ID   ACRO_RABIT              Reviewed;         431 AA.
AC   P48038;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 110.
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: Precursor;
GN   Name=ACR;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Testis;
RX   PubMed=8086468; DOI=10.1016/0167-4781(94)90275-5;
RA   Richardson R.T., O'Rand M.G.;
RT   "Cloning and sequencing of cDNAs for rabbit preproacrosin and a novel
RT   preproacrosin-related cDNA.";
RL   Biochim. Biophys. Acta 1219:215-218(1994).
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   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; U05204; AAA61630.1; -; mRNA.
DR   PIR; S47538; S47538.
DR   RefSeq; NP_001075805.1; NM_001082336.1.
DR   AlphaFoldDB; P48038; -.
DR   SMR; P48038; -.
DR   MEROPS; S01.223; -.
DR   GeneID; 100009184; -.
DR   KEGG; ocu:100009184; -.
DR   CTD; 49; -.
DR   InParanoid; P48038; -.
DR   BRENDA; 3.4.21.10; 1749.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:InterPro.
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; ISS: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   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR012267; Pept_S1A_acrosin.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001141; Acrosin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000250"
FT   CHAIN           17..431
FT                   /note="Acrosin"
FT                   /id="PRO_0000027530"
FT   CHAIN           17..39
FT                   /note="Acrosin light chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027531"
FT   CHAIN           40..350
FT                   /note="Acrosin heavy chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027532"
FT   PROPEP          351..431
FT                   /note="Pro-rich"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027533"
FT   DOMAIN          40..288
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          295..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..315
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..383
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        86
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        140
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        238
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        22..152
FT                   /note="Interchain (between light and heavy chains)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        26..160
FT                   /note="Interchain (between light and heavy chains)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        71..87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        175..244
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        207..223
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        234..264
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   431 AA;  46422 MW;  1C015A4E0BC0C668 CRC64;
     MLPTAVLLVL VVSVVAKDNA TCDGPCGLRF RQNPQGGFRV VGGQAAQQGA WPWMVSLQIF
     TPRNNRRYHA CGGVLLNAHW VLTAAHCFNN KQKVYEWRMV FGAQEIEYGT DKPVRPPLQE
     RYVEKVVTHD QYNYMTEGND IALLKITPPV PCGPFIGPGC LPNSKAGPPK AAQTCYVAGW
     GYVKENAPRP SPTLMEARVD LINLELCNST QWYNGRITAS NLCAGYPSGK IDTCQGDSGG
     PLMCRENQGE PFVVQGITSW GVGCARAKRP GIYTATWPFL DWIASRIGSN ALRMIQPATP
     TPPTTRSPGV HQPPSAHPPW YFQHASGPPH PHPHPHPHPH PRPPQPPAAQ APPPPPPPPP
     PPPPPPPPPP PPPPPPPPAS TKPPQALSFA KRLQQLVEVL KGGSTFSGAK RVDTAAAAAE
     ATEIPEVTLA S