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Protein

Actin-related protein 2/3 complex subunit 3

Gene

Arpc3

Organism
Mus musculus (Mouse)
Status
Reviewed-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.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-related protein 2/3 complex subunit 3
Alternative name(s):
Arp2/3 complex 21 kDa subunit
Short name:
p21-ARC
Gene namesi
Name:Arpc3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1928375. Arpc3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 178177Actin-related protein 2/3 complex subunit 3PRO_0000124043Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471PhosphotyrosineCombined sources
Modified residuei56 – 561N6-acetyllysineBy similarity
Modified residuei61 – 611N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9JM76.
MaxQBiQ9JM76.
PaxDbiQ9JM76.
PRIDEiQ9JM76.
TopDownProteomicsiQ9JM76.

PTM databases

iPTMnetiQ9JM76.
PhosphoSiteiQ9JM76.
SwissPalmiQ9JM76.

Expressioni

Gene expression databases

BgeeiQ9JM76.
CleanExiMM_ARPC3.
ExpressionAtlasiQ9JM76. baseline and differential.
GenevisibleiQ9JM76. MM.

Interactioni

Subunit structurei

Component of the Arp2/3 complex composed of ARP2, ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC.By similarity

Protein-protein interaction databases

BioGridi207939. 1 interaction.
IntActiQ9JM76. 4 interactions.
MINTiMINT-1857076.
STRINGi10090.ENSMUSP00000099584.

Structurei

3D structure databases

ProteinModelPortaliQ9JM76.
SMRiQ9JM76. Positions 2-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ARPC3 family.Curated

Phylogenomic databases

eggNOGiKOG3155. Eukaryota.
ENOG4111FTG. LUCA.
GeneTreeiENSGT00390000018018.
HOGENOMiHOG000161465.
HOVERGENiHBG050581.
InParanoidiQ9JM76.
KOiK05756.
OMAiESLYYWK.
OrthoDBiEOG7BS4BV.
PhylomeDBiQ9JM76.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JM76-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAYHSSLMD PDTKLIGNMA LLPLRSQFKG PAPRETKDTD IVDEAIYYFK
60 70 80 90 100
ANVFFKNYEI KNEADRTLIY ITLYISECLK KLQKCNSKSQ GEKEMYTLGI
110 120 130 140 150
TNFPIPGEPG FPLNAIYAKP ASKQEDEMMR AYLQQLRQET GLRLCEKVFD
160 170
PQSDKPSKWW TCFVKRQFMN KSLSGPGQ
Length:178
Mass (Da):20,525
Last modified:January 23, 2007 - v3
Checksum:i6B4F467F89BF4BAC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038243 mRNA. Translation: BAA90788.1.
AK003485 mRNA. Translation: BAB22813.1.
AK005437 mRNA. Translation: BAB24031.1.
AK171651 mRNA. Translation: BAE42588.1.
BC013618 mRNA. Translation: AAH13618.1.
BC054440 mRNA. Translation: AAH54440.1.
CCDSiCCDS19648.1.
RefSeqiNP_062798.1. NM_019824.4.
UniGeneiMm.275942.

Genome annotation databases

EnsembliENSMUST00000102525; ENSMUSP00000099584; ENSMUSG00000029465.
GeneIDi56378.
KEGGimmu:56378.
UCSCiuc008zlf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038243 mRNA. Translation: BAA90788.1.
AK003485 mRNA. Translation: BAB22813.1.
AK005437 mRNA. Translation: BAB24031.1.
AK171651 mRNA. Translation: BAE42588.1.
BC013618 mRNA. Translation: AAH13618.1.
BC054440 mRNA. Translation: AAH54440.1.
CCDSiCCDS19648.1.
RefSeqiNP_062798.1. NM_019824.4.
UniGeneiMm.275942.

3D structure databases

ProteinModelPortaliQ9JM76.
SMRiQ9JM76. Positions 2-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207939. 1 interaction.
IntActiQ9JM76. 4 interactions.
MINTiMINT-1857076.
STRINGi10090.ENSMUSP00000099584.

PTM databases

iPTMnetiQ9JM76.
PhosphoSiteiQ9JM76.
SwissPalmiQ9JM76.

Proteomic databases

EPDiQ9JM76.
MaxQBiQ9JM76.
PaxDbiQ9JM76.
PRIDEiQ9JM76.
TopDownProteomicsiQ9JM76.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102525; ENSMUSP00000099584; ENSMUSG00000029465.
GeneIDi56378.
KEGGimmu:56378.
UCSCiuc008zlf.1. mouse.

Organism-specific databases

CTDi10094.
MGIiMGI:1928375. Arpc3.

Phylogenomic databases

eggNOGiKOG3155. Eukaryota.
ENOG4111FTG. LUCA.
GeneTreeiENSGT00390000018018.
HOGENOMiHOG000161465.
HOVERGENiHBG050581.
InParanoidiQ9JM76.
KOiK05756.
OMAiESLYYWK.
OrthoDBiEOG7BS4BV.
PhylomeDBiQ9JM76.
TreeFamiTF314598.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi312452.
PROiQ9JM76.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JM76.
CleanExiMM_ARPC3.
ExpressionAtlasiQ9JM76. baseline and differential.
GenevisibleiQ9JM76. MM.

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. Sugiura S.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Peritoneal macrophage.
  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 and NOD.
    Tissue: Embryo, Placenta and Spleen.
  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].
    Strain: Czech II and FVB/N.
    Tissue: Colon and Mammary tumor.
  4. Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-25; 38-50; 94-119; 131-137 AND 148-158, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic fibroblast.
  5. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiARPC3_MOUSE
AccessioniPrimary (citable) accession number: Q9JM76
Secondary accession number(s): Q3TAT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 112 of the entry and version 3 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

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.