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Protein

Actin-related protein 2/3 complex subunit 3

Gene

ARPC3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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

ReactomeiREACT_307278. EPHB-mediated forward signaling.
REACT_319858. Regulation of actin dynamics for phagocytic cup formation.
REACT_358247. 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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 17

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 methioninei1 – 11RemovedBy similarity
Chaini2 – 178177Actin-related protein 2/3 complex subunit 3PRO_0000246171Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ3T035.
PRIDEiQ3T035.

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-29793N.
STRINGi9913.ENSBTAP00000007028.

Structurei

Secondary structure

1
178
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 163Combined sources
Beta strandi19 – 213Combined sources
Beta strandi36 – 383Combined sources
Helixi41 – 5212Combined sources
Helixi63 – 8220Combined sources
Helixi88 – 10013Combined sources
Turni112 – 1165Combined sources
Helixi123 – 14826Combined sources
Beta strandi151 – 1544Combined sources
Helixi158 – 1614Combined sources
Turni162 – 1654Combined sources
Helixi168 – 1703Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8KX-ray2.00E1-178[»]
1TYQX-ray2.55E1-178[»]
1U2VX-ray2.55E1-178[»]
2P9IX-ray2.46E1-178[»]
2P9KX-ray2.59E1-178[»]
2P9LX-ray2.65E1-178[»]
2P9NX-ray2.85E1-178[»]
2P9PX-ray2.90E1-178[»]
2P9SX-ray2.68E1-178[»]
2P9UX-ray2.75E1-178[»]
3DXKX-ray2.70E1-178[»]
3DXMX-ray2.85E1-178[»]
3RSEX-ray2.65E1-178[»]
3UKRX-ray2.48E1-178[»]
3UKUX-ray2.75E1-178[»]
3ULEX-ray2.50E1-178[»]
4JD2X-ray3.08E1-178[»]
ProteinModelPortaliQ3T035.
SMRiQ3T035. Positions 2-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3T035.

Family & Domainsi

Sequence similaritiesi

Belongs to the ARPC3 family.Curated

Phylogenomic databases

eggNOGiNOG324671.
GeneTreeiENSGT00390000018018.
HOGENOMiHOG000161465.
HOVERGENiHBG050581.
InParanoidiQ3T035.
KOiK05756.
OMAiTGKPSKW.
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.

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

Q3T035-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAYHSSLMD PDTKLIGNMA LLPIRSQFKG PAPRETKDTD IVDEAIYYFK
60 70 80 90 100
ANVFFKNYEI KNEADRTLIY ITLYISECLK KLQKCNSKSQ GEKEMYTLGI
110 120 130 140 150
TNFPIPGEPG FPLNAIYAKP ANKQEDEVMR AYLQQLRQET GLRLCEKVFD
160 170
PQNDKPSKWW TCFVKRQFMN KSLSGPGQ
Length:178
Mass (Da):20,547
Last modified:January 23, 2007 - v3
Checksum:i7149F598B48F0EAC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102590 mRNA. Translation: AAI02591.1.
RefSeqiNP_001029443.1. NM_001034271.2.
UniGeneiBt.59092.

Genome annotation databases

EnsembliENSBTAT00000007028; ENSBTAP00000007028; ENSBTAG00000005345.
GeneIDi506596.
KEGGibta:506596.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102590 mRNA. Translation: AAI02591.1.
RefSeqiNP_001029443.1. NM_001034271.2.
UniGeneiBt.59092.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8KX-ray2.00E1-178[»]
1TYQX-ray2.55E1-178[»]
1U2VX-ray2.55E1-178[»]
2P9IX-ray2.46E1-178[»]
2P9KX-ray2.59E1-178[»]
2P9LX-ray2.65E1-178[»]
2P9NX-ray2.85E1-178[»]
2P9PX-ray2.90E1-178[»]
2P9SX-ray2.68E1-178[»]
2P9UX-ray2.75E1-178[»]
3DXKX-ray2.70E1-178[»]
3DXMX-ray2.85E1-178[»]
3RSEX-ray2.65E1-178[»]
3UKRX-ray2.48E1-178[»]
3UKUX-ray2.75E1-178[»]
3ULEX-ray2.50E1-178[»]
4JD2X-ray3.08E1-178[»]
ProteinModelPortaliQ3T035.
SMRiQ3T035. Positions 2-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29793N.
STRINGi9913.ENSBTAP00000007028.

Proteomic databases

PaxDbiQ3T035.
PRIDEiQ3T035.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000007028; ENSBTAP00000007028; ENSBTAG00000005345.
GeneIDi506596.
KEGGibta:506596.

Organism-specific databases

CTDi10094.

Phylogenomic databases

eggNOGiNOG324671.
GeneTreeiENSGT00390000018018.
HOGENOMiHOG000161465.
HOVERGENiHBG050581.
InParanoidiQ3T035.
KOiK05756.
OMAiTGKPSKW.
OrthoDBiEOG7BS4BV.
TreeFamiTF314598.

Enzyme and pathway databases

ReactomeiREACT_307278. EPHB-mediated forward signaling.
REACT_319858. Regulation of actin dynamics for phagocytic cup formation.
REACT_358247. RHO GTPases Activate WASPs and WAVEs.

Miscellaneous databases

EvolutionaryTraceiQ3T035.
NextBioi20867671.

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. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Liver.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF ARP2/3 COMPLEX WITH BOUND ATP.

Entry informationi

Entry nameiARPC3_BOVIN
AccessioniPrimary (citable) accession number: Q3T035
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 83 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.