Reviewed, UniProtKB/Swiss-Prot O15145 (ARPC3_HUMAN)

Names and origin

Protein names

Recommended name:
    Actin-related protein 2/3 complex subunit 3
Alternative name(s):
    Arp2/3 complex 21 kDa subunit
      Short name=p21-ARC

Gene names

Name:	ARPC3
Synonyms:	ARC21

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	178 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Subunit structure	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.
Subcellular location	Cytoplasm › cytoskeleton. Cell projection Ref.1 Ref.2.
Sequence similarities	Belongs to the ARPC3 family.

Ontologies

Keywords
Cellular component	Cell projection Cytoplasm Cytoskeleton
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular component movement Ref.2 Traceable author statement. Source: ProtInc regulation of actin filament polymerization Inferred from electronic annotation. Source: InterPro
Cellular component	Arp2/3 protein complex Ref.2 Traceable author statement. Source: ProtInc cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of cytoskeleton Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACTR3B	Q9P1U1	1	EBI-351829,EBI-1047175

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 178	177	Actin-related protein 2/3 complex subunit 3		PRO_0000124042
Amino acid modifications
	Modified residue	47	1	Phosphotyrosine Ref.7
	Modified residue	56	1	N6-acetyllysine Ref.10
	Modified residue	61	1	N6-acetyllysine Ref.10
Experimental info
	Sequence conflict	134	1	Q → P in AAB61466. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O15145-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 7149F598B48F0EAC	FASTA	178	20,547
	10 20 30 40 50 60 MPAYHSSLMD PDTKLIGNMA LLPIRSQFKG PAPRETKDTD IVDEAIYYFK ANVFFKNYEI 70 80 90 100 110 120 KNEADRTLIY ITLYISECLK KLQKCNSKSQ GEKEMYTLGI TNFPIPGEPG FPLNAIYAKP 130 140 150 160 170 ANKQEDEVMR AYLQQLRQET GLRLCEKVFD PQNDKPSKWW TCFVKRQFMN KSLSGPGQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins." Machesky L.M., Reeves E., Wientjes F., Mattheyse F.J., Grogan A., Totty N.F., Burlingame A.L., Hsuan J.J., Segal A.W. Biochem. J. 328:105-112(1997) [PubMed: 9359840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[2]	"The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly." Welch M.D., Depace A.H., Verma S., Iwamatsu A., Mitchison T.J. J. Cell Biol. 138:375-384(1997) [PubMed: 9230079] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE ARP2/2 COMPLEX, SUBCELLULAR LOCATION.
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Skin.
[5]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-25. Tissue: Platelet.
[6]	"Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity." Gournier H., Goley E.D., Niederstrasser H., Trinh T., Welch M.D. Mol. Cell 8:1041-1052(2001) [PubMed: 11741539] [Abstract] Cited for: RECONSTITUTION OF THE ARP2/3 COMPLEX.
[7]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-47, MASS SPECTROMETRY.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-47, MASS SPECTROMETRY. Tissue: T-cell.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56 AND LYS-61, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF004561 mRNA. Translation: AAB61466.1. AF006086 mRNA. Translation: AAB64191.1. CR407667 mRNA. Translation: CAG28595.1. BC067747 mRNA. Translation: AAH67747.1. BC078162 mRNA. Translation: AAH78162.1.
IPI	IPI00005162.
RefSeq	NP_005710.1.
UniGene	Hs.524741
3D structure databases
SMR	O15145. Positions 1-173, 2-174.
ModBase	Search...
Protein-protein interaction databases
IntAct	O15145. 13 interactions.
STRING	O15145.
PTM databases
PhosphoSite	O15145.
2-D gel databases
OGP	O15145.
Proteomic databases
PRIDE	O15145.
Genome annotation databases
Ensembl	ENST00000228825; ENSP00000228825; ENSG00000111229; Homo sapiens. [Genome view]
GeneID	10094.
KEGG	hsa:10094.
UCSC	uc001tqq.1. human.
Organism-specific databases
CTD	10094.
GeneCards	GC12M109335.
H-InvDB	HIX0036676.
HGNC	HGNC:706. ARPC3.
HPA	HPA006550.
MIM	604225. gene.
PharmGKB	PA25000.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	O15145.
OMA	PSKWWLC.
OrthoDB	EOG9VDSJJ.
Gene expression databases
ArrayExpress	O15145.
Bgee	O15145.
Genevestigator	O15145.
GermOnline	ENSG00000111229. Homo sapiens.
Family and domain databases
InterPro	IPR007204. ARP2/3_p21-Arc. [Graphical view]
Gene3D	G3DSA:1.10.1760.10. ARP2/3_P21-Arc. 1 hit.
PANTHER	PTHR12391. P21-Arc. 1 hit.
Pfam	PF04062. P21-Arc. 1 hit. [Graphical view]
PIRSF	PIRSF016315. ARP2/3_P21-Arc. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	38177.
SOURCE	Search...

Entry information

Entry name

ARPC3_HUMAN

Accession

Primary (citable) accession number: O15145
Secondary accession number(s): O00554

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	December 15, 2009
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.