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   03-AUG-2022, entry version 127.
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; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=4000121; DOI=10.1128/mcb.5.5.1151-1162.1985;
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 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 promote actin
CC       repolymerization (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; X02648; CAA26486.1; -; Genomic_DNA.
DR   PIR; A26559; A26559.
DR   RefSeq; NP_001007825.1; NM_001007824.2.
DR   AlphaFoldDB; P53478; -.
DR   SMR; P53478; -.
DR   BioGRID; 676968; 3.
DR   STRING; 9031.ENSGALP00000039176; -.
DR   PaxDb; P53478; -.
DR   GeneID; 415296; -.
DR   KEGG; gga:415296; -.
DR   CTD; 71; -.
DR   VEuPathDB; HostDB:geneid_415296; -.
DR   eggNOG; KOG0676; Eukaryota.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; P53478; -.
DR   OrthoDB; 649708at2759; -.
DR   PhylomeDB; P53478; -.
DR   TreeFam; TF354237; -.
DR   PRO; PR:P53478; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR   GO; GO:0048870; P:cell motility; IBA:GO_Central.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding; Oxidation;
KW   Reference proteome.
FT   CHAIN           1..376
FT                   /note="Actin, cytoplasmic type 5"
FT                   /id="PRO_0000089052"
FT   MOD_RES         45
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         48
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="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