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ACT2_CAEEL
ID   ACT2_CAEEL              Reviewed;         376 AA.
AC   P10984; O45744;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 3.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Actin-2;
DE   Flags: Precursor;
GN   Name=act-2; ORFNames=T04C12.5;
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 1-83.
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.
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; X16797; CAA34718.1; -; Genomic_DNA.
DR   EMBL; Z81584; CAB04675.1; -; Genomic_DNA.
DR   EMBL; J01043; AAA27888.1; -; Genomic_DNA.
DR   PIR; S16709; S16709.
DR   PIR; T24448; T24448.
DR   RefSeq; NP_505818.1; NM_073417.5.
DR   AlphaFoldDB; P10984; -.
DR   SMR; P10984; -.
DR   BioGRID; 44561; 54.
DR   DIP; DIP-25116N; -.
DR   IntAct; P10984; 5.
DR   STRING; 6239.T04C12.5.1; -.
DR   EPD; P10984; -.
DR   PaxDb; P10984; -.
DR   PeptideAtlas; P10984; -.
DR   PRIDE; P10984; -.
DR   EnsemblMetazoa; T04C12.5.1; T04C12.5.1; WBGene00000064.
DR   GeneID; 179534; -.
DR   UCSC; T04C12.5; c. elegans.
DR   CTD; 179534; -.
DR   WormBase; T04C12.5; CE13150; WBGene00000064; act-2.
DR   eggNOG; KOG0676; Eukaryota.
DR   GeneTree; ENSGT00950000182960; -.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; P10984; -.
DR   OMA; WISRTEY; -.
DR   OrthoDB; 649708at2759; -.
DR   PhylomeDB; P10984; -.
DR   Reactome; R-CEL-190873; Gap junction degradation.
DR   Reactome; R-CEL-196025; Formation of annular gap junctions.
DR   Reactome; R-CEL-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-CEL-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-CEL-437239; Recycling pathway of L1.
DR   Reactome; R-CEL-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-CEL-446353; Cell-extracellular matrix interactions.
DR   Reactome; R-CEL-5626467; RHO GTPases activate IQGAPs.
DR   Reactome; R-CEL-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   Reactome; R-CEL-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-CEL-5674135; MAP2K and MAPK activation.
DR   Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-CEL-9035034; RHOF GTPase cycle.
DR   SignaLink; P10984; -.
DR   PRO; PR:P10984; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00000064; Expressed in embryo and 3 other tissues.
DR   GO; GO:0005884; C:actin filament; IDA:WormBase.
DR   GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR   GO; GO:0005524; F:ATP binding; ISS:WormBase.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:WormBase.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR   GO; GO:0040011; P:locomotion; IMP:WormBase.
DR   GO; GO:0007111; P:meiosis II cytokinesis; IMP: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   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_0000000652"
FT   CHAIN           3..376
FT                   /note="Actin-2"
FT                   /id="PRO_0000000653"
FT   MOD_RES         3
FT                   /note="N-acetylaspartate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        10..11
FT                   /note="VV -> IL (in Ref. 1; CAA34718)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   376 AA;  41778 MW;  69D9209F0D5C3190 CRC64;
     MCDDDVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
     TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVLDSGDGV THTVPIYEGY ALPHAILRLD
     LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS
     YELPDGQVIT VGNERFRCPE ALFQPSFLGM ESAGIHETSY NSIMKCDIDI RKDLYANTVL
     SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYDESGPSI VHRKCF
 
 
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