ID   ACTS_PONAB              Reviewed;         377 AA.
AC   Q5R9Q5;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
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 {ECO:0000250}.
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; CR859327; CAH91505.1; -; mRNA.
DR   RefSeq; NP_001125886.1; NM_001132414.1.
DR   AlphaFoldDB; Q5R9Q5; -.
DR   SMR; Q5R9Q5; -.
DR   STRING; 9601.ENSPPYP00000000129; -.
DR   Ensembl; ENSPPYT00000000138; ENSPPYP00000000129; ENSPPYG00000000127.
DR   GeneID; 100172818; -.
DR   KEGG; pon:100172818; -.
DR   CTD; 58; -.
DR   eggNOG; KOG0676; Eukaryota.
DR   GeneTree; ENSGT00940000156048; -.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; Q5R9Q5; -.
DR   OrthoDB; 649708at2759; -.
DR   TreeFam; TF354237; -.
DR   Proteomes; UP000001595; Chromosome 1.
DR   GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR   GO; GO:0044297; C:cell body; ISS:AgBase.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0030175; C:filopodium; ISS:AgBase.
DR   GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR   GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR   GO; GO:0005865; C:striated muscle thin filament; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0030240; P:skeletal muscle thin filament assembly; 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   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation;
KW   Muscle protein; Nucleotide-binding; Oxidation; 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_0000442809"
FT   CHAIN           3..377
FT                   /note="Actin, alpha skeletal muscle"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
FT                   /id="PRO_0000442810"
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