ACTA_BOVIN
ID ACTA_BOVIN Reviewed; 377 AA.
AC P62739; P03996; P04108; Q3ZCA0; Q862W5;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Actin, aortic smooth muscle;
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 3-377, AND METHYLATION AT HIS-75.
RX PubMed=499690; DOI=10.1111/j.1432-0436.1979.tb01021.x;
RA Vandekerckhove J., Weber K.;
RT "The complete amino acid sequence of actins from bovine aorta, bovine
RT heart, bovine fast skeletal muscle, and rabbit slow skeletal muscle. A
RT protein-chemical analysis of muscle actin differentiation.";
RL Differentiation 14:123-133(1979).
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: 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; BC102699; AAI02700.1; -; mRNA.
DR PIR; A02997; ATBOSM.
DR RefSeq; NP_001029674.1; NM_001034502.1.
DR RefSeq; XP_005225421.1; XM_005225364.3.
DR AlphaFoldDB; P62739; -.
DR SMR; P62739; -.
DR CORUM; P62739; -.
DR IntAct; P62739; 1.
DR PeptideAtlas; P62739; -.
DR PRIDE; P62739; -.
DR Ensembl; ENSBTAT00000037115; ENSBTAP00000036954; ENSBTAG00000014614.
DR Ensembl; ENSBTAT00000072351; ENSBTAP00000059015; ENSBTAG00000014614.
DR GeneID; 515610; -.
DR KEGG; bta:515610; -.
DR CTD; 59; -.
DR VEuPathDB; HostDB:ENSBTAG00000014614; -.
DR VGNC; VGNC:106627; ACTA2.
DR GeneTree; ENSGT00940000154148; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P62739; -.
DR OMA; PNIMVGM; -.
DR OrthoDB; 649708at2759; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000014614; Expressed in aorta and 109 other tissues.
DR ExpressionAtlas; P62739; baseline and differential.
DR GO; GO:0005884; C:actin filament; ISS:AgBase.
DR GO; GO:0044297; C:cell body; ISS:AgBase.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0005869; C:dynactin complex; IBA:GO_Central.
DR GO; GO:0030175; C:filopodium; ISS:AgBase.
DR GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR GO; GO:0030485; C:smooth muscle contractile fiber; IEA:Ensembl.
DR GO; GO:0001725; C:stress fiber; ISS:AgBase.
DR GO; GO:0005865; C:striated muscle thin filament; ISS:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0072144; P:glomerular mesangial cell development; IEA:Ensembl.
DR GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISS:AgBase.
DR GO; GO:0030240; P:skeletal muscle thin filament assembly; ISS:AgBase.
DR GO; GO:0014829; P:vascular associated smooth muscle contraction; IEA:Ensembl.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Methylation; Muscle protein; Nucleotide-binding;
KW 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_0000442601"
FT CHAIN 3..377
FT /note="Actin, aortic smooth muscle"
FT /evidence="ECO:0000269|PubMed:499690"
FT /id="PRO_0000442602"
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:0000269|PubMed:499690"
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
