ID   ACT4_CAEEL              Reviewed;         376 AA.
AC   P10986; Q7YSY2;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Actin-4;
DE   Flags: Precursor;
GN   Name=act-4; ORFNames=M03F4.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=2795655; DOI=10.1016/0022-2836(89)90503-2;
RA   Krause M., Wild M., Rosenzweig B., Hirsh D.;
RT   "Wild-type and mutant actin genes in Caenorhabditis elegans.";
RL   J. Mol. Biol. 208:381-392(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-86.
RX   PubMed=6302275; DOI=10.1016/0022-2836(83)90056-6;
RA   Files J.G., Carr S., Hirsh D.;
RT   "Actin gene family of Caenorhabditis elegans.";
RL   J. Mol. Biol. 164:355-375(1983).
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. {ECO:0000269|PubMed:2795655}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:2795655}.
CC   -!- MISCELLANEOUS: In this organism there are four genes coding for actin.
CC       The sequences coded by genes 1 and 3 are identical. There are a few
CC       variations in the actins coded by genes 2 and 4.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; X16799; CAA34720.1; -; Genomic_DNA.
DR   EMBL; X16800; CAA34720.1; JOINED; Genomic_DNA.
DR   EMBL; FO081654; CCD83476.1; -; Genomic_DNA.
DR   EMBL; J01046; AAA27890.1; -; Genomic_DNA.
DR   EMBL; J01045; AAA27890.1; JOINED; Genomic_DNA.
DR   PIR; S27135; S27135.
DR   RefSeq; NP_508841.1; NM_076440.6.
DR   AlphaFoldDB; P10986; -.
DR   SMR; P10986; -.
DR   BioGRID; 45702; 21.
DR   DIP; DIP-27204N; -.
DR   IntAct; P10986; 10.
DR   STRING; 6239.M03F4.2a; -.
DR   EPD; P10986; -.
DR   PaxDb; P10986; -.
DR   PeptideAtlas; P10986; -.
DR   EnsemblMetazoa; M03F4.2a.1; M03F4.2a.1; WBGene00000066.
DR   GeneID; 180767; -.
DR   KEGG; cel:CELE_M03F4.2; -.
DR   UCSC; M03F4.2a; c. elegans.
DR   CTD; 180767; -.
DR   WormBase; M03F4.2a; CE12358; WBGene00000066; act-4.
DR   eggNOG; KOG0676; Eukaryota.
DR   InParanoid; P10986; -.
DR   OMA; KCDESIC; -.
DR   OrthoDB; 649708at2759; -.
DR   PhylomeDB; P10986; -.
DR   PRO; PR:P10986; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00000066; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   ExpressionAtlas; P10986; baseline and differential.
DR   GO; GO:0005856; C:cytoskeleton; ISS:WormBase.
DR   GO; GO:0045121; C:membrane raft; HDA:WormBase.
DR   GO; GO:0005865; C:striated muscle thin filament; IDA:WormBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:WormBase.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISS:WormBase.
DR   GO; GO:0000281; P:mitotic cytokinesis; 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   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW   Reference proteome.
FT   PROPEP          1..2
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000000654"
FT   CHAIN           3..376
FT                   /note="Actin-4"
FT                   /id="PRO_0000000655"
FT   MOD_RES         3
FT                   /note="N-acetylaspartate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        5
FT                   /note="E -> D (in Ref. 3; AAA27890)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   376 AA;  41778 MW;  4DF86D2E14623560 CRC64;
     MCDDEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
     TQIMFETFNT PAMYVAIQAV LSLYASGRTT GVVLDSGDGV THTVPIYEGY ALPHAILRLD
     LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS
     YELPDGQVIT VGNERFRCPE ALFQPSFLGM ESAGIHETSY NSIMKCDIDI RKDLYANTVL
     SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYDESGPSI VHRKCF