholipid binding [GO:0005543]; SH3 domain binding [GO:0017124]; tubulin binding [GO:0015631] | PF10291; | 2.60.40.1170; | null | null | SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q9BQI5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9BQI5}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9BQI5}. | null | null | null | null | null | FUNCTION: May function in clathrin-mediated endocytosis. Has both a membrane binding/tubulating activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a preference for membranes enriched in phosphatidylserine and phosphoinositides and is required for the endocyto... | Rattus norvegicus (Rat) |
P0DJJ6 | VM1B_BOTLC | TLTSFGEWR | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | envenomation resulting in fibrinogenolysis in another organism [GO:0044485]; envenomation resulting in fibrinolysis in another organism [GO:0044484]; envenomation resulting in induction of edema in another organism [GO:0044398]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; host extracellular space [GO:0043655] | metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]; toxin activity [GO:0090729] | null | null | Venom metalloproteinase (M12B) family, P-I subfamily | PTM: Contains 7 disulfide bonds. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom zinc metalloprotease that has fibrino(geno)lytic activities. Hydrolyzes the alpha-chain (FGA) and more slowly the beta-chain of fibrinogen (FGB), without affecting the gamma-chain. Preferentially hydrolyzes the beta-chain (FGB) of fibrin. In vivo, shows a low edema-inducing effect. This action may... | Bothrops leucurus (Whitetail lancehead) |
P0DJJ8 | PA2B1_PROFL | MRTLWIMAVLLLGVDGSLVQLWKMIFQETGKEAAKNYGLYGCNCGVGRRGKPKDATDSCCYVHKCCYKKVTGCDPKMDSYSYSWKNKAIVCGEKNPPCLKQVCECDKAVAICLRENLGTYNKKYTIYPKPFCKKADTC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:2330604}; Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:2330604}; | 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 II subfamily, K49 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:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that has strong myotoxic activity with a low phospholipase A2 activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:2330604}. | Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis) |
P0DJJ9 | PA2B2_PROFL | MRTLWIMAVLLVGVDGSLVQLWKMIFQETGKEAAKNYGLYGCNCGVGRRGKPKDATDSCCYVHKCCYKKVTGCNPKMDSYSYSWKNKAIVCGEKNPPCLKQVCECDKAVAICLRENLGTYNKKYTIYPKPFCKKADTC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:2341374}; Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:2341374}; | 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, K49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2341374}. | 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:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that shows anticoagulant activities, strong myolytic activity, infiltration of polymorphonuclear cells, and edema in stromal tissues. Induces cell death of Jurkat cells in a concentration-dependent manner. Shows a low phospholipase A2 activity. PLA2 catalyzes the calcium-de... | Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis) |
P0DJL7 | DTXR_CORDI | MKDLVDTTEMYLRTIYELEEEGVTPLRARIAERLEQSGPTVSQTVARMERDGLVVVASDRSLQMTPTGRTLATAVMRKHRLAERLLTDIIGLDINKVHDEACRWEHVMSDEVERRLVKVLKDVSRSPFGNPIPGLDELGVGNSDAAVPGTRVIDAATSMPRKVRIVQINEIFQVETDQFTQLLDADIRVGSEVEIVDRDGHITLSHNGKDVELIDDLAHTIRIEEL | null | null | negative regulation of DNA-templated transcription [GO:0045892] | cytoplasm [GO:0005737] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; protein dimerization activity [GO:0046983]; SH3 domain binding [GO:0017124]; transition metal ion binding [GO:0046914] | PF18357;PF02742;PF01325; | 2.30.30.90;1.10.60.10;1.10.10.10; | DtxR/MntR family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Iron-binding repressor of the dipheteria toxin gene expression. May serve as a global regulator of gene expression. Represses ripA under iron excess. | Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) |
P0DJM0 | INLA_LISMO | MRKKRYVWLKSILVAILVFGSGVWINTSNGTNAQAATITQDTPINQIFTDTALAEKMKTVLGKTNVTDTVSQTDLDQVTTLQADRLGIKSIDGVEYLNNLTQINFSNNQLTDITPLKNLTKLVDILMNNNQIADITPLANLTNLTGLTLFNNQITDIDPLKNLTNLNRLELSSNTISDISALSGLTSLQQLSFGNQVTDLKPLANLTTLERLDISSNKVSDISVLAKLTNLESLIATNNQISDITPLGILTNLDELSLNGNQLKDIGTLASLTNLTDLDLANNQISNLAPLSGLTKLTELKLGANQISNISPLAGLTALT... | null | null | null | extracellular region [GO:0005576]; peptidoglycan-based cell wall [GO:0009274] | null | PF09479;PF00746;PF12354;PF12799;PF08191; | 2.60.40.1220;2.60.40.4270;3.80.10.10; | Internalin family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:10736172, ECO:0000269|PubMed:11929538, ECO:0000269|PubMed:20176794, ECO:0000269|PubMed:21725001, ECO:0000269|PubMed:22837151}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:10736172, ECO:... | null | null | null | null | null | FUNCTION: Mediates the entry of L.monocytogenes into host intestinal epithelial cells; transformation with inlA alone allows L.innocua (a non-invasive species) to be taken up by host cells (PubMed:10406800, PubMed:1905979, PubMed:8601315). Binds to human receptor cadherin-1 (E-cadherin, CDH1); the chicken homolog of ca... | Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) |
P0DJQ5 | GNAT2_STRCL | MSDSTPKTPRGFVVHTAPVGLADDGRDDFTVLASTAPATVSAVFTRSRFAGPSVVLCREAVADGQARGVVVLARNANVATGLEGEENAREVREAVARALGLPEGEMLIASTGVIGRQYPMESIREHLKTLEWPAGEGGFDRAARAIMTTDTRPKEVRVSVGGATLVGIAKGVGMLEPDMATLLTFFATDARLDPAEQDRLFRRVMDRTFNAVSIDTDTSTSDTAVLFANGLAGEVDAGEFEEALHTAALALVKDIASDGEGAAKLIEVQVTGARDDAQAKRVGKTVVNSPLVKTAVHGCDPNWGRVAMAIGKCSDDTDID... | 2.3.1.35 | null | arginine biosynthetic process [GO:0006526]; clavulanic acid biosynthetic process [GO:0033050]; ornithine biosynthetic process [GO:0006592] | cytoplasm [GO:0005737] | acetyl-CoA:L-glutamate N-acetyltransferase activity [GO:0004042]; glutamate N-acetyltransferase activity [GO:0004358] | PF01960; | 3.10.20.340;3.60.70.12; | ArgJ family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate; Xref=Rhea:RHEA:15349, ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:46911, ChEBI:CHEBI:57805; EC=2.3.1.35; Evidence={ECO:0000269|PubMed:11985581}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.6 mM for L-N-acetylornithine (at 37 degrees Celsius and pH 8.0) {ECO:0000269|PubMed:11985581}; Vmax=87 nmol/min/mg enzyme {ECO:0000269|PubMed:11985581}; | PATHWAY: Antibiotic biosynthesis; clavulanate biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 7.5-8. {ECO:0000269|PubMed:11985581}; | null | FUNCTION: Catalyzes the biosynthesis of ornithine by transacetylation between N(2)-acetylornithine and glutamate. It can also use L-arginine, L-glutamine and L-lysine as acetyl acceptors. {ECO:0000269|PubMed:11985581}. | Streptomyces clavuligerus |
P0DJY0 | 1ATF_PRRSS | MSGTFSRCMCTPAARVFWNAGQVFCTRCLSARPLLSPELQDTDLGVVGLFYKPKDKIHWKVPIGIPQVECTPSGCCWLSAVFPLARMTSGNHNFLQRLVKVADVLYRDGCLAPRHLRELQVYERGCSWYPITGPVPGMGLFANSMHVSDQPFPGATHVLTNSPLPQRACRQPFCPFEEAHSDVYRWKKFVIFTDSSPNGRFRMMWTPESDDSAALEVLPPELERQVEILTRSFPAHHPINLADWELTESPENGFSFGTSHSCGHIVQNPNVFDGKCWLTCFLGQSAEVCYHEEHLANALGYQTKWGVHGKYLQRRLQVRG... | 3.4.22.- | null | proteolysis [GO:0006508]; viral protein processing [GO:0019082] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; membrane [GO:0016020] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; helicase activity [GO:0004386]; metal ion binding [GO:0046872] | PF14757;PF14758;PF05410;PF05411;PF05412; | 3.90.70.160;4.10.80.390;2.30.31.30;3.90.70.70;3.90.70.60; | null | null | SUBCELLULAR LOCATION: [Nsp1]: Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Nsp1-alpha papain-like cysteine proteinase]: Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Nsp1-beta papain-like cysteine proteinase]: Host cytoplasm {ECO:0000250}.; SUBCEL... | null | null | null | null | null | FUNCTION: [Nsp1]: Is essential for viral subgenomic mRNA synthesis. {ECO:0000250}.; FUNCTION: [Nsp1-alpha papain-like cysteine proteinase]: Inhibits IFN-beta production. Counteracts the action of NF-kappaB by decreasing the phosphorylation of IkappaB-alpha, such that the degradation of IkappaB-alpha is suppressed. This... | Porcine reproductive and respiratory syndrome virus (isolate Pig/United States/SD 01-08/2001) (PRRSV) |
P0DJZ6 | POLSF_SFV | MNYIPTQTFYGRRWRPRPAARPWPLQATPVAPVVPDFQAQQMQQLISAVNALTMRQNAIAPARPPKPKKKKTTKPKPKTQPKKINGKTQQQKKKDKQADKKKKKPGKRERMCMKIENDCIFEVKHEGKVTGYACLVGDKVMKPAHVKGVIDNADLAKLAFKKSSKYDLECAQIPVHMRSDASKYTHEKPEGHYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGSRTALSVVTWNKDMVTRVTPEGSEEWSAPLITAMCVLANATFPCFQPPCVPCCYENNAEATLRMLEDNVDRPGYYDLLQ... | 3.4.21.90 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; proteolysis [GO:0006508]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; virion attachment to host cell [GO:0019062] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198] | PF01589;PF00943;PF01563;PF00944; | 1.10.287.2230;2.60.40.3200;2.60.40.4310;2.60.40.2400;2.40.10.10; | null | PTM: [Isoform Frameshifted structural polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2 (By similarity). The remaining polyprotein is then targeted to the host en... | SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000250|UniProtKB:P03316}. Host cytoplasm {ECO:0000250|UniProtKB:Q8JUX5}. Host cell membrane {ECO:0000250|UniProtKB:P03316}. Host nucleus {ECO:0000250|UniProtKB:Q8JUX5}. Note=Shuttles between the cytoplasm and the nucleus. {ECO:0000250|UniProtKB:Q8JUX5}.; SUBCELLULAR ... | CATALYTIC ACTIVITY: Reaction=Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000250|UniProtKB:P03315}; | null | null | null | null | FUNCTION: [Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (By similarity). The capsid protein binds to the viral RNA genome at a site adjacent to a ri... | Semliki forest virus (SFV) |
P0DJZ9 | RPOTF_PRRSL | MSGTFSRCMCTPAARVFWNAGQVFCTRCLSARSLLSPELQDTDLGAVGLFYKPRDKLHWKVPIGIPQVECTPSGCCWLSAVFPLARMTSGNHNFLQRLVKVADVLYRDGCLAPRHLRELQVYERGCNWYPITGPVPGMGLFANSMHVSDQPFPGATHVLTNSPLPQQACRQPFCPFEEAHSSVYRWKKFVVFTDSSLNGRSRMMWTPESDDSAALEVLPPELERQVEILIRSFPAHHPVDLADWELTESPENGFSFNTSHSCGHLVQNPDVFDGKCWLSCFLGQSVEVRCHEEHLADAFGYQTKWGVHGKYLQRRLQVRG... | 3.4.22.- | null | proteolysis [GO:0006508]; viral protein processing [GO:0019082] | host cell cytoplasm [GO:0030430]; host cell membrane [GO:0033644]; host cell nucleus [GO:0042025]; membrane [GO:0016020] | cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872] | PF14757;PF14758;PF05410;PF05411;PF05412; | 3.90.70.160;4.10.80.390;2.30.31.30;3.90.70.70;3.90.70.60; | null | null | SUBCELLULAR LOCATION: [Nsp1]: Host nucleus {ECO:0000269|PubMed:23287061}. Host cytoplasm {ECO:0000269|PubMed:23287061}.; SUBCELLULAR LOCATION: [Nsp1-alpha papain-like cysteine proteinase]: Host nucleus {ECO:0000269|PubMed:23287061}. Host cytoplasm {ECO:0000269|PubMed:23287061}.; SUBCELLULAR LOCATION: [Nsp1-beta papain-... | null | null | null | null | null | FUNCTION: [Nsp1-alpha papain-like cysteine proteinase]: Inhibits host IFN-beta production. Plays a role in the degradation of the host transcriptional activator CREBBP protein. The degradation of host CREBBP which is a key component of the IFN enhanceosome is likely responsible for the inhibition of interferon mediated... | Porcine reproductive and respiratory syndrome virus (strain Lelystad) (PRRSV) |
P0DKC5 | HSD1A_ARATH | MELINDFLNLTAPFFTFFGLCFFLPPFYFFKFLQSIFSTIFSENLYGKVVLITGASSGIGEQLAYEYACRGACLALTARRKNRLEEVAEIARELGSPNVVTVHADVSKPDDCRRIVDDTITHFGRLDHLVNNAGMTQISMFENIEDITRTKAVLDTNFWGSVYTTRAALPYLRQSNGKIVAMSSSAAWLTAPRMSFYNASKAALLSFFETMRIELGGDVHITIVTPGYIESELTQGKYFSGEGELIVNQDMRDVQVGPFPVASASGCAKSIVNGVCRKQRYVTEPSWFKVTYLWKVLCPELIEWGCRLLYMTGTGMSEDT... | 1.1.1.-; 1.1.1.146 | null | steroid biosynthetic process [GO:0006694]; steroid metabolic process [GO:0008202] | cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020] | 11-beta-hydroxysteroid dehydrogenase (NADP+) activity [GO:0070524]; 17-beta-hydroxysteroid dehydrogenase (NADP+) activity [GO:0072582]; cortisol dehydrogenase activity [GO:0102196]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Lipid droplet. Membrane; Single-pass type II membrane protein. | CATALYTIC ACTIVITY: Reaction=an 11beta-hydroxysteroid + NADP(+) = an 11-oxosteroid + H(+) + NADPH; Xref=Rhea:RHEA:11388, ChEBI:CHEBI:15378, ChEBI:CHEBI:35346, ChEBI:CHEBI:47787, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.146; Evidence={ECO:0000269|PubMed:17074428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RH... | null | null | null | null | FUNCTION: Catalyzes 11-beta, 17-beta-hydroxysteroid and reduces 17-beta-ketosteroids. Involved in regulating plant growth and development, probably promoting or mediating brassinosteroid effects. Plays a role during seed maturation. {ECO:0000269|PubMed:17074428, ECO:0000269|PubMed:17616511, ECO:0000269|PubMed:19542545}... | Arabidopsis thaliana (Mouse-ear cress) |
P0DKC6 | HSD1B_ARATH | MELINDFLNLTAPFFTFFGLCFFLPPFYFFKFLQSIFSTIFSENLYGKVVLITGASSGIGEQLAYEYACRGACLALTARRKNRLEEVAEIARELGSPNVVTVHADVSKPDDCRRIVDDTITHFGRLDHLVNNAGMTQISMFENIEDITRTKAVLDTNFWGSVYTTRAALPYLRQSNGKIVAMSSSAAWLTAPRMSFYNASKAALLSFFETMRIELGGDVHITIVTPGYIESELTQGKYFSGEGELIVNQDMRDVQVGPFPVASASGCAKSIVNGVCRKQRYVTEPSWFKVTYLWKVLCPELIEWGCRLLYMTGTGMSEDT... | 1.1.1.-; 1.1.1.146 | null | steroid biosynthetic process [GO:0006694] | cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020] | 11-beta-hydroxysteroid dehydrogenase (NADP+) activity [GO:0070524]; 17-beta-hydroxysteroid dehydrogenase (NADP+) activity [GO:0072582]; cortisol dehydrogenase activity [GO:0102196] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Lipid droplet. Membrane; Single-pass type II membrane protein. | CATALYTIC ACTIVITY: Reaction=an 11beta-hydroxysteroid + NADP(+) = an 11-oxosteroid + H(+) + NADPH; Xref=Rhea:RHEA:11388, ChEBI:CHEBI:15378, ChEBI:CHEBI:35346, ChEBI:CHEBI:47787, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.146; Evidence={ECO:0000269|PubMed:17074428}; | null | null | null | null | FUNCTION: Catalyzes 11-beta, 17-beta-hydroxysteroid and reduces 17-beta-ketosteroids. Involved in regulating plant growth and development, probably promoting or mediating brassinosteroid effects. Plays a role during seed maturation. {ECO:0000269|PubMed:17074428, ECO:0000269|PubMed:17616511, ECO:0000269|PubMed:19542545}... | Arabidopsis thaliana (Mouse-ear cress) |
P0DKH5 | WRK52_ARATH | MTNCEKDEEFVCISCVEEVRYSFVSHLSEALRRKGINNVVVDVDIDDLLFKESQAKIEKAGVSVMVLPGNCDPSEVWLDKFAKVLECQRNNKDQAVVSVLYGDSLLRDQWLSELDFRGLSRIHQSRKECSDSILVEEIVRDVYETHFYVGRIGIYSKLLEIENMVNKQPIGIRCVGIWGMPGIGKTTLAKAVFDQMSSAFDASCFIEDYDKSIHEKGLYCLLEEQLLPGNDATIMKLSSLRDRLNSKRVLVVLDDVRNALVGESFLEGFDWLGPGSLIIITSRDKQVFCLCGINQIYEVQGLNEKEARQLFLLSASIKED... | null | null | defense response [GO:0006952]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; sequence-specific DNA binding [GO:0043565] | PF07725;PF00931;PF03106; | 1.10.8.430;3.40.50.300;3.80.10.10;3.40.50.10140;2.20.25.80; | Disease resistance TIR-NB-LRR family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12788974}. Cytoplasm {ECO:0000305|PubMed:12788974}. Note=The nuclear localization is only detected upon interaction with PopP2. {ECO:0000269|PubMed:12788974}. | null | null | null | null | null | FUNCTION: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Acts also as a disease resistance protein involved in resistance to fungal and bacterial pathogens, including R.solanacearum, P.syringae pv. tomato and C.higginsianum... | Arabidopsis thaliana (Mouse-ear cress) |
P0DKI7 | STORR_PAPSO | MELQYISYFQPTSSVVALLLALVSILSSVVVLRKTFLNNYSSSPASSTKTAVLSHQRQQSCALPISGLLHIFMNKNGLIHVTLGNMADKYGPIFSFPTGSHRTLVVSSWEMVKECFTGNNDTAFSNRPIPLAFKTIFYACGGIDSYGLSSVPYGKYWRELRKVCVHNLLSNQQLLKFRHLIISQVDTSFNKLYELCKNSEDNHGNYTTTTTTAAGMVRIDDWLAELSFNVIGRIVCGFQSGPKTGAPSRVEQFKEAINEASYFMSTSPVSDNVPMLGWIDQLTGLTRNMKHCGKKLDLVVESIINDHRQKRRFSRTKGGD... | 1.14.19.54; 1.5.1.27 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | morphine biosynthetic process [GO:0097295] | membrane [GO:0016020] | 1,2-dehydroreticulinium reductase (NADPH) activity [GO:0047128]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water [G... | PF00248;PF00067; | 1.10.630.10;3.20.20.100; | Cytochrome P450 family; Aldo/keto reductase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(R)-reticuline + NADP(+) = 1,2-dehydroreticuline + H(+) + NADPH; Xref=Rhea:RHEA:17569, ChEBI:CHEBI:15378, ChEBI:CHEBI:18363, ChEBI:CHEBI:57783, ChEBI:CHEBI:58144, ChEBI:CHEBI:58349; EC=1.5.1.27; Evidence={ECO:0000269|PubMed:26113639}; CATALYTIC ACTIVITY: Reaction=(S)-reticuline + O2 + reduc... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for (S)-reticuline {ECO:0000269|PubMed:26113639}; KM=14 uM for 1,2-dehydroreticuline {ECO:0000269|PubMed:26113639}; | PATHWAY: Alkaloid biosynthesis; morphine biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Bifunctional protein involved in the biosynthesis of morphinan-type benzylisoquinoline alkaloids. Required for the isomerization of (S)- to (R)-reticuline. The cytochrome P450 module is responsible for the conversion of (S)-reticuline to 1,2-dehydroreticuline while the oxidoreductase module converts 1,2-dehyd... | Papaver somniferum (Opium poppy) |
P0DKL2 | OP10_MAIZE | MSLHAARGGPHEDLSWSAIGRRAPRDVVTFGDREGGGGMRSAQQGPGAVRVDEASSASTFRELDEAFLQTQTKIWLGEVLHLRFGEDALVADLLADGELLFQVSKVLWKMLLKNNREQLKQSKVYIYERLSFGRSSGKYMPYSKVDSFLKICQILGLAGIDLFTPSDVVEKRNVRKVCICIRSVSKKSLILHLNVPDFDVVTYTISMPNYVVGGIRRNLEQTQYSSSSSSGYSPCARSKVLQQQIIFGGQNDQHEDTHYDSDEAESKLSLLEPEDSVNEDNFAAVLSQFNDAHNKGSEGYGESGCGKHGEKSLAESVGSL... | null | null | actin crosslink formation [GO:0051764]; microtubule bundle formation [GO:0001578]; protein localization to microtubule plus-end [GO:1904825]; regulation of microtubule polymerization or depolymerization [GO:0031110] | actin filament [GO:0005884]; endoplasmic reticulum membrane [GO:0005789]; microtubule plus-end [GO:0035371]; stress fiber [GO:0001725] | actin filament binding [GO:0051015]; cytoskeletal anchor activity [GO:0008093]; microtubule binding [GO:0008017] | null | 1.10.418.10; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27541862}; Single-pass membrane protein {ECO:0000255}. Note=In endosperm, predominantly deposited into protein bodies, at the interface between the alpha-zein-rich region and the gamma-zein-rich region. {ECO:0000269|PubMed:27541862}. | null | null | null | null | null | FUNCTION: Cereal endosperm protein required for the ring-shaped distribution of 22 kDa alpha- and 16 kDa gamma-zeins in protein bodies. {ECO:0000269|PubMed:27541862}. | Zea mays (Maize) |
P0DKL3 | MALS_MAAAM | MATSNSKPTQVLLATFLTFFFLLLNNVNSSDELSFTINNFVPNEADLLFQGEASVSSTGVLQLTRVENGQPQKYSVGRALYAAPVRIWDNTTGSVASFSTSFTFVVKAPNPDITSDGLAFYLAPPDSQIPSGSVSKYLGLFNNSNSDSSNQIVAVELDTYFAHSYDPWDPNYRHIGIDVNGIESIKTVQWDWINGGVAFATITYLAPNKTLIASLVYPSNQTTFSVAASVDLKEILPEWVRVGFSAATGYPTEVETHDVLSWSFTSTLEANCDAATENNVHIARYTA | null | null | null | null | carbohydrate binding [GO:0030246]; metal ion binding [GO:0046872] | PF00139; | 2.60.120.200; | Leguminous lectin family | PTM: The glycosylation on N-90 is determined to by of the high mannose type in PubMed:26003537, while PubMed:27720757 found a paucimannose at this position. {ECO:0000269|PubMed:26003537, ECO:0000269|PubMed:27720757}.; PTM: Processed at its C-terminus. {ECO:0000269|PubMed:27720757}. | null | null | null | null | null | null | FUNCTION: Sialic acid-binding lectin recognizing oligosaccharides containing terminal sialic acid linked via alpha-2,3 bond to penultimate galactose residues (PubMed:3350806). Binds the trisaccharide sequence Neu5Ac-alpha-2,3-Gal-beta-1,4-GlcNAc (PubMed:1985926). Binds fetuin when fully glycosylated but not when the hi... | Maackia amurensis (Amur maackia) |
P0DKR6 | 3SX1_DENPO | MKTLLLTLLVVTIVCLDLGYSLKCYQHGKVVTCHRDMKFCYHNTGMPFRNLKLILQGCSSSCSETENNKCCSTDRCNK | null | null | null | extracellular region [GO:0005576] | ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | null | 2.10.60.10; | Snake three-finger toxin family, Short-chain subfamily, Mambalgin sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23034652}. | null | null | null | null | null | FUNCTION: This three-finger toxin inhibits ASIC channels. It acts as a gating modifier toxin by decreasing the apparent proton sensitivity of activation and by slightly increasing the apparent proton sensitivity for inactivation (PubMed:23034652). It binds more tightly to the closed state and to a much lesser extent th... | Dendroaspis polylepis polylepis (Black mamba) |
P0DKU1 | PA2H_GLOUS | SLLQFRKMIKKMTGKEPVVSYAFYGCYCGSGGRGKPKDATDRCCFVHQCCYEKVTGCDPKWDDYTYSWKDGDIVCGGDDPCKKEVCECDRAAAICFRDNLKTYKKIYMAYPDIFCSSKSEKC | 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]; potassium channel regulator activity [GO:0015459]; signaling receptor binding [GO:0005102]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, Q49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) homolog that shows local myotoxicity, apparent anticoagulant activity (PubMed:15618013), and neurotoxicity (PubMed:17299814). Shows analgesic effect on mice due to a decrease of action potentials and nerve conduction velocity. These effects are caused by inhibition of volta... | Gloydius ussuriensis (Ussuri mamushi) (Gloydius blomhoffii ussuriensis) |
P0DKU2 | PA2_PANIM | MVDLARRCSGSTEGRFLMWECTKWCGPGNNAKCESDLGPLEADKCCRTHDHCDYIASGETKYGITNYAFFTKLNCKCEEAFDRCLTEAYNKEEKESAKSSTKRLQNFYFGTYSPECYVVTCNSKRSGRDAGCENGVATWKKSYKD | 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-dependent phospholipase A2 activity [GO:0047498]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | PF05826; | 1.20.90.10; | Phospholipase A2 family, Group III 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:0... | null | null | null | null | FUNCTION: Scorpion venom phospholipase A2 (PLA2) that contains enzymatic activity, but does not inhibit ryanodine receptors in contrary to imperatoxin-1, another heterodimer of P.imperator venom. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | Pandinus imperator (Emperor scorpion) |
P0DKU9 | APOE_COLGU | MKVLWAALLVTFLAGCQAKVEQPVESEPEPELRQQTEWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTTLMDETMKELKAYKSDLEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRGEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLAGQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPSDNH | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Colobus guereza (Mantled guereza) (Eastern black-and-white colobus monkey) |
P0DKW5 | APOE_AOTNA | MKVLWAALLIALLAGCQGKMEQVVEPELEPEPELHQQADWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTALMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLAQYRSEVQAMLGQSTDELRARLTSHLRKLRTVSYTHLDVYKRQSLASQPLQERAQAWGERLRTRMEEVGSRTRDRLDEVKEQVEEVRAKLEEQAQQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASAAPVPSDNH | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Aotus nancymaae (Ma's night monkey) |
P0DKW6 | APOE_ATEGE | MKVLWAALLVAFLAGCQGKMEPELEREPELEREPELHQQADWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTALMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLAXYRSEVQAMLGQSXDELRARLASHLRKLRKRLLRDVDDLQKRLAVYQAGAREGAERGVSAIRERLVPLVEQGRARAATVGSSLAGQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVEEVRAKLEEQAQQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASAAPVPGD... | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Ateles geoffroyi (Black-handed spider monkey) (Geoffroy's spider monkey) |
P0DKW7 | APOE_PLEMO | MKVLWAALLVAFLAGCQGKVEQVVEPELEPEPELHQQADWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTALMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLAQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDVDDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRARAATVGSSLAGQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVEEVRAKLEEQAQQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASAAPVPSDNH | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Plecturocebus moloch (Dusky titi monkey) (Callicebus moloch) |
P0DKW8 | APOE_SAIBB | MKVLWAAFLVAFLAGCQGKVEQVVEPELGPEPELHPQADWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTALMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLAQYRSEVQAMLGQSTDELRARLASHLRKLRKRLLRDVDDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRARAATVGSSLASQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVEEVRAKLEEQAQQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASATPVPSDNH | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Saimiri boliviensis boliviensis (Bolivian squirrel monkey) |
P0DKX7 | CYAA_BORPE | MQQSHQAGYANAADRESGIPAAVLDGIKAVAKEKNATLMFRLVNPHSTSLIAEGVATKGLGVHAKSSDWGLQAGYIPVNPNLSKLFGRAPEVIARADNDVNSSLAHGHTAVDLTLSKERLDYLRQAGLVTGMADGVVASNHAGYEQFEFRVKETSDGRYAVQYRRKGGDDFEAVKVIGNAAGIPLTADIDMFAIMPHLSNFRDSARSSVTSGDSVTDYLARTRRAASEATGGLDRERIDLLWKIARAGARSAVGTEARRQFRYDGDMNIGVITDFELEVRNALNRRAHAVGAQDVVQHGTEQNNPFPEADEKIFVVSATG... | 4.6.1.1 | null | cAMP biosynthetic process [GO:0006171]; hemolysis in another organism [GO:0044179]; positive regulation of cytosolic calcium ion concentration [GO:0007204] | extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium- and calmodulin-responsive adenylate cyclase activity [GO:0008294]; calmodulin binding [GO:0005516]; channel activity [GO:0015267]; toxin activity [GO:0090729] | PF03497;PF06594;PF00353;PF02382; | 1.10.150.920;3.30.70.1720;3.90.1760.10;2.150.10.10; | Adenylyl cyclase class-2 family; RTX prokaryotic toxin family | PTM: Released in a processed form. {ECO:0000269|PubMed:2542030}.; PTM: [Hemolysin]: Palmitoylated at Lys-860 and Lys-983 by CyaC (PubMed:10196151, PubMed:11031260, PubMed:29625104, PubMed:32461253, PubMed:33011179, PubMed:7939682). The toxin only becomes active when modified in position Lys-983: palmitoylation is requi... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2542030}.; SUBCELLULAR LOCATION: [Hemolysin]: Host cell membrane {ECO:0000305|PubMed:8077197}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: [Calmodulin-sensitive adenylate cyclase]: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000269|PubMed:2050107, ECO:0000269|PubMed:2542030}; | null | null | null | null | FUNCTION: Bifunctional adenylate cyclase toxin-hemolysin that plays a crucial role in host colonization (PubMed:2050107, PubMed:2542030). It causes whooping cough by acting on mammalian cells by elevating cAMP-concentration and thus disrupts normal cell function (PubMed:2050107, PubMed:2542030). {ECO:0000269|PubMed:205... | Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) |
P0DKY2 | APOE_PAPHA | MKVLWAALLVTFLAGCQAKVEQPVEPETEPELRQQAEWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSPQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLASQPLQERAQALGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPSDNH | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Papio hamadryas (Hamadryas baboon) |
P0DKY4 | CEEP_RUMAL | MMISEIRQELTDHIIPFWNKLRDDENGGFYGYLSYGLGLDKKADKGVILHSRILWFYSNAYMTLGGDELLDNAKHAYEFIKNNCIDYEYGGVYWMMDFEGKPADTMKHTYNIAFAIYALSSYYRASGDKEALALAYRPFEDIEKNTLYEYGYREAFDRQWRLVDNEALSENGLKADKTMNAILHLIEAYTELYKADGNEKVADRLKFQLGQMRDIVYTPDTNALKVFFDTAFNLVGDIHSYGHDIEATWLMDRACDVLGDEDLKKQFAEMDLKISHNIQDIALEDGALNNERDKNEIDKTRVWWVQAEAVVGFINAYQHS... | 5.1.3.11 | null | 6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde [GO:0061720]; carbohydrate metabolic process [GO:0005975]; N-acetylglucosamine metabolic process [GO:0006044]; N-acetylmannosamine metabolic process [GO:0006051] | cytoplasm [GO:0005737] | cellobiose epimerase activity [GO:0047736]; N-acylglucosamine 2-epimerase activity [GO:0050121]; peptidase inhibitor activity [GO:0030414]; sulfoquinovose isomerase activity [GO:0061593] | PF07221; | 1.50.10.10; | Cellobiose 2-epimerase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:17612504}. | CATALYTIC ACTIVITY: Reaction=D-cellobiose = beta-D-glucosyl-(1->4)-D-mannopyranose; Xref=Rhea:RHEA:23384, ChEBI:CHEBI:17057, ChEBI:CHEBI:47931; EC=5.1.3.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00929, ECO:0000269|PubMed:17612504, ECO:0000269|PubMed:18392616}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.8 mM for cellobiose {ECO:0000269|PubMed:18392616}; KM=33 mM for lactose {ECO:0000269|PubMed:18392616}; Vmax=88.8 umol/min/mg enzyme with cellobiose as substrate {ECO:0000269|PubMed:18392616}; Vmax=72.5 umol/min/mg enzyme with lactose as substrate {ECO:0000269|Pu... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:18392616}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:18392616}; | FUNCTION: Catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man). Can also epimerize cellotriose to Glc-Glc-Man, cellotetraose to Glc-Glc-Glc-Man, and lactose to epilactose. {ECO:0000255|HAMAP-Rule:MF_00929, ECO:0000269|PubMed:17612504, ECO:0000269|PubMed:18392616}. | Ruminococcus albus |
P0DKY8 | NUD16_HOMVI | MSSDTGDRTWGHLAATEHYGRITDTTDYIQVDKENLKNDPYYNSSQASHCMIFARNNKKTFGVYNPRAAILMQMRFDGNLGFPGGLVDAGEDSIKALNRELTEEMNLDTSKHSVSESSYVVTHWSISKRLCLHFYALEVSLAELYEIEKRALLAKDYGSEVLGTIRMPLYTMGDGYRGFPTFLTTPS | 3.6.1.62; 3.6.1.64 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18820299}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:18820299}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:18820299}; Note=Decapping activity is higher in the presence of manganese than in Magnesiu... | mRNA catabolic process [GO:0006402]; nucleotide metabolic process [GO:0009117]; sno(s)RNA catabolic process [GO:0016077] | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654] | 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity [GO:0140933]; dIDP phosphatase activity [GO:0097383]; IDP phosphatase activity [GO:1990003]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; phosphodiesterase decapping endonuclease activity [GO:1990174]; snoRNA binding [GO:0030515] | PF00293; | 3.90.79.10; | Nudix hydrolase family, NUDT16 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96DE0}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6TEC1}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6TEC1}. Cytoplasm {ECO:0000250|UniProtKB:Q96DE0}. | CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GDP; Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:63714, ChEBI:CHEBI:138282, ChE... | null | null | null | null | FUNCTION: RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs in a metal-dependent manner. Has diphosphatase activity and removes m7G caps from U8 snoRNA (PubMed:18820299). May catalyze the cleavage of the cap structure on mRNAs. May also act as a phosphatase; hydrolyzes the non... | Homalodisca vitripennis (Glassy-winged sharpshooter) (Homalodisca coagulata) |
P0DKZ0 | CKR1B_CONRO | MQLYTYLYLLVPLVTFHLILGTGTLDHGDALTERRSTDATALKPEPVLLQKSSARSTNDNGKDTQMKRILKKRGNKARGEEELAEKAPEFARELAN | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:22594498}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:26048991}; Note=Divalent cations stabilize the toxin the in alpha-helix conformation. {ECO:0000269|PubMed:22594498, ECO:0000269|PubMed:26048991}; | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792] | ion channel regulator activity [GO:0099106]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | null | null | Conotoxin B superfamily | PTM: Hydroxylation of Pro-88 is important for NR2B/GRIN2B NMDA receptor selectivity (PubMed:26048991, PubMed:27981829). Removal of hydroxylation does not change global NMDA receptor antagonism (tested on WT neurons), but it decreases the inhibitory potency on NR2B/GRIN2B NMDA receptors and increases the inhibitory pote... | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Conantokins inhibit N-methyl-D-aspartate (NMDA) receptors. This toxin has antagonist activity on the NR2B/GRIN2B subunit (IC(50)=0.1 uM) (PubMed:22594498, PubMed:26048991, PubMed:27981829). In vivo, when delivered into the brain, is active has anticonvulsant activity in the model of epilepsy in mice (PubMed:2... | Conus rolani (Cone snail) |
P0DL10 | TD1_MAIZE | MPPPTFLLGLLLLLLLAAAAPAPASATPERDAYALSRLKASLVPSATNSTSAPLSDWDPAATPPAHCAFTGVTCDAATSRVVAINLTAVPLHGGALPPEVALLDALASLTVANCYLRGRLPPALASMPALRHLNLSNNNLSGPFPPPPPAAYFPALEIVDVYNNNLSGPLPPLGAPHARSLRYLHLGGNYFNGSIPDTFGDLAALEYLGLNGNALSGRVPPSLSRLSRLREMYVGYYNQYSGGVPREFGALQSLVRLDMSSCTLTGPIPPELARLSRLDTLFLALNQLTGEIPPELGALTSLRSLDLSINDLAGEIPASF... | 2.7.11.1 | null | cell differentiation [GO:0030154]; phosphorylation [GO:0016310]; regulation of floral meristem growth [GO:0010080]; specification of floral organ number [GO:0048833] | membrane [GO:0016020] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; receptor serine/threonine kinase binding [GO:0033612] | PF00560;PF13855;PF08263;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | 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-[pr... | null | null | null | null | FUNCTION: Receptor-like kinase protein that regulates meristem size during inflorescence and flower development. Promotes vegetative meristem growth and restricts inflorescence and floral meristem growth. Based on additive and synergistic phenotypes of double mutants, it is probable that unlike CLV1 and CLV2 in A.thali... | Zea mays (Maize) |
P0DL26 | VSP27_BOTPI | VVGGDECNINEHRSLVAIFNSTGFFCSGILLNQEWVLTASHCDSTNFQMK | 3.4.21.- | null | proteolysis [GO:0006508] | extracellular region [GO:0005576] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: N-glycosylated. {ECO:0000269|PubMed:22819993}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-10.5. {ECO:0000269|PubMed:22819993}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 4-60 degrees Celsius. {ECO:0000269|PubMed:22819993}; | FUNCTION: Snake venom serine protease that interferes with the hemostatic system of the prey. It preferentially degrades the Bbeta chain (FGB) of fibrinogen, with minor effects on the Aalpha chain (FGA). It presents a lower ability to degrade fibrin clots than BpirSP41. It hydrolyzes chromogenic substrates S-2238 (used... | Bothrops pirajai (Piraja's lancehead) |
P0DL27 | VSP41_BOTPI | VVGGDECDINEHPFLAFLYSHGYFCGLTLINQEWVLTAAHCDRRFMRIYL | 3.4.21.- | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: N-glycosylated. {ECO:0000269|PubMed:22819993}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-10.5. {ECO:0000269|PubMed:22819993}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 4-60 degrees Celsius. {ECO:0000269|PubMed:22819993}; | FUNCTION: Snake venom serine protease that interferes with the hemostatic system of the prey. It almost completely degrades both Aalpha (FGA) and Bbeta (FGB) chains of fibrinogen. It presents a higher ability to degrade fibrin clots than BpirSP27. It hydrolyzes chromogenic substrates S-2238 (used for testing thrombin a... | Bothrops pirajai (Piraja's lancehead) |
P0DL28 | FBXW8_RAT | MEDHNLEEFRQRWQEELAHSQVLRRRRRLEAGERRPRRPEAGARGEPASGYLGLAQGLLEGAGRPPAPRPGRTDRKDVSSRSRSPPDRDAAEPEPLVDQLIRDLNEMDDVPFFDVHLPYELAINIFQYLNRRELGLCAQVSKTWKVIAEDEVLWYRLCRQEGHLPHSRFSDYTCWKLILQECLAPVHLIRPSWMNRKGAVSELEHVPDAVLCDVRSHDGVVIAGYTSGEVRVWDTRTWDYVAPFLESESEEEDPGMQPYVSFVRINSSLAVAAYEDGILNVWDLRTGRFPIFRFEHDARIQALALSQEKPVVATASAFDV... | null | null | cell population proliferation [GO:0008283]; cilium assembly [GO:0060271]; Golgi organization [GO:0007030]; labyrinthine layer blood vessel development [GO:0060716]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; ... | 3M complex [GO:1990393]; centriole [GO:0005814]; ciliary basal body [GO:0036064]; Cul7-RING ubiquitin ligase complex [GO:0031467]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]; SCF ubiquitin ligase complex [GO:0019005] | null | PF12937; | 1.20.1280.50;2.130.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:21572988}. Golgi apparatus {ECO:0000269|PubMed:21572988}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading t... | Rattus norvegicus (Rat) |
P0DL29 | VM1_BOTPI | TYIEVAVVADHRMFKKYNSNLNTIRKWVHEMVNSMNGVYRSMDVHLSLANLEVWSKKDLINVQKDSRETLKSFGEWRERDLLPRISHDNAQLLTAIVFDQQTIGRAYIGGMCDPRHSVGVVMDHSKINLQVAVTMAHELGHNLGMEHDENQCHCDAPSCVMXXXXXXXXXXXXXXCXXXXXXXXXTKHNPQCILNEPL | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF01421; | 3.40.390.10; | Venom metalloproteinase (M12B) family, P-I subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-10.5. {ECO:0000269|PubMed:23385358}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:23385358}; | FUNCTION: Zinc metalloprotease that preferentially degrades Aalpha chain of fibrinogen (FGA) (at a dose of 5 ug, whereas at a dose of 10 ug, both FGA and FGB are completely degraded). Degrades fibrin gel in a dose-dependent manner, as well blood clots formed in vitro (thrombolytic activity). Induces hemorrhage (in the ... | Bothrops pirajai (Piraja's lancehead) |
P0DL37 | KAX6L_UROYA | MNAKLIYLLLVVTTMMLTFDTTQAGDIKCSGTRQCWGPCKKQTTCTNSKCMNGKCKCYGCVG | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; toxin activity [GO:0090729] | PF00451; | 3.30.30.10; | Short scorpion toxin superfamily, Potassium channel inhibitor family, Alpha-KTx 06 subfamily | PTM: C-terminal amidation is important for activity. There is a 50-70-fold decrease in ability to inhibit Kv1.2/KCNA2 when the toxin is not amidated. This decrease may be explained by a 23-fold slower association rate (k(on)) together with a 2-fold faster dissociation rate (k(off)). {ECO:0000269|PubMed:31881193}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24723491}. | null | null | null | null | null | FUNCTION: Reversible blocker of voltage-gated potassium channels with fast binding and unbinding kinetics (PubMed:24723491, PubMed:31881193). Has highest activity on human voltage-gated potassium channel Kv1.2/KCNA2 channels (IC(50)=0.11-0.16 nM), whereas its affinity for other channels tested was in the nanomolar rang... | Urodacus yaschenkoi (Inland robust scorpion) |
P0DL39 | CA1A_CONAV | SCCARNPACRHNHPCV | null | null | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792] | acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | null | null | Conotoxin A superfamily | PTM: Two isomers (with different disulfide connectivity) have been synthesized (AusIA-globular (C1-C3, C2-C4) and AusIA-ribbon (C1-C4, C2-C3)). Only AusIA-globular contains the cysteine connectivity described as typical for native alpha-conotoxins. However, AusIA-ribbon is more potent than AusIA-globular, suggesting th... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25194747}. | null | null | null | null | null | FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This peptide has been experimentally synthesized as AusIA-globular and AusIA-ribbon. Both forms are active on chicken alpha-7/CHRNA7 nAChR with similar potency (micromolar range). ... | Conus australis (Austral cone) (Asprella australis) |
P0DL49 | NA12_ANEVI | MMNRLLVFLMLGAAFMLVVSAIDQDANEDINKRGVPCLCDSDGPSVRGNTLSGIIWLAGCPSGWHNCKKHGPTIGWCCKQ | null | null | null | extracellular region [GO:0005576]; nematocyst [GO:0042151] | sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF00706; | 2.20.20.10; | Sea anemone sodium channel inhibitory toxin family, Type I subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22048953}. Nematocyst {ECO:0000305|PubMed:22048953}. Note=In nematocyst, is associated with the tubule prior to discharge. {ECO:0000305|PubMed:22048953}. | null | null | null | null | null | FUNCTION: Binds specifically to voltage-gated sodium channels (Nav) (site 3), thereby delaying their inactivation during signal transduction (By similarity). Has a strong effect on crustaceans and insects and a weaker effect on mammals (By similarity). It strongly inhibits D.melanogaster sodium channel (DmNav1) (By sim... | Anemonia viridis (Snakelocks anemone) |
P0DL68 | CA1A_CONLM | SGCCSNPACRVNNPNIC | null | null | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792] | acetylcholine receptor inhibitor activity [GO:0030550]; toxin activity [GO:0090729] | PF07365; | null | Conotoxin A superfamily | PTM: Amidation at Cys-17 plays a critical role, since a C-terminally carboxylated analog is 3-fold less potent at the alpha-7/CHRNA7 nAChR subtype and 3-fold more potent at the alpha-3-beta-2/CHRNA3-CHRNB2 subtype. {ECO:0000269|PubMed:23924607}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23924607}. | null | null | null | null | null | FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This globular toxin inhibits human alpha-7/CHRNA7 (IC(50)=0.3-10.1 nM), rat alpha-3-beta-2/CHRNA3-CHRNB2 (IC(50)=10.3 nM) and rat alpha-3-alpha-5-beta-2/CHRNA3-CHRNB5-CHRNB2 (IC(50... | Conus limpusi (Cone snail) |
P0DL72 | TX15_GRAPO | DCLGFMRKCIPDNDKCCRPNLVCSRTHKWCKYVF | null | null | null | extracellular region [GO:0005576] | calcium channel regulator activity [GO:0005246]; ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 08 (Gtx1-15) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25658507}. | null | null | null | null | null | FUNCTION: Potent voltage-gated sodium channel blocker (PubMed:25658507). Potently inhibits the voltage-gated sodium channels Nav1.7/SCN9A (IC(50)=0.58-10 nM) (PubMed:25658507, PubMed:26999206). Also shows a moderate activity on Nav1.1/SCN1A (IC(50)=6 nM), Nav1.2/SCN2A (IC(50)=5-128 nM), Nav1.3/SCN3A (IC(50)=20.3-170 nM... | Grammostola porteri (Tarantula spider) (Lasiodora porteri) |
P0DM15 | CO6A_CONMF | RDCQEKWEYCIVPILGFVYCCPGLICGPFVCV | null | null | null | extracellular region [GO:0005576] | sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22609441}. | null | null | null | null | null | FUNCTION: MuO-conotoxins are gating-modifier toxins that inhibit sodium current by trapping the domain II voltage sensor in the closed position to prevent opening of the sodium channel. This toxin shows high activity on Nav1.4/SCN4A (IC(50)=81 nM) and Nav1.8/SCN10A (IC(50)=96-529 nM). It also shows low activity on othe... | Conus magnificus (Magnificent cone) (Darioconus magnificus) |
P0DM21 | CA1A_CONTE | MFTVFLLVVLATAVVSFTSDRASDDGKAAASDLITLTIKGCCSRPPCIANNPDLCG | null | null | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792] | acetylcholine receptor inhibitor activity [GO:0030550]; toxin activity [GO:0090729] | PF07365; | null | Conotoxin A superfamily | PTM: Exists in 4 different forms, depending on hydroxylations. Tx1a-PP does not contain hydroxyproline, tx1a-OP has one hydroxyproline at position 45, tx1a-PO has one hydroxyproline at position 46, and tx1a-PP has two hydroxyprolines at positions 45 and 46. {ECO:0000269|PubMed:23031820}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17660751}. | null | null | null | null | null | FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin inhibits rat alpha-3-beta-2/CHRNA3-CHRNB2 (IC(50)=3.5 nM), rat alpha-7/CHRNA7 (IC(50)=392 nM) nAChR, and the L.stagnalis soluble acetylcholine receptor (all tested witho... | Conus textile (Cloth-of-gold cone) |
P0DM51 | PA2B1_BOTPA | DLWQFGKMILKVAGKLPFPYYGAYGCYCGWGGRGKPKDPTDRCCFVHDCC | 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]; defense response to bacterium [GO:0042742]; 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 | PTM: Contains 7 disulfide bonds. | 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:0000269|PubMed:15302537}; | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2). In vitro, shows anticoagulant activity and induces cytotoxicity when tested on C2C12 myoblasts/myotubes. In vivo, when tested on mice, induces myotoxicity (intramuscular injection), edema (injection in the subplantar region) and lethality. Also induces neurotoxic effect on... | Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis) |
P0DM64 | MRP2B_DANRE | MSEYSNRSQAGADYEWHYEYYEDEEPVSFEGLRANRYSIVIGFWVGLAVFVIFMFFVLTLLTKTGAPHPEMCDASMKPHVLIGCELEVGGSLAFSLPPLPDQSRSLFHFYIHKEERVKTHKDAVIGRGMHCGRGNAERADEDEHFMSSFNIPNFVNSEQSSSLGHDDFLLSEPPIITDGQSDELKTAEPAHLCYDIIRH | null | null | cellular localization [GO:0051641]; energy homeostasis [GO:0097009]; energy reserve metabolic process [GO:0006112]; positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106071]; protein localization to plasma membrane [GO:0072659]; regulation of adenylate cyclase-activat... | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | corticotropin hormone receptor binding [GO:0031780]; signaling receptor regulator activity [GO:0030545]; type 1 melanocortin receptor binding [GO:0070996]; type 3 melanocortin receptor binding [GO:0031781]; type 4 melanocortin receptor binding [GO:0031782]; type 5 melanocortin receptor binding [GO:0031783] | PF15183; | null | MRAP family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Activator of melanocortin receptor 4 (mc4r), a receptor involved in energy homeostasis. Plays a role after larval development in the control of energy homeostasis and body weight regulation by increasing ligand-sensitivity of mc4r and mc4r-mediated generation of cAMP once the zebrafish begins feeding, increas... | Danio rerio (Zebrafish) (Brachydanio rerio) |
P0DM65 | BECN2_MOUSE | MSPALFLCQRCKEPLKLLQQQGGPLEVQHHANTPTEIPVSAESQVRTSGRPHSDGGRVSQGSALCTFTLLTSGGPDSEGGTTSQGNACCTFTLLGESASMRTMNTIQNTVLETFEILSDQKVVDHPLCVDCTDHLLMQLDDQLALLASDNQKYKSFQDRELLVSEEEREALHAELCAELSSLEQEEARLTQELEDLDGHHARVAAELRAAQAESKELYKQHEQHRVEYSVFKMEQLELMDQLSSVENQLTYALSQQYRLRQTNIFNATFTISDEGPLGVINNFRLGCLPGVRVGWTEISSAWGQTVLLLFSLSKIAGLQF... | null | null | autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cellular response to nitrogen starvation [GO:0006995]; endosome to lysosome transport [GO:0008333]; G protein-coupled receptor catabolic process [GO:1990172]; glucose homeostasis [GO:0042593]; late endosome to vacuole transport [GO:0045324]; mitophagy [GO:000... | phagophore assembly site [GO:0000407]; phosphatidylinositol 3-kinase complex, class III, type I [GO:0034271]; phosphatidylinositol 3-kinase complex, class III, type II [GO:0034272] | phosphatidylinositol 3-kinase binding [GO:0043548]; protein-containing complex binding [GO:0044877]; protein-macromolecule adaptor activity [GO:0030674] | PF04111;PF17675; | 6.10.250.3110;1.10.418.40; | Beclin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Involved in 2 distinct lysosomal degradation pathways: acts as a regulator of autophagy and as a regulator of G-protein coupled receptors turnover. Regulates degradation in lysosomes of a variety of G-protein coupled receptors via its interaction with GPRASP1/GASP1. {ECO:0000269|PubMed:23954414}. | Mus musculus (Mouse) |
P0DM80 | PHOQ_SALTY | MNKFARHFLPLSLRVRFLLATAGVVLVLSLAYGIVALVGYSVSFDKTTFRLLRGESNLFYTLAKWENNKISVELPENLDMQSPTMTLIYDETGKLLWTQRNIPWLIKSIQPEWLKTNGFHEIETNVDATSTLLSEDHSAQEKLKEVREDDDDAEMTHSVAVNIYPATARMPQLTIVVVDTIPIELKRSYMVWSWFVYVLAANLLLVIPLLWIAAWWSLRPIEALAREVRELEDHHREMLNPETTRELTSLVRNLNQLLKSERERYNKYRTTLTDLTHSLKTPLAVLQSTLRSLRNEKMSVSKAEPVMLEQISRISQQIGY... | 2.7.13.3; 3.1.3.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:16406409}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16406409}; Note=Binds up to 3 divalent cations (Ca(2+) or Mg(2+)); increasing concentrations of divalent cations allows better binding to phospholipids. {ECO:0000269|P... | phosphorelay signal transduction system [GO:0000160] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155] | PF02518;PF08918; | 1.10.287.130;3.30.450.140;3.30.565.10; | null | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:11160113, ECO:0000269|PubMed:12618457}; | null | null | null | null | FUNCTION: Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), Pho... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0DM85 | CRFC_ECOLI | MYTQTLYELSQEAERLLQLSRQQLQLLEKMPLSVPGDDAPQLALPWSQPNIAERHAMLNNELRKISRLEMVLAIVGTMKAGKSTTINAIVGTEVLPNRNRPMTALPTLIRHTPGQKEPVLHFSHVAPIDCLIQQLQQRLRDCDIKHLTDVLEIDKDMRALMQRIENGVAFEKYYLGAQPIFHCLKSLNDLVRLAKALDVDFPFSAYAAIEHIPVIEVEFVHLAGLESYPGQLTLLDTPGPNEAGQPHLQKMLNQQLARASAVLAVLDYTQLKSISDEEVREAILAVGQSVPLYVLVNKFDQQDRNSDDADQVRALISGTL... | null | null | chromosome segregation [GO:0007059]; DNA replication [GO:0006260]; regulation of single-species biofilm formation on inanimate substrate [GO:1900231] | bacterial nucleoid [GO:0043590]; cytoplasm [GO:0005737] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; ribosome binding [GO:0043022] | PF00350; | 3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23994470}. Note=About half the protein co-localizes with beta sliding clamp (DnaN) at midcell, the rest without clamp in quarter-cell positions when chromosomes are condensed during DNA replication. | null | null | null | null | null | FUNCTION: Important for the colocalization of sister nascent DNA strands after replication fork passage during DNA replication, and for positioning and subsequent partitioning of sister chromosomes. Does not have GTPase activity on its own. {ECO:0000269|PubMed:23994470}. | Escherichia coli (strain K12) |
P0DM89 | VM32A_GLOBR | QQRYLNAKRYVKLAIVADRSMVTKHNGKLKKLRKWIYRIVNTINEVYRSLNILVALVYLEIWSKEDLINVTSAAKDTLASFGNWRATDLLKRRSHDAAHLLTNIKFDGTTVGKAYVASMCQQDSSVGINQDHSKINLLVALTMAHELGHNLGMSHDVVNTEKQCNCGTCVMAPTISDQISKLFSNCSKNDYENFLTLYKPQCILNEPSKTDIVSPPVCGNELLEVGEECDCGSPETCQNPCCDAATCKLTSGSQCAKGLCCDQCKFSKSGTECRAAKDDCDIAESCTGQSADCPTDDLQRNGKPCQNNAGYCYNGKCPIM... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF08516;PF00200;PF01421; | 3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily | PTM: Glycosylated (Ref.1). {ECO:0000269|Ref.1}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5.; | null | FUNCTION: Non-hemorrhagic metalloproteinase that degrades fibrinogen. The alpha chain (FGA) is rapidly degraded, the beta chain (FGB) is degraded very slowly, while the gamma chain is left intact. Shows a prefential cleavage at X-Leu bonds. Cleaves insulin B chain at '29-His-|-Leu-30', '33-Ser-|-His-34', '38-Ala-|-Leu-... | Gloydius brevicaudus (Korean slamosa snake) (Agkistrodon halys brevicaudus) |
P0DM90 | VM32B_GLOBR | QQRYLNAKRYVKLAIVADRSMVTKHNGKLKKLRKWIYRIVNTINEVYRSLNILVALVYLEIWSKEDLINVTSAAKDTLASFGNWRATDLLKRRSHDAAHLLTNIKFDGTTVGKAYVASMCQQDSSVGINQDHSKINLLVALTMAHELGHNLGMSHDVVNTEKQCNCGTCVMAPTISDQISKLFSNCSKNDYENFLTLYKPQCILNEPSKTDIVSPPVCGNELLEVGEECDCGSPETCQNPCCDAATCKLTSGSQCAKGLCCDQCKFSKSGTECRAAKDDCDIAESCTGQSADCPTDDLQRNGQPCGNNAQYCRKGKCPIM... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF08516;PF00200;PF01421; | 3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily | PTM: Glycosylated (Ref.1). {ECO:0000269|Ref.1}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5.; | null | FUNCTION: Non-hemorrhagic metalloproteinase that degrades fibrinogen. The alpha chain (FGA) is rapidly degraded, the beta chain (FGB) is degraded very slowly, while the gamma chain is left intact. Shows a prefential cleavage at X-Leu bonds. Cleaves insulin B chain at '29-His-|-Leu-30', '33-Ser-|-His-34', '38-Ala-|-Leu-... | Gloydius brevicaudus (Korean slamosa snake) (Agkistrodon halys brevicaudus) |
P0DM91 | APOA1_PANPA | MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSTLGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ | null | null | cholesterol metabolic process [GO:0008203]; lipid transport [GO:0006869]; lipoprotein metabolic process [GO:0042157]; phosphatidylcholine metabolic process [GO:0046470]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phospholipid efflux [... | high-density lipoprotein particle [GO:0034364] | high-density lipoprotein particle receptor binding [GO:0070653]; lipid binding [GO:0008289]; protein homodimerization activity [GO:0042803] | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility (By similarity). {ECO:0000250}. | Pan paniscus (Pygmy chimpanzee) (Bonobo) |
P0DM95 | APOA2_PANPA | MKLLAATVLLLTICSLEGALVRRQAKEPCVDNLVSQYFQTVTDYGKDLMEKVKSPELQAEAKSYFEKSKEQLTPLIKKAGTELVNFLSYFMELGTQPATQ | null | null | cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle remodeling [GO:0034375]; lipoprotein metabolic process [GO:0042157]; low-density lipoprotein particle remodelin... | blood microparticle [GO:0072562]; chylomicron [GO:0042627]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | apolipoprotein receptor binding [GO:0034190]; cholesterol binding [GO:0015485]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; lipase inhibitor activity [GO:0055102]; phosphatidylcholine binding [GO:0031210] | PF04711; | 6.10.250.100; | Apolipoprotein A2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}. | null | null | null | null | null | FUNCTION: May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism. | Pan paniscus (Pygmy chimpanzee) (Bonobo) |
P0DMA5 | SCNAA_ONYTO | MEFPIGSVGTTNFRRFTPESLAEIEKQIAAHGAAKKARAKHGERKGQDEKPRPQLDLKACNQLPRFYGELPAELVGEPLEDLDPFYSTHRTFMVLNKGRTISRFSATWALWLFSPFNLIRRTAIKVSVHAWFSIFITITILFNCVCMTQNDLPEKIEYAFTVIYTFEALIKILARGFCLNEFTYLRDPWNWLDFSVITLAYVGAAIDLRGISGLRTFRVLRALKTVSVIPGLKVIVGALIHSVRKLADVTILTVFCLSVFALVGLQLFKGNLKNKCIKRSTDPHNAYNFSSQMADNFYIKNGTTEPLLCGNGSDAGHCPS... | null | null | membrane depolarization during action potential [GO:0086010]; neuronal action potential [GO:0019228]; regulation of atrial cardiac muscle cell membrane depolarization [GO:0060371]; regulation of heart rate [GO:0002027] | axon [GO:0030424]; plasma membrane [GO:0005886]; voltage-gated sodium channel complex [GO:0001518] | voltage-gated sodium channel activity [GO:0005248]; voltage-gated sodium channel activity involved in cardiac muscle cell action potential [GO:0086006] | PF00520;PF06512; | 1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350; | Sodium channel (TC 1.A.1.10) family, Nav1.8/SCN10A subfamily | PTM: Ubiquitinated by NEDD4L; which promotes its endocytosis. {ECO:0000305}.; PTM: Phosphorylation at Ser-1453 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000250}.; PTM: Lacks the cysteine which covalently binds the conotoxin GVIIJ. This... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D0E0C2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Note=It can be translocated to the cell membrane through association with S100A10. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:24159039}; | null | null | null | null | FUNCTION: Tetrodotoxin-resistant channel that mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which sodium ions may pass in accordance wi... | Onychomys torridus (Southern grasshopper mouse) |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.