ARC1A_MOUSE
ID ARC1A_MOUSE Reviewed; 370 AA.
AC Q9R0Q6; Q3UL75;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Actin-related protein 2/3 complex subunit 1A;
DE AltName: Full=SOP2-like protein;
DE AltName: Full=Sid 329;
GN Name=Arpc1a; Synonyms=Sid329;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT "Mouse homolog of Sop2p-like protein.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 236-243 AND 359-368, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Probably functions as component of the Arp2/3 complex which
CC is involved in regulation of actin polymerization and together with an
CC activating nucleation-promoting factor (NPF) mediates the formation of
CC branched actin networks (By similarity). In addition to its role in the
CC cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin
CC polymerization in the nucleus, thereby regulating gene transcription
CC and repair of damaged DNA (By similarity).
CC {ECO:0000250|UniProtKB:Q8AVT9, ECO:0000250|UniProtKB:Q92747}.
CC -!- SUBUNIT: Probable component of the Arp2/3 complex in which it may
CC replace ARPC1B. {ECO:0000250|UniProtKB:Q92747}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q92747}. Nucleus {ECO:0000250|UniProtKB:Q8AVT9}.
CC -!- SIMILARITY: Belongs to the WD repeat ARPC1 family. {ECO:0000305}.
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DR EMBL; AB024984; BAA84685.1; -; mRNA.
DR EMBL; AK076107; BAC36187.1; -; mRNA.
DR EMBL; AK145663; BAE26575.1; -; mRNA.
DR EMBL; BC001988; AAH01988.1; -; mRNA.
DR CCDS; CCDS19855.1; -.
DR RefSeq; NP_062741.1; NM_019767.2.
DR AlphaFoldDB; Q9R0Q6; -.
DR SMR; Q9R0Q6; -.
DR BioGRID; 207984; 21.
DR IntAct; Q9R0Q6; 4.
DR MINT; Q9R0Q6; -.
DR STRING; 10090.ENSMUSP00000031625; -.
DR GlyConnect; 2106; 1 N-Linked glycan (1 site).
DR GlyGen; Q9R0Q6; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q9R0Q6; -.
DR PhosphoSitePlus; Q9R0Q6; -.
DR SwissPalm; Q9R0Q6; -.
DR EPD; Q9R0Q6; -.
DR jPOST; Q9R0Q6; -.
DR MaxQB; Q9R0Q6; -.
DR PaxDb; Q9R0Q6; -.
DR PeptideAtlas; Q9R0Q6; -.
DR PRIDE; Q9R0Q6; -.
DR ProteomicsDB; 283197; -.
DR DNASU; 56443; -.
DR Ensembl; ENSMUST00000031625; ENSMUSP00000031625; ENSMUSG00000029621.
DR GeneID; 56443; -.
DR KEGG; mmu:56443; -.
DR UCSC; uc009ama.1; mouse.
DR CTD; 10552; -.
DR MGI; MGI:1928896; Arpc1a.
DR VEuPathDB; HostDB:ENSMUSG00000029621; -.
DR eggNOG; KOG1523; Eukaryota.
DR GeneTree; ENSGT00950000183183; -.
DR HOGENOM; CLU_034396_1_0_1; -.
DR InParanoid; Q9R0Q6; -.
DR OMA; YVWEPSP; -.
DR OrthoDB; 848569at2759; -.
DR PhylomeDB; Q9R0Q6; -.
DR TreeFam; TF315041; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 56443; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Arpc1a; mouse.
DR PRO; PR:Q9R0Q6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9R0Q6; protein.
DR Bgee; ENSMUSG00000029621; Expressed in urinary bladder urothelium and 266 other tissues.
DR ExpressionAtlas; Q9R0Q6; baseline and differential.
DR Genevisible; Q9R0Q6; MM.
DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0036195; C:muscle cell projection membrane; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR030140; ARC1A.
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 PANTHER; PTHR10709:SF11; PTHR10709:SF11; 1.
DR Pfam; PF00400; WD40; 2.
DR PIRSF; PIRSF038093; ARP2/3_su1; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Direct protein sequencing; Nucleus;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..370
FT /note="Actin-related protein 2/3 complex subunit 1A"
FT /id="PRO_0000050853"
FT REPEAT 6..45
FT /note="WD 1"
FT REPEAT 50..89
FT /note="WD 2"
FT REPEAT 140..179
FT /note="WD 3"
FT REPEAT 202..241
FT /note="WD 4"
FT REPEAT 244..284
FT /note="WD 5"
FT REPEAT 322..365
FT /note="WD 6"
SQ SEQUENCE 370 AA; 41626 MW; B47F0151B27211B0 CRC64;
MSLHQFLLEP ITCHAWNRDR TQIALSPNNH EVHIYKKNGS QWTKAHELKE HNGHITGIDW
APKSDRIVTC GADRNAYVWS QKDGIWKPTL VILRINRAAT FVKWSPLENK FAVGSGARLI
SVCYFESEND WWVSKHIKKP IRSTVLSLDW HPNNVLLAAG SCDFKCRVFS AYIKEVDEKP
ASTPWGSKMP FGQLMSEFGG SGTGGWVHGV SFSASGNRLA WVSHDSTVSV ADASKSVQVS
TLRTEFLPLL SVSFVSENSV VAAGHDCCPM LFNYDDRGCL TFVSKLDVPK QSIQRNMSAM
ERFRNMDKRA TTEDRNTALE TLHQNSITQV SIYEVDKQDC RKFCTTGIDG AMTIWDFKTL
ESSIQGLRIM
