RAB3_CAEEL
ID RAB3_CAEEL Reviewed; 219 AA.
AC Q94986;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ras-related protein Rab-3;
GN Name=rab-3; ORFNames=C18A3.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nonet M.L., Staunton J.E., Kilgard M.P., Fergestad T., Jorgensen E.,
RA Hartweig E., Horvitz H.R., Meyer B.J.;
RT "Functional synapses that are partially depleted of vesicles in C. elegans
RT rab-3 mutants.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14722103; DOI=10.1074/jbc.m306812200;
RA Fukuda M., Kanno E., Yamamoto A.;
RT "Rabphilin and Noc2 are recruited to dense-core vesicles through specific
RT interaction with Rab27A in PC12 cells.";
RL J. Biol. Chem. 279:13065-13075(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF THR-36 AND GLN-81.
RX PubMed=21029864; DOI=10.1016/j.cell.2010.09.024;
RA Bai J., Hu Z., Dittman J.S., Pym E.C., Kaplan J.M.;
RT "Endophilin functions as a membrane-bending molecule and is delivered to
RT endocytic zones by exocytosis.";
RL Cell 143:430-441(2010).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF 76-TRP--CYS-219.
RX PubMed=27116976; DOI=10.1534/genetics.115.186064;
RA Bhat J.M., Hutter H.;
RT "Pioneer Axon Navigation Is Controlled by AEX-3, a Guanine Nucleotide
RT Exchange Factor for RAB-3 in Caenorhabditis elegans.";
RL Genetics 203:1235-1247(2016).
CC -!- FUNCTION: Involved in exocytosis by regulating a late step in synaptic
CC vesicle fusion. Could play a role in neurotransmitter release by
CC regulating membrane flow in the nerve terminal (By similarity). Plays a
CC role in the recruitment of endophilin unc-57 to synaptic vesicles
CC (PubMed:21029864). Probably by controlling dense-core vesicle
CC trafficking, plays a role in the AVG neuron-mediated formation of the
CC right axon tract of the ventral nerve cord (PubMed:27116976).
CC {ECO:0000250, ECO:0000269|PubMed:21029864,
CC ECO:0000269|PubMed:27116976}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; U68265; AAB16980.1; -; mRNA.
DR EMBL; U68266; AAB16981.1; -; mRNA.
DR EMBL; AB112928; BAD07033.1; -; mRNA.
DR EMBL; FO080599; CCD65021.1; -; Genomic_DNA.
DR RefSeq; NP_001021974.1; NM_001026803.2.
DR AlphaFoldDB; Q94986; -.
DR SMR; Q94986; -.
DR BioGRID; 39313; 1.
DR STRING; 6239.C18A3.6a; -.
DR EPD; Q94986; -.
DR PaxDb; Q94986; -.
DR EnsemblMetazoa; C18A3.6b.1; C18A3.6b.1; WBGene00004267.
DR UCSC; C18A3.6a; c. elegans.
DR WormBase; C18A3.6b; CE20518; WBGene00004267; rab-3.
DR eggNOG; KOG0093; Eukaryota.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q94986; -.
DR Reactome; R-CEL-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-CEL-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-CEL-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8873719; RAB geranylgeranylation.
DR Reactome; R-CEL-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-CEL-888590; GABA synthesis, release, reuptake and degradation.
DR PRO; PR:Q94986; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004267; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q94986; baseline and differential.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IDA:WormBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:WormBase.
DR GO; GO:0031489; F:myosin V binding; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IMP:WormBase.
DR GO; GO:0007617; P:mating behavior; IMP:WormBase.
DR GO; GO:1905488; P:positive regulation of anterior/posterior axon guidance; IMP:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0040012; P:regulation of locomotion; IMP:WormBase.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IMP:UniProtKB.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:WormBase.
DR GO; GO:0007419; P:ventral cord development; IMP:UniProtKB.
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 Cell membrane; Exocytosis; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..219
FT /note="Ras-related protein Rab-3"
FT /id="PRO_0000121091"
FT REGION 191..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 51..59
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT COMPBIAS 200..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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"
FT MUTAGEN 36
FT /note="T->N: Probably constitutively inactive (GDP-locked
FT form). Fails to prevent unc-57 enrichment to synaptic
FT vesicles in an unc-13 mutant background."
FT /evidence="ECO:0000269|PubMed:9851916"
FT MUTAGEN 76..219
FT /note="Missing: In js49; abnormal cross-over of the AVG
FT neuron axon during the formation of the right axon tract of
FT the ventral nerve cord in 10 percent of mutants. In a nid-1
FT (cg119) mutant background, approximately 40 percent of
FT mutants have impaired AVG axon navigation."
FT /evidence="ECO:0000269|PubMed:27116976"
FT MUTAGEN 81
FT /note="Q->L: Probably constitutively active (GTP-locked
FT form). Reduced unc-57 enrichment to synaptic vesicles in an
FT unc-13 mutant background."
FT /evidence="ECO:0000269|PubMed:9851916"
SQ SEQUENCE 219 AA; 24760 MW; 7492444BCCC27C27 CRC64;
MAAGGQPQGA TPGQPDQNFD YMFKLLIIGN SSVGKTSFLF RYCDDSFTSA FVSTVGIDFK
VKTVFRGDKR VKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NSVQDWCTQI
KTYSWENAQV VLVGNKCDMD SERVVSMDRG RQLADQLGLE FFETSAKENI NVKAVFEKLV
EIICDKMAES LDKDPQQQPK GQKLEANPTQ KPAQQQCNC
