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

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Reviewed, UniProtKB/Swiss-Prot P63012 (RAB3A_RAT)

Last modified November 24, 2009. Version 63. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Ras-related protein Rab-3A

Gene names

Name:

Rab3a

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	220 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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. Interacts with RAB3IP.
Subunit structure	Heterodimer with RIMS2. Part of a ternary complex involving PCLO and EPAC2. Interacts with RPH3A. Interacts with the exocyst complex through SEC15. Binds SYTL4, RIMS1 and RIMS2. Interacts with SGSM1 and SGSM3 By similarity.
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential.
Tissue specificity	Detected in brain.
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

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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
Gene Ontology (GO)
Biological process	Rab protein signal transduction Inferred by curator. Source: RGD protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW soluble fraction Inferred from direct assay. Source: RGD synaptic vesicle Inferred from direct assay. Source: RGD synaptosome Inferred from direct assay. Source: RGD
Molecular function	GTP binding Inferred from direct assay. Source: RGD protein binding Ref.4 Ref.6 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
Rabac1	O35394	1	EBI-440126,EBI-2028510
Rph3a	P47709	1	EBI-440126,EBI-1027524

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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 By similarity

Nucleotide binding

77 – 81

GTP By similarity

Nucleotide binding

135 – 138

GTP By similarity

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...

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Sequences

Sequence

Length

Mass (Da)

Tools

P63012-1 [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

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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: 3317403] [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: 3344209] [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: 15489334] [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: 7532276] [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: 10748113] [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: 10025402] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 19-217 IN COMPLEX WITH RABPHILIN-3A.
[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: 10196122] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-186.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X06889 mRNA. Translation: CAA30005.1.
BC087580 mRNA. Translation: AAH87580.1.

IPI

IPI00325762.

PIR

S01765.

RefSeq

NP_037150.2.

UniGene

Rn.44409

3D structure databases

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

ModBase

Search...

Protein-protein interaction databases

IntAct

P63012. 3 interactions.

STRING

P63012.

PTM databases

PhosphoSite

P63012.

Proteomic databases

PRIDE

P63012.

Genome annotation databases

Ensembl

ENSRNOT00000026391; ENSRNOP00000026392; ENSRNOG00000019433; Rattus norvegicus. [Genome view]

GeneID

25531.

KEGG

rno:25531.

UCSC

NM_013018. rat.

Organism-specific databases

CTD

25531.

RGD

3528. Rab3a.

Phylogenomic databases

HOVERGEN

P63012.

OMA

KLVEIIC

Gene expression databases

ArrayExpress

P63012.

Genevestigator

P63012.

GermOnline

ENSRNOG00000019433. Rattus norvegicus.

Family and domain databases

InterPro

IPR003579. GTPase_Rab.
IPR015596. Rab3.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR005225. Small_GTP_bd.
IPR020851. Small_GTPase.
[Graphical view]

PANTHER

PTHR11708:SF222. Rab3. 1 hit.

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 Resources

NextBio

607029.

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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:	November 24, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents