RAB3D_MOUSE
ID RAB3D_MOUSE Reviewed; 219 AA.
AC P35276;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Ras-related protein Rab-3D;
GN Name=Rab3d;
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 [MRNA].
RX PubMed=1594612; DOI=10.1073/pnas.89.11.5049;
RA Baldini G., Hohl T., Lin H.Y., Lodish H.F.;
RT "Cloning of a Rab3 isotype predominantly expressed in adipocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5049-5052(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv;
RX PubMed=10891340; DOI=10.1006/bbrc.2000.3032;
RA Adachi R., Nigam R., Tuvim M.J., DeMayo F., Dickey B.F.;
RT "Genomic organization, chromosomal localization, and expression of the
RT murine RAB3D gene.";
RL Biochem. Biophys. Res. Commun. 273:877-883(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
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 PROTEIN SEQUENCE OF 25-35; 42-60; 73-83; 122-136 AND 179-186, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH RIMS1.
RX PubMed=11431472; DOI=10.1074/jbc.m103337200;
RA Wang X., Hu B., Zimmermann B., Kilimann M.W.;
RT "Rim1 and rabphilin-3 bind Rab3-GTP by composite determinants partially
RT related through N-terminal alpha-helix motifs.";
RL J. Biol. Chem. 276:32480-32488(2001).
RN [6]
RP INTERACTION WITH RIMS1; RIMS2; RPH3A AND RPH3AL.
RX PubMed=12578829; DOI=10.1074/jbc.m212341200;
RA Fukuda M.;
RT "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2.
RT Identification of a critical determinant of Rab3A/Rab27A recognition by
RT Rim2.";
RL J. Biol. Chem. 278:15373-15380(2003).
RN [7]
RP INTERACTION WITH MADD.
RX PubMed=18849981; DOI=10.1038/ncb1785;
RA Niwa S., Tanaka Y., Hirokawa N.;
RT "KIF1Bbeta- and KIF1A-mediated axonal transport of presynaptic regulator
RT Rab3 occurs in a GTP-dependent manner through DENN/MADD.";
RL Nat. Cell Biol. 10:1269-1279(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Lung, Pancreas, 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 [9]
RP PHOSPHORYLATION AT THR-86.
RX PubMed=29125462; DOI=10.7554/elife.31012;
RA Steger M., Diez F., Dhekne H.S., Lis P., Nirujogi R.S., Karayel O.,
RA Tonelli F., Martinez T.N., Lorentzen E., Pfeffer S.R., Alessi D.R.,
RA Mann M.;
RT "Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation
RT establishes a connection to ciliogenesis.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Protein transport. Probably involved in vesicular traffic (By
CC similarity). May be involved in the insulin-induced exocytosis of
CC glut4-containing vesicles in adipocytes. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RIMS1, RIMS2, RPH3A, RPH3AL and RAB3IP
CC (PubMed:11431472, PubMed:12578829). Interacts with CHM and CHML;
CC phosphorylation at Thr-86 disrupts these interactions (By similarity).
CC Interacts with MADD (via uDENN domain); the GTP-bound form is preferred
CC for interaction (PubMed:18849981). {ECO:0000250|UniProtKB:O95716,
CC ECO:0000269|PubMed:11431472, ECO:0000269|PubMed:12578829,
CC ECO:0000269|PubMed:18849981}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the adipocyte tissue,
CC but is also expressed in several other organs including skin, spleen,
CC heart and lung.
CC -!- PTM: Phosphorylation of Thr-86 in the switch II region by LRRK2
CC prevents the association of RAB regulatory proteins, including CHM and
CC CHML. {ECO:0000250|UniProtKB:O95716}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; M89777; AAA40026.1; -; mRNA.
DR EMBL; AF263365; AAF82769.1; -; mRNA.
DR EMBL; AF263366; AAF82770.1; -; Genomic_DNA.
DR EMBL; BC010779; AAH10779.1; -; mRNA.
DR EMBL; BC020010; AAH20010.1; -; mRNA.
DR CCDS; CCDS22912.1; -.
DR PIR; A45384; A45384.
DR RefSeq; NP_001311460.1; NM_001324531.1.
DR RefSeq; NP_114080.2; NM_031874.5.
DR RefSeq; XP_011240724.1; XM_011242422.2.
DR RefSeq; XP_011240725.1; XM_011242423.2.
DR AlphaFoldDB; P35276; -.
DR SMR; P35276; -.
DR BioGRID; 202545; 9.
DR IntAct; P35276; 14.
DR MINT; P35276; -.
DR STRING; 10090.ENSMUSP00000113322; -.
DR iPTMnet; P35276; -.
DR PhosphoSitePlus; P35276; -.
DR EPD; P35276; -.
DR jPOST; P35276; -.
DR PaxDb; P35276; -.
DR PeptideAtlas; P35276; -.
DR PRIDE; P35276; -.
DR ProteomicsDB; 300225; -.
DR Antibodypedia; 25779; 165 antibodies from 28 providers.
DR DNASU; 19340; -.
DR Ensembl; ENSMUST00000115351; ENSMUSP00000111008; ENSMUSG00000019066.
DR Ensembl; ENSMUST00000122211; ENSMUSP00000113322; ENSMUSG00000019066.
DR GeneID; 19340; -.
DR KEGG; mmu:19340; -.
DR UCSC; uc009omu.1; mouse.
DR CTD; 9545; -.
DR MGI; MGI:97844; Rab3d.
DR VEuPathDB; HostDB:ENSMUSG00000019066; -.
DR eggNOG; KOG0093; Eukaryota.
DR GeneTree; ENSGT00940000157552; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; P35276; -.
DR OMA; CIVTGPP; -.
DR OrthoDB; 1218073at2759; -.
DR PhylomeDB; P35276; -.
DR TreeFam; TF313199; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 19340; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Rab3d; mouse.
DR PRO; PR:P35276; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P35276; protein.
DR Bgee; ENSMUSG00000019066; Expressed in lacrimal gland and 200 other tissues.
DR ExpressionAtlas; P35276; baseline and differential.
DR Genevisible; P35276; MM.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0099503; C:secretory vesicle; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0030133; C:transport vesicle; ISO:MGI.
DR GO; GO:0042588; C:zymogen granule; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030742; F:GTP-dependent protein binding; IPI:MGI.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0031489; F:myosin V binding; ISO:MGI.
DR GO; GO:0045453; P:bone resorption; ISO:MGI.
DR GO; GO:0018125; P:peptidyl-cysteine methylation; IDA:MGI.
DR GO; GO:1903307; P:positive regulation of regulated secretory pathway; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IDA:MGI.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR CDD; cd01865; Rab3; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR037872; Rab3.
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; Cell membrane; Direct protein sequencing; Exocytosis;
KW GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT CHAIN 2..219
FT /note="Ras-related protein Rab-3D"
FT /id="PRO_0000121089"
FT REGION 190..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 51..59
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 29..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT BINDING 48..54
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63012"
FT BINDING 77..81
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT BINDING 165..167
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT MOD_RES 86
FT /note="Phosphothreonine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:29125462"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20337"
FT MOD_RES 219
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 217
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 219
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 219 AA; 24416 MW; 438115B0B5710648 CRC64;
MASASEPPAS PRDAADQNFD YMFKLLLIGN SSVGKTSFLF RYADDSFTPA FVSTVGIDFK
VKTVYRHDKR IKLQIWDTAG QERYRTITTA YYRGAMGFLL MYDIANQESF TAVQDWATQI
KTYSWDNAQV ILVGNKCDLE DERVVPAEDG RRLADDLGFE FFEASAKENI NVKQVFERLV
DIICDKMNES LEPSSSPGSN GKGPALGDTP PPQPSSCSC
