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Protein

Actin-related protein 2/3 complex subunit 3

Gene

Arpc3

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-bindingUniRule annotation

Enzyme and pathway databases

ReactomeiR-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-3928662. EPHB-mediated forward signaling.
R-RNO-5663213. RHO GTPases Activate WASPs and WAVEs.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-related protein 2/3 complex subunit 3UniRule annotation
Alternative name(s):
Arp2/3 complex 21 kDa subunitUniRule annotation
Gene namesi
Name:Arpc3Imported
Synonyms:Arpc3_predictedImported
ORF Names:rCG_21863Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi1311985. Arpc3.

Subcellular locationi

  • Cytoplasmcytoskeleton UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, CytoskeletonUniRule annotation

Interactioni

Subunit structurei

Component of the Arp2/3 complex.UniRule annotation

Protein-protein interaction databases

MINTiMINT-7138161.
STRINGi10116.ENSRNOP00000011499.

Family & Domainsi

Sequence similaritiesi

Belongs to the ARPC3 family.UniRule annotation

Phylogenomic databases

eggNOGiKOG3155. Eukaryota.
ENOG4111FTG. LUCA.
GeneTreeiENSGT00390000018018.
HOGENOMiHOG000161465.
HOVERGENiHBG050581.
KOiK05756.
OMAiPLNQMYE.
OrthoDBiEOG7BS4BV.
TreeFamiTF314598.

Family and domain databases

Gene3Di1.10.1760.10. 1 hit.
InterProiIPR007204. ARPC3.
[Graphical view]
PANTHERiPTHR12391. PTHR12391. 1 hit.
PfamiPF04062. P21-Arc. 1 hit.
[Graphical view]
PIRSFiPIRSF016315. ARP2/3_P21-Arc. 1 hit.
SUPFAMiSSF69060. SSF69060. 1 hit.

Sequencei

Sequence statusi: Complete.

B2GV73-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAYHSSLMD PDTKLIGNMA LLPIRSQFKG PAPRETKDTD IVDEAIYYFK
60 70 80 90 100
ANVFFKNYEI KNEADRTLIY ITLYISECLK KLQKCNSRSQ GEKEMYTLGI
110 120 130 140 150
TNFPIPGEPG FPLNAIYAKP ASKQEDETMR AYLQQLRQET GLRLCDKVFD
160 170
PQNDKPSKWW TCFVKRQFMN KSLSGPGQ
Length:178
Mass (Da):20,536
Last modified:June 10, 2008 - v1
Checksum:iB9CFF43107C667B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC104314 Genomic DNA. No translation available.
BC166554 mRNA. Translation: AAI66554.1.
CH473973 Genomic DNA. Translation: EDM13687.1.
RefSeqiNP_001099403.1. NM_001105933.1.
UniGeneiRn.4233.

Genome annotation databases

EnsembliENSRNOT00000011499; ENSRNOP00000011499; ENSRNOG00000008673.
GeneIDi288669.
KEGGirno:288669.
UCSCiRGD:1311985. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC104314 Genomic DNA. No translation available.
BC166554 mRNA. Translation: AAI66554.1.
CH473973 Genomic DNA. Translation: EDM13687.1.
RefSeqiNP_001099403.1. NM_001105933.1.
UniGeneiRn.4233.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-7138161.
STRINGi10116.ENSRNOP00000011499.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000011499; ENSRNOP00000011499; ENSRNOG00000008673.
GeneIDi288669.
KEGGirno:288669.
UCSCiRGD:1311985. rat.

Organism-specific databases

CTDi10094.
RGDi1311985. Arpc3.

Phylogenomic databases

eggNOGiKOG3155. Eukaryota.
ENOG4111FTG. LUCA.
GeneTreeiENSGT00390000018018.
HOGENOMiHOG000161465.
HOVERGENiHBG050581.
KOiK05756.
OMAiPLNQMYE.
OrthoDBiEOG7BS4BV.
TreeFamiTF314598.

Enzyme and pathway databases

ReactomeiR-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-3928662. EPHB-mediated forward signaling.
R-RNO-5663213. RHO GTPases Activate WASPs and WAVEs.

Family and domain databases

Gene3Di1.10.1760.10. 1 hit.
InterProiIPR007204. ARPC3.
[Graphical view]
PANTHERiPTHR12391. PTHR12391. 1 hit.
PfamiPF04062. P21-Arc. 1 hit.
[Graphical view]
PIRSFiPIRSF016315. ARP2/3_P21-Arc. 1 hit.
SUPFAMiSSF69060. SSF69060. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: OvaryImported.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  5. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiB2GV73_RAT
AccessioniPrimary (citable) accession number: B2GV73
Secondary accession number(s): F1LRL8
Entry historyi
Integrated into UniProtKB/TrEMBL: June 10, 2008
Last sequence update: June 10, 2008
Last modified: June 8, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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 one 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.