ACTC_STRPU
ID ACTC_STRPU Reviewed; 376 AA.
AC Q07903;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Actin, cytoskeletal 2A;
DE AltName: Full=Actin, cytoskeletal IIA;
DE Contains:
DE RecName: Full=Actin, cytoskeletal 2A, intermediate form;
DE Flags: Precursor;
GN Name=CYIIA;
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-314.
RX PubMed=6302475; DOI=10.1128/mcb.3.3.448-456.1983;
RA Schuler M.A., McOsker P., Keller E.B.;
RT "DNA sequence of two linked actin genes of sea urchin.";
RL Mol. Cell. Biol. 3:448-456(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 315-376.
RX PubMed=9279375; DOI=10.1128/mcb.1.7.609-628.1981;
RA Scheller R.H., McAllister L.B., Crain W.R. Jr., Durica D.S., Posakony J.W.,
RA Thomas T.L., Britten R.J., Davidson E.H.;
RT "Organization and expression of multiple actin genes in the sea urchin.";
RL Mol. Cell. Biol. 1:609-628(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
RX PubMed=3148745; DOI=10.1007/bf02143499;
RA Durica D.S., Garza D., Restrepo M.A., Hryniewicz M.M.;
RT "DNA sequence analysis and structural relationships among the cytoskeletal
RT actin genes of the sea urchin Strongylocentrotus purpuratus.";
RL J. Mol. Evol. 28:72-86(1988).
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. Cytoplasm, cytoskeleton.
CC -!- DEVELOPMENTAL STAGE: Thought to be expressed early in embryogenesis.
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 promotes actin
CC repolymerization. {ECO:0000250|UniProtKB:P68033}.
CC -!- PTM: Monomethylation at Lys-85 (K85me1) regulates actin-myosin
CC interaction and actomyosin-dependent processes. Demethylation by ALKBH4
CC is required for maintaining actomyosin dynamics supporting normal
CC cleavage furrow ingression during cytokinesis and cell migration.
CC {ECO:0000250|UniProtKB:P68032}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; AH001097; AAA30031.1; -; Genomic_DNA.
DR EMBL; J01170; AAC41545.1; -; Genomic_DNA.
DR EMBL; J01169; AAC41544.1; -; mRNA.
DR EMBL; M35321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q07903; -.
DR SMR; Q07903; -.
DR PRIDE; Q07903; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; Q07903; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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 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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation;
KW Nucleotide-binding; Oxidation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..376
FT /note="Actin, cytoskeletal 2A, intermediate form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT /id="PRO_0000443015"
FT CHAIN 3..376
FT /note="Actin, cytoskeletal 2A"
FT /evidence="ECO:0000250|UniProtKB:P68135"
FT /id="PRO_0000000727"
FT MOD_RES 2
FT /note="N-acetylcysteine; in intermediate form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT MOD_RES 3
FT /note="N-acetylaspartate; in Actin, cytoskeletal 2A"
FT /evidence="ECO:0000250|UniProtKB:P68135"
FT MOD_RES 45
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P68033"
FT MOD_RES 48
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P68033"
FT MOD_RES 74
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P62739"
FT MOD_RES 85
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68032"
FT UNSURE 123
FT UNSURE 188
FT UNSURE 239..240
FT UNSURE 271
FT UNSURE 309..310
SQ SEQUENCE 376 AA; 41801 MW; 87E2248A466462B8 CRC64;
MCDDDVAALV VDNGSGMVKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
TQIMFETFNS PAMYVAIQAV LSLYASGRTT GIVFDSGDGV SHTVPIYEGY ALPHAILRLD
LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMQT AASSSSLEKS
YELPDGQVIT IGNERFRAPE ALFQPAFLGM ESAGIHETCY NSIMKCDVDI RKDLYANSVL
SGGSTMYPIA ADRMQKEITA LAPPTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
QEYDESGPSI VHRKCF
