ACT1_CAEEL
ID ACT1_CAEEL Reviewed; 376 AA.
AC P0DM41; P10983; P10985;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Actin-1;
DE Flags: Precursor;
GN Name=act-1; ORFNames=T04C12.6;
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].
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 2-376 IN COMPLEX WITH GELSOLIN
RP AND ATP.
RX PubMed=12732734; DOI=10.1073/pnas.0832273100;
RA Vorobiev S., Strokopytov B., Drubin D.G., Frieden C., Ono S., Condeelis J.,
RA Rubenstein P.A., Almo S.C.;
RT "The structure of nonvertebrate actin: implications for the ATP hydrolytic
RT mechanism.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5760-5765(2003).
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
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; X16796; CAA34717.1; -; Genomic_DNA.
DR EMBL; Z81584; CAB04678.1; -; Genomic_DNA.
DR EMBL; J01042; AAA27887.1; -; Genomic_DNA.
DR PIR; S16710; S16710.
DR RefSeq; NP_505817.1; NM_073416.6.
DR RefSeq; NP_505819.1; NM_073418.5.
DR PDB; 1D4X; X-ray; 1.75 A; A=2-376.
DR PDBsum; 1D4X; -.
DR AlphaFoldDB; P0DM41; -.
DR SMR; P0DM41; -.
DR BioGRID; 44560; 2.
DR BioGRID; 44562; 11.
DR STRING; 6239.T04C12.4.1; -.
DR EPD; P0DM41; -.
DR PaxDb; P0DM41; -.
DR PeptideAtlas; P0DM41; -.
DR PRIDE; P0DM41; -.
DR EnsemblMetazoa; T04C12.6.1; T04C12.6.1; WBGene00000063.
DR GeneID; 179535; -.
DR KEGG; cel:CELE_T04C12.6; -.
DR CTD; 179535; -.
DR WormBase; T04C12.6; CE13148; WBGene00000063; act-1.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00950000182960; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR OMA; EQEMDTT; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P0DM41; -.
DR PRO; PR:P0DM41; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000063; Expressed in pharyngeal muscle cell (C elegans) and 8 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:WormBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IGI:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IGI:WormBase.
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 Nucleotide-binding; Reference proteome.
FT PROPEP 1..2
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000650"
FT CHAIN 3..376
FT /note="Actin-1"
FT /id="PRO_0000000651"
FT MOD_RES 3
FT /note="N-acetylaspartate"
FT /evidence="ECO:0000250"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:1D4X"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:1D4X"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:1D4X"
FT TURN 334..337
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:1D4X"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:1D4X"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 360..366
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:1D4X"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:1D4X"
SQ SEQUENCE 376 AA; 41796 MW; BCF86DE909D4EE0D 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 AMFQPSFLGM ESAGIHETSY NSIMKCDIDI RKDLYANTVL
SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
QEYDESGPSI VHRKCF
