ID   ACT3_LIMPO              Reviewed;         376 AA.
AC   P41340;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Actin-3;
DE   Flags: Precursor;
OS   Limulus polyphemus (Atlantic horseshoe crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
OC   Xiphosura; Limulidae; Limulus.
OX   NCBI_TaxID=6850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=7822422; DOI=10.1083/jcb.128.1.51;
RA   Way M., Sanders M., Garcia C., Sakai J., Matsudaira P.;
RT   "Sequence and domain organization of scruin, an actin-cross-linking protein
RT   in the acrosomal process of Limulus sperm.";
RL   J. Cell Biol. 128:51-60(1995).
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   -!- PTM: Oxidation of Met-45 to form methionine sulfoxide promotes actin
CC       filament depolymerization. Methionine sulfoxide is produced
CC       stereospecifically, but it is not known whether the (S)-S-oxide or the
CC       (R)-S-oxide is produced (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; Z38130; CAA86290.1; -; mRNA.
DR   PIR; S49480; S49480.
DR   RefSeq; XP_013788449.1; XM_013932995.1.
DR   RefSeq; XP_013790276.1; XM_013934822.1.
DR   PDB; 3B63; EM; -; A/C/G/I/L/M=7-371, B/E/H/J/K/N=8-371, D=8-365, F=8-363.
DR   PDBsum; 3B63; -.
DR   AlphaFoldDB; P41340; -.
DR   SMR; P41340; -.
DR   PRIDE; P41340; -.
DR   GeneID; 106472357; -.
DR   GeneID; 106474132; -.
DR   OrthoDB; 649708at2759; -.
DR   EvolutionaryTrace; P41340; -.
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   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW   Nucleotide-binding; Oxidation.
FT   PROPEP          1..2
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000000686"
FT   CHAIN           3..376
FT                   /note="Actin-3"
FT                   /id="PRO_0000000687"
FT   MOD_RES         3
FT                   /note="N-acetylaspartate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         45
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         48
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   376 AA;  41808 MW;  4EEBD433E0FA097B CRC64;
     MCDDEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
     TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD
     LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFDQEMAT AASSSSLEKS
     YELPDGQVIT IGNERFRCPE ALFQPSFLGM ESSGIHETTY NSIMKCDIDI RKDLYANTVL
     SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYDESGPSI VHRKCF