ARPC4_SCHPO
ID ARPC4_SCHPO Reviewed; 168 AA.
AC Q92352; Q9URL0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Actin-related protein 2/3 complex subunit 4;
DE AltName: Full=Arp2/3 complex 20 kDa;
DE Short=p20-ARC;
GN Name=arc4; Synonyms=arp20; ORFNames=SPAC6G9.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-168.
RA Kawamukai M.;
RT "S.pombe 20kd homolog of Arp2/3 complex.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION IN THE ARP2/3 COMPLEX.
RX PubMed=10588653; DOI=10.1091/mbc.10.12.4201;
RA Morrell J.L., Morphew M., Gould K.L.;
RT "A mutant of arp2p causes partial disassembly of the Arp2/3 complex and
RT loss of cortical actin function in fission yeast.";
RL Mol. Biol. Cell 10:4201-4215(1999).
CC -!- FUNCTION: Functions as actin-binding component of the Arp2/3 complex
CC which is involved in regulation of actin polymerization and together
CC with an activating nucleation-promoting factor (NPF) mediates the
CC formation of branched actin networks. Seems to contact the mother actin
CC filament (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the Arp2/3 complex composed of arp2, act2,
CC arc1/p41-ARC, arc2/p34-ARC, arc3/p21-ARC, arc4/p20-ARC and arc5/p16-
CC ARC. {ECO:0000269|PubMed:10588653}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch.
CC -!- SIMILARITY: Belongs to the ARPC4 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB03609.1; -; Genomic_DNA.
DR EMBL; AB010050; BAA24183.1; -; mRNA.
DR PIR; T39069; T39069.
DR PIR; T43309; T43309.
DR RefSeq; NP_594116.1; NM_001019540.2.
DR PDB; 3DWL; X-ray; 3.78 A; F/K=1-168.
DR PDB; 6W17; EM; 3.90 A; F=1-168.
DR PDB; 6W18; EM; 4.20 A; F=1-168.
DR PDBsum; 3DWL; -.
DR PDBsum; 6W17; -.
DR PDBsum; 6W18; -.
DR AlphaFoldDB; Q92352; -.
DR SMR; Q92352; -.
DR BioGRID; 278261; 4.
DR IntAct; Q92352; 3.
DR STRING; 4896.SPAC6G9.07c.1; -.
DR iPTMnet; Q92352; -.
DR MaxQB; Q92352; -.
DR PaxDb; Q92352; -.
DR EnsemblFungi; SPAC6G9.07c.1; SPAC6G9.07c.1:pep; SPAC6G9.07c.
DR GeneID; 2541767; -.
DR KEGG; spo:SPAC6G9.07c; -.
DR PomBase; SPAC6G9.07c; arc4.
DR VEuPathDB; FungiDB:SPAC6G9.07c; -.
DR eggNOG; KOG1876; Eukaryota.
DR HOGENOM; CLU_084855_1_0_1; -.
DR InParanoid; Q92352; -.
DR OMA; EAYLGEF; -.
DR PhylomeDB; Q92352; -.
DR Reactome; R-SPO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-SPO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR EvolutionaryTrace; Q92352; -.
DR PRO; PR:Q92352; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030479; C:actin cortical patch; IC:PomBase.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0051015; F:actin filament binding; IDA:PomBase.
DR GO; GO:0000147; P:actin cortical patch assembly; IC:PomBase.
DR GO; GO:0030041; P:actin filament polymerization; IEA:InterPro.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:PomBase.
DR GO; GO:0006897; P:endocytosis; IC:PomBase.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 3.30.1460.20; -; 1.
DR InterPro; IPR034666; ARPC2/4.
DR InterPro; IPR008384; ARPC4.
DR PANTHER; PTHR22629; PTHR22629; 1.
DR Pfam; PF05856; ARPC4; 1.
DR PIRSF; PIRSF039100; ARPC4; 1.
DR SUPFAM; SSF69645; SSF69645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..168
FT /note="Actin-related protein 2/3 complex subunit 4"
FT /id="PRO_0000124052"
SQ SEQUENCE 168 AA; 19615 MW; 93E7D63F3907820E CRC64;
MSNTLRPYLN AVRSTLTASL ALEEFSSEIV ERQSQPEVEV GRSPEILLKP LVVSRNEQEQ
CLIESSVNSV RFSIRIKQVD EIERILVRKF MQFLMGRAES FFILRRKPVQ GYDISFLITN
YHTEEMLKHK LVDFIIEFME EVDAEISEMK LFLNGRARLV AETYLSCF