RAB32_MOUSE
ID RAB32_MOUSE Reviewed; 223 AA.
AC Q9CZE3; Q3TXU7; Q8BVD3; Q91YN4;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ras-related protein Rab-32;
GN Name=Rab32;
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 {ECO:0000312|EMBL:BAB28421.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14499590; DOI=10.1016/s1570-9639(03)00236-x;
RA Cohen-Solal K.A., Sood R., Marin Y., Crespo-Carbone S.M., Sinsimer D.,
RA Martino J.J., Robbins C., Makalowska I., Trent J., Chen S.;
RT "Identification and characterization of mouse Rab32 by mRNA and protein
RT expression analysis.";
RL Biochim. Biophys. Acta 1651:68-75(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Adipose tissue, Bone marrow, Colon, Embryo, and Thymus;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH55945.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAH55945.1}, and
RC Mammary gland {ECO:0000312|EMBL:AAH16409.1};
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 [4]
RP INTERACTION WITH ANKRD27.
RX PubMed=19403694; DOI=10.1091/mbc.e08-12-1161;
RA Tamura K., Ohbayashi N., Maruta Y., Kanno E., Itoh T., Fukuda M.;
RT "Varp is a novel Rab32/38-binding protein that regulates Tyrp1 trafficking
RT in melanocytes.";
RL Mol. Biol. Cell 20:2900-2908(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH ANKRD27, AND MUTAGENESIS OF VAL-92.
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 [7]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLN-83.
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: Acts as an A-kinase anchoring protein by binding to the type
CC II regulatory subunit of protein kinase A and anchoring it to the
CC mitochondrion. Also involved in synchronization of mitochondrial
CC fission. Plays a role in the maturation of phagosomes that engulf
CC pathogens, such as S.aureus and Mycobacterium (By similarity). Plays an
CC important role in the control of melanin production and melanosome
CC biogenesis (By similarity). In concert with RAB38, regulates the proper
CC trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to
CC melanosomes in melanocytes (PubMed:26620560).
CC {ECO:0000250|UniProtKB:Q13637, 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 (PubMed:19403694, PubMed:21187289). A
CC decreased interaction with ANKRD27 seen in the presence of SGSM2 (By
CC similarity). {ECO:0000250|UniProtKB:Q13637,
CC ECO:0000269|PubMed:19403694, ECO:0000269|PubMed:21187289}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q13637}.
CC Mitochondrion outer membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q13637}.
CC Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome
CC {ECO:0000269|PubMed:26620560}. Melanosome membrane
CC {ECO:0000250|UniProtKB:Q13637}. 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:Q13637}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in liver.
CC Strong expression also found in melanocyte, platelet, mast cell and
CC fibroblast cell lines. {ECO:0000269|PubMed:14499590}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, highest levels occur at day 7.
CC {ECO:0000269|PubMed:14499590}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AY135650; AAN11298.1; -; mRNA.
DR EMBL; AK012701; BAB28421.1; -; mRNA.
DR EMBL; AK078874; BAC37434.1; -; mRNA.
DR EMBL; AK088661; BAC40486.1; -; mRNA.
DR EMBL; AK151543; BAE30489.1; -; mRNA.
DR EMBL; AK159102; BAE34818.1; -; mRNA.
DR EMBL; AK163620; BAE37425.1; -; mRNA.
DR EMBL; BC016409; AAH16409.1; -; mRNA.
DR EMBL; BC055945; AAH55945.1; -; mRNA.
DR CCDS; CCDS23695.1; -.
DR RefSeq; NP_080681.1; NM_026405.3.
DR AlphaFoldDB; Q9CZE3; -.
DR SMR; Q9CZE3; -.
DR BioGRID; 212474; 1.
DR IntAct; Q9CZE3; 62.
DR STRING; 10090.ENSMUSP00000019974; -.
DR iPTMnet; Q9CZE3; -.
DR PhosphoSitePlus; Q9CZE3; -.
DR jPOST; Q9CZE3; -.
DR MaxQB; Q9CZE3; -.
DR PaxDb; Q9CZE3; -.
DR PRIDE; Q9CZE3; -.
DR ProteomicsDB; 300378; -.
DR ABCD; Q9CZE3; 22 sequenced antibodies.
DR DNASU; 67844; -.
DR Ensembl; ENSMUST00000019974; ENSMUSP00000019974; ENSMUSG00000019832.
DR GeneID; 67844; -.
DR KEGG; mmu:67844; -.
DR UCSC; uc007ejg.1; mouse.
DR CTD; 10981; -.
DR MGI; MGI:1915094; Rab32.
DR VEuPathDB; HostDB:ENSMUSG00000019832; -.
DR eggNOG; KOG4423; Eukaryota.
DR GeneTree; ENSGT00940000163553; -.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; Q9CZE3; -.
DR OMA; HQSFPSE; -.
DR OrthoDB; 1240760at2759; -.
DR PhylomeDB; Q9CZE3; -.
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; 67844; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Rab32; mouse.
DR PRO; PR:Q9CZE3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CZE3; protein.
DR Bgee; ENSMUSG00000019832; Expressed in granulocyte and 164 other tissues.
DR ExpressionAtlas; Q9CZE3; baseline and differential.
DR Genevisible; Q9CZE3; MM.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; 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:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
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; IEA:UniProtKB-KW.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:MGI.
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:0090382; P:phagosome maturation; ISS:UniProtKB.
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 Acetylation; Cytoplasmic vesicle; GTP-binding; Lipoprotein; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13637"
FT CHAIN 2..223
FT /note="Ras-related protein Rab-32"
FT /id="PRO_0000121236"
FT REGION 176..195
FT /note="PKA-RII subunit binding domain"
FT /evidence="ECO:0000250"
FT MOTIF 52..60
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 30..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 79..83
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 141..144
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q13637"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13637"
FT LIPID 222
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P05713"
FT LIPID 223
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P05713"
FT MUTAGEN 83
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 92
FT /note="V->A: Disrupts interaction with ANKRD27."
FT /evidence="ECO:0000269|PubMed:21187289"
FT CONFLICT 64
FT /note="V -> E (in Ref. 2; BAC37434)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="T -> S (in Ref. 3; AAH16409/AAH55945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 223 AA; 25068 MW; 58505A33167FD744 CRC64;
MAGEGLGQQG ASATAAPETR EHLFKVLVIG ELGVGKTSII KRYVHQLFSQ HYRATIGVDF
ALKVLNWDSR TLVRLQLWDI AGQERFGNMT RVYYKEALGA FVVFDISRSS TFDAVLKWKN
DLDSKVHLPN GSPIPAVLLA NKCDQKKDNS QSPSQMDQFC KDHGFTGWFE TSAKDNINID
EATRFLVENM LANQQSFPSE EIDLDRIKLV EEPPTTKPRS QCC
