(data stored in ACNUC18020 zone)

SWISSPROT: ACT5_CHICK

ID   ACT5_CHICK              Reviewed;         376 AA.
AC   P53478;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAY-2019, entry version 115.
DE   RecName: Full=Actin, cytoplasmic type 5;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=4000121; DOI=10.1128/MCB.5.5.1151;
RA   Bergsma D.J., Chang K.S., Schwartz R.J.;
RT   "Novel chicken actin gene: third cytoplasmic isoform.";
RL   Mol. Cell. Biol. 5:1151-1162(1985).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all 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.
CC       Each 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.
CC       The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote
CC       actin repolymerization (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
DR   EMBL; X02648; CAA26486.1; -; Genomic_DNA.
DR   PIR; A26559; A26559.
DR   RefSeq; NP_001007825.1; NM_001007824.2.
DR   SMR; P53478; -.
DR   BioGrid; 676968; 3.
DR   STRING; 9031.ENSGALP00000039176; -.
DR   PaxDb; P53478; -.
DR   PRIDE; P53478; -.
DR   GeneID; 415296; -.
DR   KEGG; gga:415296; -.
DR   CTD; 71; -.
DR   eggNOG; KOG0676; Eukaryota.
DR   eggNOG; COG5277; LUCA.
DR   HOGENOM; HOG000233340; -.
DR   InParanoid; P53478; -.
DR   KO; K05692; -.
DR   OMA; FHTTAER; -.
DR   OrthoDB; 649708at2759; -.
DR   PhylomeDB; P53478; -.
DR   TreeFam; TF354237; -.
DR   PRO; PR:P53478; -.
DR   Proteomes; UP000000539; Unplaced.
DR   Bgee; ENSGALG00000001381; Expressed in 11 organ(s), highest expression level in testis.
DR   GO; GO:0005856; C:cytoskeleton; ISS:AgBase.
DR   GO; GO:0097433; C:dense body; ISS:AgBase.
DR   GO; GO:0005925; C:focal adhesion; ISS:AgBase.
DR   GO; GO:0005886; C:plasma membrane; ISS:AgBase.
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   PANTHER; PTHR11937; PTHR11937; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   3: Inferred from homology;
DR   PRODOM; P53478.
DR   SWISS-2DPAGE; P53478.
KW   ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Nucleotide-binding; Oxidation; Reference proteome.
FT   CHAIN         1    376       Actin, cytoplasmic type 5.
FT                                /FTId=PRO_0000089052.
FT   MOD_RES      45     45       Methionine (R)-sulfoxide. {ECO:0000250}.
FT   MOD_RES      48     48       Methionine (R)-sulfoxide. {ECO:0000250}.
SQ   SEQUENCE   376 AA;  41836 MW;  C5E300CAF0E5B401 CRC64;
     MADEEIAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
     TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV THTVPIYEGY ALPHAILRLD
     LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS
     YELPDGQVIT IGNERFRCPE AIFQPSFLGM ESCGIHETTF NSIMKCDVDI RKDLYANTVL
     SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYDESGPSI VHRKCF
//

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