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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O52552 | RIFK_AMYMS | MNARKAPEFPAWPQYDDAERNGLVRALEQGQWWRMGGDEVNSFEREFAAHHGAAHALAVTNGTHALELALQVMGVGPGTEVIVPAFTFISSSQAAQRLGAVTVPVDVDAATYNLDPEAVAAAVTPRTKVIMPVHMAGLMADMDALAKISADTGVPLLQDAAHAHGARWQGKRVGELDSIATFSFQNGKLMTAGEGGAVVFPDGETEKYETAFLRHSCGRPRDDRRYFHKIAGSNMRLNEFSASVLRAQLARLDEQIAVRDERWTLLSRLLGAIDGVVPQGGDVRADRNSHYMAMFRIPGLTEERRNALVDRLVEAGLPAF... | 2.6.1.-; 4.2.1.144 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:10433690, ECO:0000269|PubMed:9497318}; Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000269|PubMed:10433690, ECO:0000269|PubMed:9497318}; | antibiotic biosynthetic process [GO:0017000]; polysaccharide biosynthetic process [GO:0000271] | null | dTDP-4-amino-4,6-dideoxygalactose transaminase activity [GO:0019180]; lyase activity [GO:0016829]; pyridoxal phosphate binding [GO:0030170] | PF01041; | 3.90.1150.10;3.40.640.10; | DegT/dnrJ/eryC1 family | null | null | CATALYTIC ACTIVITY: Reaction=5-deoxy-5-amino-3-dehydroshikimate = 3-amino-5-hydroxybenzoate + H(+) + H2O; Xref=Rhea:RHEA:35771, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71959, ChEBI:CHEBI:71963; EC=4.2.1.144; Evidence={ECO:0000269|PubMed:21081954, ECO:0000269|PubMed:9497318}; CATALYTIC ACTIVITY: Reaction=L-glu... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.164 mM for 5-amino-5-deoxy-3-dehydroshikimate {ECO:0000269|PubMed:9497318}; KM=0.122 mM for 5-amino-5-deoxy-3-dehydroshikimate {ECO:0000269|PubMed:21081954}; Note=kcat is 6.82 sec(-1) for AHBA synthase activity. {ECO:0000269|PubMed:21081954}; | PATHWAY: Antibiotic biosynthesis; rifamycin B biosynthesis. {ECO:0000269|PubMed:21081954}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 for AHBA synthase activity. Retains its activity over a broad range of pH. Over 84% of the maximum activity of AHBA synthase is maintained over a pH range from 7.0 to 9.0. {ECO:0000269|PubMed:9497318}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 33 degrees Celsius for AHBA synthase activity. Retains its activity over a broad range of temperature. Over 84% of the maximum activity of AHBA synthase is maintained over a temperature range from 28 to 50 degrees Celsius. {ECO:0000269|PubMe... | FUNCTION: Catalyzes the dehydration and aromatization of 5-amino-5-deoxy-3-dehydroshikimate (aminoDHS) to 3-amino-5-hydroxybenzoate (AHBA), a compound that then serves as the starter unit for the assembly of a polyketide during the biosynthesis of rifamycin B and other ansamycin antibiotics. Cannot utilize 5-deoxy-5-am... | Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei) |
O52582 | CDR_STAA8 | MPKIVVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYVIGEVVEDRRYALAYTPEKFYDRKQITVKTYHEVIAINDERQTVSVLNRKTNEQFEESYDKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQVDKVLVVGAGYVSLEVLENLNERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEINAINGNEITFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKLDRKGFIPVNDKFETNVPNIYAIGDIATSHYRHVDLPASVPLAWGAHRAASIVAEQIAGNDTIEFKGF... | 1.8.1.14 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:16981688}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:16981688}; | null | null | CoA-disulfide reductase (NADP) activity [GO:0050451]; flavin adenine dinucleotide binding [GO:0050660]; NADP binding [GO:0050661]; protein disulfide isomerase activity [GO:0003756] | PF07992;PF02852; | 3.30.390.30;3.50.50.60; | Class-III pyridine nucleotide-disulfide oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=2 CoA + NADP(+) = CoA-disulfide + H(+) + NADPH; Xref=Rhea:RHEA:14705, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62209; EC=1.8.1.14; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for NADPH; KM=11 uM for CoA disulfide; KM=140 uM for 3'-dephospho-CoA disulfide; KM=80 uM for 4,4'-diphosphopantethine; KM=1100 uM for CoA glutathione mixed disulfide; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-8.0.; | null | FUNCTION: Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide. Is also active with other disulfide substrates containing at least one 4'-phosphopantethienyl moiety such as 4,4'-diphosphopantethine, but is not able to reduce oxidized glutathione, cystine, pantethine, or H(2)O(2). | Staphylococcus aureus (strain NCTC 8325 / PS 47) |
O52623 | SOPE_SALTM | MTKITLSPQNFRIQKQETTLLKEKSTEKNSLAKSILAVKNHFIELRSKLSERFISHKNTESSATHFHRGSASEGRAVLTNKVVKDFMLQTLNDIDIRGSASKDPAYASQTREAILSAVYSKNKDQCCNLLISKGINIAPFLQEIGEAAKNAGLPGTTKNDVFTPSGAGANPFITPLISSANSKYPRMFINQHQQASFKIYAEKIIMTEVAPLFNECAMPTPQQFQLILENIANKYIQNTP | null | null | actin cytoskeleton organization [GO:0030036] | extracellular region [GO:0005576] | GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085] | PF05364;PF07487; | 1.10.4120.10; | GEF (guanine exchange factor) SopE family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9482928}. Note=Secreted via the type III secretion system 1 (SPI-1 T3SS). | null | null | null | null | null | FUNCTION: Activator for both CDC42 and RAC1 by directly engaging these Rho GTPases and acting as potent guanine nucleotide exchange factor (GEF). This activation results in actin cytoskeleton rearrangements and stimulates membrane ruffling, promoting bacterial entry into non-phagocytic cells. Also activates MAPK8, indi... | Salmonella typhimurium |
O52646 | DNRD_STRGJ | MSEQIAAVRRMVEAYNTGKTDDVADYIHPEYMNPGTLEFTSLRGPELFAINVAWVKKTFSEEARLEEVGIEERADWVRARLVLYGRHVGEMVGMAPTGRLFSGEQIHLLHFVDGKIHHHRDWPDYQGTYRQLGEPWPETEHRRP | 5.5.1.23 | null | antibiotic biosynthetic process [GO:0017000]; daunorubicin biosynthetic process [GO:1901771]; doxorubicin metabolic process [GO:0044598] | null | intramolecular lyase activity [GO:0016872] | PF07366; | 3.10.450.50; | Polyketide cyclase DnrD family | null | null | CATALYTIC ACTIVITY: Reaction=methyl aklanonate = aklaviketone; Xref=Rhea:RHEA:37879, ChEBI:CHEBI:77988, ChEBI:CHEBI:77994; EC=5.5.1.23; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for nogalonic acid methyl ester {ECO:0000269|PubMed:16414075}; Note=kcat is 1 sec(-1) for cyclization with nogalonic acid methyl ester.; | PATHWAY: Antibiotic biosynthesis; daunorubicin biosynthesis.; PATHWAY: Antibiotic biosynthesis; carminomycin biosynthesis.; PATHWAY: Antibiotic biosynthesis; rhodomycin biosynthesis.; PATHWAY: Antibiotic biosynthesis; aclacinomycin biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:16414075}; | null | FUNCTION: Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide anti... | Streptomyces galilaeus |
O52681 | HYDC_THEMA | MERHFEKVEEILKKYGYKRENLIKILLEIQEIYRYLPEDVINYVSTAMGIPPAKIYGVATFYAQFSLKPKGKYTIMVCDGTACHMAGSPEVLKAIEEETGLTPGNVTEDLMFSLDQVGCLGACALAPVMVINGEVYGNLTADKVKEILRKIKEKERESANV | 1.12.1.4 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:27396836}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:Q56221}; | null | cytoplasm [GO:0005737] | 2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491] | PF01257; | 3.40.30.10;1.10.10.1590; | Complex I 24 kDa subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19411328}. | CATALYTIC ACTIVITY: Reaction=2 H2 + NAD(+) + 2 oxidized [2Fe-2S]-[ferredoxin] = 3 H(+) + NADH + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:30279, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.12.1.4... | null | null | null | null | FUNCTION: Catalyzes the oxidation of the physiological electron carriers NADH and reduced ferredoxin, coupled to the production of H(2) (PubMed:19411328). Acts as a bifurcating [FeFe] hydrogenase, which uses the exergonic oxidation of reduced ferredoxin to drive the unfavorable oxidation of NADH to produce H(2) (PubMed... | Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
O52793 | EVAA_AMYOR | MSSFVVPSLTAVRPRDHHDYADRIALSAATTDGVQMRTEDVRAWIAERRDANVFHVERIPFADLDQWWFEGVTGNLVHRSGRFFTIEGLHVIEHDGPHGDGPYREWQQPVIRQPEVGILGILAKEFDGVLHFLMQAKMEPGNPNLVQLSPTVQATRSNYTKAHGGTNVKLIEYFAPPDPERVIVDVLQAEQGSWFFRKSNRNMIVETVDDVPLWDDFCWLTLGQIAELMHEDETINMNSRSVLSCLPYQDITPRALFSDVQLLSWFTNERSRHDVRVRRIPLADVCGWKQGAEEIEHEDGRYFKVLAVAVKGSNREKISW... | 4.2.1.159 | null | antibiotic biosynthetic process [GO:0017000] | null | lyase activity [GO:0016829] | PF03559; | 3.90.79.40; | Hexose 2,3-dehydratase family | null | null | CATALYTIC ACTIVITY: Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H2O; Xref=Rhea:RHEA:47972, ChEBI:CHEBI:15377, ChEBI:CHEBI:57649, ChEBI:CHEBI:84540; EC=4.2.1.159; Evidence={ECO:0000269|PubMed:11035791, ECO:0000269|PubMed:23473392}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=56 uM for dTDP-glucose {ECO:0000269|PubMed:23473392}; Vmax=4 umol/min/mg enzyme for dTDP-glucose {ECO:0000269|PubMed:23473392}; | PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:11035791}. | null | null | FUNCTION: Involved in the biosynthesis of the 2,3,6-trideoxysugar L-epivancosamine, the terminal sugar added to the aglycone scaffold of chloroeremomycin, a member of the glycopeptide antibiotics vancomycin family. Catalyzes the removal of the hydroxyl group at position C-2 of the hexose ring of dTDP-4-dehydro-6-deoxy-... | Amycolatopsis orientalis (Nocardia orientalis) |
O52958 | KPRS_THEKO | MFLLGSGGKHFEDELRNAGAKILEVEIKRFPDGEKYVRVMGNGDEATVVSSTFYPQDEKIVELLLLGDALREKGFEKLKLVVPYFAYSRQDRVTKDGEPISVRAVMRALGIYYEELYIFDTHNPETLRFFPGKAVNVSPARVIGEYFREKLGDGLVLAPDKGALERARAVAEVLGLEYSHFEKRRISPTEVEMHPVDVDVKGKNVLIVDDIISTGGTMVRAAELLRKLGAKKIYVSATHGVFAEGAIERVSRAVDELAVTNTIPTPVSRISIVPELLKLE | 2.7.6.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00583}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00583}; | 5-phosphoribose 1-diphosphate biosynthetic process [GO:0006015]; phosphorylation [GO:0016310]; purine nucleotide biosynthetic process [GO:0006164]; ribonucleoside monophosphate biosynthetic process [GO:0009156] | cytoplasm [GO:0005737]; ribose phosphate diphosphokinase complex [GO:0002189] | ATP binding [GO:0005524]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; ribose phosphate diphosphokinase activity [GO:0004749] | PF14572;PF13793; | 3.40.50.2020; | Ribose-phosphate pyrophosphokinase family, Class III (archaeal) subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}. | CATALYTIC ACTIVITY: Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|Ref.1}; | null | PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00583}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|Ref.1}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. Half-life of the enzyme activity is 55 minutes at 70 degrees Celsius. {ECO:0000269|Ref.1}; | FUNCTION: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). It can also use CTP and GTP as substrates in addition to ATP. {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|Ref... | Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) |
O53166 | ACNA_MYCTU | MTSKSVNSFGAHDTLKVGEKSYQIYRLDAVPNTAKLPYSLKVLAENLLRNEDGSNITKDHIEAIANWDPKAEPSIEIQYTPARVVMQDFTGVPCIVDLATMREAIADLGGNPDKVNPLAPADLVIDHSVIADLFGRADAFERNVEIEYQRNGERYQFLRWGQGAFDDFKVVPPGTGIVHQVNIEYLASVVMTRDGVAYPDTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSMLIPRVVGFRLTGEIQPGVTATDVVLTVTEMLRQHGVVGKFVEFYGEGVAEVPLANRATLGNMSPEFGSTAAIFPIDEETIKY... | 4.2.1.3; 4.2.1.99 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P09339}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250|UniProtKB:P09339}; | citrate metabolic process [GO:0006101]; propionate metabolic process, methylcitrate cycle [GO:0019679]; response to iron ion [GO:0010039]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; extracellular region [GO:0005576]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886] | 2-methylisocitrate dehydratase activity [GO:0047456]; 4 iron, 4 sulfur cluster binding [GO:0051539]; aconitate hydratase activity [GO:0003994]; iron-responsive element binding [GO:0030350]; metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729] | PF00330;PF00694; | 6.10.190.10;3.30.499.10;3.20.19.10; | Aconitase/IPM isomerase family | null | null | CATALYTIC ACTIVITY: Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; Evidence={ECO:0000269|PubMed:17384188}; CATALYTIC ACTIVITY: Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377, Ch... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.56 mM for isocitrate {ECO:0000269|PubMed:17384188}; Vmax=33.3 umol/min/mg enzyme with isocitrate as substrate {ECO:0000269|PubMed:17384188}; | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. {ECO:0000305|PubMed:17384188}.; PATHWAY: Organic acid metabolism; propanoate degradation. {ECO:0000305|PubMed:17384188}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. It retains a high specific activity over a broad pH range. {ECO:0000269|PubMed:17384188}; | null | FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53168 | RIPA_MYCTU | MRRNRRGSPARPAARFVRPAIPSALSVALLVCTPGLATADPQTDTIAALIADVAKANQRLQDLSDEVQAEQESVNKAMVDVETARDNAAAAEDDLEVSQRAVKDANAAIAAAQHRFDTFAAATYMNGPSVSYLSASSPDEIIATVTAAKTLSASSQAVMANLQRARTERVNTESAARLAKQKADKAAADAKASQDAAVAALTETRRKFDEQREEVQRLAAERDAAQARLQAARLVAWSSEGGQGAPPFRMWDPGSGPAGGRAWDGLWDPTLPMIPSANIPGDPIAVVNQVLGISATSAQVTANMGRKFLEQLGILQPTDT... | 3.4.-.- | null | cell wall organization [GO:0071555]; cell wall organization or biogenesis [GO:0071554]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; peptidoglycan-based cell wall [GO:0009274] | cysteine-type peptidase activity [GO:0008234]; N-acetylmuramoyl-L-alanine amidase activity [GO:0008745] | PF00877; | 6.10.250.3150;3.90.1720.10; | Peptidase C40 family | PTM: Exported by the Tat system (PubMed:26933057). The position of the signal peptide cleavage has not been experimentally proven (PubMed:26933057). {ECO:0000269|PubMed:26933057}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17919286, ECO:0000269|PubMed:26933057}. Note=Secreted by the TAT secretion pathway (PubMed:26933057). Localizes to the septa upon expression in M.bovis or M.smegmatis. Remains associated with the cell. {ECO:0000269|PubMed:26933057}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 5 and 5.5.; | null | FUNCTION: Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan from a number of Actinobacteria; activity is increased in the presence of RpfB and inhibited by PBP1A (ponA1). Required for normal separation of daughter cells... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53177 | RPFE_MYCTU | MKNARTTLIAAAIAGTLVTTSPAGIANADDAGLDPNAAAGPDAVGFDPNLPPAPDAAPVDTPPAPEDAGFDPNLPPPLAPDFLSPPAEEAPPVPVAYSVNWDAIAQCESGGNWSINTGNGYYGGLRFTAGTWRANGGSGSAANASREEQIRVAENVLRSQGIRAWPVCGRRG | 3.-.-.- | null | negative regulation of gene expression [GO:0010629]; positive regulation of gene expression [GO:0010628]; quorum sensing [GO:0009372]; regulation of cell population proliferation [GO:0042127] | extracellular region [GO:0005576] | hydrolase activity [GO:0016787] | PF06737; | 1.10.530.10; | Transglycosylase family, Rpf subfamily | null | null | null | null | null | null | null | FUNCTION: Factor that stimulates resuscitation of dormant cells. Has peptidoglycan (PG) hydrolytic activity. Active in the pM concentration range. Has little to no effect on actively-growing cells. PG fragments could either directly activate the resuscitation pathway of dormant bacteria or serve as a substrate for endo... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53181 | KORB_MYCTU | MTRSGDEAQLMTGVTGDLAGTELGLTPSLTKNAGVPTTDQPQKGKDFTSDQEVRWCPGCGDYVILNTIRNFLPELGLRRENIVFISGIGCSSRFPYYLETYGFHSIHGRAPAIATGLALAREDLSVWVVTGDGDALSIGGNHLIHALRRNINVTILLFNNRIYGLTKGQYSPTSEVGKVTKSTPMGSLDHPFNPVSLALGAEATFVGRALDSDRNGLTEVLRAAAQHRGAALVEILQDCPIFNDGSFDALRKEGAEERVIKVRHGEPIVFGANGEYCVVKSGFGLEVAKTADVAIDEIIVHDAQVDDPAYAFALSRLSDQ... | 1.2.7.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19936047}; | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; peptidoglycan-based cell wall [GO:0009274] | 2-oxoglutarate synthase activity [GO:0047553]; magnesium ion binding [GO:0000287]; thiamine pyrophosphate binding [GO:0030976] | PF02775; | 3.40.50.970; | null | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] + succinyl-CoA; Xref=Rhea:RHEA:17297, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI... | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle. {ECO:0000269|PubMed:19936047}. | null | null | FUNCTION: Component of KG oxidoreductase (KOR) that catalyzes the CoA-dependent oxidative decarboxylation of 2-oxoglutarate (alpha-ketoglutarate, KG) to succinyl-CoA. Methyl viologen can act as electron acceptor in vitro; the physiologic electron acceptor is unknown. Is involved in the alternative TCA pathway that func... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53223 | LDT2_MYCTO | MPKVGIAAQAGRTRVRRAWLTALMMTAVMIGAVACGSGRGPAPIKVIADKGTPFADLLVPKLTASVTDGAVGVTVDAPVSVTAADGVLAAVTMVNDNGRPVAGRLSPDGLRWSTTEQLGYNRRYTLNATALGLGGAATRQLTFQTSSPAHLTMPYVMPGDGEVVGVGEPVAIRFDENIADRGAAEKAIKITTNPPVEGAFYWLNNREVRWRPEHFWKPGTAVDVAVNTYGVDLGEGMFGEDNVQTHFTIGDEVIATADDNTKILTVRVNGEVVKSMPTSMGKDSTPTANGIYIVGSRYKHIIMDSSTYGVPVNSPNGYRT... | 2.3.2.- | null | cell wall organization [GO:0071555]; peptidoglycan metabolic process [GO:0000270]; peptidoglycan-based cell wall biogenesis [GO:0009273]; peptidoglycan-protein cross-linking [GO:0018104]; regulation of cell shape [GO:0008360] | extracellular region [GO:0005576]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886] | acyltransferase activity [GO:0016746]; metal ion binding [GO:0046872]; peptidoglycan L,D-transpeptidase activity [GO:0071972] | PF17964;PF03734; | 2.60.40.3710;2.60.40.3780;2.40.440.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. | null | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. | null | null | FUNCTION: Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap(3) of the donor stem and the side chain of mDap(3) of the acceptor stem. Is specific for donor substrates containing a stem te... | Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) |
O53289 | SERB2_MYCTU | MPAKVSVLITVTGMDQPGVTSALFEVLAQHGVELLNVEQVVIRGRLTLGVLVSCPLDVADGTALRDDVAAAIHGVGLDVAIERSDDLPIIRQPSTHTIFVLGRPITAGAFSAVARGVAALGVNIDFIRGISDYPVTGLELRVSVPPGCVGPLQIALTKVAAEEHVDVAVEDYGLAWRTKRLIVFDVDSTLVQGEVIEMLAARAGAQGQVAAITEAAMRGELDFAESLQRRVATLAGLPATVIDDVAEQLELMPGARTTIRTLRRLGFRCGVVSGGFRRIIEPLARELMLDFVASNELEIVDGILTGRVVGPIVDRPGKAK... | 3.1.3.16; 3.1.3.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25037224, ECO:0000269|PubMed:25521849}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:25037224, ECO:0000269|PubMed:25521849}; Note=Binds 1 Mg(2+) ion per subunit (By similarity). Can also use Mn(2+) (PubMed:25037224, PubMed:... | dephosphorylation [GO:0016311]; L-serine biosynthetic process [GO:0006564]; protein dephosphorylation [GO:0006470] | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; host cell cytosol [GO:0044164] | amino acid binding [GO:0016597]; L-phosphoserine phosphatase activity [GO:0036424]; magnesium ion binding [GO:0000287]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722] | PF13740;PF21086;PF12710; | 3.30.70.260;3.40.50.1000; | HAD-like hydrolase superfamily, SerB family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26984196}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:26984196}. Note=Is secreted into the cytosol of infected macrophages and is found in bronchoalveolar lavage samples of tuberculosis patients. Co-localizes with host tubulin. {ECO:0000269|PubMed:26984196}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-serine = L-serine + phosphate; Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3; Evidence={ECO:0000269|PubMed:25037224, ECO:0000269|PubMed:25521849}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-D-serine = D-serin... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=92.68 uM for O-phospho-L-serine {ECO:0000269|PubMed:25037224}; KM=135.9 uM for O-phospho-L-serine {ECO:0000269|PubMed:25521849}; Vmax=14250 nmol/min/mg enzyme {ECO:0000269|PubMed:25521849}; Note=kcat is 8.83 min(-1) (PubMed:25037224). kcat is 25400 sec(-1) (PubMed:... | PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3. {ECO:0000305|PubMed:25037224}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 (PubMed:25037224, PubMed:25521849). Activity declines progressively before pH 7.5 and is almost abolished at 6.0 while at higher pH the enzyme remains active till pH 9.0 (PubMed:25521849). {ECO:0000269|PubMed:25037224, ECO:0000269|PubMed:25521849}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. Activity declines at higher temperatures and is completely abolished by 50 degrees Celsius. {ECO:0000269|PubMed:25521849}; | FUNCTION: Catalyzes the dephosphorylation of O-phospho-L-serine into L-serine, a step in the L-serine biosynthetic pathway (PubMed:25037224, PubMed:25521849). Exhibits high specificity for L-phosphoserine compared to substrates like L-phosphothreonine (5% relative activity) and L-phosphotyrosine (1.7% relative activity... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53353 | WHB2A_MYCTU | MVPEAPAPFEEPLPPEATDQWQDRALCAQTDPEAFFPEKGGSTREAKKICMGCEVRHECLEYALAHDERFGIWGGLSERERRRLKRGII | null | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250, ECO:0000305}; Note=Binds 1 [4Fe-4S] cluster per subunit. Contains 1 [2Fe-2S] cluster after reconstitution of overexpressed protein from E.coli. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit. {ECO:00... | cell redox homeostasis [GO:0045454]; negative regulation of DNA-templated transcription [GO:0045892] | cytoplasm [GO:0005737] | 4 iron, 4 sulfur cluster binding [GO:0051539]; dinitrosyl-iron complex binding [GO:0035731]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; protein-disulfide reductase (NAD(P)) activity [GO:0047134] | PF02467; | null | WhiB family | PTM: May be phosphorylated, possibly on Ser-42. {ECO:0000269|PubMed:22686939}.; PTM: The cluster is degraded quickly in the presence of air. Upon cluster removal intramolecular disulfide bonds are formed.; PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA (By similarity). {ECO:0000250}.; FUNCTION: The apo-form functions as a chaperone, preventing aggregation or helping in correct refolding of a number of substrates; this activity does not require ATP o... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53361 | SAPM_MYCTU | MLRGIQALSRPLTRVYRALAVIGVLAASLLASWVGAVPQVGLAASALPTFAHVVIVVEENRSQAAIIGNKSAPFINSLAANGAMMAQAFAETHPSEPNYLALFAGNTFGLTKNTCPVNGGALPNLGSELLSAGYTFMGFAEDLPAVGSTVCSAGKYARKHVPWVNFSNVPTTLSVPFSAFPKPQNYPGLPTVSFVIPNADNDMHDGSIAQGDAWLNRHLSAYANWAKTNNSLLVVTWDEDDGSSRNQIPTVFYGAHVRPGTYNETISHYNVLSTLEQIYGLPKTGYATNAPPITDIWGD | 3.1.3.2; 3.1.3.64 | COFACTOR: Name=a metal cation; Xref=ChEBI:CHEBI:25213; Evidence={ECO:0000305|PubMed:11073936}; | NADP catabolic process [GO:0006742]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phospholipid catabolic process [GO:0009395]; symbiont-mediated suppression of host innate immune response [GO:0052170] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; host cell cytoplasmic vesicle [GO:0044161]; peptidoglycan-based cell wall [GO:0009274] | acid phosphatase activity [GO:0003993]; phosphatase activity [GO:0016791]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438]; phosphoenolpyruvate phosphatase activity [GO:0050189]; phosphoglycerate phosphatase activity [GO:0050192]; trehalose-phosphatase activity [GO:0004805] | PF04185; | 3.40.720.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11073936, ECO:0000269|PubMed:15753315}. Host cytoplasmic vesicle, host phagosome {ECO:0000305|PubMed:15753315}. Note=It remains to be determined how SapM, once secreted into the phagosomal lumen, gains access to PI3P within the cytofacial membrane leaflet. It is possib... | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; Evidence={ECO:0000269|PubMed:11073936}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosp... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.43 mM for p-nitrophenyl phosphate {ECO:0000269|PubMed:11073936}; Vmax=2100000 nmol/h/mg enzyme with p-nitrophenyl phosphate as substrate {ECO:0000269|PubMed:11073936}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.5. Significant phosphatase activity is observed between pH 5.5 and 8.0. {ECO:0000269|PubMed:11073936}; | null | FUNCTION: Virulence factor that plays an important role in blocking phagosome-lysosome fusion and thus participates in the intracellular survival of the pathogen (PubMed:15753315, PubMed:23923000). Acts as a phosphatase that dephosphorylates phosphatidylinositol 3-phosphate (PI3P), a membrane trafficking regulatory lip... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53423 | GDSLL_MYCTU | MPRRSTIALATAGALASTGTAYLGARNLLVGQATHARTVIPKSFDAPPRADGVYTRGGGPVQRWRREVPFDVHLMIFGDSTATGYGCASAEEVPGVLIARGLAEQTGKRIRLSTKAIVGATSKGVCGQVDAMFVVGPPPDAAVIMIGANDITALNGIGPSAQRLADCVRRLRTRGAVVVVGTCPDLGVITAIPQPLRALAHTRGVRLARAQTAAVKAAGGVPVPLGHLLAPKFRAMPELMFSADRYHPSAPAYALAADLLFLALRDALTEKLDIPIHETPSRPGTATLEPGHTRHSMMSRLRRPRPARAVPTGG | 3.1.-.-; 3.1.1.6 | null | null | peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886] | acetylesterase activity [GO:0008126]; lysophospholipase activity [GO:0004622] | PF13472; | 3.40.50.1110; | 'GDSL' lipolytic enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; EC=3.1.1.6; Evidence={ECO:0000269|PubMed:31001637}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an al... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=753 uM for pNP-acetate {ECO:0000269|PubMed:31001637}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 (with pNP-acetate as substrate). {ECO:0000269|PubMed:31001637}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius (with pNP-acetate as substrate). {ECO:0000269|PubMed:31001637}; | FUNCTION: Esterase that preferentially hydrolyzes short-chain fatty acids, particularly pNP-acetate (C2) and pNP-butyrate (C4). Has also weak activity with pNP-hexanoate (C6) and pNP-octanoate (C8). It can also hydrolyze short-chain tryglycerides such as triacetin and tributyrin (PubMed:31001637). Important for intrace... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53424 | LIPU_MYCTU | MAVRPVLAVGSYLPHAPWPWGVIDQAARVLLPASTTVRAAVSLPNASAQLVRASGVLPADGTRRAVLYLHGGAFLTCGANSHGRLVELLSKFADSPVLVVDYRLIPKHSIGMALDDCHDGYRWLRLLGYEPEQIVLAGDSAGGYLALALAQRLQEVGEEPAALVAISPLLQLAKEHKQAHPNIKTDAMFPARAFDALDALVASAAARNQVDGEPEELYEPLEHITPGLPRTLIHVSGSEVLLHDAQLAAAKLAAAGVPAEVRVWPGQVHDFQVAASMLPEAIRSLRQIGEYIREATG | 3.1.1.- | null | null | extracellular region [GO:0005576] | acetylesterase activity [GO:0008126]; triglyceride lipase activity [GO:0004806] | PF07859; | 3.40.50.1820; | 'GDXG' lipolytic enzyme family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28327423}. Note=Extracellular. {ECO:0000269|PubMed:28327423}. | CATALYTIC ACTIVITY: Reaction=a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:59388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35748; Evidence={ECO:0000269|PubMed:26398213, ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423}; CATALY... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.73 uM for pNP-butyrate {ECO:0000269|PubMed:28164792}; KM=333 uM for pNP-butyrate {ECO:0000269|PubMed:28327423}; Note=kcat is 49.8 min(-1) with pNP-butyrate as substrate. {ECO:0000269|PubMed:28164792}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 (with pNP-butyrate as substrate). {ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius (with pNP-butyrate as substrate). {ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423}; | FUNCTION: Esterase that shows preference for short chain fatty acids (PubMed:26398213, PubMed:28164792, PubMed:28327423). Contributes to the growth of M.tuberculosis during the nutritive stress (PubMed:28164792). Elicits strong humoral response in both extrapulmonary and relapsed cases of tuberculosis patients (PubMed:... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53493 | PPMNT_MYCTU | MKLGAWVAAQLPTTRTAVRTRLTRLVVSIVAGLLLYASFPPRNCWWAAVVALALLAWVLTHRATTPVGGLGYGLLFGLVFYVSLLPWIGELVGPGPWLALATTCALFPGIFGLFAVVVRLLPGWPIWFAVGWAAQEWLKSILPFGGFPWGSVAFGQAEGPLLPLVQLGGVALLSTGVALVGCGLTAIALEIEKWWRTGGQGDAPPAVVLPAACICLVLFAAIVVWPQVRHAGSGSGGEPTVTVAVVQGNVPRLGLDFNAQRRAVLDNHVEETLRLAADVHAGLAQQPQFVIWPENSSDIDPFVNPDAGQRISAAAEAIGA... | 2.3.1.269; 2.4.1.-; 2.4.1.83 | null | glycolipid biosynthetic process [GO:0009247]; lipoprotein biosynthetic process [GO:0042158]; perturbation of host innate immune response [GO:0052167] | cytosol [GO:0005829]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886] | dolichyl-phosphate beta-D-mannosyltransferase activity [GO:0004582]; hydrolase activity [GO:0016787]; N-acyltransferase activity [GO:0016410] | PF00795;PF00535;PF20154; | 3.60.110.10; | CN hydrolase family, Apolipoprotein N-acyltransferase subfamily; Glycosyltransferase 2 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12427759}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]; Xref=Rhea:RHEA:48228, Rhea:RHEA-COMP:14681, Rhea:RHEA-COMP:14684, ChEBI:CHEBI:15378, ChEBI:CHEBI:136... | null | PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl transfer). | null | null | FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. {ECO:0000269|PubMed:19661058}.; FUNCTION: Transfers mannose from GDP-mannose to lipid acceptors (works best on C20-C95 lipid monophosphate substrates in which the lipid can b... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53512 | AROG_MYCTU | MNWTVDIPIDQLPSLPPLPTDLRTRLDAALAKPAAQQPTWPADQALAMRTVLESVPPVTVPSEIVRLQEQLAQVAKGEAFLLQGGDCAETFMDNTEPHIRGNVRALLQMAVVLTYGASMPVVKVARIAGQYAKPRSADIDALGLRSYRGDMINGFAPDAAAREHDPSRLVRAYANASAAMNLVRALTSSGLASLHLVHDWNREFVRTSPAGARYEALATEIDRGLRFMSACGVADRNLQTAEIYASHEALVLDYERAMLRLSDGDDGEPQLFDLSAHTVWIGERTRQIDGAHIAFAQVIANPVGVKLGPNMTPELAVEYV... | 2.5.1.54 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16288916}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:16288916}; Name=Cd(2+); Xref=ChEBI:CHEBI:48775; Evidence={ECO:0000269|PubMed:16288916}; Note=Binds 1 divalent cation per subunit. The enzyme is active with manganese, ... | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; protein homooligomerization [GO:0051260] | cytosol [GO:0005829]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886] | 3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849]; manganese ion binding [GO:0030145] | PF01474; | 3.20.20.70; | Class-II DAHP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; Evidence={ECO:0000269|PubMed:16288916}; Physio... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25 uM for D-erythrose 4-phosphate (E4P) {ECO:0000269|PubMed:16288916}; KM=37 uM for phosphoenolpyruvate (PEP) {ECO:0000269|PubMed:16288916}; Note=kcat is 3.1 sec(-1). {ECO:0000269|PubMed:16288916}; | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000305|PubMed:16288916}. | null | null | FUNCTION: Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate. {ECO:0000269|PubMed:16288916}. | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53547 | CHSB1_MYCTU | MKLTESNRSPRTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVVDEIGAAAADAGAKAVAVAGDISQRATADELLASAVGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRDKAKDAEGGSVFGRLVNTSSEAGLVGPVGQANYAAAKAGITALTLSAARALGRYGVCANVICPRARTAMTADVFGAAPDVEAGQIDPLSPQHVVSLVQFLASPAAAEVNGQVFIVYGPQVTLVSPPHMERRFSADGTSWDPTELTATLRDYFAGRDPEQSFSATDLMRQ | 1.1.1.- | null | cholesterol catabolic process [GO:0006707] | null | oxidoreductase activity [GO:0016491] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=(22S)-hydroxy-3-oxo-chol-4-ene-24-oyl-CoA + NAD(+) = 3,22-dioxochol-4-en-24-oyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:72583, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:86014, ChEBI:CHEBI:192468; Evidence={ECO:0000269|PubMed:33826843}; PhysiologicalDirection=left-to-rig... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.3 uM for (22S)-HOCO-CoA {ECO:0000269|PubMed:33826843}; KM=70 uM for NAD(+) with (22S)-HOCO-CoA {ECO:0000269|PubMed:33826843}; KM=169 uM for (3R)-hydroxyoctanoyl-CoA {ECO:0000269|PubMed:33826843}; KM=126 uM for NAD(+) with (3R)-hydroxyoctanoyl-CoA {ECO:0000269|Pub... | PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000269|PubMed:33826843}. | null | null | FUNCTION: A reversible dehydrogenase involved in cholesterol side-chain degradation. Catalyzes the oxidation of hydroxyl-cholesterol-CoA ester metabolic intermediate (22S)-HOCO-CoA (3-oxo-chol-4-ene-(22S)-hydroxy-24-oyl-CoA), the product of ChsH3, has no activity on (22R)-HOCO-CoA (the product of EchA19). Also acts on ... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53551 | FAC17_MYCTU | MTPTHPTVTELLLPLSEIDDRGVYFEDSFTSWRDHIRHGAAIAAALRERLDPARPPHVGVLLQNTPFFSATLVAGALSGIVPVGLNPVRRGAALAGDIAKADCQLVLTGSGSAEVPADVEHINVDSPEWTDEVAAHRDTEVRFRSADLADLFMLIFTSGTSGDPKAVKCSHRKVAIAGVTITQRFSLGRDDVCYVSMPLFHSNAVLVGWAVAAACQGSMALRRKFSASQFLADVRRYGATYANYVGKPLSYVLATPELPDDADNPLRAVYGNEGVPGDIDRFGRRFGCVVMDGFGSTEGGVAITRTLDTPAGALGPLPGG... | 6.2.1.2; 6.2.1.3 | null | Actinobacterium-type cell wall biogenesis [GO:0071766]; lipid biosynthetic process [GO:0008610]; long-chain fatty acid biosynthetic process [GO:0042759]; long-chain fatty acid import into cell [GO:0044539]; long-chain fatty acid metabolic process [GO:0001676]; triglyceride homeostasis [GO:0070328]; very long-chain fatt... | cytosol [GO:0005829]; lipid droplet [GO:0005811]; peroxisome [GO:0005777]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; butyrate-CoA ligase activity [GO:0047760]; fatty acid transmembrane transporter activity [GO:0015245]; long-chain fatty acid transporter activity [GO:0005324]; long-chain fatty acid-CoA ligase activity [GO:0004467]; medium-chain fatty acid-CoA ligase activity [GO:0031956]; very long-chain fatt... | PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2; Evidence={ECO:0000269|PubMed:19182784}; Physiologic... | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the activation of medium/long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension (PubMed:15042094, PubMed:19182784). Also involved in steroid side-chain degradation. Activates cholesterol m... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53561 | ECH19_MYCTU | MATVESGPDALVERRGHTLIVTMNRPAARNALSTEMMRIMVQAWDRVDNDPDIRCCILTGAGGYFCAGMDLKAATQKPPGDSFKDGSYGPSRIDALLKGRRLTKPLIAAVEGPAIAGGTEILQGTDIRVAGESAKFGISEAKWSLYPMGGSAVRLVRQIPYTLACDLLLTGRHITAAEAKEMGLIGHVVPDGQALTKALELADAISANGPLAVQAILRSIRETECMPENEAFKIDTQIGIKVFLSDDAKEGPRAFAEKRAPNFQNR | 4.2.1.- | null | cholesterol catabolic process [GO:0006707]; fatty acid beta-oxidation [GO:0006635]; response to host immune response [GO:0052572] | null | enoyl-CoA hydratase activity [GO:0004300] | PF00378; | 1.10.12.10; | Enoyl-CoA hydratase/isomerase family | PTM: Succinylated in vitro at pH 8.1, succinylation reduces specific activity of the enzyme 5.5-fold; succinyl-CoA is a downstream by-product of cholesterol degradation. Can be de-succinylated in vitro by NAD-dependent protein deacylase (AC P9WGG3). Succinylation may be a negative feedback regulator of cholesterol meta... | null | CATALYTIC ACTIVITY: Reaction=(22E)-3-oxochola-4,22-dien-24-oyl-CoA + H2O = (22R)-hydroxy-3-oxo-chol-4-ene-24-oyl-CoA; Xref=Rhea:RHEA:72575, ChEBI:CHEBI:15377, ChEBI:CHEBI:136759, ChEBI:CHEBI:192383; Evidence={ECO:0000269|PubMed:33826843}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.4 uM for octenoyl-CoA {ECO:0000269|PubMed:32649175}; KM=5.8 uM for 3-OCDO-CoA {ECO:0000269|PubMed:32649175}; KM=8 uM for 3-OCDO-CoA with succinylated enzyme {ECO:0000269|PubMed:32649175}; Note=kcat is 181.2 sec(-1) with 3-OCDO-CoA as substrate. kcat is 45.7 sec(-... | PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000269|PubMed:32649175}. | null | null | FUNCTION: Degradation of the cholesterol side chain involves 3 multistep beta-oxidation cycles, this may be involved in the second cycle (Probable). Hydrates 3-OCDO-CoA ((22E)-3-oxo-chol-4,22-dien-24-oyl-CoA) to make (22R)-HOCO-CoA (3-oxo-chol-4-ene-(22R)-hydroxy-24-oyl-CoA). Also acts on octenoyl-CoA. Not active on (E... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53580 | FAA32_MYCTU | MFVTGESGMAYHNPFIVNGKIRFPANTNLVRHVEKWAKVRGDKLAYRFLDFSTERDGVARDILWSDFSARNRAVGARLQQVTQPGDRVAILCPQNLDYLISFFGALYSGRIAVPLFDPAEPGHVGRLHAVLDDCAPSTILTTTDSAEGVRKFIRARSAKERPRVIAVDAVPTEVAATWQQPEANEETVAYLQYTSGSTRIPSGVQITHLNLPTNVVQVLNALEGQEGDRGVSWLPFFHDMGLITVLLASVLGHSFTFMTPAAFVRRPGRWIRELARKPGETGGTFSAAPNFAFEHAAVRGVPRDDEPPLDLSNVKGILNG... | 6.2.1.20 | null | Actinobacterium-type cell wall biogenesis [GO:0071766]; fatty acid biosynthetic process [GO:0006633]; lipid biosynthetic process [GO:0008610]; mycolate cell wall layer assembly [GO:0071769] | cytosol [GO:0005829]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886] | adenylyltransferase activity [GO:0070566]; ATP binding [GO:0005524]; ligase activity [GO:0016874]; long-chain fatty acid [acyl-carrier-protein] ligase activity [GO:0008922] | PF00501; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | PTM: Phosphorylated on Thr-552 by PknA, PknB, PknD and PknF. Dephosphorylated by PstP. Phosphorylation regulates activity. {ECO:0000269|PubMed:27590338}. | null | CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479, ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20; E... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2640 uM for dodecanoate {ECO:0000269|PubMed:19477415}; KM=72.09 uM for dodecanoate {ECO:0000269|PubMed:26900152}; KM=20.5 uM for tetradecanoate {ECO:0000269|PubMed:19477415}; KM=4.77 uM for tetradecanoate {ECO:0000269|PubMed:26900152}; KM=3.2 uM for hexadecanoate {... | PATHWAY: Lipid metabolism; mycolic acid biosynthesis. {ECO:0000269|PubMed:19436070, ECO:0000269|PubMed:19477415}. | null | null | FUNCTION: Involved in the biosynthesis of mycolic acids (PubMed:19436070, PubMed:19477415). Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the phosphopantetheine arm of the polyketide synthase Pks13 for further chain extension (PubMed:15042094, PubMed:194... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53581 | CULP6_MYCTU | MAKNSRRKRHRILAWIAAGAMASVVALVIVAVVIMLRGAESPPSAVPPGVLPPGPTPAHPHKPRPAFQDASCPDVQMISVPGTWESSPQQNPLNPVQFPKALLLKVTGPIAQQFAPARVQTYTVAYTAQFHNPLTTDNQMSYNDSRAEGTRAMVAAMTDMNNRCPLTSYVLIGFSQGAVIAGDVASDIGNGRGPVDEDLVLGVTLIADGRRQQGVGNQVPPSPRGEGAEITLHEVPVLSGLGLTMTGPRPGGFGALDGRTNEICAQGDLICAAPAQAFSPANLPTTLNTLAGGAGQPVHAMYATPEFWNSDGEPATEWTL... | 3.1.1.- | null | lipid catabolic process [GO:0016042] | extracellular region [GO:0005576]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886] | carboxylesterase activity [GO:0106435]; fatty acyl-CoA hydrolase activity [GO:0047617]; lipase activity [GO:0016298]; phospholipase A1 activity [GO:0008970] | PF01083; | 3.40.50.1820; | Cutinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. Secreted, cell wall {ECO:0000269|PubMed:19225166}. | CATALYTIC ACTIVITY: Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659; Evidence={ECO:0000269|PubMed:19225166}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47365; Evid... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23.52 mM for nitrophenyl butyrate {ECO:0000269|PubMed:19169353}; KM=0.017 mM for palmitoyl-S-CoA {ECO:0000269|PubMed:19169353}; KM=2.28 mM for decanoyl-S-CoA {ECO:0000269|PubMed:19169353}; KM=4.52 mM for pNP-butyrate {ECO:0000269|PubMed:20656688}; KM=19.88 uM for 4... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is above 7.0 for lipase activity. {ECO:0000269|PubMed:19225166}; | null | FUNCTION: Shows esterase and phospholipase A activities (PubMed:19169353, PubMed:19225166, PubMed:20656688, PubMed:29247008). May be involved in cell wall biosynthesis and/or maintenance (PubMed:19169353, PubMed:19225166, PubMed:20656688). Can hydrolyze various substrates, including the p-nitrophenol-linked aliphatic e... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53585 | GLFT2_MYCTU | MSELAASLLSRVILPRPGEPLDVRKLYLEESTTNARRAHAPTRTSLQIGAESEVSFATYFNAFPASYWRRWTTCKSVVLRVQVTGAGRVDVYRTKATGARIFVEGHDFTGTEDQPAAVETEVVLQPFEDGGWVWFDITTDTAVTLHSGGWYATSPAPGTANIAVGIPTFNRPADCVNALRELTADPLVDQVIGAVIVPDQGERKVRDHPDFPAAAARLGSRLSIHDQPNLGGSGGYSRVMYEALKNTDCQQILFMDDDIRLEPDSILRVLAMHRFAKAPMLVGGQMLNLQEPSHLHIMGEVVDRSIFMWTAAPHAEYDHD... | 2.4.1.288 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|PubMed:22707726}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:22707726}; | capsule polysaccharide biosynthetic process [GO:0045227]; cell wall macromolecule biosynthetic process [GO:0044038]; cell wall organization [GO:0071555]; cell wall polysaccharide biosynthetic process [GO:0070592]; lipopolysaccharide biosynthetic process [GO:0009103]; mycolate cell wall layer assembly [GO:0071769]; UDP-... | cytosol [GO:0005829]; plasma membrane [GO:0005886] | glycosyltransferase activity [GO:0016757]; lipopolysaccharide-1,5-galactosyltransferase activity [GO:0035496]; lipopolysaccharide-1,6-galactosyltransferase activity [GO:0008921]; metal ion binding [GO:0046872]; transferase activity [GO:0016740]; UDP-galactosyltransferase activity [GO:0035250] | PF19320;PF17994;PF13641; | 3.90.550.60; | Glycosyltransferase 2 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11304545}. | CATALYTIC ACTIVITY: Reaction=beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-rhamnosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octa-cis-decaprenol + 28 UDP-alpha-D-galactofuranose = [beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->6)]14-beta-D-galactofuranosyl-(1->5)-beta-D... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.38 mM for UDP-Galf {ECO:0000269|PubMed:18423586, ECO:0000269|PubMed:22707726}; KM=0.6 mM for beta-D-Galf-(1->5)-beta-D-Galf-(1->6)-beta-D-Galf-octyl {ECO:0000269|PubMed:18423586, ECO:0000269|PubMed:22707726}; KM=1.7 mM for beta-D-Galf-(1->5)-beta-D-Galf-octyl {EC... | PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis. {ECO:0000305|PubMed:11304545, ECO:0000305|PubMed:16704275}. | null | null | FUNCTION: Involved in the galactan polymerization of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component of the mycobacteria cell wall. Thus, successively transfers approximately 28 galactofuranosyl (Galf) residues from UDP-galactofuranose (UDP-Galf) onto t... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53638 | LDT1_MYCTU | MRRVVRYLSVVVAITLMLTAESVSIATAAVPPLQPIPGVASVSPANGAVVGVAHPVVVTFTTPVTDRRAVERSIRISTPHNTTGHFEWVASNVVRWVPHRYWPPHTRVSVGVQELTEGFETGDALIGVASISAHTFTVSRNGEVLRTMPASLGKPSRPTPIGSFHAMSKERTVVMDSRTIGIPLNSSDGYLLTAHYAVRVTWSGVYVHSAPWSVNSQGYANVSHGCINLSPDNAAWYFDAVTVGDPIEVVG | 2.3.2.- | null | cell wall organization [GO:0071555]; peptidoglycan-protein cross-linking [GO:0018104]; regulation of cell shape [GO:0008360] | extracellular region [GO:0005576]; periplasmic space [GO:0042597] | acyltransferase activity [GO:0016746]; peptidoglycan L,D-transpeptidase activity [GO:0071972] | PF17964;PF03734; | 2.60.40.3710;2.40.440.10; | null | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. | null | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. | null | null | FUNCTION: Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap(3) of the donor stem and the side chain of mDap(3) of the acceptor stem. Is specific for donor substrates containing a stem te... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53664 | HTDX_MYCTU | MTQPSGLKNLLRAAAGALPVVPRTDQLPNRTVTVEELPIDPANVAAYAAVTGLRYGNQVPLTYPFALTFPSVMSLVTGFDFPFAAMGAIHTENHITQYRPIAVTDAVGVRVRAENLREHRRGLLVDLVTNVSVGNDVAWHQVTTFLHQQRTSLSGEPKPPPQKKPKLPPPAAVLRITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAVLANIEARFPDAVRYSVRFAKPVLLPATAGLYVAEGDGGWDLTLRNMAKGYPHLTATVRGL | 4.2.1.-; 4.2.1.119; 4.2.1.55 | null | fatty acid biosynthetic process [GO:0006633]; fatty acid metabolic process [GO:0006631] | fatty acid synthase complex [GO:0005835]; plasma membrane [GO:0005886] | (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity [GO:0019171]; 3-hydroxyacyl-CoA dehydratase activity [GO:0018812]; fatty acid synthase activity [GO:0004312] | PF01575; | 3.10.129.10; | Enoyl-CoA hydratase/isomerase family | null | null | CATALYTIC ACTIVITY: Reaction=a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:26526, ChEBI:CHEBI:15377, ChEBI:CHEBI:57319, ChEBI:CHEBI:58856; EC=4.2.1.119; Evidence={ECO:0000269|PubMed:20511508}; CATALYTIC ACTIVITY: Reaction=(2E)-octenoyl-CoA + H2O = (3R)-hydroxyoctanoyl-CoA; Xref=Rhea:RHEA:40187, ChEB... | null | null | null | null | FUNCTION: Shows trans-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydratase activity (PubMed:19136596, PubMed:20511508). Displays a broad chain length specificity, with a predilection for the C8 to C12 substrates (PubMed:20511508). {ECO:0000269|PubMed:19136596, ECO:0000269|PubMed:20511508}. | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53666 | FADE5_MYCTU | MSHYRSNVRDQVFNLFEVLGVDKALGHGEFSDVDVDTARDMLAEVSRLAEGPVAESFVEGDRNPPVFDPKTHSVMLPESFKKSVNAMLEAGWDKVGIDEALGGMPMPKAVVWALHEHILGANPAVWMYAGGAGFAQILYHLGTEEQKKWAVLAAERGWGSTMVLTEPDAGSDVGAARTKAVQQADGSWHIDGVKRFITSGDSGDLFENIFHLVLARPEGAGPGTKGLSLYFVPKFLFDVETGEPGERNGVFVTNVEHKMGLKVSATCELAFGQHGVPAKGWLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNAL... | 1.3.8.1; 1.3.8.7; 1.3.8.8 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305|PubMed:32601219}; | fatty acid metabolic process [GO:0006631]; response to host immune response [GO:0052572] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | long-chain fatty acyl-CoA dehydrogenase activity [GO:0004466]; medium-chain fatty acyl-CoA dehydrogenase activity [GO:0070991]; short-chain fatty acyl-CoA dehydrogenase activity [GO:0016937] | PF00441;PF12806;PF02770;PF12418; | 2.40.110.20;1.20.140.10; | Acyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=358.7 uM for butanoyl-CoA {ECO:0000269|PubMed:32601219}; KM=353 uM for hexanoyl-CoA {ECO:0000269|PubMed:32601219}; KM=162.5 uM for octadecanoyl-CoA {ECO:0000269|PubMed:32601219}; Note=kcat is 1.07 sec(-1) with butanoyl-CoA as substrate. kcat is 0.80 sec(-1) with he... | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:32601219}. | null | null | FUNCTION: Acyl-CoA dehydrogenase that exhibits broad specificity for linear acyl-CoA substrates, with a preference for long-chain substrates. {ECO:0000269|PubMed:32601219}. | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53699 | STF0_MYCTU | MSRAVRPYLVLATQRSGSTLLVESLRATGCAGEPQEFFQYLPSTGMAPQPREWFAGVDDDTILQLLDPLDPGTPDTATPVAWREHVRTSGRTPNGVWGGKLMWNQTALLQQRAAQLPDRSGDGLRAAIRDVIGNEPVFVHVHRPDVVSQAVSFWRAVQTQVWRGHPDPKRDSQAVYHAGAIAHIIRNLRDQENGWRAWFAEEGIDPIDIAYPVLWRNLTAIVASVLDAIGQDPKLAPAPMLERQANQRSDEWVDRYRAEAPRLGLPT | 2.8.2.37 | null | 3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; sulfolipid biosynthetic process [GO:0046506]; trehalose metabolic process [GO:0005991] | peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886] | 3'-phosphoadenosine 5'-phosphosulfate binding [GO:0050656]; protein homodimerization activity [GO:0042803]; sulfotransferase activity [GO:0008146] | PF09037; | 3.40.50.300; | Stf0 sulfotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + alpha,alpha-trehalose = 2-O-sulfo-alpha,alpha-trehalose + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:41608, ChEBI:CHEBI:15378, ChEBI:CHEBI:16551, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:60091; EC=2.8.2.37; Evidence={ECO:0000269|PubMed:15258569... | null | PATHWAY: Glycolipid metabolism. {ECO:0000269|PubMed:15258569}. | null | null | FUNCTION: Catalyzes the sulfuryl group transfer from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to trehalose, leading to trehalose-2-sulfate (T2S). The sulfation of trehalose is the first step in the biosynthesis of sulfolipid-1 (SL-1), a major cell wall glycolipid and the most abundant sulfated metabolite found in M... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53873 | XPB_MYCTU | MTDGPLIVQSDKTVLLEVDHELAGAARAAIAPFAELERAPEHVHTYRITPLALWNARAAGHDAEQVVDALVSYSRYAVPQPLLVDIVDTMARYGRLQLVKNPAHGLTLVSLDRAVLEEVLRNKKIAPMLGARIDDDTVVVHPSERGRVKQLLLKIGWPAEDLAGYVDGEAHPISLHQEGWQLRDYQRLAADSFWAGGSGVVVLPCGAGKTLVGAAAMAKAGATTLILVTNIVAARQWKRELVARTSLTENEIGEFSGERKEIRPVTISTYQMITRRTKGEYRHLELFDSRDWGLIIYDEVHLLPAPVFRMTADLQSKRRL... | 5.6.2.4 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19199647, ECO:0000269|PubMed:22615856}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19199647, ECO:0000269|PubMed:22615856}; Note=ATPase activity has a small preference for Mn(2+) over Mg(2+), Ca(2+) supports ATPase activit... | transcription initiation at RNA polymerase II promoter [GO:0006367] | peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]; transcription preinitiation complex [GO:0097550] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; hydrolase activity [GO:0016787] | PF16203;PF13625;PF04851; | 3.40.50.300; | Helicase family, RAD25/XPB subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000269|PubMed:19199647, ECO:0000269|PubMed:22615856}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 nM for 21-mer ssDNA substrate {ECO:0000269|PubMed:19199647}; KM=22 uM for 10-mer ssDNA substrate {ECO:0000269|PubMed:19199647}; Note=kcat is 10 sec(-1) on a ssDNA 21-mer and about 50 sec(-1) on ssDNA 5kb template. {ECO:0000269|PubMed:19199647}; | null | null | null | FUNCTION: ATP-dependent 3'-5' DNA helicase, unwinds 3'-overhangs, 3'- flaps, and splayed-arm DNA substrates but not 5'-overhangs, 5'-flap substrates, 3-way junctions or Holliday junctions. Not highly efficient in vitro (PubMed:19199647, PubMed:22615856). Requires ATP hydrolysis for helicase activity; the ATPase activit... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53896 | PEPD_MYCTU | MAKLARVVGLVQEEQPSDMTNHPRYSPPPQQPGTPGYAQGQQQTYSQQFDWRYPPSPPPQPTQYRQPYEALGGTRPGLIPGVIPTMTPPPGMVRQRPRAGMLAIGAVTIAVVSAGIGGAAASLVGFNRAPAGPSGGPVAASAAPSIPAANMPPGSVEQVAAKVVPSVVMLETDLGRQSEEGSGIILSAEGLILTNNHVIAAAAKPPLGSPPPKTTVTFSDGRTAPFTVVGADPTSDIAVVRVQGVSGLTPISLGSSSDLRVGQPVLAIGSPLGLEGTVTTGIVSALNRPVSTTGEAGNQNTVLDAIQTDAAINPGNSGGA... | 3.4.21.107 | null | cellular response to antibiotic [GO:0071236]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF13180;PF13365; | 2.30.42.10;2.40.10.10; | Peptidase S1C family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:21445360}; Single-pass membrane protein {ECO:0000255}. Secreted, cell wall {ECO:0000269|PubMed:21445360}. Secreted {ECO:0000269|PubMed:21445360}. Note=Traffics from the cytoplasm through the cell membrane to the cell wall where it is autoprocessed and eventu... | CATALYTIC ACTIVITY: Reaction=Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.; EC=3.4.21.107; Evidence={ECO:0000269|PubMed:18479146, ECO:0000269|PubMed:20061478}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 7.0 and 8.5. {ECO:0000269|PubMed:20061478}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:20061478}; | FUNCTION: Required for virulence (PubMed:18479146). Acts both as a protease, which degrades and/or refolds damaged substrate targets, and as a chaperone (PubMed:18479146, PubMed:20061478). Plays an important role in the stress response network mediated through the two-component regulatory system MprAB and SigE signalin... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O53901 | PKS5_MYCTU | MGKERTKTVDRTRVTPVAVIGMGCRLPGGIDSPDRLWEALLRGDDLVTEIPADRWDIDEYYDPEPGVPGRTDCKWGAYLDNVGDFDPEFFGIGEKEAIAIDPQHRLLLETSWEAMEHGGLTPNQMASRTGVFVGLVHTDYILVHADNQTFEGPYGNTGTNACFASGRVAYAMGLQGPAITVDTACSSGLTAIHLACRSLHDGESDIALAGGVYVMLEPRRFASGSALGMLSATGRCHAFDVSADGFVSGEGCVMLALKRLPDALADGDRILAVIRGTAANQDGHTVNIATPSRSAQVAAYREALDVAGVDPATVGMVEAH... | 2.3.1.- | null | DIM/DIP cell wall layer assembly [GO:0071770]; fatty acid biosynthetic process [GO:0006633]; secondary metabolite biosynthetic process [GO:0044550] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF08240;PF00107;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;PF14765; | 3.40.47.10;1.10.1200.10;3.30.70.250;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. | null | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000250|UniProtKB:A0R1E8}. | null | null | FUNCTION: Polyketide synthase likely involved in the biosynthesis of a polymethyl-branched fatty acid (PMB-FA) that might only be produced during host infection. Is required for the full virulence of M.tuberculosis during host infection. {ECO:0000269|PubMed:12855735, ECO:0000305}. | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
O54003 | REP75_PYRAB | MVIYTSKFKNSLLDGLGVGHLSYDDQPILCNEVHPTLTLDTFISGGSSGSRPRPRWVYLDISTTNEGISEEFSSNTESKSPLLKVCGVSSKSSEGDGSSFIWFDKYRSVISRLEHSGFVEVERTVLKLRKISKELRSINKQLSRLFLDDRERAKLLSRKRKYLDFARALIGSISKSLTLYADRFFVEVPQDYAKLIQKLGFSSDTLLLHLFVNSGVLEVFLDDNSSHKFRIAYISKVHAGKYHPVKGISKGSQEAKRVLRDLLVLSELLEGSLVSYRSGGVETIHHLIPVRHFVLTAPKELSFSIWASLKKGDSSLFRAF... | 2.7.7.31; 3.1.21.-; 6.5.1.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:9570403}; Note=DNA nicking and nucleotidyltransferase are strictly dependent on Mn(2+); Mg(2+) is able to substitute in DNA nicking 5X less efficiently. {ECO:0000269|PubMed:9570403}; | DNA replication [GO:0006260]; plasmid maintenance [GO:0006276] | null | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; DNA nucleotidylexotransferase activity [GO:0003912]; DNA topoisomerase activity [GO:0003916]; endonuclease activity [GO:0004519] | null | null | Gram-positive plasmids replication protein type 1 family | PTM: The N-terminus is blocked when overexpressed in E.coli. | null | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.31; CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-pho... | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 105 degrees Celsius for ssDNA nicking, 75 degrees Celsius for nucleotidyltransferase activity on a ssDNA substrate. Optimum temperature for ssDNA closing is substrate dependent, being 55 and 75 degrees Celsius for the 2 substrates tested. To... | FUNCTION: Required for rolling circle plasmid replication, has a site-specific endonuclease/ligase activity (nicking and closing). In vitro (no in vivo system yet exists) cleaves the double-stranded origin of replication (dso) site, on an ssDNA template, remaining covalently linked to the 5' end. Religates the appropri... | Pyrococcus abyssi (strain GE5 / Orsay) |
O54259 | SNOAB_STRNO | MPTRVNDGVDADEVTFVNRFTVHGGPAEFESVFARTAAFFARQPGFVRHTLLRERDKDNSYVNIAVWTDHDAFRRALAQPGFLPHATALRALSTSEHGLFTARQTLPEGGDTTGSGHR | 1.13.12.22 | null | antibiotic biosynthetic process [GO:0017000] | null | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases) [GO:0016703] | PF03992; | 3.30.70.100; | null | null | null | CATALYTIC ACTIVITY: Reaction=deoxynogalonate + O2 = H(+) + H2O + nogalonate; Xref=Rhea:RHEA:45056, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:84897, ChEBI:CHEBI:84900; EC=1.13.12.22; Evidence={ECO:0000305|PubMed:19255477, ECO:0000305|PubMed:20052967}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=140 uM for dithranol {ECO:0000269|PubMed:20052967}; Vmax=6.3 umol/min/mg enzyme with dithranol as substrate {ECO:0000269|PubMed:20052967}; Note=kcat is 1.5 sec(-1) for monooxygenase activity with dithranol as substrate. {ECO:0000269|PubMed:20052967}; | PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:8760909}. | null | null | FUNCTION: Involved in the biosynthesis of the anthracycline (aromatic polyketide) antibiotic nogalamycin (PubMed:8668120, PubMed:8760909). Catalyzes the oxygenation of 12-deoxy-nogalonic acid at position 12 to yield nogalonic acid (PubMed:19255477, PubMed:20052967). {ECO:0000269|PubMed:8668120, ECO:0000269|PubMed:87609... | Streptomyces nogalater |
O54288 | KDGA_SACSO | MPEIITPIITPFTKDNRIDKEKLKIHAENLIRKGIDKLFVNGTTGLGPSLSPEEKLENLKAVYDVTNKIIFQVGGLNLDDAIRLAKLSKDFDIVGIASYAPYYYPRMSEKHLVKYFKTLCEVSPHPVYLYNYPTATGKDIDAKVAKEIGCFTGVKDTIENIIHTLDYKRLNPNMLVYSGSDMLIATVASTGLDGNVAAGSNYLPEVTVTIKKLAMERKIDEALKLQFLHDEVIEASRIFGSLSSNYVLTKYFQGYDLGYPRPPIFPLDDEEERQLIKKVEGIRAKLVELKILKE | 4.1.2.55 | null | glyoxylate catabolic process [GO:0009436] | cytosol [GO:0005829] | 2-dehydro-3-deoxy-6-phosphogalactonate aldolase activity [GO:0008674]; 2-dehydro-3-deoxy-phosphogluconate aldolase activity [GO:0008675]; 4-hydroxy-2-oxoglutarate aldolase activity [GO:0008700]; 4-hydroxy-tetrahydrodipicolinate synthase activity [GO:0008840] | PF00701; | 3.20.20.70; | DapA family, KDPG aldolase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2-dehydro-3-deoxy-6-phospho-D-gluconate = D-glyceraldehyde 3-phosphate + pyruvate; Xref=Rhea:RHEA:17089, ChEBI:CHEBI:15361, ChEBI:CHEBI:57569, ChEBI:CHEBI:59776; EC=4.1.2.55; Evidence={ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170}; CATALYTIC ACTIVITY: Reaction=2-dehydro-3-deoxy-... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 mM for KDPG (at 60 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; KM=0.17 mM for KDPGal (at 60 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:000... | PATHWAY: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate: step 2/2. | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Extremely thermostable. {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}; | FUNCTION: Involved in the degradation of glucose and galactose via the Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG) forming pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde, respectively. It is also able to catalyze th... | Saccharolobus solfataricus (Sulfolobus solfataricus) |
O54329 | LANA_STRMG | MNKLNSNAVVSLNEVSDSELDTILGGNRWWQGVVPTVSYECRMNSWQHVFTCC | null | null | amino acid transport [GO:0006865]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]; regulation of membrane potential [GO:0042391] | extracellular region [GO:0005576] | signaling receptor binding [GO:0005102] | PF04604; | null | Type A lantibiotic family | PTM: Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor. {ECO:0000305}.; PTM: It is not established whether the 2,3-didehydrobutyrine is the ... | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Stable from pH 2.0 to 4.0. Activity decreases gradually with increasing pH. {ECO:0000269|PubMed:16626493, ECO:0000269|PubMed:8021218}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. {ECO:0000269|PubMed:16626493, ECO:0000269|PubMed:8021218}; | FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria including M.luteus, S.aureus, Streptococcus, P.micros, P.acidilactici, C.sporogenes, C.diphtheriae, A.viscosus, G.vaginalis, P.acnes, L.monocytogenes and M.smegmatis, and Gram-negative bacteria including C.jejuni, H.pylor... | Streptococcus mutans |
O54408 | RELA_BACSU | MANEQVLTAEQVIDKARSYLSDEHIAFVEKAYLYAEDAHREQYRKSGEPYIIHPIQVAGILVDLEMDPSTIAGGFLHDVVEDTDVTLDDLKEAFSEEVAMLVDGVTKLGKIKYKSQEEQQAENHRKMFVAMAQDIRVILIKLADRLHNMRTLKHLPQEKQRRISNETLEIFAPLAHRLGISKIKWELEDTALRYLNPQQYYRIVNLMKKKRAERELYVDEVVNEVKKRVEEVNIKADFSGRPKHIYSIYRKMVLQNKQFNEIYDLLAVRILVNSIKDCYAVLGIIHTCWKPMPGRFKDYIAMPKPNMYQSLHTTVIGPKG... | 2.7.6.5 | null | guanosine tetraphosphate biosynthetic process [GO:0015970]; phosphorylation [GO:0016310]; response to starvation [GO:0042594] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; GTP binding [GO:0005525]; GTP diphosphokinase activity [GO:0008728]; guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity [GO:0008893]; kinase activity [GO:0016301] | PF13291;PF13328;PF19296;PF04607;PF02824; | 3.10.20.30;3.30.70.260;3.30.460.10;1.10.3210.10; | RelA/SpoT family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate; Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5; | null | PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step 1/2. | null | null | FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp, it is probably the hydr... | Bacillus subtilis (strain 168) |
O54581 | DSPE_ERWAM | MELKSLGTEHKAAVHTAAHNPVGHGVALQQGSSSSSPQNAAASLAAEGKNRGKMPRIHQPSTAADGISAAHQQKKSFSLRGCLGTKKFSRSAPQGQPGTTHSKGATLRDLLARDDGETQHEAAAPDAARLTRSGGVKRRNMDDMAGRPMVKGGSGEDKVPTQQKRHQLNNFGQMRQTMLSKMAHPASANAGDRLQHSPPHIPGSHHEIKEEPVGSTSKATTAHADRVEIAQEDDDSEFQQLHQQRLARERENPPQPPKLGVATPISARFQPKLTAVAESVLEGTDTTQSPLKPQSMLKGSGAGVTPLAVTLDKGKLQLAP... | null | null | null | extracellular region [GO:0005576]; host cell [GO:0043657] | null | PF11725; | null | AvrE family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18705858, ECO:0000269|PubMed:19737101, ECO:0000269|PubMed:20110301, ECO:0000269|PubMed:9426142, ECO:0000269|PubMed:9555912}. Host cell {ECO:0000269|PubMed:18705858, ECO:0000269|PubMed:19737101, ECO:0000269|PubMed:20110301}. Note=Secreted via the Hrp type III secretion ... | null | null | null | null | null | FUNCTION: Major virulence factor that may function as a water- and solute-permeable channel dedicated to creating osmotic/water potential perturbation and a water- and nutrient-rich apoplast in which bacteria multiply within the infected plant tissues (PubMed:37704725). Expression in Xenopus oocytes results in inward a... | Erwinia amylovora (Fire blight bacteria) |
O54689 | CCR6_MOUSE | MNSTESYFGTDDYDNTEYYSIPPDHGPCSLEEVRNFTKVFVPIAYSLICVFGLLGNIMVVMTFAFYKKARSMTDVYLLNMAITDILFVLTLPFWAVTHATNTWVFSDALCKLMKGTYAVNFNCGMLLLACISMDRYIAIVQATKSFRVRSRTLTHSKVICVAVWFISIIISSPTFIFNKKYELQDRDVCEPRYRSVSEPITWKLLGMGLELFFGFFTPLLFMVFCYLFIIKTLVQAQNSKRHRAIRVVIAVVLVFLACQIPHNMVLLVTAVNTGKVGRSCSTEKVLAYTRNVAEVLAFLHCCLNPVLYAFIGQKFRNYFM... | null | null | calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; chemotaxis [GO:0006935]; DN2 thymocyte differentiation [GO:1904155]; DN3 thymocyte differentiation [GO:1904156]; immune response [GO:0006955]; isotype switching to IgA isotypes [GO:0048290]; leukocyte migration involved in inflammatory response [GO:... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; sperm flagellum [GO:0036126]; sperm midpiece [GO:0097225]; sperm plasma membrane [GO:0097524]; sperm principal piece [GO:0097228] | C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23765988}; Multi-pass membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:P51684}. | null | null | null | null | null | FUNCTION: Receptor for the C-C type chemokine CCL20. Binds to CCL20 and subsequently transduces a signal by increasing the intracellular calcium ion levels (PubMed:20068036). Although CCL20 is its major ligand it can also act as a receptor for non-chemokine ligands such as beta-defensins (PubMed:25122636). Binds to def... | Mus musculus (Mouse) |
O54692 | ZW10_MOUSE | MASFVTEVLAHSGSLEKEDLGTRISRLTRRVEEIKGEVCNMISKKYSEFLPTMQSAQALVTQVDTLSNDIDQLKSRIETEVCRDLHISTVEFTNLKQQLERDSVVLTLLKQLQEFSSAIEEYNSALAEKKYIPAARHLEEAQECLKLLKSRKCFDLKMLKSLSMELTVQKQNILYHLGEDWQKLVVWKFPPAKDTSSLESCLQTELHLCTEQPEKEDMTPLPSISSVLLAFSILGELPTKLKSFGQMLLKYILKPLVTCPSLHAVIERQPSSVSICFESLTTDLEHPSPPEAFAKIRLVLEVLQKQLLDLPLDADLEIGK... | null | null | cell division [GO:0051301]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; establishment of mitotic spindle orientation [GO:0000132]; Golgi organization [GO:0007030]; mitotic metaphase chromosome alignment [GO:0007080]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly... | cytosol [GO:0005829]; Dsl1/NZR complex [GO:0070939]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; lipid droplet [GO:0005811]; nucleus [GO:0005634]; RZZ complex [GO:1990423]; spindle pole [GO:0000922] | null | PF20666;PF20665;PF06248; | 1.10.357.150; | ZW10 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43264}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43264}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43264}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O43264}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O43264}. ... | null | null | null | null | null | FUNCTION: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ c... | Mus musculus (Mouse) |
O54693 | EDA_MOUSE | MGYPEVERREPLPAAAPRERGSQGCGCRGAPARAGEGNSCRLFLGFFGLSLALHLLTLCCYLELRSELRRERGTESRLGGPGAPGTSGTLSSPGSLDPVGPITRHLGQPSFQQQPLEPGEDPLPPDSQDRHQMALLNFFFPDEKAYSEEESRRVRRNKRSKSGEGADGPVKNKKKGKKAGPPGPNGPPGPPGPPGPQGPPGIPGIPGIPGTTVMGPPGPPGPPGPQGPPGLQGPSGAADKTGTRENQPAVVHLQGQGSAIQVKNDLSGGVLNDWSRITMNPKVFKLHPRSGELEVLVDGTYFIYSQVEVYYINFTDFASY... | null | null | animal organ development [GO:0048513]; canonical Wnt signaling pathway [GO:0060070]; cell differentiation [GO:0030154]; cell-matrix adhesion [GO:0007160]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; hair follicle development [GO:0001942]; hair follicle placode formation [GO:0060789];... | apical part of cell [GO:0045177]; collagen trimer [GO:0005581]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; lipid droplet [GO:0005811]; plasma membrane [GO:0005886] | death receptor agonist activity [GO:0038177]; death receptor binding [GO:0005123]; tumor necrosis factor receptor binding [GO:0005164] | PF00229; | 2.60.120.40; | Tumor necrosis factor family | PTM: N-glycosylated. {ECO:0000269|PubMed:10534613}.; PTM: Processing by furin produces a secreted form. {ECO:0000250|UniProtKB:Q92838}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10534613}; Single-pass type II membrane protein {ECO:0000269|PubMed:10534613}.; SUBCELLULAR LOCATION: [Ectodysplasin-A, secreted form]: Secreted {ECO:0000250|UniProtKB:Q92838}. | null | null | null | null | null | FUNCTION: Cytokine which is involved in epithelial-mesenchymal signaling during morphogenesis of ectodermal organs. Functions as a ligand activating the DEATH-domain containing receptors EDAR and EDA2R. Isoform TAA binds only to the receptor EDAR, while isoform TA-A2 binds exclusively to the receptor EDA2R (By similari... | Mus musculus (Mouse) |
O54695 | SPTC1_CRIGR | MAMAAEQWVLVEMVQALYEAPAYHLILEGILILWIIRLVFSKTYKLQERSDLTAKEKEELIEEWQPEPLVPPVSKNHPALNYNIVSGPPTHNIVVNGKECVNFASFNFLGLLANPRVKAAALASLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMRTEEAIIYSYGFSTIASAIPAYSKRGDIVFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDQKNPRKARVTRRFIVVEGLYMNTGTVCPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISIDDIDLISANMENALASVGGFCCG... | 2.3.1.50 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; | ceramide biosynthetic process [GO:0046513]; positive regulation of lipophagy [GO:1904504]; regulation of fat cell apoptotic process [GO:1904649]; sphinganine biosynthetic process [GO:0046511]; sphingomyelin biosynthetic process [GO:0006686]; sphingosine biosynthetic process [GO:0046512] | endoplasmic reticulum membrane [GO:0005789]; serine C-palmitoyltransferase complex [GO:0017059]; SPOTS complex [GO:0035339] | pyridoxal phosphate binding [GO:0030170]; serine C-palmitoyltransferase activity [GO:0004758] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-II pyridoxal-phosphate-dependent aminotransferase family | PTM: Phosphorylation at Tyr-164 inhibits activity and promotes cell survival. {ECO:0000250|UniProtKB:O15269}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12464627}; Single-pass membrane protein {ECO:0000269|PubMed:12464627}. | CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 + CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:58299; EC=2.3.1.50; Evidence={ECO:0000250|UniProtKB:O15269}; PhysiologicalDirection=left-to-rig... | null | PATHWAY: Lipid metabolism; sphingolipid metabolism. | null | null | FUNCTION: Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases. The SPT complex is also composed of SPTLC2 or SPTLC3 and S... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
O54697 | NALDL_RAT | MHWAKILGVGIGAAALLGLGIILGHFAIPKATEPLASSVSDSQDLDLAILDSVMGQLDASRIRENLRELSKEPHVATSARDEALVQLLLGRWKDSASGLDTAKTYEYTVLLSFPSTEQPNSVEVVGPNGTVFHSFQPFEKNLTGEQAEPNVLQPYAAYAPPGTPKGPLVYANRGSEDDFKKLEAEGINLKGTIALTRYGSVGRGAKAINAARHGVVGVLVYTDPGDINDGKSLPNETFPNSWGLPPSGVERGSYYEYFGDPLTPYLPAHPVSFRLDPHNISGFPPIPTQPIGFEDAKNLLCNLNGTSAPDSWQGALGCEY... | 3.4.11.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9UQQ1}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9UQQ1}; | peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | apical plasma membrane [GO:0016324]; membrane [GO:0016020] | aminopeptidase activity [GO:0004177]; calcium ion binding [GO:0005509]; carboxypeptidase activity [GO:0004180]; metallopeptidase activity [GO:0008237]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270] | PF02225;PF04389;PF04253; | 3.50.30.30;1.20.930.40;3.40.630.10; | Peptidase M28 family, M28B subfamily | PTM: N-glycosylated. {ECO:0000269|PubMed:9388249}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:9388249}; Single-pass type II membrane protein {ECO:0000305|PubMed:9388249}. Note=Ileal brush border membrane. {ECO:0000269|PubMed:9388249}. | null | null | null | null | null | FUNCTION: Aminopeptidase with broad substrate specificity. Has lower activity with substrates that have Asp or Glu in the P2' position, or Pro in the P3' position. Lacks activity with substrates that have both Pro in the P3' position and Asp or Glu in the P2' position. Lacks carboxypeptidase activity. Lacks dipeptidyl-... | Rattus norvegicus (Rat) |
O54698 | S29A1_RAT | MTTSHQPQDRYKAVWLIFFVLGLGTLLPWNFFITATQYFTSRLNTSQNISLVTNQSCESTEALADPSVSLPARSSLSAIFNNVMTLCAMLPLLIFTCLNSFLHQKVSQSLRILGSLLAILLVFLVTATLVKVQMDALSFFIITMIKIVLINSFGAILQASLFGLAGVLPANYTAPIMSGQGLAGFFTSVAMICAVASGSKLSESAFGYFITACAVVILAILCYLALPWMEFYRHYLQLNLAGPAEQETKLDLISEGEEPRGGREESGVPGPNSLPANRNQSIKAILKSIWVLALSVCFIFTVTIGLFPAVTAEVESSIAG... | null | null | adenine transport [GO:0015853]; adenosine transport [GO:0032238]; cellular response to glucose stimulus [GO:0071333]; cellular response to hypoxia [GO:0071456]; cytidine transport [GO:0015861]; excitatory postsynaptic potential [GO:0060079]; guanine transmembrane transport [GO:1903716]; hypoxanthine transport [GO:00353... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; presynapse [GO:0098793] | adenine transmembrane transporter activity [GO:0015207]; cytidine transmembrane transporter activity [GO:0015212]; guanine transmembrane transporter activity [GO:0015208]; neurotransmitter transmembrane transporter activity [GO:0005326]; nucleoside transmembrane transporter activity [GO:0005337]; purine nucleoside tran... | PF01733; | null | SLC29A/ENT transporter (TC 2.A.57) family | null | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:23639800}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:Q99808}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:11584005}; Multi-pass membrane protein {ECO:0000305}. Note=Localized... | CATALYTIC ACTIVITY: Reaction=adenosine(in) = adenosine(out); Xref=Rhea:RHEA:75343, ChEBI:CHEBI:16335; Evidence={ECO:0000269|PubMed:17379602}; CATALYTIC ACTIVITY: Reaction=guanosine(in) = guanosine(out); Xref=Rhea:RHEA:75371, ChEBI:CHEBI:16750; Evidence={ECO:0000250|UniProtKB:Q99808}; CATALYTIC ACTIVITY: Reaction=inosin... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.4 uM for adenosine {ECO:0000269|PubMed:17379602}; Vmax=530 pmol/min/mg enzyme {ECO:0000269|PubMed:17379602}; | null | null | null | FUNCTION: Uniporter involved in the facilitative transport of nucleosides and nucleobases, and contributes to maintaining their cellular homeostasis (PubMed:9353301). Functions as a Na(+)-independent transporter (By similarity). Involved in the transport of nucleosides such as adenosine, thymidine and uridine (PubMed:2... | Rattus norvegicus (Rat) |
O54699 | S29A2_RAT | MAHGNAPRDSYHLVGISFFILGLGTLLPWNFFITAIPYFQGRLAGTNSSAETPSTNHTSPTDTFNFNNWVTLLSQLPLLLFTLLNSFLYQCIPESVRILGSLLAILLLFALTAALVKVDLSPGLFFSITMASVWFINSFCAVLQGSLFGQLGTMPSTYSTLFLSGQGLAGIFAALAMLTSLASGVDPQTSALGYFITPCVGILLSIICYLSLPHLKFARYYLTKKPQAPVQELETKAELLGADEKNGIPVSPQQAGPTLDLDPEKELELGLEEPQKPGKPSVFVVFRKIWLTALCLVLVFTVTLSVFPAITAMVTTSSNS... | null | null | adenine transport [GO:0015853]; adenosine transport [GO:0032238]; cellular response to insulin stimulus [GO:0032869]; cytidine transport [GO:0015861]; guanine transmembrane transport [GO:1903716]; guanine transport [GO:0015854]; hypoxanthine transport [GO:0035344]; inosine transport [GO:0035340]; lactation [GO:0007595]... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886] | adenine transmembrane transporter activity [GO:0015207]; cytidine transmembrane transporter activity [GO:0015212]; guanine transmembrane transporter activity [GO:0015208]; neurotransmitter transmembrane transporter activity [GO:0005326]; nucleobase transmembrane transporter activity [GO:0015205]; nucleoside transmembra... | PF01733; | null | SLC29A/ENT transporter (TC 2.A.57) family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:23639800}; Multi-pass membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q14542}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the apical membrane of Sertoli cells. {ECO:0000269|PubMed:23639800}. | CATALYTIC ACTIVITY: Reaction=uridine(out) = uridine(in); Xref=Rhea:RHEA:71519, ChEBI:CHEBI:16704; Evidence={ECO:0000269|PubMed:9353301}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71520; Evidence={ECO:0000305|PubMed:9353301}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71521; Evidence={ECO:0000305|Pu... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=300 uM for hypoxanthine (for influx kinetics) {ECO:0000269|PubMed:18048066}; KM=189 uM for hypoxanthine (for efflux kinetics) {ECO:0000269|PubMed:18048066}; | null | null | null | FUNCTION: Bidirectional uniporter involved in the facilitative transport of nucleosides and nucleobases, and contributes to maintaining their cellular homeostasis (PubMed:18048066, PubMed:9353301). Functions as a Na(+)-independent, passive transporter (By similarity). Involved in the transport of nucleosides such as in... | Rattus norvegicus (Rat) |
O54701 | NCKX2_RAT | MDLHQSATVRLLQEWCSHESPSGCRRHYNTRKKLKLIRVIGLVMGLVAVSTVPFSISAFTETYSQNNRGEASDVTGPRAAPGHRQRTLLDLNDKIRDYTPQPPASQEDRSENGTDHAQGDYPKDVFSLEERRKGAIILHVIGMIYMFIALAIVCDEFFVPSLTVITEKLGISDDVAGATFMAAGGSAPELFTSLIGVFIAHSNVGIGTIVGSAVFNILFVIGMCALFSREILNLTWWPLFRDVSFYIVDLIMLIIFFLDNVIMWWESLLLLTAYFAYVVFMKFNVQVERWVKQMINRNKVVKVTVSEAQAKASTAGDKEE... | null | null | calcium ion import [GO:0070509]; calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; establishment of localization in cell [GO:0051649]; intracellular calcium ion homeostasis [GO:0006874]; learning [GO:0007612]; long-term synaptic... | membrane [GO:0016020]; plasma membrane [GO:0005886] | calcium channel activity [GO:0005262]; calcium, potassium:sodium antiporter activity [GO:0008273]; symporter activity [GO:0015293] | PF01699; | 1.20.1420.30; | Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family, SLC24A subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9461611}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Ca(2+)(out) + K(+)(out) + 4 Na(+)(in) = Ca(2+)(in) + K(+)(in) + 4 Na(+)(out); Xref=Rhea:RHEA:69967, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:9461611}; | null | null | null | null | FUNCTION: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+) (PubMed:9461611). Required for learming and memory by regulating neuronal Ca(2+), which is essential for the development of synaptic plasticity (By similarity). {ECO:0000250|UniProtKB:Q8BUN9, ECO:0000269|PubMed:94... | Rattus norvegicus (Rat) |
O54702 | CHSTA_RAT | MHHQWLLLAACFWVIFMFMVASKFITLTFKDPDGYSAKQEFVFLTAMPEAEKLRGEKHFSEVMKPTGKMLSESHPDQPPVYLERLELIRNACKEEALRNLSHTEVSKFVLDRIFVCDKHKILFCQTPKVGNTQWKKVLIVLNGAFSSIEEIPENVVHDHEKNGLPRLSSFSKIGIQKRLKTYFKFFIVRDPFERLISAFKDKFVHNPRFEPWYRHEIAPGIIRKYRKNRTETRGIQFEDFVRYLGDPNRRWLDLQFGDHIIHWVTYVKLCAPCEIKYSVIGHHETLEADAPYILKEAGIDHLVSYPTIPPGITMYNRTKV... | 2.8.2.- | null | androgen metabolic process [GO:0008209]; carbohydrate biosynthetic process [GO:0016051]; estrogen metabolic process [GO:0008210]; learning [GO:0007612]; long-term memory [GO:0007616]; proteoglycan biosynthetic process [GO:0030166] | Golgi membrane [GO:0000139] | HNK-1 sulfotransferase activity [GO:0016232]; sulfotransferase activity [GO:0008146] | PF03567; | null | Sulfotransferase 2 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:23723439}; Single-pass type II membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3-O-{beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] = 3-O-{O-3-S-beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-bet... | null | PATHWAY: Steroid metabolism. {ECO:0000250|UniProtKB:O43529}.; PATHWAY: Protein modification; carbohydrate sulfation. {ECO:0000250|UniProtKB:O43529}. | null | null | FUNCTION: Catalyzes the transfer of sulfate from 3'-phosphoadenylyl sulfate (PAPS) to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure 3-O-sulfo-beta-D-GlcA-(1->3)-beta-D-Gal-(1->4)-D-GlcNAc-R, a sulfated glucuronyl-l... | Rattus norvegicus (Rat) |
O54705 | NOS2_CAVPO | MACPWNFLWKLKSSRYDLTEEKDINNNVGKASHLYSPEIQDDPKYCSPGKHQNGSSQSLTGTAKKVPESQSKPHKPSPTCSQHMKIKNWGNGMILQDTLHTKAKTNFTCKPKSCLGSVMNPRSMTRGPRDTPIPPDELLPQAIEFVNQYYDSFKEAKIEEYLARVETVTKEIETTGTYQLTGDELIFATKLAWRNAPRCIGRIQWSNLQVFDARSCHTAQEMFEHICRHVRYSTNNGNIRSAITVFPQRTDGKHDFRVWNAQLIRYAGYQMPDGTIQGDPANLEFTQLCIDLGWKPRYGRFDVLPLILQADGRDPELFEI... | 1.14.13.39 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P35228}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P29476}; Note=Binds 1 FAD. {ECO:0000250|UniProtKB:P29476}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P35228}; Note=Binds 1... | defense response to bacterium [GO:0042742]; nitric oxide biosynthetic process [GO:0006809]; peptidyl-cysteine S-nitrosylation [GO:0018119]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; prostaglandin secretion [GO:0032310]; regulation of cyto... | cytosol [GO:0005829] | calmodulin binding [GO:0005516]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; nitric-oxide synthase activity [GO:0004517] | PF00667;PF00258;PF00175;PF02898; | 3.40.50.360;6.10.250.410;3.90.440.10;3.40.50.80;2.40.30.10; | NOS family | PTM: Polyubiquitinated; mediated by SPSB1, SPSB2 and SPSB4, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P35228}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35228}. Note=Localizes as discrete foci scattered throughout the cytosol and in the presence of SPSB1 and SPSB4, exhibits a more diffuse cytosolic localization. {ECO:0000250|UniProtKB:P35228}. | CATALYTIC ACTIVITY: Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39; Evidence={... | null | null | null | null | FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2. As component of the iNOS-S1... | Cavia porcellus (Guinea pig) |
O54709 | NKG2D_MOUSE | MALIRDRKSHHSEMSKCHNYDLKPAKWDTSQEQQKQRLALTTSQPGENGIIRGRYPIEKLKISPMFVVRVLAIALAIRFTLNTLMWLAIFKETFQPVLCNKEVPVSSREGYCGPCPNNWICHRNNCYQFFNEEKTWNQSQASCLSQNSSLLKIYSKEEQDFLKLVKSYHWMGLVQIPANGSWQWEDGSSLSYNQLTLVEIPKGSCAVYGSSFKAYTEDCANLNTYICMKRAV | null | null | adaptive immune response [GO:0002250]; cell differentiation [GO:0030154]; cellular response to lipopolysaccharide [GO:0071222]; defense response to Gram-positive bacterium [GO:0050830]; natural killer cell activation [GO:0030101]; natural killer cell mediated cytotoxicity [GO:0042267]; negative regulation of natural ki... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | carbohydrate binding [GO:0030246]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; MHC class I protein binding [GO:0042288]; MHC class Ib receptor activity [GO:0032394]; signaling receptor activity [GO:0038023] | PF00059; | 3.10.100.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:15294961}; Single-pass type II membrane protein {ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:15294961}. Note=Colocalized with HCST and TYROBP on the cell surface. | null | null | null | null | null | FUNCTION: Functions as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (N... | Mus musculus (Mouse) |
O54714 | PIAS3_MOUSE | MAELGELKHMVMSFRVSELQVLLGFAGRNKSGRKHELLAKALHLLKSSCAPSVQMKIKELYRRRFPRKTLGPSDLSLLSLPPGTSPVGSPGPLAPIPPTLLTPGTLLGPKREVDMHPPLPQPVHPDVTMKPLPFYEVYGELIRPTTLASTSSQRFEEAHFTFALTPQQLQQILTSREVLPGAKCDYTIQVQLRFCLCETSCPQEDYFPPNLFVKVNGKLCPLPGYLPPTKNGAEPKRPSRPINITPLARLSATVPNTIVVNWSSEFGRNYSLSVYLVRQLTAGTLLQKLRAKGIRNPDHSRALIKEKLTADPDSEVATTS... | 2.3.2.- | null | negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of protein sumoylation [GO:0033234]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive ... | cytoplasm [GO:0005737]; dendrite [GO:0030425]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | ionotropic glutamate receptor binding [GO:0035255]; potassium channel regulator activity [GO:0015459]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; transcription coregulator activity [GO:0003712]; transmembrane transporter binding [GO:0044325]; zinc ion binding [GO:0008270] | PF14324;PF02891; | 2.60.120.780;1.10.720.30;3.30.40.10; | PIAS family | PTM: Sumoylated. {ECO:0000269|PubMed:12387893}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11709556}. Nucleus {ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11709556, ECO:0000269|PubMed:14596924}. Nucleus speckle {ECO:0000269|PubMed:12077349}. Note=Colocalizes with MITF in the nucleus (PubMed:11709556). Colocalizes with GFI1 i... | null | null | PATHWAY: Protein modification; protein sumoylation. | null | null | FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway and the steroid hormone signaling pa... | Mus musculus (Mouse) |
O54715 | VAS1_RAT | MMAATVVSRIRTGTRWAPVLWLLLSLVAVAAAVAAEQQVPLVLWSSDRDLWAPVADTHEGHITSDMQLSTYLDPALELGPRNVLLFLQDKLSIEDFTAYGGVFGNKQDSAFSNLENALDLAPSSLVLPAVDWYAISTLTTYLQEKLGASPLHVDLATLKELKLNASLPALLLIRLPYTASSGLMAPREVLTGNDEVIGQVLSTLESEDVPYTAALTAVRPSRVARDVAMVAGGLGRQLLQTQVASPAIHPPVSYNDTAPRILFWAQNFSVAYKDEWKDLTSLTFGVENLNLTGSFWNDSFAMLSLTYEPLFGATVTFKFI... | null | null | cellular response to increased oxygen levels [GO:0036295]; endosome to plasma membrane protein transport [GO:0099638]; intracellular iron ion homeostasis [GO:0006879]; osteoclast development [GO:0036035]; regulation of cellular pH [GO:0030641]; synaptic vesicle lumen acidification [GO:0097401] | clathrin-coated vesicle membrane [GO:0030665]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endosome membrane [GO:0010008]; membrane [GO:0016020]; proton-transporting V-type ATPase complex [GO:0033176]; synaptic vesicle membrane [GO:0030672] | ATPase activator activity [GO:0001671]; small GTPase binding [GO:0031267]; transporter activator activity [GO:0141109] | PF20520;PF05827; | 2.40.160.110; | Vacuolar ATPase subunit S1 family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q15904}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15904}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q15904}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q15904}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:00... | null | null | null | null | null | FUNCTION: Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles (PubMed:32165585). Guides the V-type ATPase into specialized subcellular compartments, such as neuroendocrine regulated secretory vesicles or the ruffled border of t... | Rattus norvegicus (Rat) |
O54724 | CAVN1_MOUSE | MEDVTLHIVERPYSGFPDASSEGPEPTQGEARATEEPSGTGSDELIKSDQVNGVLVLSLLDKIIGAVDQIQLTQAQLEERQAEMEGAVQSIQGELSKLGKAHATTSNTVSKLLEKVRKVSVNVKTVRGSLERQAGQIKKLEVNEAELLRRRNFKVMIYQDEVKLPAKLSVSKSLKESEALPEKEGDELGEGERPEDDTAAIELSSDEAVEVEEVIEESRAERIKRSGLRRVDDFKKAFSKEKMEKTKVRTRENLEKTRLKTKENLEKTRHTLEKRMNKLGTRLVPVERREKLKTSRDKLRKSFTPDHVVYARSKTAVYKV... | null | null | positive regulation of cell motility [GO:2000147]; protein secretion [GO:0009306]; rRNA transcription [GO:0009303]; termination of RNA polymerase I transcription [GO:0006363]; transcription initiation at RNA polymerase I promoter [GO:0006361] | caveola [GO:0005901]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | identical protein binding [GO:0042802]; rRNA primary transcript binding [GO:0042134] | PF15237; | null | CAVIN family | PTM: Phosphorylated. Present in active and inactive forms. Changes in phosphorylation pattern may alter activity. Phosphorylation at Tyr-158 is essential for its function in the regulation of the ribosomal transcriptional activity. {ECO:0000269|PubMed:11139612, ECO:0000269|PubMed:27528195}.; PTM: Monoubiquitinated. {EC... | SUBCELLULAR LOCATION: Membrane, caveola {ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:25514038}. Cell membrane {ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225}. Microsome {ECO:0000250|UniProtKB:Q6NZI2}. Endoplasmic reticulum {ECO:0000269|PubMed:3018... | null | null | null | null | null | FUNCTION: Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18056712, PubMed:18191225, PubMed:18840361, PubMed:30188967). Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calv... | Mus musculus (Mouse) |
O54728 | PLB1_RAT | MESWPGVSLVGLLLLLLLGQGPSQIHGSSGENTSQPQQVFRTLKNFSFPCKPKKLELSVLSKSVHSLRPSDIKLVAAIGNLETPPAPGSGVVNMEKPQSLESELQNVCIGIMTALSDIIRHFNPSVLMPTCSPGKGTAGHTTIAEDLWIQAKELVRHLKDNPELDFEKDWKLITVLFSNTSQCHLCSSDQQKRHLMKHMEMLSGVLDYLHREVPRAFVNLVDLSEVLTMAQQHQETGFSPAPEICKCSEEITKLSKAVMQWSYQEAWEDLLASSKFNKHETFAVVFQSFFSEVELPLERPSPQDSTTLALRIWNSMMEPV... | 3.1.1.3; 3.1.1.4; 3.1.1.5 | null | diacylglycerol catabolic process [GO:0046340]; phosphatidylcholine catabolic process [GO:0034638]; phosphatidylethanolamine catabolic process [GO:0046338]; phosphatidylglycerol catabolic process [GO:0034478]; phospholipid metabolic process [GO:0006644]; positive regulation of acrosome reaction [GO:2000344]; retinol met... | apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526] | calcium-independent phospholipase A2 activity [GO:0047499]; lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; phospholipase A2 activity [GO:0004623]; retinyl-palmitate esterase activity [GO:0050253]; triglyceride lipase activity [GO:0004806] | PF00657; | 3.40.50.1110; | 'GDSL' lipolytic enzyme family, Phospholipase B1 subfamily | PTM: Undergoes proteolytic cleavage in the ileum. {ECO:0000269|PubMed:9442065}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065}; Single-pass type I membrane protein {ECO:0000255}. Note=Present in the intestinal brush border membranes. | 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:11401559, ECO:0000269|Pu... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9. {ECO:0000269|PubMed:9442064}; | null | FUNCTION: Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity) (By similarity). Has dual phospholipase and lysophospholipase activities toward diacylphos... | Rattus norvegicus (Rat) |
O54732 | MMP15_MOUSE | MGSDRSALGRPGCTGSCLSSRASLLPLLLVLLDCLGHGTASKDAEVYAAENWLRLYGYLPQPSRHMSTMRSAQILASALAEMQSFYGIPVTGVLDEETKTWMKRPRCGVPDQFGVHVKANLRRRRKRYTLTGKAWNNYHLTFSIQNYTEKLGWYNSMEAVRRAFQVWEQVTPLVFQEVSYDDIRLRRRAEADIMVLFASGFHGDSSPFDGVGGFLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGISLFLVAVHELGHALGLEHSSNPSAIMAPFYQWMDTDNFQLPEDDLRGIQQLYGSPDGKPQPTRPLPTVRPRRP... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | collagen catabolic process [GO:0030574]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]; response to estradiol [GO:0032355] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; membrane [GO:0016020] | metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF11857;PF00045;PF00413;PF01471; | 3.40.390.10;2.110.10.10; | Peptidase M10A family | PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}. | null | null | null | null | null | FUNCTION: Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A. | Mus musculus (Mouse) |
O54735 | PDE5A_RAT | MLPFGDKTRDMVNAWFSERVHNIPVCKEGIRAHTESCSCSLPQSPHADNTTPGAPARKISASEFDRPLRPIVVKDSEGTVSFLSDSGKKEQMPLTSPRFDSDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSKDKFLVSRLFDVAEGSTLEEASNNCIRLEWNKGIVGHVAAFGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFM... | 3.1.4.35 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O76074}; Note=Binds 1 Zn(2+) ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Tightly binds zinc. {ECO:0000250|UniProtKB:O76074}; COFACTOR: Name=Mg(2+... | cAMP-mediated signaling [GO:0019933]; cGMP catabolic process [GO:0046069]; cGMP metabolic process [GO:0046068]; negative regulation of cardiac muscle contraction [GO:0055118]; negative regulation of T cell proliferation [GO:0042130]; nervous system development [GO:0007399]; oocyte development [GO:0048599]; positive reg... | null | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; 3',5'-cyclic-nucleotide phosphodiesterase activity [GO:0004114]; cGMP binding [GO:0030553]; cyclic-nucleotide phosphodiesterase activity [GO:0004112]; metal ion binding [GO:0046872] | PF01590;PF00233; | 3.30.450.40;1.10.1300.10; | Cyclic nucleotide phosphodiesterase family | PTM: Phosphorylation is regulated by binding of cGMP to the two allosteric sites. Phosphorylation by PRKG1 leads to its activation. {ECO:0000250}. | null | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; EC=3.1.4.35; Evidence={ECO:0000250|UniProtKB:O76074}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958; Evidence={ECO:0000250|UniProtKB:O76074}; | null | PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1. | null | null | FUNCTION: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. Specifically regulates nitric-oxide-generated cGMP. {ECO:0000250|UniProtKB:O76074}. | Rattus norvegicus (Rat) |
O54743 | FOXF2_MOUSE | MSTEGGPPPPPPRPPPAPLRRACSPAPGALQAALMSPPPAATLESTSSSSSSSSASCASSSSNSVSASAGACKSAASSGGAGAGSGGTKKATSGLRRPEKPPYSYIALIVMAIQSSPSKRLTLSEIYQFLQARFPFFRGAYQGWKNSVRHNLSLNECFIKLPKGLGRPGKGHYWTIDPASEFMFEEGSFRRRPRGFRRKCQALKPMYHRVVSGLGFGASLLPQGFDFQAPPSAPLGCHGQGGYGGLDMMPAGYDTGAGAPGHAHPHHLHHHHVPHMSPNPGSTYMASCPVPAGPAGVGAAAGGGGGGGDYGPDSSSSPVP... | null | null | animal organ morphogenesis [GO:0009887]; embryonic camera-type eye morphogenesis [GO:0048596]; embryonic digestive tract development [GO:0048566]; establishment of planar polarity of embryonic epithelium [GO:0042249]; extracellular matrix organization [GO:0030198]; genitalia development [GO:0048806]; negative regulatio... | nuclear body [GO:0016604]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA bindi... | PF00250; | 1.10.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q12947}. | null | null | null | null | null | FUNCTION: Probable transcription activator for a number of lung-specific genes (PubMed:9676429). Mediates up-regulation of the E3 ligase IRF2BPL and drives ubiquitination and degradation of CTNNB1 (By similarity). {ECO:0000250|UniProtKB:Q12947, ECO:0000269|PubMed:9676429}. | Mus musculus (Mouse) |
O54747 | DPOD1_RAT | MDGKRRQAPSSGVPPKRACKGLWDEDEPSQFEENLALLEEIEAENRLQEAEEELQLPPEGIVGGQFSTADIDPRWLRPTPLALDPSTEPLIFQQLEIDHYVGTSPPLPEGPPASRNSVPILRAFGVTDEGFSVCCHIHGFAPYFYTPAPPGFGAEHLSELQRELNAAISRDQRGGKELSGPAVLAIELCSRESMFGYHGHGPSPFLRITLALPRLMAPARRLLEQGIRVPGLGTPSFAPYEANVDFEIRFMVDADIVGCNWLELPAGKYVRRAEKKATLCQLEVDVLWSDVISHPPEGQWQRIAPLRVLSFDIECAGRKG... | 2.7.7.7; 3.1.11.- | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250}; | base-excision repair, gap-filling [GO:0006287]; cellular response to UV [GO:0034644]; DNA biosynthetic process [GO:0071897]; DNA replication [GO:0006260]; DNA replication proofreading [GO:0045004]; DNA synthesis involved in DNA repair [GO:0000731]; DNA-templated DNA replication [GO:0006261]; error-free translesion synt... | delta DNA polymerase complex [GO:0043625]; nucleotide-excision repair complex [GO:0000109]; nucleus [GO:0005634] | 3'-5' exonuclease activity [GO:0008408]; 3'-5'-DNA exonuclease activity [GO:0008296]; 4 iron, 4 sulfur cluster binding [GO:0051539]; chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; enzyme binding [GO:0019899]; metal ion bindi... | PF00136;PF03104;PF14260; | 6.10.140.1540;1.10.132.60;3.30.342.10;1.10.287.690;3.90.1600.10;3.30.420.10; | DNA polymerase type-B family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P28340}. Note=Colocalizes with PCNA and POLD3 at S phase replication sites. After UV irradiation, recruited to DNA damage sites within 2 hours, independently on the cell cycle phase, nor on PCNA ubiquitination. This recruitment requires POLD3, PCNA and RFC1-replicati... | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000250|UniProtKB:P28340}; | null | null | null | null | FUNCTION: As the catalytic component of the trimeric (Pol-delta3 complex) and tetrameric DNA polymerase delta complexes (Pol-delta4 complex), plays a crucial role in high fidelity genome replication, including in lagging strand synthesis, and repair. Exhibits both DNA polymerase and 3'- to 5'-exonuclease activities. Re... | Rattus norvegicus (Rat) |
O54748 | STK3_RAT | MEQPPAPKSKLKKLSEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDVQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILKSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKSPEQRATATQLLQHPFIKNAKPVSILRELITEGMEIKAKRHEEQQRELEDEEENSDEDE... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13188}; | apoptotic process [GO:0006915]; canonical Wnt signaling pathway [GO:0060070]; cell differentiation involved in embryonic placenta development [GO:0060706]; cell population proliferation [GO:0008283]; central nervous system development [GO:0007417]; endocardium development [GO:0003157]; epithelial cell proliferation [GO... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF11629;PF00069; | 1.10.287.4270;4.10.170.10;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Autophosphorylated on two residues Thr-174 and Thr-180, leading to activation. Phosphorylation at Thr-117 and Thr-384 by PKB/AKT1, leads to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation, and increase in its binding to RAF1. Phosphorylated ... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13188}. Nucleus {ECO:0000250|UniProtKB:Q13188}. Note=The caspase-cleaved form cycles between nucleus and cytoplasm (By similarity). Phosphorylation at Thr-117 leads to inhibition of nuclear translocation (By similarity). {ECO:0000250|UniProtKB:Q13188}. | 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; Evidence={ECO:0000250|UniProtKB:Q13188}; Physiolo... | null | null | null | null | FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting pro... | Rattus norvegicus (Rat) |
O54750 | CP2J6_MOUSE | MLAATGSLLATIWAALHPRTLLVAAVTFLLLADYFKNRRPKNYPPGPWGLPFVGNIFQLDFGQPHLSIQPLVKKYGNIFSLNLGDITSVVITGLPLIKEALTQMEQNIMNRPLSVMQERISNKNGLIFSSGQIWKEQRRFALMTLRNFGLGKKSLEERMQEEASHLVEAIREEEGKPFNPHFSINNAVSNIICSVTFGERFDYHDSRFQEMLRLLDEVMYLETTMISQLYNIFPWIMKYIPGSHQKVFRNWEKLKLFVSCMIDDHRKDWNPDEPRDFIDAFLKEMTKYPEKTTSFNEENLICSTLDLFFAGTETTSTTLR... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | arachidonic acid metabolic process [GO:0019369]; negative regulation of collagen biosynthetic process [GO:0032966]; negative regulation of peroxisome proliferator activated receptor signaling pathway [GO:0035359]; organic acid metabolic process [GO:0006082]; positive regulation of extracellular matrix organization [GO:... | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | arachidonic acid epoxygenase activity [GO:0008392]; arachidonic acid monooxygenase activity [GO:0008391]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; NADPH-hemoprotein reductase activity [GO:0003958]; oxidoreductase activity, acting on paired donors, with incorporation or ... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | null | Mus musculus (Mouse) |
O54751 | CRX_MOUSE | MMAYMNPGPHYSVNALALSGPNVDLMHQAVPYSSAPRKQRRERTTFTRSQLEELEALFAKTQYPDVYAREEVALKINLPESRVQVWFKNRRAKCRQQRQQQKQQQQPPGAQTKARPAKRKAGTSPRPSTDVCTDPLGISDSYSPSLPGPSGSPTTAVATVSIWSPASEAPLPEAQRAGLVASGPSLTSAPYAMTYAPASAFCSSPSAYASPSSYFSGLDPYLSPMVPQLGGPALSPLSGPSVGPSLAQSPTSLSGQSYSTYSPVDSLEFKDPTGTWKFTYNPMDPLDYKDQSAWKFQIL | null | null | cell differentiation [GO:0030154]; nervous system development [GO:0007399]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to stimulus [GO:0050896]; retina development... | chromatin [GO:0000785]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; nuclear receptor binding [GO:0016922]; RNA polymerase II cis-re... | PF00046;PF03529; | 1.10.10.60; | Paired homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:16574740}. | null | null | null | null | null | FUNCTION: Transcription factor that binds and transactivates the sequence 5'-TAATC[CA]-3' which is found upstream of several photoreceptor-specific genes, including the opsin genes. Acts synergistically with other transcription factors, such as NRL, RORB and RAX, to regulate photoreceptor cell-specific gene transcripti... | Mus musculus (Mouse) |
O54753 | H17B6_RAT | MWFYLVTLVGLYYLLRWYRERQVVSHLHDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELKSKTSDRLETVILDVTNTDSISAATQWVKEHVGDKGLWGLVNNAGVFQAFAYIEWCRPEDCMSIFQVNLIGLAQVTLSMLFLVKKARGRIVNVSSVLGRVALFGGFYSCSKYGVEAFSDVLRREIRDFGVKVSIIEPGSFKTRMTDAELIIEKTKKTWEATPEHIRESYGQQFFDDFCNTTRRELKKCSTNLSLVTDCMEHALTSKYPRTRYSAGWDARLFFIPLSYLPTSLVDCLLAISRRKPAQAV | 1.1.1.105; 1.1.1.209; 1.1.1.239; 1.1.1.53; 1.1.1.62 | null | androgen metabolic process [GO:0008209]; brexanolone catabolic process [GO:0062175]; retinol metabolic process [GO:0042572]; steroid metabolic process [GO:0008202] | endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | 5alpha-androstane-3beta,17beta-diol dehydrogenase activity [GO:0047024]; androstan-3-alpha,17-beta-diol dehydrogenase activity [GO:0047044]; androsterone dehydrogenase activity [GO:0047023]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; NAD-retinol dehydrogenase activity [GO:0004745]; testosterone 17-... | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:O14756}; Peripheral membrane protein {ECO:0000250|UniProtKB:O14756}; Lumenal side {ECO:0000250|UniProtKB:O14756}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O14756}; Peripheral membrane protein {ECO:0000250|UniProtKB:O14756}; Lumenal side {ECO:0... | CATALYTIC ACTIVITY: Reaction=all-trans-retinol--[retinol-binding protein] + NAD(+) = all-trans-retinal--[retinol-binding protein] + H(+) + NADH; Xref=Rhea:RHEA:48488, Rhea:RHEA-COMP:14428, Rhea:RHEA-COMP:14430, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 uM for 5-alpha-androstan-3-alpha,17-beta-diol {ECO:0000269|PubMed:9188497}; KM=0.2 uM for androsterone {ECO:0000269|PubMed:9188497}; KM=0.5 uM for dihydrotestosterone {ECO:0000269|PubMed:9188497}; KM=1.1 uM for testosterone {ECO:0000269|PubMed:9188497}; KM=0.8 ... | null | null | null | FUNCTION: NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (in vitro). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro) (By similarity). Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (in vitro). Converts 5-... | Rattus norvegicus (Rat) |
O54754 | AOXA_MOUSE | MDPIQLLFYVNGQKVVEKNVDPEMMLLPYLRKNLRLTGTKYGCGGGGCGACTVMISRYNPSTKAIRHHPVNACLTPICSLHGTAVTTVEGLGNTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKASACCQSKENGVCCLDQEINGLAESQEEDKTSPELFSEEEFLPLDPTQELIFPPELMRIAEKQPPKTRVFYGERVTWISPVTLKELVEAKFKYPQAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELGVISQARDGLTLGAGLSLDQVKDILAD... | 1.17.3.-; 1.2.3.1 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:19401776}; Note=Binds 2 [2Fe-2S] clusters per subunit. {ECO:0000269|PubMed:19401776}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:19401776}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:19401776}; CO... | lipid metabolic process [GO:0006629]; xenobiotic metabolic process [GO:0006805] | cytosol [GO:0005829] | 2 iron, 2 sulfur cluster binding [GO:0051537]; aldehyde oxidase activity [GO:0004031]; electron transfer activity [GO:0009055]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; iron ion binding [GO:0005506]; molybdopterin cofactor binding [GO:0043546]; NAD binding [GO:0051287]; protein homodi... | PF01315;PF03450;PF00941;PF00111;PF01799;PF02738;PF20256; | 3.10.20.30;3.30.465.10;1.10.150.120;3.90.1170.50;3.30.365.10;3.30.390.50;3.30.43.10; | Xanthine dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10377246}. | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2; Xref=Rhea:RHEA:16829, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067; EC=1.2.3.1; Evidence={ECO:0000269|PubMed:10190983, ECO:0000269|PubMed:19401776}; CATALYTIC ACTIVITY: ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.8 uM for retinal (at 37 degrees Celsius and pH 7.8) {ECO:0000269|PubMed:10190983}; KM=97.7 uM for benzaldehyde (at 30 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:19401776}; KM=11.4 uM for phthalazine (at 30 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:1940... | null | null | null | FUNCTION: Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheter... | Mus musculus (Mouse) |
O54766 | ZP1_RAT | MAWGCFVVLLLLVAAPLRLGQHLHLKPGFQYSYDCGVQGMQLLVFPRPNQTIQFKVLDEFGNRFEVNNCSICYHWVISEAQKPAVFSADYKGCHVLEKQDGRFHLRVFIQAVLPNGRVDTAQDVTLICPKPDHILTPESYLAPPTTPQPFIPHTFALHPISGHTLAGSGHTGLTTLYPETHPTPAPPSSEPGPVGPTVPQSQWGTLGSWELTELDSIGTHLLQERCQVASGHIPCMVKGSSEEACQQAGCCYDNTKEMPCYYGNTVTLQCFRSGYFTLVMSQETALTHGVMLDNVHLAYAPNGCPPTQKTSAFVVFHVPL... | null | null | binding of sperm to zona pellucida [GO:0007339]; prevention of polyspermy [GO:0060468] | collagen-containing extracellular matrix [GO:0062023]; egg coat [GO:0035805]; extracellular region [GO:0005576]; plasma membrane [GO:0005886] | acrosin binding [GO:0032190]; structural constituent of egg coat [GO:0035804] | PF00088;PF00100; | 2.60.40.4100;2.60.40.3210; | ZP domain family, ZPB subfamily | PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.; PTM: O-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein 1]: Zona pellucida {ECO:0000250|UniProtKB:P60852}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48829}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP1 ensures the structural integrity of the ... | Rattus norvegicus (Rat) |
O54767 | ZP2_RAT | MARWQRVYWLRSLFFALVTSVNSLSLPQSENPAFPGTLICDKDEVRVEFSSRFDMEKWNPSLVDTFGNEISNCTYALDLEKFILKFPYETCTIKVIGGYQVNIRVQDTNADVSYKDDVHHFFCPAIQAEIHEVSEIVVCMEDLISFSFPQLFSRLADENQNVSEMGWIIKIGNGTRVHTLPLKDAIVQGFNLLIDSQKITLHVPANATGVAHYVQESSYLYTVQLKLLFSSPGQKITFSSQAICAPDLSVACNVTHMSLTIPEFPGKLKSVGFGQRNIPEDQWHANGIDKEATNGLRLHFRKSLLKTKPSEKCPFYQFYF... | null | null | binding of sperm to zona pellucida [GO:0007339]; prevention of polyspermy [GO:0060468] | collagen-containing extracellular matrix [GO:0062023]; egg coat [GO:0035805]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; multivesicular body [GO:0005771]; plasma membrane [GO:0005886] | acrosin binding [GO:0032190]; identical protein binding [GO:0042802]; structural constituent of egg coat [GO:0035804] | PF00100; | 2.60.40.4100;2.60.40.3210; | ZP domain family, ZPA subfamily | PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida. {ECO:0000250|UniProtKB:P20239}.; PTM: Proteolytically cleaved in the N-terminal part by the metalloendopeptidase ASTL exocytosed from cortical granules after fertilization, yielding a N-ter... | SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein 2]: Zona pellucida {ECO:0000250|UniProtKB:P20239}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20239}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP2 may act as a secondary sperm receptor. {... | Rattus norvegicus (Rat) |
O54774 | AP3D1_MOUSE | MALKMVKGSIDRMFDKNLQDLVRGIRNHKEDEAKYISQCIDEIKQELKQDNIAVKANAVCKLTYLQMLGYDISWAAFNIIEVMSASKFTFKRVGYLAASQCFHEGTDVIMLTTNQIRKDLSSPSQYDTGVALTGLSCFVTPDLARDLANDIMTLMSHTKPYIRKKAVLIMYKVFLKYPESLRPAFPRLKEKLEDPDPGVQSAAVNVICELARRNPKNYLSLAPLFFKLMTSSTNNWVLIKIIKLFGALTPLEPRLGKKLIEPLTNLIHSTSAMSLLYECVNTVIAVLISLSSGMPNHSASIQLCVQKLRILIEDSDQNLK... | null | null | anterograde axonal transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; antigen processing and presentation [GO:0019882]; antigen processing and presentation, exogenous lipid antigen via MHC class Ib [GO:0048007]; clathrin-coated vesicle cargo loading, AP-3-mediated [GO:0035654]; endosome to mel... | AP-3 adaptor complex [GO:0030123]; axon [GO:0030424]; axon cytoplasm [GO:1904115]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; postsynapse [GO:0098794]; presynapse [GO:0098793]; presynaptic endosome [GO:0098830]; terminal bouton [GO:00431... | null | PF01602;PF06375; | 1.25.10.10;3.30.450.50; | Adaptor complexes large subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. | null | null | null | null | null | FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes (By similarity).... | Mus musculus (Mouse) |
O54775 | CCN4_MOUSE | MRWLLPWTLAAVAVLRVGNILATALSPTPTTMTFTPAPLEETTTRPEFCKWPCECPQSPPRCPLGVSLITDGCECCKICAQQLGDNCTEAAICDPHRGLYCDYSGDRPRYAIGVCAQVVGVGCVLDGVRYTNGESFQPNCRYNCTCIDGTVGCTPLCLSPRPPRLWCRQPRHVRVPGQCCEQWVCDDDARRPRQTALLDTRAFAASGAVEQRYENCIAYTSPWSPCSTTCGLGISTRISNVNARCWPEQESRLCNLRPCDVDIQLHIKAGKKCLAVYQPEEATNFTLAGCVSTRTYRPKYCGVCTDNRCCIPYKSKTISV... | null | null | bone development [GO:0060348]; cell adhesion [GO:0007155]; glucose homeostasis [GO:0042593]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of fat cell differentiation [GO:0045599]; osteoblast differentiation [GO:0001649]; osteoclast differentiation [GO:0030316]; positive regulatio... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | heparin binding [GO:0008201]; integrin binding [GO:0005178] | PF00007;PF00219;PF19035;PF00093; | 2.10.70.10;2.20.100.10; | CCN family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Downstream regulator in the Wnt/Frizzled-signaling pathway (By similarity). Associated with cell survival. Adheres to skin and melanoma fibroblasts (By similarity). In vitro binding to skin fibroblasts occurs through the proteoglycans, decorin and biglycan (By similarity). Suppresses tumor growth in vivo. {EC... | Mus musculus (Mouse) |
O54781 | SRPK2_MOUSE | MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPLPDPAPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKILEENITSAEASGEQDGEYQPE... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9446799}; | angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; intracellular signal transduction [GO:0035556]; negative regulation of viral genome replication [GO:0045071]; nuclear speck organization [GO:0035063]; positive regulation of cell cycle [GO:0045787]; positive regulation of cell population proliferation [GO:00... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 14-3-3 protein binding [GO:0071889]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family | PTM: Phosphorylation at Thr-485 by PKB/AKT1 enhances its stimulatory activity in triggering cyclin-D1 (CCND1) expression and promoting apoptosis in neurons, which can be blocked by YWHAB. It also enhances its protein kinase activity toward ACIN1 and SRSF2, promotes its nuclear translocation and prevents its proteolytic... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9446799}. Nucleus, nucleoplasm {ECO:0000269|PubMed:9446799}. Nucleus speckle {ECO:0000250|UniProtKB:P78362}. Chromosome {ECO:0000250|UniProtKB:P78362}. Note=Shuttles between the nucleus and the cytoplasm (By similarity). KAT5/TIP60 inhibits its nuclear translocation (... | 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; Evidence={ECO:0000269|PubMed:9446799}; CATALYTIC ... | null | null | null | null | FUNCTION: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing (PubMed:9446799). Promotes ne... | Mus musculus (Mouse) |
O54784 | DAPK3_MOUSE | MSTFRQEDVEDHYEMGEELGSGQFAIVRKCQQKGTGMEYAAKFIKKRRLPSSRRGVSREEIEREVSILREIRHPNIITLHDVFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKHAASPRIKLIDFGIAHRIEAGSEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSSTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKVRRREDGARKPERRRLRAARLREYSLKSHSSMPRNTSYASFERF... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9488481}; | apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cellular response to type II interferon [GO:0071346]; chromatin organization [GO:0006325]; intracellular signal transduction [GO:0035556]; negative regulation of translation [GO:0017148]; positive regulation of apoptotic process [GO:0043065]; pos... | actin filament [GO:0005884]; centrosome [GO:0005813]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane raft [GO:0045121]; nucleus [GO:0005634]; PML body [GO:0016605] | ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; kinase activity [GO:0016301]; leucine zipper domain binding [GO:0043522]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; small GTPase bind... | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, DAP kinase subfamily | PTM: Ubiquitinated. Ubiquitination mediated by the UBE2D3 E3 ligase does not lead to proteasomal degradation, but influences promyelocytic leukemia protein nuclear bodies (PML-NBs) formation in the nucleus. {ECO:0000269|PubMed:18515077}.; PTM: The phosphorylation status is critical for kinase activity, oligomerization ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18515077, ECO:0000269|PubMed:20854903, ECO:0000269|PubMed:9488481}. Nucleus, PML body {ECO:0000269|PubMed:12917339}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O88764}. Chromosome, centromere {ECO:0000250|UniProtKB:O88764}.... | 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; Evidence={ECO:0000269|PubMed:15096528, ECO:000026... | null | null | null | null | FUNCTION: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involve... | Mus musculus (Mouse) |
O54785 | LIMK2_MOUSE | MAALAGDEAWRCRGCGTYVPLSQRLYRTANEAWHGSCFRCSECQESLTNWYYEKDGKLYCHKDYWAKFGEFCHGCSLLMTGPAMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCHNEVVLAPMFERLSTESVQDQLPYSVTLISMPATTECRRGFSVTVESASSNYATTVQVKEVNRMHISPNNRNAIHPGDRILEINGTPVRTLRVEEVEDAIKQTSQTLQLLIEHDPVPQRLDQLRLDARLPPHMQSTGHTLMLSTLDTKENQEGTLRRRSLRRSNSISKSPGPSSPKEPLLLSRDISRSESLRCSSS... | 2.7.11.1 | null | actin cytoskeleton organization [GO:0030036]; astral microtubule organization [GO:0030953]; cornea development in camera-type eye [GO:0061303]; establishment of vesicle localization [GO:0051650]; head development [GO:0060322]; negative regulation of cilium assembly [GO:1902018]; positive regulation of protein localizat... | centrosome [GO:0005813]; cis-Golgi network [GO:0005801]; cytoplasm [GO:0005737]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00412;PF00595;PF07714; | 2.30.42.10;2.10.110.10;1.10.510.10; | Protein kinase superfamily, TKL Ser/Thr protein kinase family | PTM: Phosphorylated on serine and/or threonine residues by ROCK1. {ECO:0000250|UniProtKB:P53671}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P53671}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P53671}.; SUBCELLULAR LOCATION: [Isoform LIMK2a]: Cytoplasm {ECO:0000250|UniProtKB:P53671}. Nucleus {ECO:0000250|UniProtKB:P53671}.; SUBCELLULA... | 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; Evidence={ECO:0000250|UniProtKB:P53671}; Physiolo... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Involved in astral microtubule organization and mitotic spindle orientation during early stages of mitosis by mediating phosphor... | Mus musculus (Mouse) |
O54786 | DFFA_MOUSE | MELSRGASAPDPDDVRPLKPCLLRRNHSRDQHGVAASSLEELRSKACELLAIDKSLTPITLVLAEDGTIVDDDDYFLCLPSNTKFVALACNEKWIYNDSDGGTAWVSQESFEADEPDSRAGVKWKNVARQLKEDLSSIILLSEEDLQALIDIPCAELAQELCQSCATVQGLQSTLQQVLDQREEARQSKQLLELYLQALEKEGNILSNQKESKAALSEELDAVDTGVGREMASEVLLRSQILTTLKEKPAPELSLSSQDLESVSKEDPKALAVALSWDIRKAETVQQACTTELALRLQQVQSLHSLRNLSARRSPLPGEP... | null | null | apoptotic DNA fragmentation [GO:0006309]; chaperone-mediated protein folding [GO:0061077]; negative regulation of apoptotic DNA fragmentation [GO:1902511]; negative regulation of execution phase of apoptosis [GO:1900118]; positive regulation of apoptotic process [GO:0043065]; thymocyte apoptotic process [GO:0070242] | chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | deoxyribonuclease inhibitor activity [GO:0060703]; protein domain specific binding [GO:0019904]; protein folding chaperone [GO:0044183] | PF02017;PF09033; | 3.10.20.10;1.10.1490.10; | null | PTM: Caspase-3 cleaves DFF45 at 2 sites to generate an active factor. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Inhibitor of the caspase-activated DNase (DFF40). | Mus musculus (Mouse) |
O54788 | DFFB_MOUSE | MCAVLRQPKCVKLRALHSACKFGVAARSCQELLRKGCVRFQLPMPGSRLCLYEDGTEVTDDCFPGLPNDAELLLLTAGETWHGYVSDITRFLSVFNEPHAGVIQAARQLLSDEQAPLRQKLLADLLHHVSQNITAETREQDPSWFEGLESRFRNKSGYLRYSCESRIRGYLREVSAYTSMVDEAAQEEYLRVLGSMCQKLKSVQYNGSYFDRGAEASSRLCTPEGWFSCQGPFDLESCLSKHSINPYGNRESRILFSTWNLDHIIEKKRTVVPTLAEAIQDGREVNWEYFYSLLFTAENLKLVHIACHKKTTHKLECDRS... | 3.-.-.- | null | apoptotic chromosome condensation [GO:0030263]; apoptotic DNA fragmentation [GO:0006309]; negative regulation of apoptotic DNA fragmentation [GO:1902511] | chromatin [GO:0000785]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | disordered domain specific binding [GO:0097718]; DNA binding [GO:0003677]; DNA endonuclease activity [GO:0004520]; DNA nuclease activity [GO:0004536]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; nuclease activity [GO:0004518] | PF02017;PF09230; | 3.10.20.10;6.10.140.170; | null | null | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. | null | null | null | null | null | FUNCTION: Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology. | Mus musculus (Mouse) |
O54790 | MAFG_MOUSE | MTTPNKGNKALKVKREPGENGTSLTDEELVTMSVRELNQHLRGLSKEEIIQLKQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQNFARTVARSPVAPARGPLAAGLGPLVPGKVAATSVITIVKSKTDARS | null | null | adult behavior [GO:0030534]; in utero embryonic development [GO:0001701]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell population proliferation [GO:0042127]; regulation of cellular pH [GO:0030641]; regulation of epidermal... | nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF03131; | 1.20.5.170; | BZIP family, Maf subfamily | PTM: Sumoylation at Lys-14 is required for active transcriptional repression. {ECO:0000269|PubMed:16738329}.; PTM: Acetylated in erythroid cells by CREB-binding protein (CBP). Acetylation augments the DNA-binding activity of NFE2, but has no effect on binding NFE2. {ECO:0000250|UniProtKB:O15525}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15525, ECO:0000255|PROSITE-ProRule:PRU00978}. | null | null | null | null | null | FUNCTION: Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves (PubMed:16738329, PubMed:9679061). However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2,... | Mus musculus (Mouse) |
O54794 | AQP7_MOUSE | MAPRSVLETIQSVLQKNMVREFLAEFLSTYVMMVFGLGSVAHMVLGENSGSYLGVNLGFGFGVTMGVHVAGGISGAHMNAAVTFTNCALGRMTWKKFPVYVLGQFLGSFSAAATTYLIFYGAINHFAGGDLLVTGSKATANIFATYLPEYMTLWRGFLDEAFVTGMLQLCLFAITDKKNSPALQGTEPLVIGILVTVLGVSLGMNSGYAINPSRDLPPRLFTFIAGWGKQVFRAGNNWWWVPVVAPLLGAYLGGIVYLGLIHPSIPQDPQRLENFTARDQKVTASYKNAASANISGSVPLEHF | null | null | glycerol transmembrane transport [GO:0015793]; renal water absorption [GO:0070295]; urea transport [GO:0015840]; water transport [GO:0006833] | basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; cell cortex [GO:0005938]; cytoplasmic vesicle membrane [GO:0030659]; lipid droplet [GO:0005811]; plasma membrane [GO:0005886]; ribonucleoprotein complex [GO:1990904] | glycerol channel activity [GO:0015254]; urea channel activity [GO:0015265]; urea transmembrane transporter activity [GO:0015204]; water channel activity [GO:0015250] | PF00230; | 1.20.1080.10; | MIP/aquaporin (TC 1.A.8) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15746100, ECO:0000269|PubMed:17077387, ECO:0000269|PubMed:25643985}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55087}. Cytoplasm, cell cortex {ECO:0000269|PubMed:25643985}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25643985}; Multi-pass membrane p... | null | null | null | null | null | FUNCTION: Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH (PubMed:15591341, PubMed:15746100, PubMed:16009937). The channel is also permeable to urea (By similarity). Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving r... | Mus musculus (Mouse) |
O54799 | NMBR_MOUSE | MPPRSLSNLSFPTEANESELVPEVWEKDFLPDSDGTTAELVIRCVIPSLYLIIISVGLLGNIMLVKIFLTNSAMRNVPNIFISNLAAGDLLLLLTCVPVDASRYFFDEWVFGKLGCKLIPAIQLTSVGVSVFTLTALSADRYRAIVNPMDMQTSGVLLWTSLKAVGIWVVSVLLAVPEAVFSEVARIGSLDNSSFTACIPYPQTDELHPKIHSVLIFLVYFLIPLVIISIYYYHIAKTLIKSAHNLPGEYNEHTKKQMETRKRLAKIVLVFVGCFVFCWFPNHVLYLYRSFNYKEIDPSLGHMIVTLVARVLSFSNSCVN... | null | null | antiviral innate immune response [GO:0140374]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of interleukin-6 production [GO:0032715]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of osteoclast proliferation [GO:0090290]; positive regulation of re... | cytosol [GO:0005829]; plasma membrane [GO:0005886] | bombesin receptor activity [GO:0004946]; neuropeptide receptor activity [GO:0008188] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Receptor for neuromedin-B (By similarity). Contributes to the maintenance of basal sigh rate through signaling in the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (PubMed:26855425). Contributes to the inductio... | Mus musculus (Mouse) |
O54800 | CADH8_RAT | MPERLAETLLDLWTPLIILWITLPSFVYMAPMNQAHVLTTGSPLELSRQSEEMRILNRSKRGWVWNQMFVLEEFSGPEPILVGRLHTDLDPGSKKIKYILSGDGAGTIFQINDITGDIHAIKRLDREEKAEYTLTAQAVDWETNKPLEPPSEFIIKVQDINDNAPEFLNGPYHATVPEMSILGTSVTNVTATDADDPVYGNSAKLVYSILEGQPYFSIEPETAIIKTALPNMDREAKEEYLVVIQAKDMGGHSGGLSGTTTLTVTLTDVNDNPPKFAQSLYHFSVPEDVVLGTAIGRVKANDQDIGENAQSSYDIIDGDG... | null | null | adherens junction organization [GO:0034332]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell morphogenesis [GO:0000902]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction assembly [GO:0007043]; chemical synaptic ... | adherens junction [GO:0005912]; axon terminus [GO:0043679]; catenin complex [GO:0016342]; glutamatergic synapse [GO:0098978]; synaptic cleft [GO:0043083]; synaptic membrane [GO:0097060] | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802] | PF01049;PF00028; | 2.60.40.60;4.10.900.10; | null | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. | Rattus norvegicus (Rat) |
O54803 | P2RX6_MOUSE | MQLQPAGTGNMASAAAAALVSWGFLDYKTEKYVLTRNCRVGVSQRLLQLAVVVYVIGWALLAKKGYQERDLAPQTSVITKLKGVSVTQVKELENRLWDVADFVKPSQGENVFFLVTNFLVTPAQVQGRCPEHPSVPLANCWADEDCPEGETGTYSHGIKTGQCVVFNGTHRTCEIWSWCPVESGAVPRKPLLAQAKNFTLFIKNTVTFSKFNFSRSNALLTWDNTYFKHCLYDPLSSPYCPVFRIGDLVAMAGGDFEDLALLGGAVGISIHWDCNLDTKGSDCCPQYSFQLQQKGYNFRTANHWWAASGVETRSLLKLYG... | null | null | calcium ion transmembrane transport [GO:0070588]; response to ATP [GO:0033198] | cell junction [GO:0030054]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; parallel fiber to Purkinje cell synapse [GO:0098688]; plasma membrane [GO:0005886]; postsynaptic specialization membrane [GO:0099634]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; extracellularly ATP-gated monoatomic cation channel activity [GO:0004931]; protein-containing complex binding [GO:0044877]; purinergic nucleotide receptor activity [GO:0001614] | PF00864; | 1.10.287.940;2.60.490.10; | P2X receptor family | PTM: N-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel. {ECO:0000250}. | Mus musculus (Mouse) |
O54804 | CHKA_MOUSE | MKTKFCTGGEAEPSPLGLLLSCGGNAAPTPGVGQQRDAAGELESKQLGGRTQPLALPPPPPPPLPLPPPPSPPLADEQPEPRTRRRAYLWCKEFLPGAWRGLREDQFHISVIRGGLSNMLFQCSLPDSIASVGDEPRKVLLRLYGAILKMRSCNKEGSEQAQNENEFQGAEAMVLESVMFAILAERSLGPKLFGIFPQGRLEQFIPSRRLDTEELRLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLNQVLRLKFSREARVQQLHKILSYNLPLELENLRSLLQYTRSPVVFCHNDCQEGNILLLEGQENSERR... | 2.7.1.32; 2.7.1.82 | null | CDP-choline pathway [GO:0006657]; cellular response to glucose starvation [GO:0042149]; choline metabolic process [GO:0019695]; ethanolamine metabolic process [GO:0006580]; lipid droplet disassembly [GO:1905691]; phosphatidylcholine biosynthetic process [GO:0006656]; phosphatidylethanolamine biosynthetic process [GO:00... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; lipid droplet [GO:0005811] | ATP binding [GO:0005524]; choline binding [GO:0033265]; choline kinase activity [GO:0004103]; cholinesterase activity [GO:0004104]; ethanolamine kinase activity [GO:0004305]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein tyrosine kinase activity [GO:0004713] | PF01633; | 3.90.1200.10; | Choline/ethanolamine kinase family | PTM: [Isoform 1]: Phosphorylated at Ser-275 by AMPK in response to glucose deprivation, leading to localization to lipid droplets. {ECO:0000250|UniProtKB:P35790}.; PTM: [Isoform 1]: Acetylated by KAT5 at Lys-243 following phosphorylation by AMPK, leading to monomerization and conversion into a tyrosine-protein kinase. ... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35790}.; SUBCELLULAR LOCATION: [Isoform 1]: Lipid droplet {ECO:0000250|UniProtKB:P35790}. Note=Isoform 1 localizes to lipid droplets following phosphorylation by AMPK. {ECO:0000250|UniProtKB:P35790}. | CATALYTIC ACTIVITY: Reaction=ATP + choline = ADP + H(+) + phosphocholine; Xref=Rhea:RHEA:12837, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:295975, ChEBI:CHEBI:456216; EC=2.7.1.32; Evidence={ECO:0000250|UniProtKB:P35790}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12838; Evidence={ECO... | null | PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine from choline: step 1/1. {ECO:0000250|UniProtKB:P35790}.; PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3. {ECO:0000250|UniProtKB:P35790}. | null | null | FUNCTION: Plays a key role in phospholipid biosynthesis by catalyzing the phosphorylation of free choline to phosphocholine, the first step in phosphatidylcholine biosynthesis. Also phosphorylates ethanolamine, thereby contributing to phosphatidylethanolamine biosynthesis. Has higher activity with choline. May contribu... | Mus musculus (Mouse) |
O54814 | CCR3_RAT | MASNEEELKTVVETFETTPYEYEWAPPCEKVSIRELGSWLLPPLYSLVFIVGLLGNMMVVLILIKYRKLQIMTNIYLLNLAISDLLFLFTVPFWIHYVLWNEWGFGHCMCKMLSGLYYLALYSEIFFIILLTIDRYLAIVHAVLALRARTVTFATITSIITWGFAVLAALPEFIFHESQDNFGDLSCSPRYPEGEEDSWKRFHALRMNIFGLALPLLIMVICYSGIIKTLLRCPNKKKHKAIQLIFVVMIVFFIFWTPYNLVLLLSAFHSTFLETSCQQSIHLDLAMQVTEVITHTHCCINPIIYAFVGERFRKHLRLFF... | null | null | angioblast cell migration [GO:0035476]; calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; chemotaxis [GO:0006935]; eosinophil chemotaxis [GO:0048245]; ERK1 and ERK2 cascade [GO:0070371]; immune response [GO:0006955]; inflammatory response [GO:0006954]; mast cell chemotaxis [GO:0002551]; positive re... | cytoplasm [GO:0005737]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615] | C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; chemokine receptor activity [GO:0004950] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Receptor for C-C type chemokine. Binds and responds to a variety of chemokines, including CCL11, CCL26, CCL7, CCL13, RANTES(CCL5) and CCL15. Subsequently transduces a signal by increasing the intracellular calcium ions level. In addition acts as a possible functional receptor for NARS1. {ECO:0000250|UniProtKB... | Rattus norvegicus (Rat) |
O54824 | IL16_MOUSE | MEPHGHSGKSRKSTKFRSISRSLILCNAKTSDDGSSPDEKYPDPFETSLCQGKEGFFHSSMQLADTFEAGLSNIPDLALASDSAQLAAAGSDRGKHCRKMFFMKESSSTSSKEKSGKPEAQSSSFLFPKACHQRTRSNSTSVNPYSAGEIDFPMTKKSAAPTDRQPYSLCSNRKSLSQQLDYPILGTARPTRSLSTAQLGQLSGGLQASVISNIVLMKGQAKGLGFSIVGGKDSIYGPIGIYVKSIFAGGAAAADGRLQEGDEILELNGESMAGLTHQDALQKFKQAKKGLLTLTVRTRLTTPPSLCSHLSPPLCRSLSS... | null | null | induction of positive chemotaxis [GO:0050930]; leukocyte chemotaxis [GO:0030595]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 alpha production [GO:0032730]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-6 production ... | collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular space [GO:0005615]; Flemming body [GO:0090543]; focal adhesion [GO:0005925]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886] | CD4 receptor binding [GO:0042609]; cytokine activity [GO:0005125] | PF00595; | 2.30.42.10; | null | PTM: Synthesized as a chemo-attractant inactive precursor which is proteolytically cleaved by caspase-3 to yield IL-16. {ECO:0000269|PubMed:10479680}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:10479680}. Note=Colocalizes with GRIN2C in neuronal cell bodies and neurites.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4.; FUNCTION: Isoform 1 may act as a scaffolding protein that anchors ion channels... | Mus musculus (Mouse) |
O54825 | BYST_MOUSE | MPKFKVTRGASNREKHAPLAEQILAGNAVRAGTREKRRGREVEEEEEYVGPRLSRRILQQARQQQEELETDHGAGDRSAPPRERATRLGPGLPQDGSDEEDEEWPTLEKAAKMAGVDHQAEVIVDPEDERAIEMFMNKNPPVRRTLADIIMEKLTEKQTEVETVMSEVSGFPMPQLDPRVLEVYRGVREVLCKYRSGKLPKAFKVIPALSNWEQILYVTEPEAWTAAAMYQATRIFASNLKERMAQRFYNLVLLPRVRDDIAEYKRLNFHLYMALKKALFKPGAWFKGILIPLCESGTCTLREAIIVGSIITKCSIPVLH... | null | null | blastocyst formation [GO:0001825]; in utero embryonic development [GO:0001701]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; rRNA processing [GO:0006364]; stem cell proliferation [GO:0072089]; trophectodermal cell differentiation [GO:0001829] | apical part of cell [GO:0045177]; cell projection [GO:0042995]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; preribosome, small subunit precursor [GO:0030688] | snoRNA binding [GO:0030515] | PF05291; | null | Bystin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17242206}. Nucleus, nucleolus {ECO:0000269|PubMed:17242206}. Note=Associated with 40S ribosomal subunits. | null | null | null | null | null | FUNCTION: Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits. {ECO:0000269|PubMed:17055491, ECO:0000269|PubMed:17242206}. | Mus musculus (Mouse) |
O54827 | AT10A_MOUSE | MERELPAAEESASSGWRRPRRRRWEGRTRTVRSNLLPPLGTEDSTIGAPKGERLLMRGCIQHLADNRLKTTKYTLLSFLPKNLFEQFHRLANVYFVFIALLNFVPAVNAFQPGLALAPVLFILAVTAIKDLWEDYSRHRSDHEINHLGCLVFSREEKKYVNRYWKEIRVGDFVRLCCNEIIPADILLLSSSDPDGLCHIETANLDGETNLKRRQVVRGFSELVSEFNPLTFTSVIECEKPNNDLSRFRGYIMHSNGEKAGLHKENLLLRGCTIRNTEAVAGIVIYAGHETKALLNNSGPRYKRSQLERQMNCDVLWCVLL... | 7.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2Q0}; | phospholipid translocation [GO:0045332]; positive regulation of membrane tubulation [GO:1903527] | endoplasmic reticulum membrane [GO:0005789]; phospholipid-translocating ATPase complex [GO:1990531]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; glycosylceramide flippase activity [GO:0140351]; magnesium ion binding [GO:0000287]; phosphatidylcholine flippase activity [GO:0140345]; phosphatidylcholine floppase activity [GO:0090554... | PF13246;PF16212;PF16209; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily | PTM: Autophosphorylated at the conserved aspartate of the P-type ATPase signature sequence. {ECO:0000250|UniProtKB:O94823}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60312}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O60312}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O60312}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not that of TMEM30B. {ECO:0000250|UniProtKB:O60312... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:O60312}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate; Xref=R... | null | null | null | null | FUNCTION: Catalytic component of P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine (PC) from the outer to the inner leaflet of the plasma membrane. Initiates inward plasma membrane bending and recruitment of Bin/amphiphysin/Rvs (BAR) domain-containing prot... | Mus musculus (Mouse) |
O54828 | RGS9_MOUSE | MTIRHQGQQYRPRMAFLQKIEALVKDMQNPETGVRMHNQRVLVTSVPHAMTGGDVLQWITQRLWISNLEAQNLGNFIVKYGYIYPLQDPKNLILKPDSSLYRFQTPYFWPTQQWPAEDTDYAIYLAKRNIKKKGILEEYEKENYDFLNKKINYKWDFVIMQAKEQYRTGKERNKADRYALDCQEKAYWLVHRSPPGMNNVLDYGLDRVTNPNEVKKQTVTAVRKEIMYYQQALMRSTVKSSVSLGGIVKYSEQFSSNDAIMSGCLPSNPWITDDTQFWDLNAKLVEIPTKMRVERWAFNFSELIRDPKGRQSFQYFLKKE... | null | null | dark adaptation [GO:1990603]; dopamine receptor signaling pathway [GO:0007212]; G protein-coupled receptor signaling pathway [GO:0007186]; intracellular signal transduction [GO:0035556]; light adaption [GO:0036367]; negative regulation of signal transduction [GO:0009968]; nervous system development [GO:0007399]; regula... | cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734] | GTPase activator activity [GO:0005096] | PF00610;PF00631;PF00615;PF18148; | 1.10.1240.60;1.10.167.10;4.10.260.10;1.10.10.10; | null | PTM: Retinal isoform 1 is light-dependent phosphorylated at 'Ser-475'. Phosphorylation is decreased by light exposition. Interaction with RGS9BP is decreased when isoform 1 is phosphorylated at 'Ser-475'. {ECO:0000269|PubMed:11292825}. | SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Peripheral membrane protein. Note=Isoform 1 is targeted to the membrane via its interaction with RGS9BP. | null | null | null | null | null | FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to GNAT1. Involved in phototransduction; key element in the recovery phase of visual transduction. | Mus musculus (Mouse) |
O54829 | RGS7_MOUSE | MAQGNNYGQTSNGVADESPNMLVYRKMEDVIARMQDEKNGIPIRTVKSFLSKIPSVFSGSDIVQWLIKNLTIEDPVEALHLGTLMAAHGYFFPISDHVLTLKDDGTFYRFQTPYFWPSNCWEPENTDYAVYLCKRTMQNKARLELADYEAESLARLQRAFARKWEFIFMQAEAQAKVDKKRDKIERKILDSQERAFWDVHRPVPGCVNTTEVDIKKSSRMRNPHKTRKSVYGLQNDIRSHSPTHTPTPETKPPTEDELHQQIKYWQIQLDRHRLKMSKVADSLLSYTEQYVEYDPFLVPPDPSNPWLSDDTTFWELEASK... | null | null | G protein-coupled receptor signaling pathway [GO:0007186]; intracellular signal transduction [GO:0035556]; negative regulation of G protein-coupled receptor signaling pathway [GO:0045744]; positive regulation of potassium ion transmembrane transport [GO:1901381]; regulation of G protein-coupled receptor signaling pathw... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite terminus [GO:0044292]; glutamatergic synapse [GO:0098978]; neuron projection [GO:0043005]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynapse [GO:0098793]; protein-containing complex [GO... | G-protein alpha-subunit binding [GO:0001965]; G-protein beta-subunit binding [GO:0031681]; GTPase activator activity [GO:0005096] | PF00610;PF00631;PF00615;PF18148; | 1.10.1240.60;1.10.167.10;4.10.260.10;1.10.10.10; | null | PTM: Palmitoylated. {ECO:0000250|UniProtKB:O46470}.; PTM: Ubiquitinated, leading to rapid proteasomal degradation. {ECO:0000250|UniProtKB:P49802}.; PTM: Phosphorylation and subsequent interaction with 14-3-3 proteins inhibits GAP activity. {ECO:0000250|UniProtKB:P49802}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49802}. Cytoplasm {ECO:0000250|UniProtKB:P49802}. Cell membrane {ECO:0000269|PubMed:22689652, ECO:0000269|PubMed:25792749, ECO:0000269|PubMed:30546127}. Membrane {ECO:0000250|UniProtKB:P49802}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49802}; C... | null | null | null | null | null | FUNCTION: GTPase activator component of the RGS7-GNB5 complex that regulates G protein-coupled receptor signaling cascades (PubMed:25792749). The RGS7-GNB5 complex acts as an inhibitor signal transduction by promoting the GTPase activity of G protein alpha subunits, such as GNAO1, thereby driving them into their inacti... | Mus musculus (Mouse) |
O54833 | CSK22_MOUSE | MPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGQDNYDQLVRIAKVLGTDELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAM... | 2.7.11.1 | null | apoptotic process [GO:0006915]; cell cycle [GO:0007049]; double-strand break repair [GO:0006302]; negative regulation of ubiquitin-dependent protein catabolic process [GO:2000059]; phosphorylation [GO:0016310]; regulation of cell cycle [GO:0051726]; regulation of chromosome separation [GO:1905818]; spermatogenesis [GO:... | acrosomal vesicle [GO:0001669]; chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634]; PcG protein complex [GO:0031519]; protein kinase CK2 complex [GO:0005956] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CK2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28355567}. Cytoplasm {ECO:0000269|PubMed:28355567}. Note=Interaction with SIRT6 prevents translocation into the nucleus. {ECO:0000269|PubMed:28355567}. | 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: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcript... | Mus musculus (Mouse) |
O54834 | RHG06_MOUSE | MSAQSLLHSVFSCSSPASGGTASAKGFSKRKLRQTRSLDPALIGGCGSEMGAEGGLRGSTVSRLHSPQLLAEGLGSRLASSPRSQHLRATRFQTPRPLCSSFSTPSTPQEKSPSGSFHFDYEVPLSRSGLKKSMAWDLPSVLAGSGSASSRSPASILSSSGGGPNGIFSSPRRWLQQRKFQPPPNSRSHPYVVWRSEGDFTWNSMSGRSVRLRSVPIQSLSELERARLQEVAFYQLQQDCDLGCQITIPKDGQKRKKSLRKKLDSLGKEKNKDKEFIPQAFGMPLSQVIANDRAYKLKQDLQREEQKDASSDFVSSLLPF... | null | null | actin filament organization [GO:0007015]; focal adhesion assembly [GO:0048041]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of stress fiber assembly [GO:0051497]; positive regulation of GTPase activity [GO:0043547]; signal transduction [GO:0007165] | actin cytoskeleton [GO:0015629]; cytosol [GO:0005829] | GTPase activator activity [GO:0005096]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274]; SH3 domain binding [GO:0017124] | PF00620; | 1.10.555.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing th... | Mus musculus (Mouse) |
O54835 | SMAD9_RAT | MHPSTPISSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGAMDELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVETPVLPPVLVPRHSEYNPQLSLLAKFRSASLHSEPLMPHNATYPDSFQQSLGPAPPSSPGHVFPQSPCPTSYPQSPGSPSESDSPYQHSDFRPVCYEEPLHWCSVAYYELNNRVGETFQASSRSVLIDGFTDPSNNRNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECVSDSSIFV... | null | null | anatomical structure morphogenesis [GO:0009653]; BMP signaling pathway [GO:0030509]; bone development [GO:0060348]; cartilage development [GO:0051216]; cell differentiation [GO:0030154]; cellular response to organic cyclic compound [GO:0071407]; hindbrain development [GO:0030902]; midbrain development [GO:0030901]; Mul... | cytoplasm [GO:0005737]; heteromeric SMAD protein complex [GO:0071144]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; I-SMAD binding [GO:0070411]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF03165;PF03166; | 2.60.200.10;3.90.520.10; | Dwarfin/SMAD family | PTM: Phosphorylated on serine by BMP (bone morphogenetic proteins) type 1 receptor kinase (By similarity). Phosphorylated by activin type I receptor-like kinase-2 (ALK-2). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with SMAD4 (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD9 is a receptor-regulated SMAD (R-SMAD) (By similarity). Has been shown to be activated by activin type I receptor-like kinase-2 (ALK-2) which stimulates heteromerization between SMAD9 and SMAD4. ALK-2 binds T... | Rattus norvegicus (Rat) |
O54838 | DUS5_RAT | MKVTSLDGRRLRKMLRKEAEARCVVLDCRPYLAFAASSVRGSLNVNLNSVVLRRARGGAVSARYVLADEAARARLLQEGGGGVAAVVVLDQGSRHWQKLREESAARVVLTSLLACLSAGPRVYFLKGGYETFYSQYPECCVDAKPISQEKLEGERGLLSQCGKPILSVAYRPAYDQGGPVEILPFLYLGSAYHASKCEFLANLHITALLNVSRRTSEACTTHLHYKWIPVEDSHTADISSHFQEAIDFIDCVREEGGKVLVHCEAGVSRSPTICMAYLMKTKQFRLKEAFEYIKQRRSVVSPNFGFMGQLLQYESEILPS... | 3.1.3.16; 3.1.3.48 | null | dephosphorylation [GO:0016311]; endoderm formation [GO:0001706]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of vasoconstriction [GO:0045906]; peptidyl-threonine dephosphorylation [GO:0035970]; peptidyl-tyrosine dephosphorylation... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | MAP kinase tyrosine phosphatase activity [GO:0033550]; MAP kinase tyrosine/serine/threonine phosphatase activity [GO:0017017]; myosin phosphatase activity [GO:0017018]; phosphatase activity [GO:0016791]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; protein tyrosine/threonine phosphatase activity... | PF00782;PF00581; | 3.90.190.10;3.40.250.10; | Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:Q16690, ECO:0000255|PROSITE-ProRu... | null | null | null | null | FUNCTION: Dual specificity protein phosphatase; active with phosphotyrosine, phosphoserine and phosphothreonine residues. The highest relative activity is toward ERK1. {ECO:0000250|UniProtKB:Q16690}. | Rattus norvegicus (Rat) |
O54839 | EOMES_MOUSE | MQLGEQLLVSSVNLPGAHFYSLESARGGGGGGGGGGGGGGGSVSLLPGAAPSPQRLDLDKASKKFPGSLPCQAGSAEPAGAGAGAPAAMLSDADAGDTFGSTSAVAKPGPPDGRKGSPCAEEELPSAATAAATARYSMDSLSSERYYLPSPGPQGSELAAPCSLFQYPAAAGAAHGPVYPASNGARYPYGSMLPPGGFPAAVCPPARAQFGPAAGSGSGAGSSGGGAGGPGAYPYGQGSPLYGPYAGTSAAGSCGGLGGLGVPGSGFRAHVYLCNRPLWLKFHRHQTEMIITKQGRRMFPFLSFNINGLNPTAHYNVFVE... | null | null | adaptive immune response [GO:0002250]; anatomical structure morphogenesis [GO:0009653]; astrocyte differentiation [GO:0048708]; blastocyst development [GO:0001824]; cardioblast differentiation [GO:0010002]; CD8-positive, alpha-beta T cell differentiation involved in immune response [GO:0002302]; cell differentiation [G... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227];... | PF00907;PF16176; | 2.60.40.820; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Functions as a transcriptional activator playing a crucial role during development. Functions in trophoblast differentiation and later in gastrulation, regulating both mesoderm delamination and endoderm specification. Plays a role in brain development being required for the specification and the proliferation... | Mus musculus (Mouse) |
O54842 | NUPR1_RAT | MATLPPTAHTSQQPVNIEDEDGILDEYDQYSLAQSYVVGGGRKGRTKREAAANTNRPSPGGHERKLLTKFQNSERKKAWR | null | null | acute inflammatory response [GO:0002526]; fibroblast apoptotic process [GO:0044346]; fibroblast proliferation [GO:0048144]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; male gonad development [GO:0008584]; negative regulation of apoptotic process [GO:0043066]; nega... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; protein-DNA complex [GO:0032993] | acetyltransferase activator activity [GO:0010698]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; transcription coactivator activity [GO:0003713] | PF10195; | null | NUPR family | PTM: Phosphorylated. Phosphorylation promotes DNA-binding activity. {ECO:0000250|UniProtKB:O60356}.; PTM: Acetylated. {ECO:0000250|UniProtKB:O60356}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O60356}. Cytoplasm {ECO:0000250|UniProtKB:O60356}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O60356}. | null | null | null | null | null | FUNCTION: Transcription regulator that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Thereby participates in regulation of many process namely cell-cycle, apoptosis, autophagy and DNA repair responses (PubMed:20... | Rattus norvegicus (Rat) |
O54851 | CXD2_MOUSE | MGEWTILERLLEAAVQQHSTMIGRILLTVVVIFRILIVAIVGETVYDDEQTMFVCNTLQPGCNQACYDRAFPISHIRYWVFQIIMVCTPSLCFITYSVHQSAKQRERRYSTVFLALDRDPAESIGGPGGTGGGGSGGSKREDKKLQNAIVNGVLQNTETTSKETEPDCLEVKELTPHPSGLRTAARSKLRRQEGISRFYIIQVVFRNALEIGFLVGQYFLYGFSVPGLYECNRYPCIKEVECYVSRPTEKTVFLVFMFAVSGICVVLNLAELNHLGWRKIKLAVRGAQAKRKSVYEIRNKDLPRVSVPNFGRTQSSDSAY... | null | null | cell-cell signaling [GO:0007267]; chemical synaptic transmission [GO:0007268]; neuronal action potential [GO:0019228]; visual perception [GO:0007601] | connexin complex [GO:0005922]; gap junction [GO:0005921]; synapse [GO:0045202] | gap junction channel activity [GO:0005243] | PF00029; | 1.20.1440.80; | Connexin family, Delta-type subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. | null | null | null | null | null | FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. | Mus musculus (Mouse) |
O54852 | KCNH7_RAT | MPVRRGHVAPQNTFLGTIIRKFEGQNKKFIIANARVQNCAIIYCNDGFCEMTGFSRPDVMQKPCTCDFLHGPETKRHDIAQIAQALLGSEERKVEVTYYHKNGSTFICNTHIIPVKNQEGVAMMFIINFEYVTDEDNAASPERVNPILPVKSVNRKLFGFKFPGLRVLTYRKQSLPQEDPDVVVIDSSKHSDDSVAMKHFKSPTKESCSPSEADDTKALIQPSQCSPLVNISGPLDHSSPKRQWDRLYPDMLQSSSQLTHSRSRESLCSIRRASSVHDIEGFNVHPKNIFRDRHASEDNGRNVKGPFNHIKSSLLGSTSD... | null | null | circadian rhythm [GO:0007623]; membrane repolarization during action potential [GO:0086011]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of membrane potential [GO:0042391] | monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886] | inward rectifier potassium channel activity [GO:0005242]; potassium channel activity [GO:0005267]; protein-containing complex binding [GO:0044877]; voltage-gated potassium channel activity [GO:0005249] | PF00027;PF00520;PF13426; | 1.10.1200.260;1.10.287.70;2.60.120.10;3.30.450.20; | Potassium channel family, H (Eag) (TC 1.A.1.20) subfamily, Kv11.3/KCNH7 sub-subfamily | null | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel. Channel properties may be modulated by cAMP and subunit assembly. {ECO:0000269|PubMed:11212207}. | Rattus norvegicus (Rat) |
O54853 | KCNH6_RAT | MPVRRGHVAPQNTYLDTIIRKFEGQSRKFLIANAQMENCAIIYCNDGFCELFGYSRVEVMQRPCTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDGAVIMFILNFEDLAQLLAKSSSRSLTQRLLSHSFLGSEGSHSRPSGQGPGPGRGKYRTVSQIPQFTLNFVEFNLEKHRSGSTTEIEIIAPHKVVERTQNVTEKVTQVLSLGADVLPEYKLQAPRIHRGTILHYSPFKAVWDWLILLLVIYTAVFTPYSAAFLLSDQDESQRGTCGYTCSPLTVVDLIVDIMFVVDIVINFR... | null | null | membrane repolarization during cardiac muscle cell action potential [GO:0086013]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307] | monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886] | inward rectifier potassium channel activity [GO:0005242]; potassium channel activity [GO:0005267]; protein-containing complex binding [GO:0044877]; voltage-gated potassium channel activity [GO:0005249] | PF00027;PF00520;PF13426; | 1.10.1200.260;1.10.287.70;2.60.120.10;3.30.450.20; | Potassium channel family, H (Eag) (TC 1.A.1.20) subfamily, Kv11.2/KCNH6 sub-subfamily | null | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a slowly activating, rectifying current. Channel properties may be modulated by cAMP and subunit assembly. | Rattus norvegicus (Rat) |
O54857 | PTEN_RAT | MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKLMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTL... | 3.1.3.-; 3.1.3.16; 3.1.3.48; 3.1.3.67 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O08586}; | adult behavior [GO:0030534]; angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; B cell proliferation [GO:0042100]; brain morphogenesis [GO:0048854]; canonical Wnt signaling pathway [GO:0060070]; cardiac muscle tissue development [GO:0048738]; cell migration [GO:0016477]; cell motility [GO:0048870]; cell populat... | apical plasma membrane [GO:0016324]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; myelin sheath adaxonal region [GO:0035749]; neuron projection [GO:0043005]; nucleus [GO:0005634]; plasma membrane [GO:0005886];... | anaphase-promoting complex binding [GO:0010997]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; inositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity [GO:0030351]; inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity [GO:0051717]; ionotropic glutamate receptor binding [GO:0035255]; myos... | PF10409;PF00102; | 2.60.40.1110;3.90.190.10; | PTEN phosphatase protein family | PTM: Constitutively phosphorylated by CK2 under normal conditions. Phosphorylation results in an inhibited activity towards PIP3. Phosphorylation can both inhibit or promote PDZ-binding. Phosphorylation at Tyr-336 by FRK/PTK5 protects this protein from ubiquitin-mediated degradation probably by inhibiting its binding t... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O08586}. Nucleus {ECO:0000250|UniProtKB:O08586}. Nucleus, PML body {ECO:0000250|UniProtKB:P60484}. Synapse, synaptosome {ECO:0000250|UniProtKB:O08586}. Cell projection, dendritic spine {ECO:0000269|PubMed:20628354}. Postsynaptic density {ECO:0000269|PubMed:20628354... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:25017, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57836, ChEBI:CHEBI:58456; EC=3.1.3.67; Evidence={ECO:0000... | null | null | null | null | FUNCTION: Dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also functions as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring of PtdIns(3,4,5)P3/phosphatidylinositol 3,4,5-trisphosphate, PtdIns(3,4)P2/phosphatidylinosito... | Rattus norvegicus (Rat) |
O54861 | SORT_RAT | MERPRGAADGLLRWPLGLLLLLQLLPPAAVGQDRLDAPPPPAPPLLRWAGPVGVSWGLRAAAPGGPVPRAGRWRRGAPAEDQDCGRLPDFIAKLTNNTHQHVFDDLSGSVSLSWVGDSTGVILVLTTFQVPLVIVSFGQSKLYRSEDYGKNFKDITNLINNTFIRTEFGMAIGPENSGKVILTAEVSGGSRGGRVFRSSDFAKNFVQTDLPFHPLTQMMYSPQNSDYLLALSTENGLWVSKNFGEKWEEIHKAVCLAKWGPNNIIFFTTHVNGSCKADLGALELWRTSDLGKTFKTIGVKIYSFGLGGRFLFASVMADKD... | null | null | endocytosis [GO:0006897]; endosome to lysosome transport [GO:0008333]; endosome transport via multivesicular body sorting pathway [GO:0032509]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; G protein-coupled receptor signaling pathway [GO:0007186]; glucose import [GO:0046323]; Golgi to ... | cell surface [GO:0009986]; cerebellar climbing fiber to Purkinje cell synapse [GO:0150053]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; dendrite [GO:0030425]; early endosome [GO:0005769]; endop... | enzyme binding [GO:0019899]; G protein-coupled neurotensin receptor activity [GO:0016492]; nerve growth factor binding [GO:0048406]; nerve growth factor receptor activity [GO:0010465]; neurotensin receptor activity, non-G protein-coupled [GO:0030379]; retromer complex binding [GO:1905394] | PF15902;PF15901; | 2.10.70.80;3.30.60.270;2.130.10.10; | VPS10-related sortilin family, SORT1 subfamily | PTM: The N-terminal propeptide is cleaved by furin and possibly other homologous proteases. {ECO:0000250|UniProtKB:Q99523}.; PTM: Phosphorylation at Ser-819 facilitates the interaction with GGA1. {ECO:0000250|UniProtKB:Q99523}.; PTM: Palmitoylated. Undergoes cysteine S-palmitoylation which promotes the partitioning of ... | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Endosome membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Endoplasmic reticulum membrane {ECO:000025... | null | null | null | null | null | FUNCTION: Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Lysosomal proteins bind specifically to the receptor i... | Rattus norvegicus (Rat) |
O54862 | MBTP2_CRIGR | MIPVSLVVVVVGGWTAVYLADLVLKSSVYFKHSYEDWLEKNGLSISPFHIRWQTSVFNRAFYSWGRRKARMLYQWFNFGMVFGVIAMFSSFFLLGKTLMQTLAQMMADSPSSSSSSSSSSSSSSSSSIHNEQVLQVVVPGINLPVNQLTYFFAAVLISGVVHEIGHGIAAIREQVRFNGFGIFLFIIYPGAFVDLFTTHLQLISPVQQLRIFCAGIWHNFVLALLGILALVLLPVILLPFYYTGVGVLITEVAEDSPAIGPRGLFVGDLVTHLQDCPVTNVQDWNECLDTIAYEPQIGYCISASTLQQLSFPVRAYKRLD... | 3.4.24.85 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O43462}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O43462}; | bone maturation [GO:0070977]; cholesterol metabolic process [GO:0008203]; membrane protein intracellular domain proteolysis [GO:0031293]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein maturation [GO:0051604]; regulation of respon... | cytoplasm [GO:0005737]; Golgi membrane [GO:0000139] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription regulator activator activity [GO:0140537] | PF02163; | 2.30.42.10; | Peptidase M50A family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O43462}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:O43462}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O43462}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site 477-DRSRILL-|... | null | null | null | null | FUNCTION: Zinc metalloprotease that mediates intramembrane proteolysis of proteins such as ATF6, ATF6B, SREBF1/SREBP1 and SREBF2/SREBP2. Catalyzes the second step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2: cleaves SREBPs within the first tra... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
O54863 | TSSK2_MOUSE | MDDAAVLRKKGYIVGINLGKGSYAKVKSAYSERLKFNVAVKIIDRKKTPTDFVERFLPREMDILATVNHRSIIKTYEIFETSDGRIYIVMELGVQGDLLEFIKCRGALHEDVARKMFRQLSSAVKYCHDLDVVHRDLKCENLLLDKDFNIKLSDFGFSKRCLRDGSGRIVLSKTFCGSAAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSDIKKMLRIQKEHRVDFPRSKNLTGECKDLIYRILQPDVNRRLHIDEILSHSWLQPPKPKAMSSASFKREGEGKYRADCKLDTRPGSRPEHRPDHKLATKPQ... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23599433}; Note=Mg(2+) and Mn(2+) were both present in the kinase buffer but Mg(2+) is likely to be the in vivo cofactor. {ECO:0000305|PubMed:23599433}; | intracellular signal transduction [GO:0035556]; peptidyl-serine phosphorylation [GO:0018105]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; spermatid development [GO:0007286] | acrosomal vesicle [GO:0001669]; centriole [GO:0005814]; cytoplasm [GO:0005737] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q96PF2}.; PTM: Ubiquitinated; HSP90 activity negatively regulates ubiquitination and degradation. {ECO:0000269|PubMed:23599433}. | SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasmic vesicle, secretory vesicle, acrosome. Note=Present in the cytoplasm of elongating spermatids. In spermatozoa, localizes in the equatorial segment, neck, the midpiece and in a specific sperm head c... | 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; Evidence={ECO:0000269|PubMed:23599433}; CATALYTIC... | null | null | null | null | FUNCTION: Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates 'Ser-281' of TSKS and SPAG16. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure aro... | Mus musculus (Mouse) |
O54864 | SUV91_MOUSE | MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGVSKKNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHKDLERELVRRHRRSKPPRHLDPNLANYLVQKAKQRRALQRWEQELNAKRSHLGRITVENEVDLDGPPRSFVYINEYRVGEGITLNQVAVGCECQDCLLAPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVVQKGIRYDLCIFRTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISH... | 2.1.1.355 | null | blastocyst hatching [GO:0001835]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to glucose starvation [GO:0042149]; cellular response to hypoxia [GO:0071456]; chromosome organization [GO:0051276]; circadian rhythm [GO:0007623]; determination of adult lifespan [GO:0008340]; DNA damage res... | chromatin silencing complex [GO:0005677]; chromosome, centromeric region [GO:0000775]; eNoSc complex [GO:0061773]; heterochromatin [GO:0000792]; nuclear lamina [GO:0005652]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | histone H3K9 methyltransferase activity [GO:0046974]; histone H3K9 trimethyltransferase activity [GO:0140949]; histone H3K9me2 methyltransferase activity [GO:0140947]; protein methyltransferase activity [GO:0008276]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; transcrip... | PF00385;PF05033;PF00856; | 2.40.50.40;2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, Suvar3-9 subfamily | PTM: Phosphorylated on serine residues, and to a lesser degree, on threonine residues. {ECO:0000250}.; PTM: Acetylated at Lys-266, leading to inhibition of enzyme activity. SIRT1-mediated deacetylation relieves this inhibition (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the DCX(DCAF13) E3 ubiquitin ligase co... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43463}. Nucleus lamina {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin. | CATALYTIC ACTIVITY: Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:... | null | null | null | null | FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functio... | Mus musculus (Mouse) |
O54865 | GCYB1_MOUSE | MYGFVNHALELLVIRNYGPEVWEDIKKEAQLDEEGQFLVRIIYDDSKTYDLVAAASKVLNLNAGEILQMFGKMFFVFCQESGYDTILRVLGSNVREFLQNLDALHDHLATIYPGMRAPSFRCTDAEKGKGLILHYYSEREGLQDIVIGIIKTVAQQIHGTEIDMKVIQQRNEECDHTQFLIEEKESKEEDFYEDLDRFEENGTQESRISPYTFCKAFPFHIIFDRNLVVTQCGNAIYRVLPQLQPGNCSLLSVFSLVRPHIDISFHGILSHINTVFVLRSKEGLLDVEKLECEDELTGAEISCLRLKGQMIYLPEADSIL... | 4.6.1.2 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P16068}; Note=Binds 1 or 2 heme groups per heterodimer. Heme is required for responding to nitric oxide, but not for catalytic activity. {ECO:0000250|UniProtKB:P16068}; | cellular response to nitric oxide [GO:0071732]; cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; nitric oxide-cGMP-mediated signaling pathway [GO:0038060]; response to oxygen levels [GO:0070482]; trans-synaptic signaling by nitric oxide, modulating synaptic transmission [GO:0099555] | cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; guanylate cyclase complex, soluble [GO:0008074]; presynaptic active zone [GO:0048786]; presynaptic active zone cytoplasmic component [GO:0098831]; protein-containing complex [GO:0032991] | adenylate cyclase activity [GO:0004016]; cytidylate cyclase activity [GO:0047805]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; heme binding [GO:0020037]; Hsp90 protein binding [GO:0051879]; ion binding [GO:0043167]; metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877] | PF00211;PF07700;PF07701; | 6.10.250.780;3.90.1520.10;3.30.450.260;3.30.70.1230; | Adenylyl cyclase class-4/guanylyl cyclase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16068}. | CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:Q02153}; | null | null | null | null | FUNCTION: Mediates responses to nitric oxide (NO) by catalyzing the biosynthesis of the signaling molecule cGMP. {ECO:0000250|UniProtKB:P16068}. | Mus musculus (Mouse) |
O54874 | MRCKA_RAT | MSGEVRLRQLEQFILDGPAQTNGQCFSVETLLDILICLYDECNNSPLRREKNILEYLEWAKPFTSKVKQMRLHREDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSKWITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFEDRLPEEMARFYLAEMVIAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAVGTPDYISPEILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFPTQVTDVSENAKDLIRR... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9418861}; | actin cytoskeleton organization [GO:0030036]; actomyosin structure organization [GO:0031032]; cell migration [GO:0016477]; cytoskeleton organization [GO:0007010]; microtubule cytoskeleton organization [GO:0000226]; nuclear migration [GO:0007097]; protein phosphorylation [GO:0006468]; regulation of small GTPase mediated... | actomyosin [GO:0042641]; cell leading edge [GO:0031252]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; lamellipodium [GO:0030027] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00130;PF00780;PF08826;PF15796;PF00069;PF00433; | 1.10.287.1490;1.20.5.340;3.30.60.20;2.30.29.30;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, DMPK subfamily | PTM: Proteolytically cleaved by caspases upon apoptosis induction. The cleavage at Asp-478 by CASP3 increases its kinase activity (in vitro). {ECO:0000250|UniProtKB:Q5VT25}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9418861}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q3UU96}. Note=Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction. This concentration is PH-domain dependent (PubMed... | 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; Evidence={ECO:0000269|PubMed:9418861}; CATALYTIC ... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration (PubMed:9418861). Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12A and MYL9/MLC2 (PubMed:21457715). In concert with... | Rattus norvegicus (Rat) |
O54879 | HMGB3_MOUSE | MAKGDPKKPKGKMSAYAFFVQTCREEHKKKNPEVPVNFAEFSKKCSERWKTMSSKEKSKFDEMAKADKVRYDREMKDYGPAKGGKKKKDPNAPKRPPSGFFLFCSEFRPKIKSTNPGISIGDVAKKLGEMWNNLSDNEKQPYVTKAAKLKEKYEKDVADYKSKGKFDGAKGPAKVARKKVEEEEEEEEEEEEEEEEEEDE | null | null | DNA geometric change [GO:0032392]; innate immune response [GO:0045087]; negative regulation of B cell differentiation [GO:0045578]; negative regulation of myeloid cell differentiation [GO:0045638]; regulation of transcription by RNA polymerase II [GO:0006357] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA binding, bending [GO:0008301]; four-way junction DNA binding [GO:0000400]; RNA binding [GO:0003723] | PF00505;PF09011; | 1.10.30.10; | HMGB family | PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-104 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB3 (HMGB3C23hC45hC104h), 2- disulfide HMGB3 (HMGB... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40618, ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:19890330}. | null | null | null | null | null | FUNCTION: Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. Associates with chromatin and binds DNA with a preference for non-canonical DNA structures such as single-stranded DNA. Can bend DNA and enhance DNA flexibility by looping thus providing a mecha... | Mus musculus (Mouse) |
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