RAB3D_RAT
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 03-AUG-2022, entry version 169.
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; Q63942; -.
DR PRIDE; Q63942; -.
DR Ensembl; ENSRNOT00000015609; ENSRNOP00000015609; ENSRNOG00000011582.
DR GeneID; 140665; -.
DR KEGG; rno:140665; -.
DR UCSC; RGD:620924; rat.
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; 1218073at2759; -.
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 tissues.
DR Genevisible; Q63942; RN.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:RGD.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; 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:0030133; C:transport vesicle; IDA:RGD.
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:0018125; P:peptidyl-cysteine methylation; 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; -; 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; 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
