GenomeNet

Database: UniProt
Entry: P18601
LinkDB: P18601
Original site: P18601 
ID   ACT2_ARTSX              Reviewed;         376 AA.
AC   P18601;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-APR-2013, entry version 67.
DE   RecName: Full=Actin, clone 211;
DE   Flags: Precursor;
OS   Artemia sp. (Brine shrimp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Anostraca; Artemiidae; Artemia.
OX   NCBI_TaxID=6662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2402445; DOI=10.1093/nar/18.17.5219;
RA   Macias M.-T., Sastre L.;
RT   "Molecular cloning and expression of four actin isoforms during
RT   Artemia development.";
RL   Nucleic Acids Res. 18:5219-5225(1990).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- FUNCTION: Multiple isoforms are involved in various cellular
CC       functions such as cytoskeleton structure, cell mobility,
CC       chromosome movement and muscle contraction.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- PTM: Oxidation of Met-45 to form methionine sulfoxide promotes
CC       actin filament depolymerization. Methionine sulfoxide is produced
CC       stereospecifically, but it is not known whether the (S)-S-oxide or
CC       the (R)-S-oxide is produced (By similarity).
CC   -!- MISCELLANEOUS: There are at least 4 actin isoforms expressed
CC       during artemia development.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X52603; CAA36836.1; -; mRNA.
DR   PIR; S11451; S11451.
DR   ProteinModelPortal; P18601; -.
DR   SMR; P18601; 3-376.
DR   PRIDE; P18601; -.
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-related.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
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;
KW   Oxidation.
FT   PROPEP        1      2       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000612.
FT   CHAIN         3    376       Actin, clone 211.
FT                                /FTId=PRO_0000000613.
FT   MOD_RES       3      3       N-acetylaspartate (By similarity).
FT   MOD_RES      45     45       Methionine sulfoxide (By similarity).
FT   MOD_RES      48     48       Methionine sulfoxide (By similarity).
SQ   SEQUENCE   376 AA;  41784 MW;  7EF88D8ADF3BD19B CRC64;
     MCDDDVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE EHPILLTEAP LNPKANREKM
     TQIMFETFNS PAMYVAIQAV LSIYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD
     LAGRDLIDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS
     YELPDGQVIT IGNERFRCPE ALFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANTVL
     SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYDESGPGI VHRKCF
//
DBGET integrated database retrieval system