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ACTC_BRALA
ID   ACTC_BRALA              Reviewed;         375 AA.
AC   O17503;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Actin, cytoplasmic;
DE   Contains:
DE     RecName: Full=Actin, cytoplasmic, N-terminally processed;
OS   Branchiostoma lanceolatum (Common lancelet) (Amphioxus lanceolatum).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomidae; Branchiostoma.
OX   NCBI_TaxID=7740;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9419242; DOI=10.1007/pl00006269;
RA   Bovenschulte M., Weber K.;
RT   "Deuterostomic actin genes and the definition of the chordates: cDNA
RT   cloning and gene organization for cephalochordates and hemichordates.";
RL   J. Mol. Evol. 45:653-660(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, cytoskeleton.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; Y13663; CAA74014.1; -; mRNA.
DR   AlphaFoldDB; O17503; -.
DR   SMR; O17503; -.
DR   PRIDE; O17503; -.
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   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding.
FT   CHAIN           1..375
FT                   /note="Actin, cytoplasmic"
FT                   /id="PRO_0000367112"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..375
FT                   /note="Actin, cytoplasmic, N-terminally processed"
FT                   /id="PRO_0000000647"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine; in Actin, cytoplasmic;
FT                   alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylaspartate; in Actin, cytoplasmic, N-
FT                   terminally processed"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   375 AA;  41713 MW;  19FDA9F9584FFCDF CRC64;
     MDDDVAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP VEHGIVTNWD DMEKIWHHTF YNELRIAPEE NPLLLTEAPL NPKANREKMT
     QIMFETFNSP AMYVAIQAVL SLYASGRTTG IVLDSGDGVS HTVPIYEGYA LPHAILRLDL
     AGRDQTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMSTA ASSSSLEKSY
     ELPDGQVITI GNERFRCPES LFQPSFLGME STGVHETTYN SIMKCDIDIR KDLYANTVLS
     GGTTMFPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
 
 
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