ARPC5_SCHPO
ID ARPC5_SCHPO Reviewed; 152 AA.
AC Q10316;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Actin-related protein 2/3 complex subunit 5;
DE AltName: Full=Arp2/3 complex 16 kDa subunit;
DE Short=p16-ARC;
GN Name=arc5; Synonyms=arc16; ORFNames=SPAC17G8.04c;
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 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 component of the Arp2/3 complex which is
CC involved in regulation of actin polymerization and together with an
CC activating nucleation-promoting factor (NPF) mediates the formation of
CC branched actin networks. {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 ARPC5 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAA93687.1; -; Genomic_DNA.
DR PIR; T37856; T37856.
DR RefSeq; NP_593727.1; NM_001019158.2.
DR PDB; 3DWL; X-ray; 3.78 A; G/L=1-152.
DR PDB; 6W17; EM; 3.90 A; G=1-152.
DR PDB; 6W18; EM; 4.20 A; G=1-152.
DR PDBsum; 3DWL; -.
DR PDBsum; 6W17; -.
DR PDBsum; 6W18; -.
DR AlphaFoldDB; Q10316; -.
DR SMR; Q10316; -.
DR BioGRID; 278744; 4.
DR IntAct; Q10316; 4.
DR STRING; 4896.SPAC17G8.04c.1; -.
DR iPTMnet; Q10316; -.
DR MaxQB; Q10316; -.
DR PaxDb; Q10316; -.
DR EnsemblFungi; SPAC17G8.04c.1; SPAC17G8.04c.1:pep; SPAC17G8.04c.
DR GeneID; 2542275; -.
DR KEGG; spo:SPAC17G8.04c; -.
DR PomBase; SPAC17G8.04c; arc5.
DR VEuPathDB; FungiDB:SPAC17G8.04c; -.
DR eggNOG; KOG3380; Eukaryota.
DR HOGENOM; CLU_101888_2_0_1; -.
DR InParanoid; Q10316; -.
DR OMA; GMALPGW; -.
DR PhylomeDB; Q10316; -.
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-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR EvolutionaryTrace; Q10316; -.
DR PRO; PR:Q10316; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA: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: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; 1.25.40.190; -; 1.
DR InterPro; IPR006789; ARPC5.
DR InterPro; IPR036743; ARPC5_sf.
DR PANTHER; PTHR12644; PTHR12644; 1.
DR Pfam; PF04699; P16-Arc; 1.
DR PIRSF; PIRSF039096; p16-ARC; 1.
DR SUPFAM; SSF69103; SSF69103; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..152
FT /note="Actin-related protein 2/3 complex subunit 5"
FT /id="PRO_0000124058"
SQ SEQUENCE 152 AA; 16910 MW; C892291720BA6161 CRC64;
MTFRTLDVDS ITEPVLTEQD IFPIRNETAE QVQAAVSQLI PQARSAIQTG NALQGLKTLL
SYVPYGNDVQ EVRTQYLNAF VDVLSNIRAA DIPAFVKECS TEEIDNIVNF IYRGLANPQA
YNSSVLLNWH EKVVEISGIG CIVRVLNSRP DL
