ID   ACTA_CHICK              Reviewed;         377 AA.
AC   P08023;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Actin, aortic smooth muscle;
DE   AltName: Full=Alpha-actin;
DE   Contains:
DE     RecName: Full=Actin, aortic smooth muscle, intermediate form;
DE   Flags: Precursor;
GN   Name=ACTA2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3013870; DOI=10.1016/s0021-9258(19)84476-9;
RA   Carroll S.L., Bergsma D.J., Schwartz R.J.;
RT   "Structure and complete nucleotide sequence of the chicken alpha-smooth
RT   muscle (aortic) actin gene. An actin gene which produces multiple messenger
RT   RNAs.";
RL   J. Biol. Chem. 261:8965-8976(1986).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC       various types of cell motility and are ubiquitously expressed in all
CC       eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix. Each
CC       actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- PTM: Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or
CC       MICAL3) to form methionine sulfoxide promotes actin filament
CC       depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The
CC       (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin
CC       repolymerization. {ECO:0000250|UniProtKB:P62737}.
CC   -!- PTM: Methylated at His-75 by SETD3. {ECO:0000250|UniProtKB:P62736}.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, alpha,
CC       beta and gamma have been identified. The alpha actins are found in
CC       muscle tissues and are a major constituent of the contractile
CC       apparatus. The beta and gamma actins coexist in most cell types as
CC       components of the cytoskeleton and as mediators of internal cell
CC       motility.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; M13756; AAB12010.1; -; Genomic_DNA.
DR   RefSeq; NP_001026400.1; NM_001031229.1.
DR   AlphaFoldDB; P08023; -.
DR   SMR; P08023; -.
DR   STRING; 9031.ENSGALP00000010239; -.
DR   GeneID; 423787; -.
DR   KEGG; gga:423787; -.
DR   CTD; 59; -.
DR   VEuPathDB; HostDB:geneid_423787; -.
DR   eggNOG; KOG0676; Eukaryota.
DR   InParanoid; P08023; -.
DR   OrthoDB; 649708at2759; -.
DR   PhylomeDB; P08023; -.
DR   PRO; PR:P08023; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0044297; C:cell body; IDA:AgBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030175; C:filopodium; IDA:AgBase.
DR   GO; GO:0030027; C:lamellipodium; IDA:AgBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0090131; P:mesenchyme migration; IMP:AgBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   3: Inferred from homology;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation;
KW   Muscle protein; Nucleotide-binding; Oxidation; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
FT   CHAIN           2..377
FT                   /note="Actin, aortic smooth muscle, intermediate form"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
FT                   /id="PRO_0000442611"
FT   CHAIN           3..377
FT                   /note="Actin, aortic smooth muscle"
FT                   /id="PRO_0000442612"
FT   MOD_RES         2
FT                   /note="N-acetylcysteine; in intermediate form"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
FT   MOD_RES         3
FT                   /note="N-acetylglutamate; in Actin, aortic smooth muscle"
FT                   /evidence="ECO:0000250|UniProtKB:P62736"
FT   MOD_RES         46
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
FT   MOD_RES         49
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
FT   MOD_RES         75
FT                   /note="Tele-methylhistidine"
FT                   /evidence="ECO:0000250|UniProtKB:P62739"
SQ   SEQUENCE   377 AA;  41995 MW;  591654262AB10CA7 CRC64;
     MCEEEDSTAL VCDNGSGLCK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH SFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
     DLAGRDLTDY LMKILSERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
     KQEYDEAGPS IVHRKCF