RAB15_HUMAN
ID RAB15_HUMAN Reviewed; 212 AA.
AC P59190; G5EMR7; Q86TX7; Q8IW89;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Ras-related protein Rab-15;
GN Name=RAB15;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Pham T., Hartoma T., Nishimura N.;
RT "Aberrant Rab15 expression.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 42-212 (ISOFORM 2).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH REP15.
RX PubMed=16195351; DOI=10.1091/mbc.e05-03-0204;
RA Strick D.J., Elferink L.A.;
RT "Rab15 effector protein: a novel protein for receptor recycling from the
RT endocytic recycling compartment.";
RL Mol. Biol. Cell 16:5699-5709(2005).
RN [7]
RP INTERACTION WITH MICAL1; MICALCL; MICAL3; EHBP1 AND EHBP1L1.
RX PubMed=27552051; DOI=10.7554/elife.18675;
RA Rai A., Oprisko A., Campos J., Fu Y., Friese T., Itzen A., Goody R.S.,
RA Gazdag E.M., Muller M.P.;
RT "bMERB domains are bivalent Rab8 family effectors evolved by gene
RT duplication.";
RL Elife 5:E18675-E18675(2016).
CC -!- FUNCTION: May act in concert with RAB3A in regulating aspects of
CC synaptic vesicle membrane flow within the nerve terminal.
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:0000269|PubMed:16195351, ECO:0000269|PubMed:27552051}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P59190-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P59190-2; Sequence=VSP_010420;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AB678452; BAL14289.1; -; mRNA.
DR EMBL; AL139022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW80893.1; -; Genomic_DNA.
DR EMBL; BC040679; AAH40679.2; -; mRNA.
DR EMBL; BX248046; CAD62353.1; -; mRNA.
DR CCDS; CCDS76691.1; -. [P59190-1]
DR CCDS; CCDS9768.1; -. [P59190-2]
DR RefSeq; NP_001295083.1; NM_001308154.1. [P59190-1]
DR RefSeq; NP_941959.1; NM_198686.2. [P59190-2]
DR AlphaFoldDB; P59190; -.
DR SMR; P59190; -.
DR BioGRID; 132005; 28.
DR IntAct; P59190; 15.
DR MINT; P59190; -.
DR STRING; 9606.ENSP00000267512; -.
DR iPTMnet; P59190; -.
DR PhosphoSitePlus; P59190; -.
DR SwissPalm; P59190; -.
DR BioMuta; RAB15; -.
DR DMDM; 27734452; -.
DR EPD; P59190; -.
DR jPOST; P59190; -.
DR MassIVE; P59190; -.
DR MaxQB; P59190; -.
DR PeptideAtlas; P59190; -.
DR PRIDE; P59190; -.
DR ProteomicsDB; 57135; -. [P59190-1]
DR ProteomicsDB; 57136; -. [P59190-2]
DR Antibodypedia; 24725; 119 antibodies from 26 providers.
DR DNASU; 376267; -.
DR Ensembl; ENST00000267512.9; ENSP00000267512.5; ENSG00000139998.16. [P59190-2]
DR Ensembl; ENST00000533601.7; ENSP00000434103.3; ENSG00000139998.16. [P59190-1]
DR GeneID; 376267; -.
DR KEGG; hsa:376267; -.
DR MANE-Select; ENST00000533601.7; ENSP00000434103.3; NM_001308154.2; NP_001295083.1.
DR UCSC; uc001xhz.2; human. [P59190-1]
DR CTD; 376267; -.
DR DisGeNET; 376267; -.
DR GeneCards; RAB15; -.
DR HGNC; HGNC:20150; RAB15.
DR HPA; ENSG00000139998; Low tissue specificity.
DR MIM; 619547; gene.
DR neXtProt; NX_P59190; -.
DR OpenTargets; ENSG00000139998; -.
DR PharmGKB; PA134901572; -.
DR VEuPathDB; HostDB:ENSG00000139998; -.
DR GeneTree; ENSGT00940000157848; -.
DR HOGENOM; CLU_041217_20_0_1; -.
DR InParanoid; P59190; -.
DR PhylomeDB; P59190; -.
DR TreeFam; TF314097; -.
DR PathwayCommons; P59190; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; P59190; -.
DR BioGRID-ORCS; 376267; 10 hits in 1071 CRISPR screens.
DR GeneWiki; RAB15; -.
DR GenomeRNAi; 376267; -.
DR Pharos; P59190; Tbio.
DR PRO; PR:P59190; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P59190; protein.
DR Bgee; ENSG00000139998; Expressed in right hemisphere of cerebellum and 174 other tissues.
DR ExpressionAtlas; P59190; baseline and differential.
DR Genevisible; P59190; HS.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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; IDA:UniProtKB.
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; IMP:UniProtKB.
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 Alternative splicing; Cell membrane; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..212
FT /note="Ras-related protein Rab-15"
FT /id="PRO_0000121188"
FT REGION 193..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"
FT VAR_SEQ 109..212
FT /note="YAPEGVQKILIGNKADEEQKRQVGREQGQQLAKEYGMDFYETSACTNLNIKE
FT SFTRLTELVLQAHRKELEGLRMRASNELALAELEEEEGKPEGPANSSKTCWC -> VGD
FT ATSLPGCGEGASPGKARRGPDGKANASRKLCLPQPWMKTSGTHQKASRRSLLGIRLMRS
FT RNGRWEESKGSSWRRSMAWTSMKQVPAPTSTLKSHSRV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.5"
FT /id="VSP_010420"
SQ SEQUENCE 212 AA; 24391 MW; D16A0C71797ED782 CRC64;
MAKQYDVLFR LLLIGDSGVG KTCLLCRFTD NEFHSSHIST IGVDFKMKTI EVDGIKVRIQ
IWDTAGQERY QTITKQYYRR AQGIFLVYDI SSERSYQHIM KWVSDVDEYA PEGVQKILIG
NKADEEQKRQ VGREQGQQLA KEYGMDFYET SACTNLNIKE SFTRLTELVL QAHRKELEGL
RMRASNELAL AELEEEEGKP EGPANSSKTC WC
