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Protein

Ras-related protein Rab-3A

Gene

Rab3a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 368GTPBy similarity
Nucleotide bindingi48 – 547GTPBy similarity
Nucleotide bindingi77 – 815GTPBy similarity
Nucleotide bindingi135 – 1384GTPBy similarity

GO - Molecular functioni

GO - Biological processi

  • axonogenesis Source: MGI
  • evoked neurotransmitter secretion Source: ParkinsonsUK-UCL
  • intracellular protein transport Source: GO_Central
  • lung development Source: MGI
  • maintenance of presynaptic active zone structure Source: MGI
  • metabolic process Source: MGI
  • mitochondrion organization Source: MGI
  • neuromuscular synaptic transmission Source: MGI
  • positive regulation of regulated secretory pathway Source: MGI
  • post-embryonic development Source: MGI
  • protein secretion Source: GO_Central
  • Rab protein signal transduction Source: GO_Central
  • regulation of exocytosis Source: MGI
  • regulation of long-term synaptic potentiation Source: ParkinsonsUK-UCL
  • regulation of short-term neuronal synaptic plasticity Source: ParkinsonsUK-UCL
  • regulation of synaptic vesicle fusion to presynaptic membrane Source: ParkinsonsUK-UCL
  • respiratory system process Source: MGI
  • response to electrical stimulus Source: MGI
  • sensory perception of touch Source: MGI
  • synaptic vesicle exocytosis Source: ParkinsonsUK-UCL
  • synaptic vesicle maturation Source: MGI
  • synaptic vesicle recycling Source: ParkinsonsUK-UCL
  • synaptic vesicle transport Source: ParkinsonsUK-UCL
  • vesicle docking involved in exocytosis Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Exocytosis, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_281668. Acetylcholine Neurotransmitter Release Cycle.
REACT_287745. Glutamate Neurotransmitter Release Cycle.
REACT_319523. GABA synthesis, release, reuptake and degradation.
REACT_325189. Norepinephrine Neurotransmitter Release Cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-3A
Gene namesi
Name:Rab3a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:97843. Rab3a.

Subcellular locationi

GO - Cellular componenti

  • acrosomal vesicle Source: MGI
  • axon Source: ParkinsonsUK-UCL
  • cytosol Source: Ensembl
  • endosome Source: MGI
  • plasma membrane Source: GO_Central
  • protein complex Source: Ensembl
  • secretory granule membrane Source: GO_Central
  • synaptic vesicle Source: MGI
  • terminal bouton Source: ParkinsonsUK-UCL
  • vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 220220Ras-related protein Rab-3APRO_0000121078Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi218 – 2181S-geranylgeranyl cysteineBy similarity
Modified residuei220 – 2201Cysteine methyl esterBy similarity
Lipidationi220 – 2201S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP63011.
PaxDbiP63011.
PRIDEiP63011.

PTM databases

PhosphoSiteiP63011.

Expressioni

Gene expression databases

BgeeiP63011.
CleanExiMM_RAB3A.
ExpressionAtlasiP63011. baseline and differential.
GenevisibleiP63011. MM.

Interactioni

Subunit structurei

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, RIMS1 and RIMS2. Interacts with RAB3IP. Interacts with SGSM1 and SGSM3.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Rph3aP477082EBI-398393,EBI-398376
SYTL5Q8TDW52EBI-398393,EBI-2939487From a different organism.

Protein-protein interaction databases

BioGridi202544. 7 interactions.
DIPiDIP-31051N.
IntActiP63011. 12 interactions.
MINTiMINT-85820.
STRINGi10090.ENSMUSP00000034301.

Structurei

3D structure databases

ProteinModelPortaliP63011.
SMRiP63011. Positions 18-186.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi51 – 599Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP63011.
KOiK07882.
OMAiQLTEQPA.
OrthoDBiEOG7JQBPC.
PhylomeDBiP63011.
TreeFamiTF313199.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P63011-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASATDSRYG QKESSDQNFD YMFKILIIGN SSVGKTSFLF RYADDSFTPA
60 70 80 90 100
FVSTVGIDFK VKTIYRNDKR IKLQIWDTAG QERYRTITTA YYRGAMGFIL
110 120 130 140 150
MYDITNEESF NAVQDWSTQI KTYSWDNAQV LLVGNKCDME DERVVSSERG
160 170 180 190 200
RQLADHLGFE FFEASAKDNI NVKQTFERLV DVICEKMSES LDTADPAVTG
210 220
AKQGPQLTDQ QAPPHQDCAC
Length:220
Mass (Da):24,970
Last modified:August 31, 2004 - v1
Checksum:i1A3E9F8C9D09EB40
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72966 Genomic DNA. Translation: CAA51470.1.
AK005362 mRNA. Translation: BAB23976.1.
AK158727 mRNA. Translation: BAE34630.1.
AK161975 mRNA. Translation: BAE36661.1.
BC053519 mRNA. Translation: AAH53519.1.
CCDSiCCDS22379.1.
PIRiS34070.
RefSeqiNP_001159871.1. NM_001166399.2.
NP_033027.1. NM_009001.6.
XP_006509665.1. XM_006509602.2.
XP_006509666.1. XM_006509603.2.
UniGeneiMm.5083.

Genome annotation databases

EnsembliENSMUST00000034301; ENSMUSP00000034301; ENSMUSG00000031840.
ENSMUST00000110090; ENSMUSP00000105717; ENSMUSG00000031840.
ENSMUST00000110092; ENSMUSP00000105719; ENSMUSG00000031840.
ENSMUST00000110093; ENSMUSP00000105720; ENSMUSG00000031840.
GeneIDi19339.
KEGGimmu:19339.
UCSCiuc009mbi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72966 Genomic DNA. Translation: CAA51470.1.
AK005362 mRNA. Translation: BAB23976.1.
AK158727 mRNA. Translation: BAE34630.1.
AK161975 mRNA. Translation: BAE36661.1.
BC053519 mRNA. Translation: AAH53519.1.
CCDSiCCDS22379.1.
PIRiS34070.
RefSeqiNP_001159871.1. NM_001166399.2.
NP_033027.1. NM_009001.6.
XP_006509665.1. XM_006509602.2.
XP_006509666.1. XM_006509603.2.
UniGeneiMm.5083.

3D structure databases

ProteinModelPortaliP63011.
SMRiP63011. Positions 18-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202544. 7 interactions.
DIPiDIP-31051N.
IntActiP63011. 12 interactions.
MINTiMINT-85820.
STRINGi10090.ENSMUSP00000034301.

PTM databases

PhosphoSiteiP63011.

Proteomic databases

MaxQBiP63011.
PaxDbiP63011.
PRIDEiP63011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034301; ENSMUSP00000034301; ENSMUSG00000031840.
ENSMUST00000110090; ENSMUSP00000105717; ENSMUSG00000031840.
ENSMUST00000110092; ENSMUSP00000105719; ENSMUSG00000031840.
ENSMUST00000110093; ENSMUSP00000105720; ENSMUSG00000031840.
GeneIDi19339.
KEGGimmu:19339.
UCSCiuc009mbi.2. mouse.

Organism-specific databases

CTDi5864.
MGIiMGI:97843. Rab3a.

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP63011.
KOiK07882.
OMAiQLTEQPA.
OrthoDBiEOG7JQBPC.
PhylomeDBiP63011.
TreeFamiTF313199.

Enzyme and pathway databases

ReactomeiREACT_281668. Acetylcholine Neurotransmitter Release Cycle.
REACT_287745. Glutamate Neurotransmitter Release Cycle.
REACT_319523. GABA synthesis, release, reuptake and degradation.
REACT_325189. Norepinephrine Neurotransmitter Release Cycle.

Miscellaneous databases

ChiTaRSiRab3a. mouse.
NextBioi296339.
PROiP63011.
SOURCEiSearch...

Gene expression databases

BgeeiP63011.
CleanExiMM_RAB3A.
ExpressionAtlasiP63011. baseline and differential.
GenevisibleiP63011. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the murine rab3A gene: correlation of genomic organization with antibody epitopes."
    Baumert M., Fischer von Mollard G., Jahn R., Suedhof T.C.
    Biochem. J. 293:157-163(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum and Visual cortex.
  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: Eye.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 13-35; 42-60; 73-83; 122-136; 152-167 AND 179-202, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  5. Cited for: INTERACTION WITH RIMS2.
  6. "Rim1 and rabphilin-3 bind Rab3-GTP by composite determinants partially related through N-terminal alpha-helix motifs."
    Wang X., Hu B., Zimmermann B., Kilimann M.W.
    J. Biol. Chem. 276:32480-32488(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RIMS1.
  7. "Piccolo, a Ca2+ sensor in pancreatic beta-cells. Involvement of cAMP-GEFII.Rim2.Piccolo complex in cAMP-dependent exocytosis."
    Fujimoto K., Shibasaki T., Yokoi N., Kashima Y., Matsumoto M., Sasaki T., Tajima N., Iwanaga T., Seino S.
    J. Biol. Chem. 277:50497-50502(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RIMS2.
  8. "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2."
    Fukuda M.
    J. Biol. Chem. 278:15373-15380(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RIMS1; RIMS2; RPH3A AND RPH3AL.
  9. "Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through interaction with the GDP-bound form of Rab27A in PC12 cells."
    Fukuda M.
    J. Biol. Chem. 278:15390-15396(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYTL4.
  10. "Identification of three novel proteins (SGSM1, 2, 3) which modulate small G protein (RAP and RAB)-mediated signaling pathway."
    Yang H., Sasaki T., Minoshima S., Shimizu N.
    Genomics 90:249-260(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGSM1 AND SGSM3.

Entry informationi

Entry nameiRAB3A_MOUSE
AccessioniPrimary (citable) accession number: P63011
Secondary accession number(s): P05713, Q3TSL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: June 24, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.