ACTH_CHICK
ID ACTH_CHICK Reviewed; 376 AA.
AC P63270; O73680; P12718;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Actin, gamma-enteric smooth muscle;
DE AltName: Full=Alpha-actin-3;
DE AltName: Full=Gamma-2-actin;
DE AltName: Full=Smooth muscle gamma-actin;
DE Contains:
DE RecName: Full=Actin, gamma-enteric smooth muscle, intermediate form;
DE Flags: Precursor;
GN Name=ACTG2; Synonyms=ACTA3, ACTSG;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Smooth muscle;
RX PubMed=8319268; DOI=10.1002/cm.970240108;
RA Kovacs A.M., Zimmer W.E.;
RT "Molecular cloning and expression of the chicken smooth muscle gamma-actin
RT mRNA.";
RL Cell Motil. Cytoskeleton 24:67-81(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Smooth muscle;
RA Kovacs A.M., Zimmer W.E.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:3W3D}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 3-376 IN COMPLEX WITH ATP AND
RP MANNOSE, AND METHYLATION AT HIS-74.
RX DOI=10.1107/S0108767378096798;
RA Sasaki K., Sakabe K., Sakabe N., Kondo H., Shimomur M.;
RT "Refined structure and solvent network of chicken gizzard G-actin DNase 1
RT complex at 1.8A resolution.";
RL Acta Crystallogr. A 49:C111-C112(1993).
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-45 and Met-48 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:P63268}.
CC -!- PTM: Monomethylation at Lys-85 (K85me1) 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-74 by SETD3. {ECO:0000250|UniProtKB:P63267}.
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; S63494; AAB27386.1; -; mRNA.
DR EMBL; AF012348; AAC05823.1; -; Genomic_DNA.
DR PIR; I51208; ATCHSM.
DR RefSeq; NP_990503.1; NM_205172.1.
DR PDB; 3W3D; X-ray; 1.80 A; A=3-376.
DR PDBsum; 3W3D; -.
DR AlphaFoldDB; P63270; -.
DR SMR; P63270; -.
DR BioGRID; 676350; 1.
DR Ensembl; ENSGALT00000065171; ENSGALP00000048103; ENSGALG00000041634.
DR GeneID; 396084; -.
DR KEGG; gga:396084; -.
DR CTD; 72; -.
DR VEuPathDB; HostDB:geneid_396084; -.
DR GeneTree; ENSGT00940000154148; -.
DR InParanoid; P63270; -.
DR OMA; THKEEYI; -.
DR OrthoDB; 649708at2759; -.
DR PRO; PR:P63270; -.
DR Proteomes; UP000000539; Chromosome 22.
DR Bgee; ENSGALG00000041634; Expressed in colon and 12 other tissues.
DR ExpressionAtlas; P63270; baseline and differential.
DR GO; GO:0071944; C:cell periphery; IEA:Ensembl.
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 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..376
FT /note="Actin, gamma-enteric smooth muscle, intermediate
FT form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT /id="PRO_0000442955"
FT CHAIN 3..376
FT /note="Actin, gamma-enteric smooth muscle"
FT /evidence="ECO:0000250|UniProtKB:P63267"
FT /id="PRO_0000442956"
FT MOD_RES 2
FT /note="N-acetylcysteine; in intermediate form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT MOD_RES 3
FT /note="N-acetylglutamate; in Actin, gamma-enteric smooth
FT muscle"
FT /evidence="ECO:0000250|UniProtKB:P63267"
FT MOD_RES 45
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P63268"
FT MOD_RES 48
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P63268"
FT MOD_RES 74
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:3W3D"
FT MOD_RES 85
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68133"
FT CONFLICT 221
FT /note="A -> P (in Ref. 2; AAC05823)"
FT /evidence="ECO:0000305"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:3W3D"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:3W3D"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:3W3D"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:3W3D"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:3W3D"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3W3D"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:3W3D"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:3W3D"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:3W3D"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:3W3D"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:3W3D"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3W3D"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:3W3D"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:3W3D"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:3W3D"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:3W3D"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 310..319
FT /evidence="ECO:0007829|PDB:3W3D"
FT TURN 334..337
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:3W3D"
FT HELIX 360..364
FT /evidence="ECO:0007829|PDB:3W3D"
SQ SEQUENCE 376 AA; 41877 MW; 6EC08CD5EEAD445E CRC64;
MCEEETTALV CDNGSGLCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
SKRGILTLKY PIEHGIITNW DDMEKIWHHS FYNELRVAPE EHPTLLTEAP LNPKANREKM
TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSGDGV THNVPIYEGY ALPHAIMRLD
LAGRDLTDYL MKILTERGYS FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKS
YELPDGQVIT IGNERFRCPE TLFQPSFIGM ESAGIHETTY NSIMKCDIDI RKDLYANNVL
SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
PEYDEAGPSI VHRKCF
