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   22-APR-2020, entry version 178.
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   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   [8]
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       {ECO:0000250|UniProtKB:O95716, ECO:0000269|PubMed:11431472,
CC       ECO:0000269|PubMed:12578829}.
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   SMR; P35276; -.
DR   BioGrid; 202545; 6.
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   Antibodypedia; 25779; 151 antibodies.
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   eggNOG; KOG0093; Eukaryota.
DR   eggNOG; ENOG410ZZXQ; LUCA.
DR   GeneTree; ENSGT00940000157552; -.
DR   HOGENOM; CLU_041217_10_1_1; -.
DR   InParanoid; P35276; -.
DR   KO; K07884; -.
DR   OMA; MERYCED; -.
DR   OrthoDB; 1218073at2759; -.
DR   PhylomeDB; P35276; -.
DR   TreeFam; TF313199; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-8873719; RAB geranylgeranylation.
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 233 other tissues.
DR   ExpressionAtlas; P35276; baseline and differential.
DR   Genevisible; P35276; MM.
DR   GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; 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:0031982; C:vesicle; IBA:GO_Central.
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:0006886; P:intracellular protein transport; IBA:GO_Central.
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:0032482; P:Rab protein signal transduction; 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   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   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   NP_BIND         29..37
FT                   /note="GTP"
FT                   /evidence="ECO:0000250|UniProtKB:O95716"
FT   NP_BIND         48..54
FT                   /note="GTP"
FT                   /evidence="ECO:0000250|UniProtKB:P63012"
FT   NP_BIND         77..81
FT                   /note="GTP"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   NP_BIND         135..138
FT                   /note="GTP"
FT                   /evidence="ECO:0000250|UniProtKB:O95716"
FT   NP_BIND         165..167
FT                   /note="GTP"
FT                   /evidence="ECO:0000250|UniProtKB:O95716"
FT   MOTIF           51..59
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
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
//