ID   ACTA_LIMPO              Reviewed;         376 AA.
AC   P41339;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Actin, acrosomal process isoform;
DE   AltName: Full=Actin-5;
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 and Met-48 to form methionine sulfoxide
CC       promotes actin filament depolymerization. Methionine sulfoxide is
CC       produced stereospecifically, but it is not known whether the (S)-S-
CC       oxide or the (R)-S-oxide is produced. {ECO:0000250|UniProtKB:P62737}.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; Z38131; CAA86291.1; -; mRNA.
DR   PIR; S49481; S49481.
DR   RefSeq; NP_001301052.1; NM_001314123.1.
DR   AlphaFoldDB; P41339; -.
DR   SMR; P41339; -.
DR   GeneID; 106476934; -.
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;
KW   Oxidation.
FT   PROPEP          1..2
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000000690"
FT   CHAIN           3..376
FT                   /note="Actin, acrosomal process isoform"
FT                   /id="PRO_0000000691"
FT   MOD_RES         3
FT                   /note="N-acetylaspartate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         45
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
FT   MOD_RES         48
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
SQ   SEQUENCE   376 AA;  41775 MW;  01C4D6F20337DD9C CRC64;
     MCDEDVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
     TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD
     LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEHEMTT AASSSSLEKS
     YELPDGQVIT IGNERFRCPE AMFQPSFLGM EACGIHETTF NSIMKCDVDI RKDLYANTVL
     SGGSTMFPGI ADRMQKEIGA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYDESGPSI VHRKCF