P11023 (RAB3A_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-3A

Alternative name(s):
SMG P25A

Gene names

Name:

RAB3A

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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	Heterodimer with RIMS2. Part of a ternary complex involving PCLO and EPAC2. Interacts with RPH3A and RPH3AL. Interacts with the exocyst complex through SEC15. Binds SYTL4 and RIMS1. Interacts with RAB3IP. Interacts with SGSM1 and SGSM3 By similarity.
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential.
Tissue specificity	Specifically expressed 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	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	axonogenesis Inferred from sequence or structural similarity. Source: AgBase lung development Inferred from sequence or structural similarity. Source: AgBase maintenance of presynaptic active zone structure Inferred from sequence or structural similarity. Source: AgBase mitochondrion organization Inferred from sequence or structural similarity. Source: AgBase neuromuscular synaptic transmission Inferred from sequence or structural similarity. Source: AgBase post-embryonic development Inferred from sequence or structural similarity. Source: AgBase protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of synaptic vesicle fusion to presynaptic membrane Inferred from sequence or structural similarity. Source: AgBase respiratory system process Inferred from sequence or structural similarity. Source: AgBase response to electrical stimulus Inferred from sequence or structural similarity. Source: AgBase sensory perception of touch Inferred from sequence or structural similarity. Source: AgBase small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro synaptic vesicle exocytosis Inferred from sequence or structural similarity. Source: AgBase synaptic vesicle maturation Inferred from sequence or structural similarity. Source: AgBase
Cellular_component	acrosomal vesicle Inferred from electronic annotation. Source: Compara membrane Inferred from direct assay PubMed 2115118. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell synaptic vesicle Inferred from sequence or structural similarity. Source: AgBase
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from sequence or structural similarity. Source: AgBase
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_0000121075
Regions
	Nucleotide binding	29 – 36	8	GTP By similarity
	Nucleotide binding	48 – 54	7	GTP By similarity
	Nucleotide binding	77 – 81	5	GTP By similarity
	Nucleotide binding	135 – 138	4	GTP By similarity
	Motif	51 – 59	9	Effector region By similarity
Amino acid modifications
	Modified residue	37	1	Phosphoserine By similarity
	Modified residue	188	1	Phosphoserine By similarity
	Modified residue	220	1	Cysteine methyl ester
	Lipidation	218	1	S-geranylgeranyl cysteine Ref.3
	Lipidation	220	1	S-geranylgeranyl cysteine Ref.3
Experimental info
	Sequence conflict	125	1	W → S in AAA30416. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P11023 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: B77FB461DC25E79E	FASTA	220	24,954
	10 20 30 40 50 60 MASATDARYG 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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide and deduced amino acid sequences of a GTP-binding protein family with molecular weights of 25,000 from bovine brain." Matsui Y., Kikuchi A., Kondo J., Hishida T., Teranishi Y., Takai Y. J. Biol. Chem. 263:11071-11074(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Brain cortex.
[3]	"C-terminus of the small GTP-binding protein smg p25A contains two geranylgeranylated cysteine residues and a methyl ester." Farnsworth C.C., Kawata M., Yoshida Y., Takai Y., Gelb M.H., Glomset J.A. Proc. Natl. Acad. Sci. U.S.A. 88:6196-6200(1991) [PubMed] [Europe PMC] [Abstract] Cited for: ISOPRENYLATION AT CYS-218 AND CYS-220.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M19885 mRNA. Translation: AAA30416.1. BC118278 mRNA. Translation: AAI18279.1.
IPI	IPI00703436.
PIR	A29224.
RefSeq	NP_776871.2. NM_174446.3.
UniGene	Bt.2362.
3D structure databases
ProteinModelPortal	P11023.
SMR	P11023. Positions 18-186.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000014062.
Proteomic databases
PRIDE	P11023.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000014062; ENSBTAP00000014062; ENSBTAG00000010635.
GeneID	282029.
KEGG	bta:282029.
Organism-specific databases
CTD	5864.
Phylogenomic databases
eggNOG	COG1100.
GeneTree	ENSGT00690000101942.
HOGENOM	HOG000233968.
HOVERGEN	HBG009351.
InParanoid	P11023.
KO	K07882.
OMA	QLTEQPA.
OrthoDB	EOG4TB4C6.
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
NextBio	20805892.

Entry information

Entry name

RAB3A_BOVIN

Accession

Primary (citable) accession number: P11023
Secondary accession number(s): Q17QM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program