ACTS_ORYLA
ID ACTS_ORYLA Reviewed; 377 AA.
AC Q98972;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Actin, alpha skeletal muscle;
DE AltName: Full=Alpha-actin-1;
DE AltName: Full=OlMA1;
DE Contains:
DE RecName: Full=Actin, alpha skeletal muscle, intermediate form;
DE Flags: Precursor;
GN Name=acta1;
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kusakabe R., Kusakabe T., Suzuki N.;
RT "Medaka actin genes.";
RL Submitted (SEP-1996) 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.
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: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; D87740; BAA13446.1; -; mRNA.
DR RefSeq; NP_001098276.1; NM_001104806.1.
DR AlphaFoldDB; Q98972; -.
DR SMR; Q98972; -.
DR Ensembl; ENSORLT00000013650; ENSORLP00000013649; ENSORLG00000010881.
DR Ensembl; ENSORLT00015013382; ENSORLP00015022329; ENSORLG00015001620.
DR Ensembl; ENSORLT00020010920; ENSORLP00020002664; ENSORLG00020003451.
DR GeneID; 100049431; -.
DR KEGG; ola:100049431; -.
DR CTD; 407658; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00940000164361; -.
DR InParanoid; Q98972; -.
DR OrthoDB; 649708at2759; -.
DR Proteomes; UP000001038; Chromosome 3.
DR Proteomes; UP000265180; Chromosome 3.
DR Proteomes; UP000265200; Chromosome 3.
DR Bgee; ENSORLG00000010881; Expressed in muscle tissue and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005869; C:dynactin complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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_0000442827"
FT CHAIN 3..377
FT /note="Actin, alpha skeletal muscle"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT /id="PRO_0000442828"
FT MOD_RES 2
FT /note="N-acetylcysteine; in intermediate form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT MOD_RES 3
FT /note="N-acetylaspartate; in Actin, alpha skeletal muscle"
FT /evidence="ECO:0000250|UniProtKB:P68135"
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 75
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P68135"
FT MOD_RES 86
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68133"
SQ SEQUENCE 377 AA; 41959 MW; BC348535F7F38690 CRC64;
MCDDEETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDAGDG VTHNVPVYEG YALPHAIMRL
DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETA YNSIMKCDID IRKDLYANNV
LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
KQEYDEAGPS IVHRKCF
