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RAB15_RAT
ID   RAB15_RAT               Reviewed;         212 AA.
AC   P35289; Q504L6;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Ras-related protein Rab-15;
GN   Name=Rab15;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=1313420; DOI=10.1016/s0021-9258(18)42619-1;
RA   Elferink L.A., Anzai K., Scheller R.H.;
RT   "Rab15, a novel low molecular weight GTP-binding protein specifically
RT   expressed in rat brain.";
RL   J. Biol. Chem. 267:5768-5775(1992).
RN   [2]
RP   ERRATUM OF PUBMED:1313420.
RX   PubMed=1429617; DOI=10.1016/s0021-9258(18)41727-9;
RA   Elferink L.A., Anzai K., Scheller R.H.;
RL   J. Biol. Chem. 267:22693-22693(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May act in concert with RAB3A in regulating aspects of
CC       synaptic vesicle membrane flow within the nerve terminal.
CC   -!- SUBUNIT: The GTP bound form of RAB15 interacts with REP15. Interacts
CC       (GTP-bound form) with MICAL1, MICAL3, MICALCL, EHBP1 and EHBP1L1.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in neural tissues.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; M83679; AAA41995.1; -; mRNA.
DR   EMBL; BC094954; AAH94954.1; -; mRNA.
DR   PIR; F42148; F42148.
DR   RefSeq; NP_942044.1; NM_198749.2.
DR   AlphaFoldDB; P35289; -.
DR   SMR; P35289; -.
DR   BioGRID; 256132; 1.
DR   STRING; 10116.ENSRNOP00000010043; -.
DR   iPTMnet; P35289; -.
DR   PhosphoSitePlus; P35289; -.
DR   jPOST; P35289; -.
DR   PaxDb; P35289; -.
DR   PRIDE; P35289; -.
DR   Ensembl; ENSRNOT00000010043; ENSRNOP00000010043; ENSRNOG00000007364.
DR   GeneID; 299156; -.
DR   KEGG; rno:299156; -.
DR   UCSC; RGD:735172; rat.
DR   CTD; 376267; -.
DR   RGD; 735172; Rab15.
DR   eggNOG; KOG0078; Eukaryota.
DR   GeneTree; ENSGT00940000157848; -.
DR   HOGENOM; CLU_041217_23_1_1; -.
DR   InParanoid; P35289; -.
DR   OMA; ACTNFNI; -.
DR   OrthoDB; 1149105at2759; -.
DR   PhylomeDB; P35289; -.
DR   TreeFam; TF314097; -.
DR   Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR   PRO; PR:P35289; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000007364; Expressed in frontal cortex and 17 other tissues.
DR   Genevisible; P35289; RN.
DR   GO; GO:0005929; C:cilium; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0010008; C:endosome membrane; ISO:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0032593; C:insulin-responsive compartment; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; TAS:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR   GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; TAS:RGD.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IBA:GO_Central.
DR   GO; GO:0007269; P:neurotransmitter secretion; TAS:RGD.
DR   GO; GO:1903307; P:positive regulation of regulated secretory pathway; ISO:RGD.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR   GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR   GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR   GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR   CDD; cd04117; Rab15; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041826; Rab15.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..212
FT                   /note="Ras-related protein Rab-15"
FT                   /id="PRO_0000121190"
FT   BINDING         15..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         63..67
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         121..124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         212
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           210
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           212
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   212 AA;  24283 MW;  04817DDA66CADE12 CRC64;
     MAKQYDVLFR LLLIGDSGVG KTCLLCRFTD NEFHSSHIST IGVDFKMKTI EVDGIKVRIQ
     IWDTAGQERY QTITKQYYRR AQGIFLVYDI SSERSYQHIM KWVSDVDEYA PEGVQKILIG
     NKADEEQKRQ VGREQGQQLA KEYGMDFYET SACTNLNIKE SFTRLTELVL QAHRKELDGL
     RTCASNELAL AELEEDEGKT EGPANSSKTC WC
 
 
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