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Protein

Actin-related protein 2/3 complex subunit 4

Gene

ARPC4

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 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

  1. structural constituent of cytoskeleton Source: Ensembl

GO - Biological processi

  1. actin filament polymerization Source: InterPro
  2. Arp2/3 complex-mediated actin nucleation Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_307278. EPHB-mediated forward signaling.
REACT_319858. Regulation of actin dynamics for phagocytic cup formation.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 22

Subcellular locationi

Cytoplasmcytoskeleton By similarity. Cell projection By similarity

GO - Cellular componenti

  1. Arp2/3 protein complex Source: InterPro
  2. cell projection Source: UniProtKB-SubCell
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 168167Actin-related protein 2/3 complex subunit 4PRO_0000269565Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ148J6.

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.

Protein-protein interaction databases

DIPiDIP-29794N.
STRINGi9913.ENSBTAP00000010469.

Structurei

Secondary structure

1
168
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1915Combined sources
Beta strandi28 – 303Combined sources
Helixi37 – 404Combined sources
Helixi44 – 463Combined sources
Beta strandi51 – 588Combined sources
Beta strandi60 – 7516Combined sources
Helixi81 – 9616Combined sources
Turni97 – 1004Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi113 – 1197Combined sources
Helixi120 – 1256Combined sources
Helixi128 – 16538Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8KX-ray2.00F1-168[»]
1TYQX-ray2.55F1-168[»]
1U2VX-ray2.55F1-168[»]
2P9IX-ray2.46F1-168[»]
2P9KX-ray2.59F1-168[»]
2P9LX-ray2.65F1-168[»]
2P9NX-ray2.85F1-168[»]
2P9PX-ray2.90F1-168[»]
2P9SX-ray2.68F1-168[»]
2P9UX-ray2.75F1-168[»]
3DXKX-ray2.70F1-168[»]
3DXMX-ray2.85F1-168[»]
3RSEX-ray2.65F1-168[»]
3UKRX-ray2.48F1-168[»]
3UKUX-ray2.75F1-168[»]
3ULEX-ray2.50F1-168[»]
4JD2X-ray3.08F1-168[»]
ProteinModelPortaliQ148J6.
SMRiQ148J6. Positions 2-168.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ148J6.

Family & Domainsi

Sequence similaritiesi

Belongs to the ARPC4 family.Curated

Phylogenomic databases

eggNOGiNOG261545.
GeneTreeiENSGT00390000016233.
HOGENOMiHOG000202303.
HOVERGENiHBG050582.
InParanoidiQ148J6.
KOiK05755.
OMAiMLKHKIV.
OrthoDBiEOG7VTDPM.
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.

Q148J6-1 [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 22, 2007 - v3
Checksum:i273CCB230AC703DF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC118263 mRNA. Translation: AAI18264.1.
RefSeqiNP_001069631.1. NM_001076163.1.
UniGeneiBt.106660.

Genome annotation databases

EnsembliENSBTAT00000010469; ENSBTAP00000010469; ENSBTAG00000007964.
GeneIDi539459.
KEGGibta:539459.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC118263 mRNA. Translation: AAI18264.1.
RefSeqiNP_001069631.1. NM_001076163.1.
UniGeneiBt.106660.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8KX-ray2.00F1-168[»]
1TYQX-ray2.55F1-168[»]
1U2VX-ray2.55F1-168[»]
2P9IX-ray2.46F1-168[»]
2P9KX-ray2.59F1-168[»]
2P9LX-ray2.65F1-168[»]
2P9NX-ray2.85F1-168[»]
2P9PX-ray2.90F1-168[»]
2P9SX-ray2.68F1-168[»]
2P9UX-ray2.75F1-168[»]
3DXKX-ray2.70F1-168[»]
3DXMX-ray2.85F1-168[»]
3RSEX-ray2.65F1-168[»]
3UKRX-ray2.48F1-168[»]
3UKUX-ray2.75F1-168[»]
3ULEX-ray2.50F1-168[»]
4JD2X-ray3.08F1-168[»]
ProteinModelPortaliQ148J6.
SMRiQ148J6. Positions 2-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29794N.
STRINGi9913.ENSBTAP00000010469.

Proteomic databases

PRIDEiQ148J6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000010469; ENSBTAP00000010469; ENSBTAG00000007964.
GeneIDi539459.
KEGGibta:539459.

Organism-specific databases

CTDi10093.

Phylogenomic databases

eggNOGiNOG261545.
GeneTreeiENSGT00390000016233.
HOGENOMiHOG000202303.
HOVERGENiHBG050582.
InParanoidiQ148J6.
KOiK05755.
OMAiMLKHKIV.
OrthoDBiEOG7VTDPM.
TreeFamiTF105621.

Enzyme and pathway databases

ReactomeiREACT_307278. EPHB-mediated forward signaling.
REACT_319858. Regulation of actin dynamics for phagocytic cup formation.

Miscellaneous databases

EvolutionaryTraceiQ148J6.
NextBioi20878000.

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. NIH - Mammalian Gene Collection (MGC) project
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Basal ganglia.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF ARP2/3 COMPLEX.
  3. "Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP."
    Nolen B.J., Littlefield R.S., Pollard T.D.
    Proc. Natl. Acad. Sci. U.S.A. 101:15627-15632(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF ARP2/3 COMPLEX WITH BOUND ATP.

Entry informationi

Entry nameiARPC4_BOVIN
AccessioniPrimary (citable) accession number: Q148J6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 11, 2006
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 76 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.