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ARP3_NEUCR
ID   ARP3_NEUCR              Reviewed;         439 AA.
AC   P78712; Q7RV67; Q9P6D0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Actin-related protein 3;
DE   AltName: Full=Actin-like protein 3;
GN   Name=arp-3; Synonyms=arp3; ORFNames=B17C10.190, NCU01756;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9819052; DOI=10.1007/s004380050853;
RA   Tinsley J.H., Lee I.H., Minke P.F., Plamann M.;
RT   "Analysis of actin and actin-related protein 3 (ARP3) gene expression
RT   following induction of hyphal tip formation and apolar growth in
RT   Neurospora.";
RL   Mol. Gen. Genet. 259:601-609(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Functions as ATP-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 pointed end
CC       of the daughter actin filament (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the Arp2/3 complex composed. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily. {ECO:0000305}.
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DR   EMBL; U79737; AAC78497.1; -; mRNA.
DR   EMBL; AL355926; CAB91239.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA27943.2; -; Genomic_DNA.
DR   PIR; T49438; T49438.
DR   RefSeq; XP_957179.2; XM_952086.3.
DR   AlphaFoldDB; P78712; -.
DR   SMR; P78712; -.
DR   STRING; 5141.EFNCRP00000001861; -.
DR   PRIDE; P78712; -.
DR   EnsemblFungi; EAA27943; EAA27943; NCU01756.
DR   GeneID; 3873331; -.
DR   KEGG; ncr:NCU01756; -.
DR   VEuPathDB; FungiDB:NCU01756; -.
DR   HOGENOM; CLU_027965_3_0_1; -.
DR   InParanoid; P78712; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR   GO; GO:0005885; C:Arp2/3 protein complex; IBA:GO_Central.
DR   GO; GO:0051285; C:cell cortex of cell tip; IEA:EnsemblFungi.
DR   GO; GO:0032153; C:cell division site; IEA:EnsemblFungi.
DR   GO; GO:0051015; F:actin filament binding; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0044396; P:actin cortical patch organization; IEA:EnsemblFungi.
DR   GO; GO:0030041; P:actin filament polymerization; IEA:EnsemblFungi.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR   GO; GO:0000281; P:mitotic cytokinesis; IEA:EnsemblFungi.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR015623; Arp3.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   PANTHER; PTHR11937:SF175; PTHR11937:SF175; 1.
DR   Pfam; PF00022; Actin; 1.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..439
FT                   /note="Actin-related protein 3"
FT                   /id="PRO_0000089089"
FT   REGION          40..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        7
FT                   /note="A -> T (in Ref. 1; AAC78497)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   439 AA;  47852 MW;  AD4C275AFE28B1F0 CRC64;
     MANTTPAVVM DNGTGFSKLG FAGNDSPSFV FPTAIATKSP SAGTGGSGSG RPAVANKPSF
     LTGGAGPGGH LSAKRGTEDL DYFIGDEAVA AANGPGYGLH YPIRHGQIEN WDHMERFWSN
     SIFKYLRVEP EDHHFLLTEP PLNPPENREN TAEIFFESFN CAGLYIAVQA VLALAASWTS
     SKVQDRSLTG TVIDSGDGVT HVIPVAEGYV IGSSIKSIPI AGRDITYFVQ SLLRDRGEPD
     SSLKTAQEIK EEYCYVCPDI VKEFAKYDRD RSRFLKHTIT QPGGRQVTVD VGYERFMAPE
     IFFNPEIYSS DFLTPLPVVV DGVIQSSPID VRRGLYKNIV LSGGSTLYKD FGRRLQRDIK
     QLVDTRIKAS EVRSGGAKSG GLDVQVITHK RQRHGPWFGG SLLGQTPEFR SYCHTKAEYQ
     EYGPSIVRRF ALLGGPGGS
 
 
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