RAB38_MOUSE
ID RAB38_MOUSE Reviewed; 211 AA.
AC Q8QZZ8; Q9D7E8;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Ras-related protein Rab-38;
GN Name=Rab38;
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 [GENOMIC DNA / MRNA], AND VARIANT CHT VAL-19.
RC STRAIN=C57BL/6J;
RX PubMed=11917121; DOI=10.1073/pnas.072087599;
RA Loftus S.K., Larson D.M., Baxter L.L., Antonellis A., Chen Y., Wu X.,
RA Jiang Y., Bittner M., Hammer J.A. III, Pavan W.J.;
RT "Mutation of melanosome protein RAB38 in chocolate mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4471-4476(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary, Retina, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, INTERACTION WITH ANKRD27, AND MUTAGENESIS OF VAL-78.
RX PubMed=21187289; DOI=10.1074/jbc.m110.191205;
RA Tamura K., Ohbayashi N., Ishibashi K., Fukuda M.;
RT "Structure-function analysis of VPS9-ankyrin-repeat protein (Varp) in the
RT trafficking of tyrosinase-related protein 1 in melanocytes.";
RL J. Biol. Chem. 286:7507-7521(2011).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLN-69.
RX PubMed=26620560; DOI=10.1074/jbc.m115.684043;
RA Marubashi S., Shimada H., Fukuda M., Ohbayashi N.;
RT "RUTBC1 functions as a GTPase-activating protein for Rab32/38 and regulates
RT melanogenic enzyme trafficking in melanocytes.";
RL J. Biol. Chem. 291:1427-1440(2016).
CC -!- FUNCTION: Plays a role in the maturation of phagosomes that engulf
CC pathogens, such as S.aureus and Mycobacterium (By similarity). May be
CC involved in melanosomal transport and docking. Involved in the proper
CC sorting of TYRP1. Involved in peripheral melanosomal distribution of
CC TYRP1 in melanocytes; the function, which probably is implicating
CC vesicle-trafficking, includes cooperation with ANKRD27 and VAMP7
CC (PubMed:21187289). Plays an important role in the control of melanin
CC production and melanosome biogenesis (By similarity). In concert with
CC RAB32, regulates the proper trafficking of melanogenic enzymes TYR,
CC TYRP1 and DCT/TYRP2 to melanosomes in melanocytes (PubMed:26620560).
CC {ECO:0000250|UniProtKB:P57729, ECO:0000269|PubMed:21187289,
CC ECO:0000269|PubMed:26620560}.
CC -!- ACTIVITY REGULATION: Regulated by a guanine nucleotide-exchange factor
CC (GEF) and a GTPase-activating protein (GAP) and alternates between an
CC inactive GDP-bound and an active GTP-bound form. The BLOC-3 complex
CC composed of HPS1 and HPS4 acts as its GEF, promotes the exchange of GDP
CC to GTP, converting it from an inactive GDP-bound form into an active
CC GTP-bound form. SGSM2 acts as its GAP and inactivates it by stimulating
CC its GTPase activity (PubMed:26620560). {ECO:0000269|PubMed:26620560}.
CC -!- SUBUNIT: Interacts with ANKRD27 (By similarity).
CC {ECO:0000250|UniProtKB:P57729}.
CC -!- INTERACTION:
CC Q8QZZ8; Q3UMR0: Ankrd27; NbExp=5; IntAct=EBI-1993463, EBI-1993429;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle,
CC phagosome {ECO:0000250|UniProtKB:P57729}. Cytoplasmic vesicle,
CC phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305};
CC Cytoplasmic side {ECO:0000305}. Melanosome
CC {ECO:0000269|PubMed:26620560}. Melanosome membrane
CC {ECO:0000250|UniProtKB:P57729}. Note=Recruited to phagosomes containing
CC S.aureus or M.tuberculosis. The BLOC-3 complex, a heterodimer of HPS1
CC and HPS4 promotes its membrane localization.
CC {ECO:0000250|UniProtKB:P57729}.
CC -!- DISEASE: Note=Defects in Rab38 are the cause of a form of
CC oculocutaneous albinism known as the chocolate (cht) phenotype. Mice
CC exhibit a brown coat similar in color to mice with a mutation in
CC tyrosinase-related protein 1 (TYRP1). The targeting of TYRP1 protein to
CC the melanosome is impaired in Rab38(cht)/Rab38(cht) melanocytes.
CC {ECO:0000269|PubMed:11917121}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AY062237; AAL38663.1; -; mRNA.
DR EMBL; AF448443; AAM12528.1; -; Genomic_DNA.
DR EMBL; AF448441; AAM12528.1; JOINED; Genomic_DNA.
DR EMBL; AF448442; AAM12528.1; JOINED; Genomic_DNA.
DR EMBL; AK009296; BAB26198.1; -; mRNA.
DR EMBL; AK044783; BAC32089.1; -; mRNA.
DR EMBL; AK054253; BAC35704.1; -; mRNA.
DR CCDS; CCDS21439.1; -.
DR RefSeq; NP_082514.4; NM_028238.7.
DR AlphaFoldDB; Q8QZZ8; -.
DR SMR; Q8QZZ8; -.
DR BioGRID; 215371; 6.
DR DIP; DIP-46949N; -.
DR IntAct; Q8QZZ8; 64.
DR STRING; 10090.ENSMUSP00000102877; -.
DR iPTMnet; Q8QZZ8; -.
DR PhosphoSitePlus; Q8QZZ8; -.
DR jPOST; Q8QZZ8; -.
DR MaxQB; Q8QZZ8; -.
DR PaxDb; Q8QZZ8; -.
DR PRIDE; Q8QZZ8; -.
DR ProteomicsDB; 253146; -.
DR ABCD; Q8QZZ8; 21 sequenced antibodies.
DR Antibodypedia; 31470; 223 antibodies from 31 providers.
DR DNASU; 72433; -.
DR Ensembl; ENSMUST00000107256; ENSMUSP00000102877; ENSMUSG00000030559.
DR GeneID; 72433; -.
DR KEGG; mmu:72433; -.
DR UCSC; uc009ifv.1; mouse.
DR CTD; 23682; -.
DR MGI; MGI:1919683; Rab38.
DR VEuPathDB; HostDB:ENSMUSG00000030559; -.
DR eggNOG; KOG4423; Eukaryota.
DR GeneTree; ENSGT00940000157301; -.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; Q8QZZ8; -.
DR OMA; NIHIDDA; -.
DR OrthoDB; 1240760at2759; -.
DR PhylomeDB; Q8QZZ8; -.
DR TreeFam; TF324491; -.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 72433; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Rab38; mouse.
DR PRO; PR:Q8QZZ8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8QZZ8; protein.
DR Bgee; ENSMUSG00000030559; Expressed in animal zygote and 181 other tissues.
DR ExpressionAtlas; Q8QZZ8; baseline and differential.
DR Genevisible; Q8QZZ8; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IDA:UniProtKB.
DR GO; GO:0033162; C:melanosome membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0035650; F:AP-1 adaptor complex binding; ISO:MGI.
DR GO; GO:0035651; F:AP-3 adaptor complex binding; ISO:MGI.
DR GO; GO:0036461; F:BLOC-2 complex binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0035646; P:endosome to melanosome transport; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:1903232; P:melanosome assembly; ISS:UniProtKB.
DR GO; GO:0032438; P:melanosome organization; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
DR GO; GO:0090383; P:phagosome acidification; ISS:UniProtKB.
DR GO; GO:0060155; P:platelet dense granule organization; ISO:MGI.
DR GO; GO:2001247; P:positive regulation of phosphatidylcholine biosynthetic process; ISO:MGI.
DR GO; GO:0072657; P:protein localization to membrane; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd04107; Rab32_Rab38; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR030697; Rab29/Rab38/Rab32.
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 Albinism; Cell membrane; Cytoplasmic vesicle; Disease variant; GTP-binding;
KW Lipoprotein; Membrane; Nucleotide-binding; Palmitate; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..211
FT /note="Ras-related protein Rab-38"
FT /id="PRO_0000121252"
FT MOTIF 38..46
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 65..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 127..130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 205
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 208
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VARIANT 19
FT /note="G -> V (in cht)"
FT /evidence="ECO:0000269|PubMed:11917121"
FT MUTAGEN 69
FT /note="Q->L: Inhibits the proper trafficking of melanogenic
FT enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in
FT melanocytes."
FT /evidence="ECO:0000269|PubMed:26620560"
FT MUTAGEN 78
FT /note="V->A: Disrupts interaction with ANKRD27; inhibits
FT peripheral distribution of TYRP1 in melanocytes."
FT /evidence="ECO:0000269|PubMed:21187289"
FT CONFLICT 149..150
FT /note="EH -> DD (in Ref. 2; BAB26198)"
FT /evidence="ECO:0000305"
FT CONFLICT 161..162
FT /note="KE -> QR (in Ref. 2; BAB26198)"
FT /evidence="ECO:0000305"
FT CONFLICT 173..175
FT /note="LVK -> RGQ (in Ref. 2; BAB26198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 23776 MW; 61F84A88CDACC486 CRC64;
MQTPHKEHLY KLLVIGDLGV GKTSIIKRYV HQNFSSHYRA TIGVDFALKV LHWDPETVVR
LQLWDIAGQE RFGNMTRVYY REAMGAFIVF DVTRPATFEA VAKWKNDLDS KLTLPNGKPV
SVVLLANKCD QGKDVLMNNG LKMDQFCKEH GFVGWFETSA KENINIDEAS RCLVKHILAN
ECDLLESIEP DIVKPHLTSP KVVSCSGCAK S
