Ras-related protein Rab-3A - Rattus norvegicus (Rat)

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P63012 (RAB3A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-3A

Gene names

Name:

Rab3a

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	220 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Exocytosis Protein transport Transport
Cellular component	Cell membrane Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Rab protein signal transduction Inferred by curator PubMed 8807639. Source: RGD axonogenesis Inferred from electronic annotation. Source: Compara lung development Inferred from electronic annotation. Source: Compara maintenance of presynaptic active zone structure Inferred from electronic annotation. Source: Compara mitochondrion organization Inferred from electronic annotation. Source: Compara neuromuscular synaptic transmission Inferred from electronic annotation. Source: Compara post-embryonic development Inferred from electronic annotation. Source: Compara protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of synaptic vesicle fusion to presynaptic membrane Inferred from electronic annotation. Source: Compara respiratory system process Inferred from electronic annotation. Source: Compara response to electrical stimulus Inferred from electronic annotation. Source: Compara sensory perception of touch Inferred from electronic annotation. Source: Compara synaptic vesicle exocytosis Inferred from electronic annotation. Source: Compara synaptic vesicle maturation Inferred from electronic annotation. Source: Compara
Cellular_component	acrosomal vesicle Inferred from electronic annotation. Source: Compara cytosol 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_function	ATPase 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: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 220

220

Ras-related protein Rab-3A

PRO_0000121079

Regions

Nucleotide binding

29 – 36

GTP

Nucleotide binding

48 – 54

GTP

Nucleotide binding

77 – 81

GTP

Nucleotide binding

135 – 138

GTP

Motif

51 – 59

Effector region By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

188

Phosphoserine By similarity

Modified residue

220

Cysteine methyl ester By similarity

Lipidation

218

S-geranylgeranyl cysteine By similarity

Lipidation

220

S-geranylgeranyl cysteine By similarity

Experimental info

Mutagenesis

T → N: No significant effect on interaction with RAB3IP. Ref.4

Mutagenesis

F → L: Disrupts the interaction with RAB3IP. Ref.4

Mutagenesis

V → A: No significant effect on interaction with RAB3IP.

Mutagenesis

V → E: Disrupts the interaction with RAB3IP. Ref.4

Mutagenesis

G → D: Disrupts the interaction with RAB3IP. Ref.4

Sequence conflict

196

P → L in CAA30005. Ref.2

Secondary structure

220

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P63012 [UniParc].

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

220

24,970

        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' referencesShow '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.

IPI

IPI00325762.

PIR

S01765.

RefSeq

NP_037150.2. NM_013018.2.

UniGene

Rn.44409.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZBD	X-ray	2.60	A	19-217	[»]
3RAB	X-ray	2.00	A	18-186	[»]

ProteinModelPortal

P63012.

SMR

P63012. Positions 18-186.

ModBase

Search...

Protein-protein interaction databases

IntAct

P63012. 4 interactions.

MINT

MINT-1506235.

PTM databases

PhosphoSite

P63012.

Proteomic databases

PaxDb

P63012.

PRIDE

P63012.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000026391; ENSRNOP00000026392; ENSRNOG00000019433.

GeneID

25531.

KEGG

rno:25531.

UCSC

RGD:3528. rat.

Organism-specific databases

CTD

5864.

RGD

3528. Rab3a.

Phylogenomic databases

eggNOG

COG1100.

GeneTree

ENSGT00690000101942.

HOGENOM

HOG000233968.

HOVERGEN

HBG009351.

InParanoid

P63012.

K07882.

OMA

QLTEQPA.

OrthoDB

EOG4TB4C6.

Gene expression databases

ArrayExpress

P63012.

Genevestigator

P63012.

GermOnline

ENSRNOG00000019433. Rattus norvegicus.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00175. RAB. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51419. RAB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P63012.

NextBio

296339.

Entry information

Entry name

RAB3A_RAT

Accession

Primary (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:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents