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Ras-related protein Rab-27A (Rab-27) (GTP-binding protein Ram)

 RB27A_HUMAN             Reviewed;         221 AA.
P51159; O00195; Q6FI40; Q9UIR9; Q9Y5U3;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
20-DEC-2017, entry version 183.
RecName: Full=Ras-related protein Rab-27A;
Short=Rab-27;
AltName: Full=GTP-binding protein Ram;
Name=RAB27A; Synonyms=RAB27;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND PARTIAL PROTEIN
SEQUENCE.
TISSUE=Retina;
PubMed=7592656; DOI=10.1074/jbc.270.41.24420;
Seabra M.C., Ho Y.K., Anant J.S.;
"Deficient geranylgeranylation of Ram/Rab27 in choroideremia.";
J. Biol. Chem. 270:24420-24427(1995).
[2]
SEQUENCE REVISION TO 99.
Seabra M.C.;
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Melanocyte;
PubMed=9066979; DOI=10.1006/bmme.1996.2559;
Chen D., Guo J., Miki T., Tachibana M., Gahl W.A.;
"Molecular cloning and characterization of rab27a and rab27b, novel
human rab proteins shared by melanocytes and platelets.";
Biochem. Mol. Med. 60:27-37(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
PubMed=10571040; DOI=10.1016/S0378-1119(99)00371-6;
Tolmachova T., Ramalho J.S., Anant J.S., Schultz R.A., Huxley C.M.,
Seabra M.C.;
"Cloning, mapping and characterization of the human RAB27A gene.";
Gene 239:109-116(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
TISSUE=Pituitary;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
LONG).
Anderson P.D., Huizing M., Anikster Y., Gahl W.A.;
"Genomic organization of the human RAB27A gene.";
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
INTERACTION WITH MLPH.
PubMed=12062444; DOI=10.1016/S0014-5793(02)02634-0;
Nagashima K., Torii S., Yi Z., Igarashi M., Okamoto K., Takeuchi T.,
Izumi T.;
"Melanophilin directly links Rab27a and myosin Va through its distinct
coiled-coil regions.";
FEBS Lett. 517:233-238(2002).
[11]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=12643545; DOI=10.1021/pr025562r;
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
Hearing V.J., Hunt D.F., Appella E.;
"Proteomic analysis of early melanosomes: identification of novel
melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
[12]
SUBCELLULAR LOCATION, INTERACTION WITH UNC13D, TISSUE SPECIFICITY,
MUTAGENESIS OF THR-23, AND CHARACTERIZATION OF VARIANT GS2 GLY-73.
PubMed=15548590; DOI=10.1091/mbc.E04-10-0923;
Neeft M., Wieffer M., de Jong A.S., Negroiu G., Metz C.H.,
van Loon A., Griffith J., Krijgsveld J., Wulffraat N., Koch H.,
Heck A.J.R., Brose N., Kleijmeer M., van der Sluijs P.;
"Munc13-4 is an effector of rab27a and controls secretion of lysosomes
in hematopoietic cells.";
Mol. Biol. Cell 16:731-741(2005).
[13]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[14]
INTERACTION WITH UNC13D, AND SUBCELLULAR LOCATION.
PubMed=17237785; DOI=10.1038/ni1431;
Menager M.M., Menasche G., Romao M., Knapnougel P., Ho C.-H.,
Garfa M., Raposo G., Feldmann J., Fischer A., de Saint Basile G.;
"Secretory cytotoxic granule maturation and exocytosis require the
effector protein hMunc13-4.";
Nat. Immunol. 8:257-267(2007).
[15]
FUNCTION, INTERACTION WITH SYTL2, AND MUTAGENESIS OF LEU-70 AND
ALA-76.
PubMed=18812475; DOI=10.1182/blood-2008-02-141069;
Menasche G., Menager M.M., Lefebvre J.M., Deutsch E., Athman R.,
Lambert N., Mahlaoui N., Court M., Garin J., Fischer A.,
de Saint Basile G.;
"A newly identified isoform of Slp2a associates with Rab27a in
cytotoxic T cells and participates in cytotoxic granule secretion.";
Blood 112:5052-5062(2008).
[16]
LACK OF INTERACTION WITH THE BLOC-3 COMPLEX.
PubMed=20048159; DOI=10.1074/jbc.M109.069088;
Kloer D.P., Rojas R., Ivan V., Moriyama K., van Vlijmen T., Murthy N.,
Ghirlando R., van der Sluijs P., Hurley J.H., Bonifacino J.S.;
"Assembly of the biogenesis of lysosome-related organelles complex-3
(BLOC-3) and its interaction with Rab9.";
J. Biol. Chem. 285:7794-7804(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[21]
VARIANTS GS2 GLY-73; PRO-130 AND PRO-152.
PubMed=10835631; DOI=10.1038/76024;
Menasche G., Pastural E., Feldmann J., Certain S., Ersoy F.,
Dupuis S., Wulffraat N., Bianchi D., Fischer A., Le Deist F.,
de Saint Basile G.;
"Mutations in RAB27A cause Griscelli syndrome associated with
haemophagocytic syndrome.";
Nat. Genet. 25:173-176(2000).
[22]
INVOLVEMENT IN GRISCELLI SYNDROME.
PubMed=12058346; DOI=10.1086/341606;
Anikster Y., Huizing M., Anderson P.D., Fitzpatrick D.L., Klar A.,
Gross-Kieselstein E., Berkun Y., Shazberg G., Gahl W.A., Hurvitz H.;
"Evidence that Griscelli syndrome with neurological involvement is
caused by mutations in RAB27A, not MYO5A.";
Am. J. Hum. Genet. 71:407-414(2002).
[23]
ERRATUM.
Anikster Y., Huizing M., Anderson P.D., Fitzpatrick D.L., Klar A.,
Gross-Kieselstein E., Berkun Y., Shazberg G., Gahl W.A., Hurvitz H.;
Am. J. Hum. Genet. 71:1007-1007(2002).
[24]
CHARACTERIZATION OF VARIANTS GS2 GLY-73; PRO-130 AND PRO-152.
PubMed=12446441; DOI=10.1182/blood-2002-09-2789;
Menasche G., Feldmann J., Houdusse A., Desaymard C., Fischer A.,
Goud B., de Saint Basile G.;
"Biochemical and functional characterization of Rab27a mutations
occurring in Griscelli syndrome patients.";
Blood 101:2736-2742(2003).
[25]
CHARACTERIZATION OF VARIANTS GS2 GLY-73; PRO-130 AND PRO-152.
PubMed=12531900; DOI=10.1074/jbc.M211996200;
Bahadoran P., Busca R., Chiaverini C., Westbroek W., Lambert J.,
Bille K., Valony G., Fukuda M., Naeyaert J.-M., Ortonne J.-P.,
Ballotti R.;
"Characterization of the molecular defects in Rab27a, caused by RAB27A
missense mutations found in patients with Griscelli syndrome.";
J. Biol. Chem. 278:11386-11392(2003).
-!- FUNCTION: Plays a role in cytotoxic granule exocytosis in
lymphocytes. Required for both granule maturation and granule
docking and priming at the immunologic synapse.
{ECO:0000269|PubMed:18812475}.
-!- SUBUNIT: Binds SYTL1, SLAC2B, MYRIP, SYTL3, SYTL4 and SYTL5.
Interacts with RPH3A and RPH3A (By similarity). Binds MLPH and
SYTL2. Interacts with UNC13D. Does not interact with the BLOC-3
complex (heterodimer of HPS1 and HPS4) (PubMed:20048159).
{ECO:0000250|UniProtKB:Q9ERI2, ECO:0000269|PubMed:12062444,
ECO:0000269|PubMed:15548590, ECO:0000269|PubMed:17237785,
ECO:0000269|PubMed:18812475, ECO:0000269|PubMed:20048159}.
-!- INTERACTION:
Q9BV36:MLPH; NbExp=3; IntAct=EBI-716881, EBI-7042162;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}. Melanosome {ECO:0000269|PubMed:12643545,
ECO:0000269|PubMed:17081065}. Late endosome
{ECO:0000269|PubMed:15548590}. Lysosome
{ECO:0000269|PubMed:15548590}. Note=Identified by mass
spectrometry in melanosome fractions from stage I to stage IV
(PubMed:12643545, PubMed:17081065). Localizes to endosomal
exocytic vesicles (PubMed:17237785). {ECO:0000269|PubMed:12643545,
ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:17237785}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P51159-1; Sequence=Displayed;
Name=Short;
IsoId=P51159-2; Sequence=VSP_005529;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Found in all the examined tissues except in
brain. Low expression was found in thymus, kidney, muscle and
placenta. Detected in melanocytes, and in most tumor cell lines
examined. Expressed in cytotoxic T-lymphocytes (CTL) and mast
cells. {ECO:0000269|PubMed:15548590}.
-!- DISEASE: Griscelli syndrome 2 (GS2) [MIM:607624]: Rare autosomal
recessive disorder that results in pigmentary dilution of the skin
and hair, the presence of large clumps of pigment in hair shafts,
and an accumulation of melanosomes in melanocytes. GS2 patients
also develop an uncontrolled T-lymphocyte and macrophage
activation syndrome, known as hemophagocytic syndrome, leading to
death in the absence of bone marrow transplantation. Neurological
impairment is present in some patients, likely as a result of
hemophagocytic syndrome. {ECO:0000269|PubMed:10835631,
ECO:0000269|PubMed:12446441, ECO:0000269|PubMed:12531900,
ECO:0000269|PubMed:15548590}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=RAB27Abase; Note=RAB27A mutation db;
URL="http://structure.bmc.lu.se/idbase/RAB27Abase/";
-!- WEB RESOURCE: Name=Mutations of the RAB27A gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/rab27mut.htm";
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EMBL; U38654; AAC50271.2; -; mRNA.
EMBL; U57094; AAC51195.1; -; mRNA.
EMBL; AF154840; AAD47629.1; -; Genomic_DNA.
EMBL; AF154836; AAD47629.1; JOINED; Genomic_DNA.
EMBL; AF154837; AAD47629.1; JOINED; Genomic_DNA.
EMBL; AF154838; AAD47629.1; JOINED; Genomic_DNA.
EMBL; AF154839; AAD47629.1; JOINED; Genomic_DNA.
EMBL; AF125393; AAD43049.1; -; mRNA.
EMBL; AF443871; AAL39097.1; -; Genomic_DNA.
EMBL; AF498953; AAM21101.1; -; mRNA.
EMBL; CR536496; CAG38735.1; -; mRNA.
EMBL; CR541693; CAG46494.1; -; mRNA.
EMBL; BC107680; AAI07681.1; -; mRNA.
CCDS; CCDS10153.1; -. [P51159-1]
PIR; I39198; I39198.
RefSeq; NP_004571.2; NM_004580.4. [P51159-1]
RefSeq; NP_899057.1; NM_183234.2. [P51159-1]
RefSeq; NP_899058.1; NM_183235.2. [P51159-1]
RefSeq; NP_899059.1; NM_183236.2. [P51159-1]
RefSeq; XP_005254633.1; XM_005254576.4. [P51159-1]
RefSeq; XP_011520154.1; XM_011521852.1. [P51159-1]
RefSeq; XP_011520156.1; XM_011521854.1. [P51159-1]
RefSeq; XP_011520157.1; XM_011521855.2. [P51159-1]
RefSeq; XP_011520158.1; XM_011521856.2. [P51159-1]
UniGene; Hs.654978; -.
UniGene; Hs.735555; -.
ProteinModelPortal; P51159; -.
SMR; P51159; -.
BioGrid; 111811; 35.
CORUM; P51159; -.
DIP; DIP-44244N; -.
IntAct; P51159; 16.
MINT; MINT-1377654; -.
STRING; 9606.ENSP00000337761; -.
GuidetoPHARMACOLOGY; 2916; -.
iPTMnet; P51159; -.
PhosphoSitePlus; P51159; -.
SwissPalm; P51159; -.
BioMuta; RAB27A; -.
DMDM; 116242744; -.
EPD; P51159; -.
MaxQB; P51159; -.
PaxDb; P51159; -.
PeptideAtlas; P51159; -.
PRIDE; P51159; -.
DNASU; 5873; -.
Ensembl; ENST00000336787; ENSP00000337761; ENSG00000069974. [P51159-1]
Ensembl; ENST00000396307; ENSP00000379601; ENSG00000069974. [P51159-1]
Ensembl; ENST00000564609; ENSP00000455012; ENSG00000069974. [P51159-1]
Ensembl; ENST00000569493; ENSP00000456059; ENSG00000069974. [P51159-1]
GeneID; 5873; -.
KEGG; hsa:5873; -.
UCSC; uc002aco.4; human. [P51159-1]
CTD; 5873; -.
DisGeNET; 5873; -.
EuPathDB; HostDB:ENSG00000069974.15; -.
GeneCards; RAB27A; -.
HGNC; HGNC:9766; RAB27A.
HPA; CAB034046; -.
HPA; HPA001333; -.
MalaCards; RAB27A; -.
MIM; 603868; gene.
MIM; 607624; phenotype.
neXtProt; NX_P51159; -.
OpenTargets; ENSG00000069974; -.
Orphanet; 79477; Griscelli disease type 2.
PharmGKB; PA34117; -.
eggNOG; KOG0081; Eukaryota.
eggNOG; ENOG410XQ3T; LUCA.
GeneTree; ENSGT00890000139330; -.
HOGENOM; HOG000233968; -.
HOVERGEN; HBG009351; -.
InParanoid; P51159; -.
KO; K07885; -.
OMA; LVMQRIQ; -.
OrthoDB; EOG091G0I51; -.
PhylomeDB; P51159; -.
TreeFam; TF312895; -.
Reactome; R-HSA-264876; Insulin processing.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-8873719; RAB geranylgeranylation.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
ChiTaRS; RAB27A; human.
GeneWiki; RAB27A; -.
GenomeRNAi; 5873; -.
PRO; PR:P51159; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000069974; -.
CleanEx; HS_RAB27A; -.
ExpressionAtlas; P51159; baseline and differential.
Genevisible; P51159; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0070382; C:exocytic vesicle; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IDA:UniProtKB.
GO; GO:0033162; C:melanosome membrane; TAS:Reactome.
GO; GO:0032585; C:multivesicular body membrane; IDA:UniProtKB.
GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
GO; GO:0030141; C:secretory granule; IBA:GO_Central.
GO; GO:0030667; C:secretory granule membrane; IEA:Ensembl.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:0045202; C:synapse; IEA:GOC.
GO; GO:0033093; C:Weibel-Palade body; IEA:Ensembl.
GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
GO; GO:0031489; F:myosin V binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0019882; P:antigen processing and presentation; IMP:UniProtKB.
GO; GO:0007596; P:blood coagulation; IEA:Ensembl.
GO; GO:0097278; P:complement-dependent cytotoxicity; IMP:UniProtKB.
GO; GO:0043316; P:cytotoxic T cell degranulation; IEA:Ensembl.
GO; GO:0006887; P:exocytosis; IDA:UniProtKB.
GO; GO:1990182; P:exosomal secretion; IMP:UniProtKB.
GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
GO; GO:0032400; P:melanosome localization; IMP:UniProtKB.
GO; GO:0032402; P:melanosome transport; IBA:GO_Central.
GO; GO:0036257; P:multivesicular body organization; IMP:UniProtKB.
GO; GO:0071985; P:multivesicular body sorting pathway; IMP:UniProtKB.
GO; GO:0043320; P:natural killer cell degranulation; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:1903435; P:positive regulation of constitutive secretory pathway; IMP:UniProtKB.
GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0050766; P:positive regulation of phagocytosis; IMP:UniProtKB.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IMP:UniProtKB.
GO; GO:1903307; P:positive regulation of regulated secretory pathway; IMP:UniProtKB.
GO; GO:0006605; P:protein targeting; IEA:Ensembl.
GO; GO:0048489; P:synaptic vesicle transport; TAS:ParkinsonsUK-UCL.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51419; RAB; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond; Endosome;
Exocytosis; GTP-binding; Lipoprotein; Lysosome; Membrane; Methylation;
Nucleotide-binding; Phosphoprotein; Polymorphism; Prenylation;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712}.
CHAIN 2 221 Ras-related protein Rab-27A.
/FTId=PRO_0000121221.
NP_BIND 16 24 GTP. {ECO:0000250}.
NP_BIND 74 78 GTP. {ECO:0000250}.
NP_BIND 133 136 GTP. {ECO:0000250}.
NP_BIND 163 165 GTP. {ECO:0000250}.
MOTIF 38 46 Effector region. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 221 221 Cysteine methyl ester. {ECO:0000250}.
LIPID 219 219 S-geranylgeranyl cysteine. {ECO:0000250}.
LIPID 221 221 S-geranylgeranyl cysteine. {ECO:0000250}.
DISULFID 123 188 {ECO:0000250}.
VAR_SEQ 146 153 Missing (in isoform Short).
{ECO:0000303|PubMed:10931946}.
/FTId=VSP_005529.
VARIANT 62 62 T -> S (in dbSNP:rs1050930).
/FTId=VAR_028206.
VARIANT 73 73 W -> G (in GS2; does not affect GTP
binding; cannot interact with MLPH;
significant reduction in interaction with
UNC13D; abolishes localization to
lysosomes; dbSNP:rs28938176).
{ECO:0000269|PubMed:10835631,
ECO:0000269|PubMed:12446441,
ECO:0000269|PubMed:12531900,
ECO:0000269|PubMed:15548590}.
/FTId=VAR_010654.
VARIANT 84 84 L -> F (in dbSNP:rs4340274).
/FTId=VAR_028207.
VARIANT 85 85 T -> P (in dbSNP:rs719705).
/FTId=VAR_028208.
VARIANT 130 130 L -> P (in GS2; strongly affects GTP
binding; cannot interact with MLPH;
dbSNP:rs104894498).
{ECO:0000269|PubMed:10835631,
ECO:0000269|PubMed:12446441,
ECO:0000269|PubMed:12531900}.
/FTId=VAR_011334.
VARIANT 152 152 A -> P (in GS2; interferes with
melanosome transport; dbSNP:rs104894499).
{ECO:0000269|PubMed:10835631,
ECO:0000269|PubMed:12446441,
ECO:0000269|PubMed:12531900}.
/FTId=VAR_011335.
MUTAGEN 23 23 T->N: Abolishes interaction with UNC13D
and localization to lysosomes.
{ECO:0000269|PubMed:15548590}.
MUTAGEN 70 70 L->P: Abolishes interaction with SYTL2.
{ECO:0000269|PubMed:18812475}.
MUTAGEN 76 76 A->V: Abolishes interaction with SYTL2.
{ECO:0000269|PubMed:18812475}.
CONFLICT 48 48 E -> P (in Ref. 3; AAC51195 and 5;
AAD43049). {ECO:0000305}.
CONFLICT 61 62 AT -> PV (in Ref. 3; AAC51195 and 5;
AAD43049). {ECO:0000305}.
SEQUENCE 221 AA; 24868 MW; 4A6A0C8C5CC41A20 CRC64;
MSDGDYDYLI KFLALGDSGV GKTSVLYQYT DGKFNSKFIT TVGIDFREKR VVYRASGPDG
ATGRGQRIHL QLWDTAGQER FRSLTTAFFR DAMGFLLLFD LTNEQSFLNV RNWISQLQMH
AYCENPDIVL CGNKSDLEDQ RVVKEEEAIA LAEKYGIPYF ETSAANGTNI SQAIEMLLDL
IMKRMERCVD KSWIPEGVVR SNGHASTDQL SEEKEKGACG C


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