ARPC1_DICDI
ID ARPC1_DICDI Reviewed; 369 AA.
AC O96622; Q54YR5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Actin-related protein 2/3 complex subunit 1;
DE AltName: Full=Arp2/3 complex 41 kDa subunit;
DE AltName: Full=p41-Arc;
GN Name=arcA; Synonyms=Arc40, arpD; ORFNames=DDB_G0277825;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=AX2;
RX PubMed=11807934; DOI=10.1002/cm.10005;
RA Insall R., Mueller-Taubenberger A., Machesky L., Koehler J., Simmeth E.,
RA Atkinson S.J., Weber I., Gerisch G.;
RT "Dynamics of the Dictyostelium Arp2/3 complex in endocytosis, cytokinesis,
RT and chemotaxis.";
RL Cell Motil. Cytoskeleton 50:115-128(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP PROTEIN SEQUENCE OF 149-160, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11425877; DOI=10.1083/jcb.153.7.1479;
RA Jung G., Remmert K., Wu X., Volosky J.M., Hammer J.A. III;
RT "The Dictyostelium CARMIL protein links capping protein and the Arp2/3
RT complex to type I myosins through their SH3 domains.";
RL J. Cell Biol. 153:1479-1497(2001).
RN [4]
RP IDENTIFICATION IN THE ARP2/3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=17296313; DOI=10.1016/j.pep.2007.01.001;
RA Meima M.E., Weening K.E., Schaap P.;
RT "Vectors for expression of proteins with single or combinatorial
RT fluorescent protein and tandem affinity purification tags in
RT Dictyostelium.";
RL Protein Expr. Purif. 53:283-288(2007).
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. Seems to contact the pointed end of the
CC daughter actin filament. The Arp2/3 complex is involved in organizing
CC the actin system in cell motility and chemotaxis, in phagocytosis and
CC macropinocytosis, at late steps of endosome processing, and in mitosis.
CC In concert with a group of other proteins, the Arp2/3 complex plays a
CC general role in the rapid activation and adaptation of the actin system
CC to its multiple functions. {ECO:0000269|PubMed:11807934}.
CC -!- SUBUNIT: Component of the Arp2/3 complex composed of arpB/Arp2,
CC arpC/Arp3, arcA/p41-arc, arcB/p34-arc, arcC/p21-arc, arcD/p20-arc and
CC arcE/p16-arc. Interacts with carmil (via the region between the LRR
CC domain and COOH-terminal proline-rich domain); carmil is required for
CC Arp2/3-dependent actin nucleation. Arp2/3 complex, MyoB, MyoC, and the
CC alpha and beta subunits of capping protein all form a larger complex
CC with carmil. {ECO:0000269|PubMed:11425877,
CC ECO:0000269|PubMed:17296313}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection.
CC Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection,
CC pseudopodium.
CC -!- SIMILARITY: Belongs to the WD repeat ARPC1 family. {ECO:0000305}.
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DR EMBL; AF095930; AAC99777.1; -; mRNA.
DR EMBL; AAFI02000023; EAL68085.1; -; Genomic_DNA.
DR RefSeq; XP_642137.1; XM_637045.1.
DR AlphaFoldDB; O96622; -.
DR SMR; O96622; -.
DR STRING; 44689.DDB0214932; -.
DR PaxDb; O96622; -.
DR EnsemblProtists; EAL68085; EAL68085; DDB_G0277825.
DR GeneID; 8621345; -.
DR KEGG; ddi:DDB_G0277825; -.
DR dictyBase; DDB_G0277825; arcA.
DR eggNOG; KOG1523; Eukaryota.
DR HOGENOM; CLU_034396_0_0_1; -.
DR InParanoid; O96622; -.
DR OMA; YVWEPSP; -.
DR PhylomeDB; O96622; -.
DR Reactome; R-DDI-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DDI-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:O96622; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:dictyBase.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0031252; C:cell leading edge; IC:dictyBase.
DR GO; GO:0042995; C:cell projection; IDA:dictyBase.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:dictyBase.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IC:dictyBase.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0030175; C:filopodium; IC:dictyBase.
DR GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IDA:dictyBase.
DR GO; GO:0031143; C:pseudopodium; IC:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030041; P:actin filament polymerization; TAS:dictyBase.
DR GO; GO:0045010; P:actin nucleation; TAS:dictyBase.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IEP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IEP:dictyBase.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR017383; ARPC1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10709; PTHR10709; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF00400; WD40; 1.
DR PIRSF; PIRSF038093; ARP2/3_su1; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell projection; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..369
FT /note="Actin-related protein 2/3 complex subunit 1"
FT /id="PRO_0000327629"
FT REPEAT 8..47
FT /note="WD 1"
FT REPEAT 52..91
FT /note="WD 2"
FT REPEAT 141..180
FT /note="WD 3"
FT REPEAT 200..239
FT /note="WD 4"
FT REPEAT 322..365
FT /note="WD 5"
SQ SEQUENCE 369 AA; 41066 MW; E967BDCDFD236811 CRC64;
MSAFEIEHLA SCITAHAWNA DRSRVALCPN NNEVHIYAKQ GTSWVVEHVL AEHDQLVTSI
DWAPKTNRIL TSSQDRNAYV WTFKDGQWKP VLVLLRINRA ATHVKWSPQE NKFAVATGAK
LVCICFFEEE HDWWASNHIK KHKSTVLKVD WHPNNLLLAT SSSDYKVRVF DAYIKKADGR
SVTRPYGEVA FGEPVFEFDQ CASWVHALKW SPSGSTLAYS SHDGVFAVAN FSTNPPTIEK
LRVRNLPLRD LLYITENSIA GVGYDCAPLL ITNQNGWKYS GEMDKASEGG AAAGSETSAR
KLFQNKVDLG ESKSADKKLT TVHQNCITSI VPFKSVGGVV SDFSTSGLDG NIVVWHVKAL
EAKNKFKVI
