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ACTM_STYPL
ID   ACTM_STYPL              Reviewed;         379 AA.
AC   Q00214;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Actin, muscle;
OS   Styela plicata (Wrinkled sea squirt) (Ascidia plicata).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC   Styelidae; Styela.
OX   NCBI_TaxID=7726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Muscle;
RX   PubMed=8315656; DOI=10.1007/bf00182183;
RA   Kovilur S., Jacobson J.W., Beach R.L., Jeffery W.R., Tomlinson C.R.;
RT   "Evolution of the chordate muscle actin gene.";
RL   J. Mol. Evol. 36:361-368(1993).
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   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix. Each
CC       actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   PIR; S33387; S33387.
DR   AlphaFoldDB; Q00214; -.
DR   SMR; Q00214; -.
DR   PRIDE; Q00214; -.
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   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   ATP-binding; Cytoplasm; Cytoskeleton; Muscle protein; Nucleotide-binding.
FT   CHAIN           1..379
FT                   /note="Actin, muscle"
FT                   /id="PRO_0000089029"
SQ   SEQUENCE   379 AA;  42354 MW;  F6ABA2A98D7D2DCD CRC64;
     MEDDQDEEQT ALVCDNGSGL VKAGFPGDAP PRAVFPLTVG RPRHQGVMVG MGQKDSYVGD
     EAQSKRGILT LKYPIEHGII TNWDNMEKIW HHTFYNELRV APEEHPVLLT EAPLNPKANR
     EKMTQIMFET FNVPAMYVAI QAVLSLYASG RTTGIVLDSG DGVSHNVPIY EGYALPHAIM
     RLDLAGRDLT DYLMKILTER GYSFVTTAER EIVRDIKEKL CYVALDFEQE MATAASSSSL
     EKSYELPDGQ VITIGNERFR CPETLFQPSF IGMESSGVHE TTYNSIMKCD IDIRKDLYAN
     NVLSGGTTMY PGIADRMQKE ITALAPSTMK SKIIAPPERK YSVWIGASIL ASLSTFQQMW
     ITKQEYDESG PSIVHRKCF
 
 
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