ID   RAB3D_RAT               Reviewed;         219 AA.
AC   Q63942; P35291;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=GTP-binding protein Rab-3D;
GN   Name=Rab3d; Synonyms=Rab16;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9300704;
RA   Roa M., Paumet F., le Mao J., David B., Blank U.;
RT   "Involvement of the ras-like GTPase rab3d in RBL-2H3 mast cell exocytosis
RT   following stimulation via high affinity IgE receptors (Fc epsilonRI).";
RL   J. Immunol. 159:2815-2823(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 16-82.
RC   TISSUE=Mast cell;
RX   PubMed=7508866; DOI=10.1016/0014-5793(94)80409-5;
RA   Oberhauser A.F., Balan V., Fernandez-Badilla C.L., Fernandez J.M.;
RT   "RT-PCR cloning of Rab3 isoforms expressed in peritoneal mast cells.";
RL   FEBS Lett. 339:171-174(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-219, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=1313420; DOI=10.1016/s0021-9258(18)42619-1;
RA   Elferink L.A., Anzai K., Scheller R.H.;
RT   "Rab15, a novel low molecular weight GTP-binding protein specifically
RT   expressed in rat brain.";
RL   J. Biol. Chem. 267:5768-5775(1992).
RN   [5]
RP   INTERACTION WITH RAB3IP.
RX   PubMed=7532276; DOI=10.1128/mcb.15.3.1137;
RA   Brondyk W.H., McKiernan C.J., Fortner K.A., Stabila P., Holz R.W.,
RA   Macara I.G.;
RT   "Interaction cloning of Rabin3, a novel protein that associates with the
RT   Ras-like GTPase Rab3A.";
RL   Mol. Cell. Biol. 15:1137-1143(1995).
RN   [6]
RP   METHYLATION AT CYS-219.
RC   TISSUE=Pancreas;
RX   PubMed=9716267; DOI=10.1016/s0171-9335(98)80035-6;
RA   Valentijn J.A., Jamieson J.D.;
RT   "Carboxyl methylation of rab3D is developmentally regulated in the rat
RT   pancreas: correlation with exocrine function.";
RL   Eur. J. Cell Biol. 76:204-211(1998).
CC   -!- FUNCTION: Protein transport. Probably involved in regulated exocytosis
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RIMS1, RIMS2, RPH3A and RPH3AL (By similarity).
CC       Interacts with RAB3IP (PubMed:7532276). Interacts with CHM;
CC       phosphorylation at Thr-86 disrupts this interaction (By similarity).
CC       Interacts with MADD (via uDENN domain); the GTP-bound form is preferred
CC       for interaction (By similarity). {ECO:0000250|UniProtKB:O95716,
CC       ECO:0000250|UniProtKB:P35276, ECO:0000269|PubMed:7532276}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highest levels found in lung.
CC       {ECO:0000269|PubMed:1313420}.
CC   -!- PTM: In fetal glands the majority of the proteins are methylated,
CC       whereas in neonatal and adult glands, only 50% are methylated.
CC       {ECO:0000269|PubMed:9716267}.
CC   -!- PTM: Phosphorylation of Thr-86 in the switch II region by LRRK2
CC       prevents the association of RAB regulatory proteins, including CHM.
CC       {ECO:0000250|UniProtKB:O95716}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; U90206; AAB81202.1; -; mRNA.
DR   EMBL; BC081741; AAH81741.1; -; mRNA.
DR   EMBL; S68808; AAB29895.1; -; mRNA.
DR   EMBL; M83681; AAA41996.1; -; mRNA.
DR   PIR; I67631; I67631.
DR   RefSeq; NP_542147.1; NM_080580.2.
DR   RefSeq; XP_006242656.1; XM_006242594.3.
DR   RefSeq; XP_017450911.1; XM_017595422.1.
DR   AlphaFoldDB; Q63942; -.
DR   SMR; Q63942; -.
DR   BioGRID; 250825; 4.
DR   IntAct; Q63942; 4.
DR   MINT; Q63942; -.
DR   STRING; 10116.ENSRNOP00000015609; -.
DR   iPTMnet; Q63942; -.
DR   PhosphoSitePlus; Q63942; -.
DR   jPOST; Q63942; -.
DR   PaxDb; 10116-ENSRNOP00000015609; -.
DR   Ensembl; ENSRNOT00000015609.6; ENSRNOP00000015609.3; ENSRNOG00000011582.6.
DR   GeneID; 140665; -.
DR   KEGG; rno:140665; -.
DR   UCSC; RGD:620924; rat.
DR   AGR; RGD:620924; -.
DR   CTD; 9545; -.
DR   RGD; 620924; Rab3d.
DR   eggNOG; KOG0093; Eukaryota.
DR   GeneTree; ENSGT00940000157552; -.
DR   HOGENOM; CLU_041217_10_1_1; -.
DR   InParanoid; Q63942; -.
DR   OMA; CIVTGPP; -.
DR   OrthoDB; 8685at2759; -.
DR   PhylomeDB; Q63942; -.
DR   TreeFam; TF313199; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR   PRO; PR:Q63942; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000011582; Expressed in pancreas and 20 other cell types or tissues.
DR   GO; GO:0005881; C:cytoplasmic microtubule; ISO:RGD.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0099503; C:secretory vesicle; ISO:RGD.
DR   GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR   GO; GO:0042588; C:zymogen granule; ISO:RGD.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030742; F:GTP-dependent protein binding; ISO:RGD.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0031489; F:myosin V binding; ISO:RGD.
DR   GO; GO:0045453; P:bone resorption; ISO:RGD.
DR   GO; GO:1903307; P:positive regulation of regulated secretory pathway; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR   CDD; cd01865; Rab3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR037872; Rab3.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47980; LD44762P; 1.
DR   PANTHER; PTHR47980:SF17; RAS-RELATED PROTEIN RAB-3D; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   Genevisible; Q63942; RN.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Exocytosis; GTP-binding; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW   Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O95716"
FT   CHAIN           2..219
FT                   /note="GTP-binding protein Rab-3D"
FT                   /id="PRO_0000121090"
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"
FT                   /evidence="ECO:0000250|UniProtKB:O95716"
FT   MOD_RES         190
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20337"
FT   MOD_RES         219
FT                   /note="Cysteine methyl ester; partial"
FT                   /evidence="ECO:0000269|PubMed:9716267"
FT   LIPID           217
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           219
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        205
FT                   /note="A -> S (in Ref. 4; AAA41996)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   219 AA;  24290 MW;  ED82C97D66BF194A CRC64;
     MASASEPPAS PRDAADQNFD YMFKLLLIGN SSVGKTSFLF RYADDSFTPA FVSTVGIDFK
     VKTVYRHDKR IKLQIWDTAG QERYRTITTA YYRGAMGFLL MYDIANQESF TAVQDWATQI
     KTYSWDNAQV ILVGNKCDLE DERVVSAEDG QRLAGDLGFE FFEASAKENI NVKQVFERLV
     DIICDKMNES LEPSSSPGSN GKGPALGDTP PPQPSSCGC
//