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Protein

Actin-related protein 2/3 complex subunit 4

Gene

Arpc4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Functions as actin-binding 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. Seems to contact the mother actin filament (By similarity).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 4
Alternative name(s):
Arp2/3 complex 20 kDa subunit
Short name:
p20-ARC
Gene namesi
Name:Arpc4
Synonyms:Arc20
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1915339. Arpc4.

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 – 168167Actin-related protein 2/3 complex subunit 4PRO_0000124050Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP59999.
MaxQBiP59999.
PaxDbiP59999.
PRIDEiP59999.
TopDownProteomicsiP59999.

PTM databases

iPTMnetiP59999.
PhosphoSiteiP59999.

Expressioni

Gene expression databases

BgeeiP59999.
CleanExiMM_ARPC4.
ExpressionAtlasiP59999. baseline and differential.
GenevisibleiP59999. 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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi212649. 2 interactions.
IntActiP59999. 5 interactions.
MINTiMINT-1858871.
STRINGi10090.ENSMUSP00000114839.

Structurei

3D structure databases

ProteinModelPortaliP59999.
SMRiP59999. Positions 2-168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ARPC4 family.Curated

Phylogenomic databases

eggNOGiKOG1876. Eukaryota.
ENOG4111G2F. LUCA.
GeneTreeiENSGT00390000016233.
HOGENOMiHOG000202303.
HOVERGENiHBG050582.
InParanoidiP59999.
KOiK05755.
OMAiMLKHKIV.
OrthoDBiEOG7VTDPM.
PhylomeDBiP59999.
TreeFamiTF105621.

Family and domain databases

InterProiIPR008384. ARPC4.
[Graphical view]
PANTHERiPTHR22629. PTHR22629. 1 hit.
PfamiPF05856. ARPC4. 1 hit.
[Graphical view]
PIRSFiPIRSF039100. ARPC4. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P59999-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTATLRPYLS AVRATLQAAL CLENFSSQVV ERHNKPEVEV RSSKELLLQP
60 70 80 90 100
VTISRNEKEK VLIEGSINSV RVSIAVKQAD EIEKILCHKF MRFMMMRAEN
110 120 130 140 150
FFILRRKPVE GYDISFLITN FHTEQMYKHK LVDFVIHFME EIDKEISEMK
160
LSVNARARIV AEEFLKNF
Length:168
Mass (Da):19,667
Last modified:January 23, 2007 - v3
Checksum:i273CCB230AC703DF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278129 mRNA. Translation: CAC34583.1.
AK017993 mRNA. Translation: BAB31026.1.
AK039215 mRNA. Translation: BAC30279.1.
AK077325 mRNA. Translation: BAC36751.1.
AK133626 mRNA. Translation: BAE21755.1.
AK136082 mRNA. Translation: BAE22810.1.
AK150690 mRNA. Translation: BAE29769.1.
AK153380 mRNA. Translation: BAE31946.1.
AK166440 mRNA. Translation: BAE38777.1.
BC015280 mRNA. No translation available.
CCDSiCCDS20417.1.
RefSeqiNP_001163956.1. NM_001170485.1.
NP_001163957.1. NM_001170486.1.
NP_080828.1. NM_026552.3.
UniGeneiMm.289306.
Mm.472172.

Genome annotation databases

EnsembliENSMUST00000156898; ENSMUSP00000114839; ENSMUSG00000079426.
GeneIDi68089.
KEGGimmu:68089.
UCSCiuc009dfs.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278129 mRNA. Translation: CAC34583.1.
AK017993 mRNA. Translation: BAB31026.1.
AK039215 mRNA. Translation: BAC30279.1.
AK077325 mRNA. Translation: BAC36751.1.
AK133626 mRNA. Translation: BAE21755.1.
AK136082 mRNA. Translation: BAE22810.1.
AK150690 mRNA. Translation: BAE29769.1.
AK153380 mRNA. Translation: BAE31946.1.
AK166440 mRNA. Translation: BAE38777.1.
BC015280 mRNA. No translation available.
CCDSiCCDS20417.1.
RefSeqiNP_001163956.1. NM_001170485.1.
NP_001163957.1. NM_001170486.1.
NP_080828.1. NM_026552.3.
UniGeneiMm.289306.
Mm.472172.

3D structure databases

ProteinModelPortaliP59999.
SMRiP59999. Positions 2-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212649. 2 interactions.
IntActiP59999. 5 interactions.
MINTiMINT-1858871.
STRINGi10090.ENSMUSP00000114839.

PTM databases

iPTMnetiP59999.
PhosphoSiteiP59999.

Proteomic databases

EPDiP59999.
MaxQBiP59999.
PaxDbiP59999.
PRIDEiP59999.
TopDownProteomicsiP59999.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000156898; ENSMUSP00000114839; ENSMUSG00000079426.
GeneIDi68089.
KEGGimmu:68089.
UCSCiuc009dfs.2. mouse.

Organism-specific databases

CTDi10093.
MGIiMGI:1915339. Arpc4.

Phylogenomic databases

eggNOGiKOG1876. Eukaryota.
ENOG4111G2F. LUCA.
GeneTreeiENSGT00390000016233.
HOGENOMiHOG000202303.
HOVERGENiHBG050582.
InParanoidiP59999.
KOiK05755.
OMAiMLKHKIV.
OrthoDBiEOG7VTDPM.
PhylomeDBiP59999.
TreeFamiTF105621.

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

PROiP59999.
SOURCEiSearch...

Gene expression databases

BgeeiP59999.
CleanExiMM_ARPC4.
ExpressionAtlasiP59999. baseline and differential.
GenevisibleiP59999. MM.

Family and domain databases

InterProiIPR008384. ARPC4.
[Graphical view]
PANTHERiPTHR22629. PTHR22629. 1 hit.
PfamiPF05856. ARPC4. 1 hit.
[Graphical view]
PIRSFiPIRSF039100. ARPC4. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Full-length sequencing of some human and murine muscular transcripts (Telethon Italy project B41)."
    Ievolella C., Campagna D., Lanfranchi G.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  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: Bone marrow, Egg, Hypothalamus, Mammary gland, Pituitary and Thymus.
  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: Kidney.
  4. Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-41; 45-55; 61-71; 98-105; 107-128; 131-150 AND 159-166, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic fibroblast.
  5. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 98-105, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  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 nameiARPC4_MOUSE
AccessioniPrimary (citable) accession number: P59999
Secondary accession number(s): O15509, Q3UWV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 107 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.