ID   ACTA_RABIT              Reviewed;         377 AA.
AC   P62740; P03996; P04108;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 113.
DE   RecName: Full=Actin, aortic smooth muscle;
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P68137};
DE   AltName: Full=Alpha-actin-2;
DE   Contains:
DE     RecName: Full=Actin, aortic smooth muscle, intermediate form;
DE   Flags: Precursor;
GN   Name=ACTA2; Synonyms=ACTSA, ACTVS;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Uterus;
RX   PubMed=1555776; DOI=10.1016/0378-1119(92)90388-6;
RA   Harris D.E., Warshaw D.M., Periasamy M.;
RT   "Nucleotide sequences of the rabbit alpha-smooth-muscle and beta-non-muscle
RT   actin mRNAs.";
RL   Gene 112:265-266(1992).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:P68137};
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: [Actin, aortic smooth muscle, intermediate form]: N-terminal
CC       cleavage of acetylated cysteine of intermediate muscle actin by ACTMAP.
CC       {ECO:0000250|UniProtKB:P62737}.
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: Monomethylation at Lys-86 (K84me1) regulates actin-myosin
CC       interaction and actomyosin-dependent processes. Demethylation by ALKBH4
CC       is required for maintaining actomyosin dynamics supporting normal
CC       cleavage furrow ingression during cytokinesis and cell migration (By
CC       similarity). {ECO:0000250}.
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; X60732; CAA43139.1; -; mRNA.
DR   PIR; JH0636; ATRBSM.
DR   RefSeq; NP_001095152.1; NM_001101682.2.
DR   AlphaFoldDB; P62740; -.
DR   SMR; P62740; -.
DR   BioGRID; 1172292; 4.
DR   MINT; P62740; -.
DR   STRING; 9986.ENSOCUP00000007086; -.
DR   PaxDb; 9986-ENSOCUP00000007086; -.
DR   GeneID; 100009271; -.
DR   KEGG; ocu:100009271; -.
DR   CTD; 59; -.
DR   eggNOG; KOG0676; Eukaryota.
DR   InParanoid; P62740; -.
DR   OrthoDB; 5245715at2759; -.
DR   TreeFam; TF354237; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0044297; C:cell body; ISS:AgBase.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030175; C:filopodium; ISS:AgBase.
DR   GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB.
DR   GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; ACTIN; 1.
DR   PANTHER; PTHR11937:SF445; ACTIN, AORTIC SMOOTH MUSCLE; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase; Methylation;
KW   Muscle protein; Nucleotide-binding; Oxidation; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P62736"
FT   CHAIN           2..377
FT                   /note="Actin, aortic smooth muscle, intermediate form"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
FT                   /id="PRO_0000442607"
FT   CHAIN           3..377
FT                   /note="Actin, aortic smooth muscle"
FT                   /id="PRO_0000442608"
FT   MOD_RES         2
FT                   /note="N-acetylcysteine; in intermediate form"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
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"
FT   MOD_RES         86
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P68032"
SQ   SEQUENCE   377 AA;  42009 MW;  2D0543262DB35CA5 CRC64;
     MCEEEDSTAL VCDNGSGLCK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH SFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
     DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
     KQEYDEAGPS IVHRKCF
//