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P63012 (RAB3A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-3A
Gene names
Name:Rab3a
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in exocytosis by regulating a late step in synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal By similarity.

Subunit structure

Part of a ternary complex involving PCLO and EPAC2. Interacts with RPH3AL. Interacts with the exocyst complex through SEC15. Binds SYTL4 and RIMS1. Interacts with SGSM1 and SGSM3 By similarity. Heterodimer with RIMS2. Interacts with RPH3A. Interacts with RAB3IP. Ref.4 Ref.5 Ref.6

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential.

Tissue specificity

Detected in brain.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processExocytosis
Protein transport
Transport
   Cellular componentCell membrane
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Methylation
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRab protein signal transduction

Inferred by curator PubMed 8807639. Source: RGD

axonogenesis

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

maintenance of presynaptic active zone structure

Inferred from electronic annotation. Source: Ensembl

mitochondrion organization

Inferred from electronic annotation. Source: Ensembl

neuromuscular synaptic transmission

Inferred from electronic annotation. Source: Ensembl

positive regulation of ATPase activity

Inferred from direct assay PubMed 11062069. Source: GOC

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of synaptic vesicle fusion to presynaptic membrane

Inferred from electronic annotation. Source: Ensembl

respiratory system process

Inferred from electronic annotation. Source: Ensembl

response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

sensory perception of touch

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle exocytosis

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle maturation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from direct assay PubMed 10340764. Source: RGD

intracellular organelle

Inferred from direct assay PubMed 10340764. Source: RGD

membrane

Inferred from direct assay PubMed 8807639. Source: RGD

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from direct assay PubMed 12426384. Source: RGD

synaptic vesicle

Inferred from direct assay PubMed 8043272. Source: RGD

   Molecular_functionATPase activator activity

Inferred from direct assay PubMed 11062069. Source: RGD

ATPase binding

Inferred from direct assay PubMed 11062069. Source: RGD

GTP binding

Inferred from direct assay PubMed 8807639. Source: RGD

GTPase activity

Inferred from electronic annotation. Source: Ensembl

GTPase binding

Inferred from physical interaction Ref.4. Source: RGD

protein C-terminus binding

Inferred from physical interaction PubMed 9341137. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Rph3aP477092EBI-440126,EBI-1027524

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 220220Ras-related protein Rab-3A
PRO_0000121079

Regions

Nucleotide binding29 – 368GTP
Nucleotide binding48 – 547GTP
Nucleotide binding77 – 815GTP
Nucleotide binding135 – 1384GTP
Motif51 – 599Effector region By similarity

Amino acid modifications

Modified residue2201Cysteine methyl ester By similarity
Lipidation2181S-geranylgeranyl cysteine By similarity
Lipidation2201S-geranylgeranyl cysteine By similarity

Experimental info

Mutagenesis361T → N: No significant effect on interaction with RAB3IP. Ref.4
Mutagenesis511F → L: Disrupts the interaction with RAB3IP. Ref.4
Mutagenesis521V → A: No significant effect on interaction with RAB3IP.
Mutagenesis551V → E: Disrupts the interaction with RAB3IP. Ref.4
Mutagenesis561G → D: Disrupts the interaction with RAB3IP. Ref.4
Sequence conflict1961P → L in CAA30005. Ref.2

Secondary structure

............................... 220
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63012 [UniParc].

Last modified August 31, 2004. Version 1.
Checksum: 1A3E9F8C9D09EB40

FASTA22024,970
        10         20         30         40         50         60 
MASATDSRYG QKESSDQNFD YMFKILIIGN SSVGKTSFLF RYADDSFTPA FVSTVGIDFK 

        70         80         90        100        110        120 
VKTIYRNDKR IKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWSTQI 

       130        140        150        160        170        180 
KTYSWDNAQV LLVGNKCDME DERVVSSERG RQLADHLGFE FFEASAKDNI NVKQTFERLV 

       190        200        210        220 
DVICEKMSES LDTADPAVTG AKQGPQLTDQ QAPPHQDCAC 

« Hide

References

« Hide 'large scale' references
[1]"Four additional members of the ras gene superfamily isolated by an oligonucleotide strategy: molecular cloning of YPT-related cDNAs from a rat brain library."
Touchot N., Chardin P., Tavitian A.
Proc. Natl. Acad. Sci. U.S.A. 84:8210-8214(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Complete coding sequences of the ras related rab 3 and 4 cDNAs."
Zahraoui A., Touchot N., Chardin P., Tavitian A.
Nucleic Acids Res. 16:1204-1204(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Interaction cloning of Rabin3, a novel protein that associates with the Ras-like GTPase Rab3A."
Brondyk W.H., McKiernan C.J., Fortner K.A., Stabila P., Holz R.W., Macara I.G.
Mol. Cell. Biol. 15:1137-1143(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB3IP, MUTAGENESIS OF THR-36; PHE-51; VAL-55 AND GLY-56.
[5]"The RIM/NIM family of neuronal C2 domain proteins. Interactions with Rab3 and a new class of Src homology 3 domain proteins."
Wang Y., Sugita S., Suedhof T.C.
J. Biol. Chem. 275:20033-20044(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RIMS2.
[6]"Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A."
Ostermeier C., Brunger A.T.
Cell 96:363-374(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 19-217 IN COMPLEX WITH GTP AND RPH3A, INTERACTION WITH RPH3A.
[7]"Structural basis of activation and GTP hydrolysis in rab proteins."
Dumas J.J., Zhu Z., Connolly J.L., Lambright D.G.
Structure 7:413-423(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-186 IN COMPLEX WITH GTP ANALOG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06889 mRNA. Translation: CAA30005.1.
BC087580 mRNA. Translation: AAH87580.1.
PIRS01765.
RefSeqNP_037150.2. NM_013018.2.
UniGeneRn.44409.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZBDX-ray2.60A19-217[»]
3RABX-ray2.00A18-186[»]
ProteinModelPortalP63012.
SMRP63012. Positions 18-186.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247563. 2 interactions.
IntActP63012. 4 interactions.
MINTMINT-1506235.

PTM databases

PhosphoSiteP63012.

Proteomic databases

PaxDbP63012.
PRIDEP63012.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026391; ENSRNOP00000026392; ENSRNOG00000019433.
GeneID25531.
KEGGrno:25531.
UCSCRGD:3528. rat.

Organism-specific databases

CTD5864.
RGD3528. Rab3a.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00740000115041.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidP63012.
KOK07882.
OMAQLTEQPA.
OrthoDBEOG7JQBPC.
PhylomeDBP63012.
TreeFamTF313199.

Gene expression databases

GenevestigatorP63012.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP63012.
NextBio296339.
PROP63012.

Entry information

Entry nameRAB3A_RAT
AccessionPrimary (citable) accession number: P63012
Secondary accession number(s): P05713
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references