ID   ACRO_CAPHI              Reviewed;          60 AA.
AC   P10626;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Acrosin;
DE            EC=3.4.21.10;
DE   Contains:
DE     RecName: Full=Acrosin light chain;
DE   Contains:
DE     RecName: Full=Acrosin heavy chain;
DE   Flags: Fragment;
GN   Name=ACR;
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Sperm;
RX   PubMed=2930460; DOI=10.1042/bj2570447;
RA   Hardy D.M., Schoots A.F.M., Hedrick J.L.;
RT   "Caprine acrosin. Purification, characterization and proteolysis of the
RT   porcine zona pellucida.";
RL   Biochem. J. 257:447-453(1989).
CC   -!- FUNCTION: Acrosin is the major protease of mammalian spermatozoa. It is
CC       a serine protease of trypsin-like cleavage specificity, it is
CC       synthesized in a zymogen form, proacrosin and stored in the acrosome.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.10;
CC   -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
CC   -!- SUBUNIT: Heavy chain (catalytic) and a light chain linked by two
CC       disulfide bonds. Forms a heterodimer with SERPINA5 (By similarity).
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: X's in position 19 to 22 were introduced by homology
CC       with the pig sequence.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   PIR; S02175; S02175.
DR   PIR; S02176; S02176.
DR   STRING; 9925.ENSCHIP00000027035; -.
DR   MEROPS; S01.223; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:CAFA.
DR   GO; GO:0004040; F:amidase activity; ISS:UniProtKB.
DR   GO; GO:0042806; F:fucose binding; ISS:UniProtKB.
DR   GO; GO:0005537; F:mannose binding; ISS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR   GO; GO:0007340; P:acrosome reaction; ISS:UniProtKB.
DR   GO; GO:0007190; P:activation of adenylate cyclase activity; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0007338; P:single fertilization; ISS:UniProtKB.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001254; Trypsin_dom.
DR   Pfam; PF00089; Trypsin; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Reference proteome; Serine protease; Zymogen.
FT   CHAIN           1..23
FT                   /note="Acrosin light chain"
FT                   /id="PRO_0000027516"
FT   CHAIN           24..>60
FT                   /note="Acrosin heavy chain"
FT                   /id="PRO_0000027517"
FT   DOMAIN          24..>60
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        6
FT                   /note="Interchain (with heavy chain)"
FT                   /evidence="ECO:0000305"
FT   DISULFID        10
FT                   /note="Interchain (with heavy chain)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         60
SQ   SEQUENCE   60 AA;  6879 MW;  BF76512CB2A86752 CRC64;
     RDNTTCDGPC GIRFRQNRXX XXRIIGGQDA AHGSWPWMVS LQIFTYHNNR RYHVCGGSLL