Reviewed, UniProtKB/Swiss-Prot P20336 (RAB3A_HUMAN)

Names and origin

Protein names

Recommended name:
    Ras-related protein Rab-3A

Gene names

Name:

RAB3A

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	220 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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 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
Gene Ontology (GO)
Biological process	protein transport Inferred from electronic annotation. Source: UniProtKB-KW small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	clathrin sculpted acetylcholine transport vesicle membrane Inferred from Experiment. Source: Reactome plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW synaptic vesicle Traceable author statement. Source: ProtInc
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Ref.1 Inferred from mutant phenotype. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB
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_0000121076
Regions
	Nucleotide binding	29 – 36	8	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.10
	Lipidation	220	1	S-geranylgeranyl cysteine Ref.10
Experimental info
	Sequence conflict	70	1	R → K in AAF67748. Ref.2
	Sequence conflict	180	1	V → E in AAF67748. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P20336-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 08B59F8C9BD2EB40	FASTA	220	24,984
	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 AKQGPQLSDQ QVPPHQDCAC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion." Zahraoui A., Touchot N., Chardin P., Tavitian A. J. Biol. Chem. 264:12394-12401(1989) [PubMed: 2501306] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genomic organisation of the human cyclic AMP-specific phosphodiesterase PDE4C gene and its chromosomal localisation to 19p13.1, between RAB3A and JUND." Sullivan M., Olsen A.S., Houslay M.D. Cell. Signal. 11:735-742(1999) [PubMed: 10574328] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Functional cloning and characterization of human fetal brain cDNAs." Liu Y., Li J., He J.J. Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[4]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Puhl H.L. III, Ikeda S.R., Aronstam R.S. Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[6]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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: Lung.
[9]	"Isoprenoid modification of rab proteins terminating in CC or CXC motifs." Khosravi-Far R., Lutz R.J., Cox A.D., Conroy L., Bourne J.R., Sinensky M., Balch W.E., Buss J.E., Der C.J. Proc. Natl. Acad. Sci. U.S.A. 88:6264-6268(1991) [PubMed: 1648736] [Abstract] Cited for: ISOPRENYLATION AT CYS-218 AND CYS-220.
[10]	"Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A." Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A. Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994) [PubMed: 7991565] [Abstract] Cited for: ISOPRENYLATION AT CYS-218 AND CYS-220, MASS SPECTROMETRY.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M28210 mRNA. Translation: AAA60242.1. AF157809 , AF157806, AF157807, AF157808 Genomic DNA. Translation: AAD46811.1. AF254795 mRNA. Translation: AAF67748.1. AF498931 mRNA. Translation: AAM21079.1. AK289559 mRNA. Translation: BAF82248.1. AC068499 Genomic DNA. Translation: AAF67385.1. CH471106 Genomic DNA. Translation: EAW84672.1. BC011782 mRNA. Translation: AAH11782.1.
IPI	IPI00023504.
PIR	C34323.
RefSeq	NP_002857.1.
UniGene	Hs.27744
3D structure databases
SMR	P20336. Positions 19-192.
ModBase	Search...
Protein-protein interaction databases
IntAct	P20336. 1 interaction.
STRING	P20336.
PTM databases
PhosphoSite	P20336.
Proteomic databases
PRIDE	P20336.
Genome annotation databases
Ensembl	ENST00000222256; ENSP00000222256; ENSG00000105649; Homo sapiens. [Genome view]
GeneID	5864.
KEGG	hsa:5864.
UCSC	uc002nie.1. human.
Organism-specific databases
CTD	5864.
GeneCards	GC19M018168.
H-InvDB	HIX0014906.
HGNC	HGNC:9777. RAB3A.
HPA	CAB009949. HPA003160.
MIM	179490. gene.
PharmGKB	PA34132.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P20336.
HOVERGEN	P20336.
OMA	KLVEIIC
Enzyme and pathway databases
Reactome	REACT_13685. Synaptic Transmission.
Gene expression databases
ArrayExpress	P20336.
Bgee	P20336.
CleanEx	HS_RAB3A.
Genevestigator	P20336.
GermOnline	ENSG00000105649. Homo sapiens.
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	22774.
SOURCE	Search...

Entry information

Entry name

RAB3A_HUMAN

Accession

Primary (citable) accession number: P20336
Secondary accession number(s): A8K0J4, Q9NYE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	November 24, 2009
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.