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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
 
 
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