ACTS_PIG
ID ACTS_PIG Reviewed; 377 AA.
AC P68137; P02568; P99020;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Actin, alpha skeletal muscle;
DE AltName: Full=Alpha-actin-1;
DE Contains:
DE RecName: Full=Actin, alpha skeletal muscle, intermediate form;
DE Flags: Precursor;
GN Name=ACTA1; Synonyms=ACTA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=8973342; DOI=10.1016/s0378-1119(96)00394-0;
RA Reecy J.M., Bidwell C.A., Briley G.P., Grant A.L.;
RT "Structure and regulation of the porcine skeletal alpha-actin-encoding
RT gene.";
RL Gene 180:23-28(1996).
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 (By similarity). Interacts with alpha-
CC actinin. Identified in a complex composed of ACTA1, COBL, GSN AND
CC TMSB4X (By similarity). Interacts with TTID. Interacts (via its C-
CC terminus) with USP25 (By similarity). {ECO:0000250|UniProtKB:P68133,
CC ECO:0000250|UniProtKB:P68135}.
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:P68134}.
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.
CC {ECO:0000250|UniProtKB:P68133}.
CC -!- PTM: Methylated at His-75 by SETD3. {ECO:0000250|UniProtKB:P68133}.
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; U16368; AAC48692.1; -; Genomic_DNA.
DR PIR; JC5301; JC5301.
DR RefSeq; NP_001161267.1; NM_001167795.1.
DR RefSeq; XP_005671033.1; XM_005670976.1.
DR PDB; 5NOG; EM; 11.00 A; A/B/C/D/E=7-373.
DR PDB; 5NOJ; EM; 11.00 A; A/B/C/D/E=7-373.
DR PDB; 5NOL; EM; 8.00 A; A/B/C/D/E=7-373.
DR PDB; 7KO4; EM; 8.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=3-377.
DR PDB; 7KO5; EM; 7.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=3-377.
DR PDB; 7KO7; EM; 8.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=3-377.
DR PDB; 7KON; EM; 8.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=3-377.
DR PDB; 7KOR; EM; 7.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=3-377.
DR PDBsum; 5NOG; -.
DR PDBsum; 5NOJ; -.
DR PDBsum; 5NOL; -.
DR PDBsum; 7KO4; -.
DR PDBsum; 7KO5; -.
DR PDBsum; 7KO7; -.
DR PDBsum; 7KON; -.
DR PDBsum; 7KOR; -.
DR AlphaFoldDB; P68137; -.
DR SMR; P68137; -.
DR STRING; 9823.ENSSSCP00000010867; -.
DR PaxDb; P68137; -.
DR PeptideAtlas; P68137; -.
DR Ensembl; ENSSSCT00015064766; ENSSSCP00015025920; ENSSSCG00015047339.
DR Ensembl; ENSSSCT00040062959; ENSSSCP00040026558; ENSSSCG00040044916.
DR Ensembl; ENSSSCT00055049539; ENSSSCP00055039593; ENSSSCG00055024685.
DR Ensembl; ENSSSCT00065106117; ENSSSCP00065047178; ENSSSCG00065076746.
DR GeneID; 100154254; -.
DR KEGG; ssc:100154254; -.
DR CTD; 58; -.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P68137; -.
DR OMA; DESHACE; -.
DR OrthoDB; 649708at2759; -.
DR TreeFam; TF354237; -.
DR Reactome; R-SSC-390522; Striated Muscle Contraction.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P68137; SS.
DR GO; GO:0005884; C:actin filament; ISS:UniProtKB.
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:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0005865; C:striated muscle thin filament; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISS:UniProtKB.
DR GO; GO:0030240; P:skeletal muscle thin filament assembly; ISS:UniProtKB.
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 3D-structure; Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW Methylation; Muscle protein; Nucleotide-binding; Oxidation;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..377
FT /note="Actin, alpha skeletal muscle, intermediate form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT /id="PRO_0000442807"
FT CHAIN 3..377
FT /note="Actin, alpha skeletal muscle"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT /id="PRO_0000442808"
FT REGION 112..125
FT /note="Interaction with alpha-actinin"
FT /evidence="ECO:0000250|UniProtKB:P68135"
FT REGION 360..372
FT /note="Interaction with alpha-actinin"
FT /evidence="ECO:0000250|UniProtKB:P68135"
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:P68134"
FT MOD_RES 49
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P68134"
FT MOD_RES 63
FT /note="N6-malonyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 75
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P68138"
FT MOD_RES 86
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68133"
SQ SEQUENCE 377 AA; 42051 MW; DF2A3A046346A179 CRC64;
MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
MSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIT
KQEYDEAGPS IVHRKCF
