ARC1A_HUMAN
ID ARC1A_HUMAN Reviewed; 370 AA.
AC Q92747; A4D276; B4DLQ7; D6W5S1; Q7Z5U8; Q86WU5; Q8IXQ0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Actin-related protein 2/3 complex subunit 1A;
DE AltName: Full=SOP2-like protein;
GN Name=ARPC1A; Synonyms=SOP2L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=8978670; DOI=10.1002/j.1460-2075.1996.tb01034.x;
RA Balasubramanian M.K., Feoktostiva A., McCollum D., Gould K.L.;
RT "Fission yeast Sop2p: a novel and evolutionarily conserved protein that
RT interacts with Arp3p and modulates profilin function.";
RL EMBO J. 15:6426-6437(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas, and Uterus;
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).
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. {ECO:0000305|PubMed:8978670}.
CC -!- SUBUNIT: Probable component of the Arp2/3 complex in which it may
CC replace ARPC1B (Probable). In addition to its role in the cytoplasmic
CC cytoskeleton, the Arp2/3 complex also promotes actin polymerization in
CC the nucleus, thereby regulating gene transcription and repair of
CC damaged DNA (By similarity). {ECO:0000250|UniProtKB:Q8AVT9,
CC ECO:0000305|PubMed:8978670}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:8978670}. Nucleus {ECO:0000250|UniProtKB:Q8AVT9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92747-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92747-2; Sequence=VSP_056389, VSP_056390;
CC -!- SIMILARITY: Belongs to the WD repeat ARPC1 family. {ECO:0000305}.
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DR EMBL; Y08999; CAA70203.1; -; mRNA.
DR EMBL; AK297111; BAG59619.1; -; mRNA.
DR EMBL; AC004834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236956; EAL23883.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76682.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76683.1; -; Genomic_DNA.
DR EMBL; BC039594; AAH39594.2; -; mRNA.
DR EMBL; BC047889; AAH47889.2; -; mRNA.
DR EMBL; BC054027; AAH54027.1; -; mRNA.
DR CCDS; CCDS5660.1; -. [Q92747-1]
DR RefSeq; NP_006400.2; NM_006409.3. [Q92747-1]
DR PDB; 6YW7; EM; 4.50 A; C=1-370.
DR PDBsum; 6YW7; -.
DR AlphaFoldDB; Q92747; -.
DR SMR; Q92747; -.
DR BioGRID; 115803; 64.
DR DIP; DIP-33142N; -.
DR IntAct; Q92747; 24.
DR MINT; Q92747; -.
DR STRING; 9606.ENSP00000262942; -.
DR GlyGen; Q92747; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92747; -.
DR PhosphoSitePlus; Q92747; -.
DR SwissPalm; Q92747; -.
DR BioMuta; ARPC1A; -.
DR DMDM; 88984001; -.
DR EPD; Q92747; -.
DR jPOST; Q92747; -.
DR MassIVE; Q92747; -.
DR MaxQB; Q92747; -.
DR PaxDb; Q92747; -.
DR PeptideAtlas; Q92747; -.
DR PRIDE; Q92747; -.
DR ProteomicsDB; 4550; -.
DR ProteomicsDB; 75438; -. [Q92747-1]
DR Antibodypedia; 34784; 244 antibodies from 30 providers.
DR DNASU; 10552; -.
DR Ensembl; ENST00000262942.10; ENSP00000262942.5; ENSG00000241685.10. [Q92747-1]
DR GeneID; 10552; -.
DR KEGG; hsa:10552; -.
DR MANE-Select; ENST00000262942.10; ENSP00000262942.5; NM_006409.4; NP_006400.2.
DR CTD; 10552; -.
DR DisGeNET; 10552; -.
DR GeneCards; ARPC1A; -.
DR HGNC; HGNC:703; ARPC1A.
DR HPA; ENSG00000241685; Low tissue specificity.
DR MIM; 604220; gene.
DR neXtProt; NX_Q92747; -.
DR OpenTargets; ENSG00000241685; -.
DR PharmGKB; PA24997; -.
DR VEuPathDB; HostDB:ENSG00000241685; -.
DR eggNOG; KOG1523; Eukaryota.
DR GeneTree; ENSGT00950000183183; -.
DR HOGENOM; CLU_034396_1_0_1; -.
DR InParanoid; Q92747; -.
DR OMA; YVWEPSP; -.
DR PhylomeDB; Q92747; -.
DR TreeFam; TF315041; -.
DR PathwayCommons; Q92747; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; Q92747; -.
DR SIGNOR; Q92747; -.
DR BioGRID-ORCS; 10552; 33 hits in 1079 CRISPR screens.
DR ChiTaRS; ARPC1A; human.
DR GeneWiki; ARPC1A; -.
DR GenomeRNAi; 10552; -.
DR Pharos; Q92747; Tbio.
DR PRO; PR:Q92747; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q92747; protein.
DR Bgee; ENSG00000241685; Expressed in lower esophagus mucosa and 111 other tissues.
DR ExpressionAtlas; Q92747; baseline and differential.
DR Genevisible; Q92747; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
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 3D-structure; Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Nucleus; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..370
FT /note="Actin-related protein 2/3 complex subunit 1A"
FT /id="PRO_0000050852"
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"
FT VAR_SEQ 1..57
FT /note="MSLHQFLLEPITCHAWNRDRTQIALSPNNHEVHIYKKNGSQWVKAHELKEHN
FT GHITG -> MHERFIHCFC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056389"
FT VAR_SEQ 359..370
FT /note="TLESSIQGLRIM -> EPSRHGLPQLPGGAHQLPRLEQGPHPDCHLPQQP
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056390"
FT CONFLICT 127
FT /note="S -> A (in Ref. 1; CAA70203)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="P -> K (in Ref. 1; CAA70203)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="N -> I (in Ref. 1; CAA70203)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 41569 MW; 57FA5AC69997636E CRC64;
MSLHQFLLEP ITCHAWNRDR TQIALSPNNH EVHIYKKNGS QWVKAHELKE HNGHITGIDW
APKSDRIVTC GADRNAYVWS QKDGVWKPTL VILRINRAAT FVKWSPLENK FAVGSGARLI
SVCYFESEND WWVSKHIKKP IRSTVLSLDW HPNNVLLAAG SCDFKCRVFS AYIKEVDEKP
ASTPWGSKMP FGQLMSEFGG SGTGGWVHGV SFSASGSRLA WVSHDSTVSV ADASKSVQVS
TLKTEFLPLL SVSFVSENSV VAAGHDCCPM LFNYDDRGCL TFVSKLDIPK QSIQRNMSAM
ERFRNMDKRA TTEDRNTALE TLHQNSITQV SIYEVDKQDC RKFCTTGIDG AMTIWDFKTL
ESSIQGLRIM
