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Ras-related protein Rab-38 (Melanoma antigen NY-MEL-1)

 RAB38_HUMAN             Reviewed;         211 AA.
P57729; Q53XK7;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 1.
28-FEB-2018, entry version 156.
RecName: Full=Ras-related protein Rab-38;
AltName: Full=Melanoma antigen NY-MEL-1;
Name=RAB38;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10910072;
Jaeger D., Stockert E., Jaeger E., Guere A.O., Scanlan M.J., Knuth A.,
Old L.J., Chen Y.-T.;
"Serological cloning of a melanocyte rab guanosine 5'-triphosphate-
binding protein and a chromosome condensation protein from a melanoma
complementary DNA library.";
Cancer Res. 60:3584-3591(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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).
[5]
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).
[6]
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).
[7]
ISOPRENYLATION AT CYS-208.
PubMed=17114793; DOI=10.1074/jbc.M605557200;
Leung K.F., Baron R., Ali B.R., Magee A.I., Seabra M.C.;
"Rab GTPases containing a CAAX motif are processed post-
geranylgeranylation by proteolysis and methylation.";
J. Biol. Chem. 282:1487-1497(2007).
[8]
INTERACTION WITH ANKRD27.
PubMed=19403694; DOI=10.1091/mbc.E08-12-1161;
Tamura K., Ohbayashi N., Maruta Y., Kanno E., Itoh T., Fukuda M.;
"Varp is a novel Rab32/38-binding protein that regulates Tyrp1
trafficking in melanocytes.";
Mol. Biol. Cell 20:2900-2908(2009).
[9]
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).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x;
Seto S., Tsujimura K., Koide Y.;
"Rab GTPases regulating phagosome maturation are differentially
recruited to mycobacterial phagosomes.";
Traffic 12:407-420(2011).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23084991; DOI=10.1016/j.cub.2012.09.020;
Gerondopoulos A., Langemeyer L., Liang J.R., Linford A., Barr F.A.;
"BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine
nucleotide exchange factor.";
Curr. Biol. 22:2135-2139(2012).
[12]
VARIANT [LARGE SCALE ANALYSIS] THR-111.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: May be involved in melanosomal transport and docking.
Involved in the proper sorting of TYRP1. Involved in peripheral
melanosomal distribution of TYRP1 in melanocytes; the function,
which probably is implicating vesicle-trafficking, includes
cooperation with ANKRD27 and VAMP7 (By similarity). Plays a role
in the maturation of phagosomes that engulf pathogens, such as
S.aureus and M.tuberculosis (PubMed:21255211). Plays an important
role in the control of melanin production and melanosome
biogenesis (PubMed:23084991). In concert with RAB32, regulates the
proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2
to melanosomes in melanocytes (By similarity).
{ECO:0000250|UniProtKB:Q8QZZ8, ECO:0000269|PubMed:21255211,
ECO:0000269|PubMed:23084991}.
-!- ENZYME REGULATION: Regulated by a guanine nucleotide-exchange
factor (GEF) and a GTPase-activating protein (GAP) and alternates
between an inactive GDP-bound and an active GTP-bound form. The
BLOC-3 complex composed of HPS1 and HPS4 acts as its GEF, promotes
the exchange of GDP to GTP, converting it from an inactive GDP-
bound form into an active GTP-bound form. SGSM2 acts as its GAP
and inactivates it by stimulating its GTPase activity.
{ECO:0000250|UniProtKB:Q8QZZ8}.
-!- SUBUNIT: Interacts with ANKRD27 (PubMed:19403694).
{ECO:0000269|PubMed:19403694}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome
{ECO:0000269|PubMed:12643545}. Cytoplasmic vesicle, phagosome
{ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome
membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic
side {ECO:0000305}. Melanosome membrane
{ECO:0000269|PubMed:23084991}. Note=Recruited to phagosomes
containing S.aureus or M.tuberculosis (PubMed:21255211). The BLOC-
3 complex, a heterodimer of HPS1 and HPS4 promotes its membrane
localization (PubMed:23084991). {ECO:0000269|PubMed:21255211,
ECO:0000269|PubMed:23084991}.
-!- TISSUE SPECIFICITY: Expressed in melanocytes.
-!- PTM: Although at least one in vitro system can process and
methylate the prenylated C-terminal, in an in vitro system that
normally express Rab-38 and in vivo the prenylated C-terminal is
not proteolytically processed and not methylated.
{ECO:0000269|PubMed:17114793}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/rab38/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AF235022; AAG30731.1; -; mRNA.
EMBL; BT009842; AAP88844.1; -; mRNA.
EMBL; DQ178619; ABA03166.1; -; Genomic_DNA.
EMBL; BC015808; AAH15808.1; -; mRNA.
CCDS; CCDS8281.1; -.
RefSeq; NP_071732.1; NM_022337.2.
UniGene; Hs.591975; -.
ProteinModelPortal; P57729; -.
SMR; P57729; -.
BioGrid; 117198; 2.
DIP; DIP-60520N; -.
IntAct; P57729; 2.
STRING; 9606.ENSP00000243662; -.
iPTMnet; P57729; -.
PhosphoSitePlus; P57729; -.
SwissPalm; P57729; -.
BioMuta; RAB38; -.
DMDM; 12230516; -.
EPD; P57729; -.
MaxQB; P57729; -.
PaxDb; P57729; -.
PeptideAtlas; P57729; -.
PRIDE; P57729; -.
DNASU; 23682; -.
Ensembl; ENST00000243662; ENSP00000243662; ENSG00000123892.
GeneID; 23682; -.
KEGG; hsa:23682; -.
UCSC; uc001pcj.3; human.
CTD; 23682; -.
DisGeNET; 23682; -.
EuPathDB; HostDB:ENSG00000123892.11; -.
GeneCards; RAB38; -.
HGNC; HGNC:9776; RAB38.
HPA; HPA071701; -.
MIM; 606281; gene.
neXtProt; NX_P57729; -.
OpenTargets; ENSG00000123892; -.
PharmGKB; PA34129; -.
eggNOG; KOG4423; Eukaryota.
eggNOG; ENOG410YITC; LUCA.
GeneTree; ENSGT00760000119125; -.
HOGENOM; HOG000233968; -.
HOVERGEN; HBG009351; -.
InParanoid; P57729; -.
KO; K07923; -.
OMA; KRYVHHN; -.
OrthoDB; EOG091G0K53; -.
PhylomeDB; P57729; -.
TreeFam; TF324491; -.
Reactome; R-HSA-8873719; RAB geranylgeranylation.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
ChiTaRS; RAB38; human.
GeneWiki; RAB38; -.
GenomeRNAi; 23682; -.
PRO; PR:P57729; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000123892; -.
CleanEx; HS_RAB38; -.
ExpressionAtlas; P57729; baseline and differential.
Genevisible; P57729; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005769; C:early endosome; IDA:ParkinsonsUK-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0044233; C:ER-mitochondrion membrane contact site; IDA:ParkinsonsUK-UCL.
GO; GO:0005764; C:lysosome; IDA:ParkinsonsUK-UCL.
GO; GO:0042470; C:melanosome; IDA:ParkinsonsUK-UCL.
GO; GO:0033162; C:melanosome membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005802; C:trans-Golgi network; IEA:InterPro.
GO; GO:0035650; F:AP-1 adaptor complex binding; IPI:ParkinsonsUK-UCL.
GO; GO:0035651; F:AP-3 adaptor complex binding; IPI:ParkinsonsUK-UCL.
GO; GO:0036461; F:BLOC-2 complex binding; IPI:ParkinsonsUK-UCL.
GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
GO; GO:0030742; F:GTP-dependent protein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
GO; GO:0035646; P:endosome to melanosome transport; IMP:ParkinsonsUK-UCL.
GO; GO:1903232; P:melanosome assembly; IDA:UniProtKB.
GO; GO:0007005; P:mitochondrion organization; IMP:ParkinsonsUK-UCL.
GO; GO:0090383; P:phagosome acidification; IMP:UniProtKB.
GO; GO:0060155; P:platelet dense granule organization; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0072657; P:protein localization to membrane; IMP:ParkinsonsUK-UCL.
GO; GO:0015031; P:protein transport; NAS:UniProtKB.
GO; GO:0007264; P:small GTPase mediated signal transduction; NAS:UniProtKB.
GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
CDD; cd04107; Rab32_Rab38; 1.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR030697; Rab29/Rab38/Rab32.
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;
Cell membrane; Complete proteome; Cytoplasmic vesicle; GTP-binding;
Lipoprotein; Membrane; Nucleotide-binding; Palmitate; Polymorphism;
Prenylation; Protein transport; Reference proteome; Transport.
CHAIN 1 211 Ras-related protein Rab-38.
/FTId=PRO_0000121251.
NP_BIND 16 23 GTP. {ECO:0000250}.
NP_BIND 65 69 GTP. {ECO:0000250}.
NP_BIND 127 130 GTP. {ECO:0000250}.
MOTIF 38 46 Effector region. {ECO:0000250}.
SITE 208 208 Not methylated.
LIPID 205 205 S-palmitoyl cysteine. {ECO:0000255}.
LIPID 208 208 S-geranylgeranyl cysteine.
{ECO:0000305|PubMed:17114793}.
VARIANT 111 111 K -> T (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036415.
SEQUENCE 211 AA; 23712 MW; 0D16B42A1B237539 CRC64;
MQAPHKEHLY KLLVIGDLGV GKTSIIKRYV HQNFSSHYRA TIGVDFALKV LHWDPETVVR
LQLWDIAGQE RFGNMTRVYY REAMGAFIVF DVTRPATFEA VAKWKNDLDS KLSLPNGKPV
SVVLLANKCD QGKDVLMNNG LKMDQFCKEH GFVGWFETSA KENINIDEAS RCLVKHILAN
ECDLMESIEP DVVKPHLTST KVASCSGCAK S


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