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   24-JAN-2024, entry version 180.
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; 30.
DR   IntAct; P59190; 15.
DR   MINT; P59190; -.
DR   STRING; 9606.ENSP00000434103; -.
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   PaxDb; 9606-ENSP00000267512; -.
DR   PeptideAtlas; P59190; -.
DR   ProteomicsDB; 57135; -. [P59190-1]
DR   ProteomicsDB; 57136; -. [P59190-2]
DR   Pumba; P59190; -.
DR   Antibodypedia; 24725; 124 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   AGR; HGNC:20150; -.
DR   CTD; 376267; -.
DR   DisGeNET; 376267; -.
DR   GeneCards; RAB15; -.
DR   HGNC; HGNC:20150; RAB15.
DR   HPA; ENSG00000139998; Tissue enhanced (brain).
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   OrthoDB; 8685at2759; -.
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 1147 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 175 other cell types or tissues.
DR   ExpressionAtlas; P59190; baseline and differential.
DR   GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:1903307; P:positive regulation of regulated secretory pathway; IMP:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR   CDD; cd04117; Rab15; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041826; Rab15.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47980; LD44762P; 1.
DR   PANTHER; PTHR47980:SF4; RAS-RELATED PROTEIN RAB-15; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   Genevisible; P59190; HS.
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
//