RAB15_MOUSE
ID RAB15_MOUSE Reviewed; 212 AA.
AC Q8K386;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ras-related protein Rab-15;
GN Name=Rab15;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [2]
RP PROTEIN SEQUENCE OF 11-21 AND 59-69, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May act in concert with RAB3A in regulating aspects of
CC synaptic vesicle membrane flow within the nerve terminal. EHBP1L1.
CC {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; BC027769; AAH27769.1; -; mRNA.
DR CCDS; CCDS25997.1; -.
DR AlphaFoldDB; Q8K386; -.
DR SMR; Q8K386; -.
DR DIP; DIP-37728N; -.
DR IntAct; Q8K386; 2.
DR STRING; 10090.ENSMUSP00000021459; -.
DR SwissPalm; Q8K386; -.
DR jPOST; Q8K386; -.
DR MaxQB; Q8K386; -.
DR PaxDb; Q8K386; -.
DR PRIDE; Q8K386; -.
DR ProteomicsDB; 255063; -.
DR MGI; MGI:1916865; Rab15.
DR eggNOG; KOG0078; Eukaryota.
DR InParanoid; Q8K386; -.
DR PhylomeDB; Q8K386; -.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR ChiTaRS; Rab15; mouse.
DR PRO; PR:Q8K386; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8K386; protein.
DR GO; GO:0005929; C:cilium; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
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:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
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; IEA:UniProtKB-KW.
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:1903307; P:positive regulation of regulated secretory pathway; ISO:MGI.
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 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; GTP-binding; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..212
FT /note="Ras-related protein Rab-15"
FT /id="PRO_0000121189"
FT REGION 192..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 24318 MW; E5C492846DD47F12 CRC64;
MAKQYDVLFR LLLIGDSGVG KTCLLCRFTD NEFHSSHIST IGVDFKMKTI DVDGIKVRIQ
IWDTAGQERY QTITKQYYRR AQGIFLVYDI SSERSYQHIM KWVSDVDEYA PEGVQKILIG
NKADEEQKRQ VGREQGQQLA KEYGMDFYET SACTNLNIKE SFTRLTELVL QAHRKELDGL
RTRASNELAL AELEEDEGKP EGPANSSKTC WC
