ACTS_CHICK
ID ACTS_CHICK Reviewed; 377 AA.
AC P68139; P02568; P99020;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 136.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP PROTEIN SEQUENCE OF 3-377, AND ACETYLATION AT ASP-3.
RC TISSUE=Skeletal muscle;
RX PubMed=456601; DOI=10.1016/0014-5793(79)80004-6;
RA Vandekerckhove J., Weber K.;
RT "The amino acid sequence of actin from chicken skeletal muscle actin and
RT chicken gizzard smooth muscle actin.";
RL FEBS Lett. 102:219-222(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6287424; DOI=10.1093/nar/10.13.3861;
RA Fornwald J.A., Kuncio G., Peng I., Ordahl C.P.;
RT "The complete nucleotide sequence of the chick a-actin gene and its
RT evolutionary relationship to the actin gene family.";
RL Nucleic Acids Res. 10:3861-3876(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2347492; DOI=10.1016/0378-1119(90)90029-q;
RA French B.A., Bergsma D.J., Schwartz R.J.;
RT "Analysis of a CR1 (chicken repeat) sequence flanking the 5' end of the
RT gene encoding alpha-skeletal actin.";
RL Gene 88:173-180(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Mammary gland;
RA Ordahl C.P.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43.
RC TISSUE=Mammary gland;
RX PubMed=6729461; DOI=10.1126/science.6729461;
RA Paterson B.M., Eldridge J.D.;
RT "Alpha-cardiac actin is the major sarcomeric isoform expressed in embryonic
RT avian skeletal muscle.";
RL Science 224:1436-1438(1984).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RX PubMed=6513927; DOI=10.1128/mcb.4.11.2498-2508.1984;
RA Chang K.S., Zimmer W.E. Jr., Bergsma D.J., Dodgson J.B., Schwartz R.J.;
RT "Isolation and characterization of six different chicken actin genes.";
RL Mol. Cell. Biol. 4:2498-2508(1984).
RN [7] {ECO:0000269|PubMed:12356759, ECO:0007744|PDB:1MDU}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ATP, AND METHYLATION
RP AT HIS-75.
RX PubMed=12356759; DOI=10.1074/jbc.m209160200;
RA Dawson J.F., Sablin E.P., Spudich J.A., Fletterick R.J.;
RT "Structure of an F-actin trimer disrupted by gelsolin and implications for
RT the mechanism of severing.";
RL J. Biol. Chem. 278:1229-1238(2003).
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. {ECO:0000269|PubMed:12356759}.
CC -!- INTERACTION:
CC P68139; P41832: BNI1; Xeno; NbExp=2; IntAct=EBI-3058728, EBI-3692;
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; V01507; CAA24753.1; -; Genomic_DNA.
DR PIR; A93432; ATCH.
DR RefSeq; NP_001026234.1; NM_001031063.1.
DR RefSeq; XP_015139542.1; XM_015284056.1.
DR PDB; 1MDU; X-ray; 2.20 A; B/E=1-377.
DR PDB; 5YU8; EM; 3.80 A; A/B/C/D/E=3-377.
DR PDB; 6D8C; EM; 3.54 A; H/J/K/L/M=3-377.
DR PDB; 6DJM; EM; 3.10 A; A/B/C/D=3-377.
DR PDB; 6DJN; EM; 3.10 A; A/B/C/D=3-377.
DR PDB; 6DJO; EM; 3.60 A; A/B/C/D=3-377.
DR PDB; 6M5G; EM; 3.60 A; A/B/C/D/E=1-377.
DR PDB; 6UPV; EM; 3.20 A; A/B/C/D/E=3-377.
DR PDB; 6UPW; EM; 2.90 A; A/B/C/D/E=3-377.
DR PDB; 6X5Z; EM; 4.24 A; A/B/C=1-377.
DR PDB; 7BT7; EM; 3.80 A; A/B/C/D/E=1-377.
DR PDB; 7BTE; EM; 4.20 A; A/C/E/G/I=1-377.
DR PDB; 7BTI; EM; 3.60 A; A/B/C/D/E=1-377.
DR PDB; 7K20; EM; 3.20 A; A/B/C/D=3-377.
DR PDB; 7K21; EM; 3.00 A; A/B/C/D=3-377.
DR PDB; 7KCH; EM; 4.33 A; B/C/G=1-377.
DR PDB; 7R8V; EM; 2.82 A; A/B/C/D/E=7-377.
DR PDB; 7R91; EM; 2.83 A; A/B/C=7-377.
DR PDB; 7RB8; EM; 3.63 A; A/B/C=5-377.
DR PDB; 7RB9; EM; 3.76 A; A/B/C=5-377.
DR PDBsum; 1MDU; -.
DR PDBsum; 5YU8; -.
DR PDBsum; 6D8C; -.
DR PDBsum; 6DJM; -.
DR PDBsum; 6DJN; -.
DR PDBsum; 6DJO; -.
DR PDBsum; 6M5G; -.
DR PDBsum; 6UPV; -.
DR PDBsum; 6UPW; -.
DR PDBsum; 6X5Z; -.
DR PDBsum; 7BT7; -.
DR PDBsum; 7BTE; -.
DR PDBsum; 7BTI; -.
DR PDBsum; 7K20; -.
DR PDBsum; 7K21; -.
DR PDBsum; 7KCH; -.
DR PDBsum; 7R8V; -.
DR PDBsum; 7R91; -.
DR PDBsum; 7RB8; -.
DR PDBsum; 7RB9; -.
DR AlphaFoldDB; P68139; -.
DR PCDDB; P68139; -.
DR SMR; P68139; -.
DR BioGRID; 682339; 4.
DR DIP; DIP-41824N; -.
DR ELM; P68139; -.
DR IntAct; P68139; 3.
DR STRING; 9031.ENSGALP00000018042; -.
DR iPTMnet; P68139; -.
DR Ensembl; ENSGALT00000088724; ENSGALP00000060685; ENSGALG00000011086.
DR GeneID; 421534; -.
DR KEGG; gga:421534; -.
DR CTD; 58; -.
DR VEuPathDB; HostDB:geneid_421534; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00940000154710; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P68139; -.
DR OMA; DESHACE; -.
DR OrthoDB; 649708at2759; -.
DR EvolutionaryTrace; P68139; -.
DR PRO; PR:P68139; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000011086; Expressed in skeletal muscle tissue and 13 other tissues.
DR ExpressionAtlas; P68139; baseline and differential.
DR GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR GO; GO:0005869; C:dynactin complex; IBA:GO_Central.
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: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 Direct protein sequencing; Methylation; Muscle protein; Nucleotide-binding;
KW 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_0000442815"
FT CHAIN 3..377
FT /note="Actin, alpha skeletal muscle"
FT /evidence="ECO:0000269|PubMed:456601"
FT /id="PRO_0000442816"
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:0000269|PubMed:456601"
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:0000269|PubMed:12356759,
FT ECO:0007744|PDB:1MDU"
FT MOD_RES 86
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68133"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:7R8V"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:7R91"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:1MDU"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:6UPW"
FT HELIX 208..218
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:1MDU"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:7K21"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 255..261
FT /evidence="ECO:0007829|PDB:1MDU"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 276..284
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 311..322
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:7R8V"
FT TURN 335..338
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 340..350
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 352..357
FT /evidence="ECO:0007829|PDB:1MDU"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 361..367
FT /evidence="ECO:0007829|PDB:1MDU"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:1MDU"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:6DJM"
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
