ID   ACTC_BRAFL              Reviewed;         375 AA.
AC   Q93131;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Actin, cytoplasmic;
DE   AltName: Full=BfCA1;
DE   Contains:
DE     RecName: Full=Actin, cytoplasmic, N-terminally processed;
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Larva;
RX   PubMed=9931404; DOI=10.1016/s0378-1119(98)00608-8;
RA   Kusakabe R., Satoh N., Holland L.Z., Kusakabe T.;
RT   "Genomic organization and evolution of actin genes in the amphioxus
RT   Branchiostoma belcheri and Branchiostoma floridae.";
RL   Gene 227:1-10(1999).
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; D87406; BAA13350.1; -; mRNA.
DR   RefSeq; XP_002606072.1; XM_002606026.1.
DR   AlphaFoldDB; Q93131; -.
DR   SMR; Q93131; -.
DR   STRING; 7739.XP_002606072.1; -.
DR   PRIDE; Q93131; -.
DR   eggNOG; KOG0676; Eukaryota.
DR   OMA; KCDESIC; -.
DR   OrthoDB; 649708at2759; -.
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_0000367111"
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_0000000645"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine; in Actin, cytoplasmic;
FT                   alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylglutamate; in Actin, cytoplasmic, N-
FT                   terminally processed"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   375 AA;  41721 MW;  9EAF8A4E3AD5172E CRC64;
     MEDDVAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNSP AMYVAIQAVL SLYASGRTTG IVLDSGDGVS HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMSTA ASSSSLEKSY
     ELPDGQVITI GNERFRCPES LFQPSFLGME STGVHETTYN SIMKCDIDIR KDLYANTVLS
     GGTTMFPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF