P59998 (ARPC4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin-related protein 2/3 complex subunit 4

Alternative name(s):
Arp2/3 complex 20 kDa subunit
Short name=p20-ARC

Gene names

Name:	ARPC4
Synonyms:	ARC20

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	168 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 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.
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.
Sequence similarities	Belongs to the ARPC4 family.
Sequence caution	The sequence AAH12596.3 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell projection Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Ligand	Actin-binding
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Arp2/3 complex-mediated actin nucleation Inferred from electronic annotation. Source: InterPro actin filament polymerization Inferred from electronic annotation. Source: InterPro actin nucleation Non-traceable author statement PubMed 11162547. Source: UniProtKB
Cellular_component	Arp2/3 protein complex Inferred from direct assay PubMed 11162547Ref.2. Source: UniProtKB cell projection Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P59998-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P59998-2)

The sequence of this isoform differs from the canonical sequence as follows:
     110-168: EGYDISFLIT...IVAEEFLKNF → EQKKIFTIQG...LRPCRPQARP

Note: No experimental confirmation available.

Isoform 3 (identifier: P59998-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVREPGPRPGTPGCSASGQW

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 168	167	Actin-related protein 2/3 complex subunit 4		PRO_0000124049
Amino acid modifications
	Modified residue	2	1	N-acetylthreonine Ref.6
Natural variations
	Alternative sequence	1	1	M → MVREPGPRPGTPGCSASGQW in isoform 3.		VSP_046150
	Alternative sequence	110 – 168	59	EGYDI…FLKNF → EQKKIFTIQGCYPVIRCLLR RRGWVEKKMVHRSGPTLLPP QKDLDSSAMGDSDTTEDEDE DEDEEFQPSQLFDFDDLLKF DDLDGTHALMVGLCLNLRNL PWFDEVDANSFFPRCYCLGA EDDKKAFIGDKQPKKQEKNP VLVSPEFVDEALCACEEYLS NLAHMDIDKDLEAPLYLTPE GWSLFLQRYYQVVHEGAELR HLDTQVQRCEDILQQLQAVV PQIDMEGDRNIWIVKPGAKS RGRGIMCMDHLEEMLKLVNG NPVVMKDGKWVVQKYIERPL LIFGTKFDLRQWFLVTDWNP LTVWFYRDSYIRFSTQPFSL KNLDNSVHLCNNSIQKHLEN SCHRHPLLPPDNMWSSQRFQ AHLQEMGAPNAWSTIIVPGM KDAVIHALQTSQDTVQCRKA SFELYGADFVFGEDFQPWLI EINASPTMAPSTAVTARLCA GVQADTLRVVIDRMLDRNCD TGAFELIYKQPVTTSPASTP RPSCLLPMYSDTRARSSDDS TASWWALRPCRPQARP in isoform 2.		VSP_046151
Experimental info
	Sequence conflict	94	1	M → T in AAH12596. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 273CCB230AC703DF	FASTA	168	19,667
	10 20 30 40 50 60 MTATLRPYLS AVRATLQAAL CLENFSSQVV ERHNKPEVEV RSSKELLLQP VTISRNEKEK 70 80 90 100 110 120 VLIEGSINSV RVSIAVKQAD EIEKILCHKF MRFMMMRAEN FFILRRKPVE GYDISFLITN 130 140 150 160 FHTEQMYKHK LVDFVIHFME EIDKEISEMK LSVNARARIV AEEFLKNF
	Isoform 2 [UniParc]. Checksum: E05F7DC236DF9674	FASTA	625	71,719
	10 20 30 40 50 60 MTATLRPYLS AVRATLQAAL CLENFSSQVV ERHNKPEVEV RSSKELLLQP VTISRNEKEK 70 80 90 100 110 120 VLIEGSINSV RVSIAVKQAD EIEKILCHKF MRFMMMRAEN FFILRRKPVE QKKIFTIQGC 130 140 150 160 170 180 YPVIRCLLRR RGWVEKKMVH RSGPTLLPPQ KDLDSSAMGD SDTTEDEDED EDEEFQPSQL 190 200 210 220 230 240 FDFDDLLKFD DLDGTHALMV GLCLNLRNLP WFDEVDANSF FPRCYCLGAE DDKKAFIGDK 250 260 270 280 290 300 QPKKQEKNPV LVSPEFVDEA LCACEEYLSN LAHMDIDKDL EAPLYLTPEG WSLFLQRYYQ 310 320 330 340 350 360 VVHEGAELRH LDTQVQRCED ILQQLQAVVP QIDMEGDRNI WIVKPGAKSR GRGIMCMDHL 370 380 390 400 410 420 EEMLKLVNGN PVVMKDGKWV VQKYIERPLL IFGTKFDLRQ WFLVTDWNPL TVWFYRDSYI 430 440 450 460 470 480 RFSTQPFSLK NLDNSVHLCN NSIQKHLENS CHRHPLLPPD NMWSSQRFQA HLQEMGAPNA 490 500 510 520 530 540 WSTIIVPGMK DAVIHALQTS QDTVQCRKAS FELYGADFVF GEDFQPWLIE INASPTMAPS 550 560 570 580 590 600 TAVTARLCAG VQADTLRVVI DRMLDRNCDT GAFELIYKQP VTTSPASTPR PSCLLPMYSD 610 620 TRARSSDDST ASWWALRPCR PQARP
	Isoform 3 [UniParc]. Checksum: F61DD748D01B8880	FASTA	187	21,588
	10 20 30 40 50 60 MVREPGPRPG TPGCSASGQW TATLRPYLSA VRATLQAALC LENFSSQVVE RHNKPEVEVR 70 80 90 100 110 120 SSKELLLQPV TISRNEKEKV LIEGSINSVR VSIAVKQADE IEKILCHKFM RFMMMRAENF 130 140 150 160 170 180 FILRRKPVEG YDISFLITNF HTEQMYKHKL VDFVIHFMEE IDKEISEMKL SVNARARIVA EEFLKNF

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Fetal brain.
[5]	"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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-168 (ISOFORM 1). Tissue: Choriocarcinoma and Prostate.
[6]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13, ACETYLATION AT THR-2. Tissue: Platelet.
[7]	"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] [Europe PMC] [Abstract] Cited for: ACTIN-BINDING, RECONSTITUTION OF THE ARP2/3 COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF019888 mRNA. Translation: AAB71548.1. AF006087 mRNA. Translation: AAB64192.1. BX419672 mRNA. No translation available. AC022382 Genomic DNA. No translation available. BC012596 mRNA. Translation: AAH12596.3. Different initiation. BC025289 mRNA. No translation available.
IPI	IPI00554811. IPI00790262. IPI00925052.
RefSeq	NP_001185709.1. NM_001198780.1. NP_001185722.1. NM_001198793.1. NP_005709.1. NM_005718.4.
UniGene	Hs.323342.
3D structure databases
ProteinModelPortal	P59998.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-33188N.
IntAct	P59998. 9 interactions.
STRING	9606.ENSP00000380431.
PTM databases
PhosphoSite	P59998.
Polymorphism databases
DMDM	38372625.
Proteomic databases
PaxDb	P59998.
PRIDE	P59998.
Protocols and materials databases
DNASU	10093.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000397261; ENSP00000380431; ENSG00000241553. ENST00000433034; ENSP00000388169; ENSG00000241553.
GeneID	100526693. 10093.
KEGG	hsa:100526693. hsa:10093.
UCSC	uc003bsz.2. human.
Organism-specific databases
CTD	100526693. 10093.
GeneCards	GC03P009834.
HGNC	HGNC:707. ARPC4.
MIM	604226. gene.
neXtProt	NX_P59998.
PharmGKB	PA25002.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG261545.
HOGENOM	HOG000202303.
HOVERGEN	HBG050582.
KO	K05755.
OrthoDB	EOG4HDSVQ.
Gene expression databases
ArrayExpress	P59998.
Bgee	P59998.
CleanEx	HS_ARPC4.
Genevestigator	P59998.
GermOnline	ENSG00000156983. Homo sapiens.
Family and domain databases
InterPro	IPR008384. ARPC4. IPR004344. Tub_tyr_ligase. [Graphical view]
PANTHER	PTHR22629. PTHR22629. 1 hit.
Pfam	PF05856. ARPC4. 1 hit. PF03133. TTL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ARPC4. human.
GenomeRNAi	10093.
NextBio	34054911.
SOURCE	Search...

Entry information

Entry name

ARPC4_HUMAN

Accession

Primary (citable) accession number: P59998
Secondary accession number(s): C9JWM7 , E7ETI0, O15509, Q6P0W5, Q96QJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.