ACTM_HELTB
ID ACTM_HELTB Reviewed; 376 AA.
AC P53464;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Actin, cytoskeletal;
DE AltName: Full=M;
DE Flags: Precursor;
OS Heliocidaris tuberculata (Sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Echinometridae;
OC Heliocidaris.
OX NCBI_TaxID=7635;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9190067; DOI=10.1093/oxfordjournals.molbev.a025805;
RA Kissinger J.C., Hahn J.-H., Raff R.A.;
RT "Rapid evolution in a conserved gene family. Evolution of the actin gene
RT family in the sea urchin genus Heliocidaris and related genera.";
RL Mol. Biol. Evol. 14:654-665(1997).
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 -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; U32357; AAA86534.1; -; Genomic_DNA.
DR EMBL; U32353; AAA86534.1; JOINED; Genomic_DNA.
DR EMBL; U32354; AAA86534.1; JOINED; Genomic_DNA.
DR EMBL; U32355; AAA86534.1; JOINED; Genomic_DNA.
DR EMBL; U32356; AAA86534.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; P53464; -.
DR SMR; P53464; -.
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 3: Inferred from homology;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding.
FT PROPEP 1..2
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000682"
FT CHAIN 3..376
FT /note="Actin, cytoskeletal"
FT /id="PRO_0000000683"
FT MOD_RES 3
FT /note="N-acetylaspartate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 376 AA; 41762 MW; 2964E6E5405FA692 CRC64;
MCDDEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
TQIMFETFNA PAMYVAIQAV LSLYASGRTT GIVLDSGDGV THTVPIYEGY ALPHAILRLD
LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYT ALDFEQEMAT AAASSSLEKS
YELPDGQVIT IGNERFRCPE TLFQPAFIGM ESAGIHETTY NSIMKCDIDI RKDLYANTVL
SGGTSMYPGI ADRMQKEITA LAPSSMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
QEYDESGPSI VHRKCF