ID   PRS37_MACFA             Reviewed;         235 AA.
AC   Q4R7Y7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Probable inactive serine protease 37 {ECO:0000305};
DE   AltName: Full=Probable inactive trypsin-X2;
DE   Flags: Precursor;
GN   Name=PRSS37 {ECO:0000250|UniProtKB:A4D1T9}; Synonyms=TRYX2;
GN   ORFNames=QtsA-14071;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in male fertility. May have a role in sperm
CC       migration or binding to zona-intact eggs. Involved in the activation of
CC       the proacrosin/acrosin system. {ECO:0000250|UniProtKB:A4D1T9,
CC       ECO:0000250|UniProtKB:Q9DAA4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC       {ECO:0000250|UniProtKB:A4D1T9}. Secreted
CC       {ECO:0000250|UniProtKB:A4D1T9}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   -!- CAUTION: Although related to peptidase S1 family, lacks the conserved
CC       active Ser residue in position 192 which is replaced by an Ala,
CC       suggesting that it has no protease activity. Lacks also metal binding
CC       sites Glu in position 67 which is replaced by Asn and Asn in position
CC       69 which is replaced by Lys. {ECO:0000305}.
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DR   EMBL; AB168674; BAE00785.1; -; mRNA.
DR   RefSeq; NP_001271811.1; NM_001284882.1.
DR   AlphaFoldDB; Q4R7Y7; -.
DR   SMR; Q4R7Y7; -.
DR   STRING; 9541.XP_005551045.1; -.
DR   GeneID; 101926589; -.
DR   CTD; 136242; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   OrthoDB; 1314811at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:2000344; P:positive regulation of acrosome reaction; ISS:UniProtKB.
DR   GO; GO:1905516; P:positive regulation of fertilization; ISS:UniProtKB.
DR   GO; GO:0051604; P:protein maturation; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0070613; P:regulation of protein processing; ISS:UniProtKB.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; Disulfide bond; Fertilization; Metal-binding;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..235
FT                   /note="Probable inactive serine protease 37"
FT                   /id="PRO_0000326071"
FT   DOMAIN          20..233
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        40..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        131..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        163..177
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   235 AA;  26416 MW;  3E03E1B83DCAD2AE CRC64;
     MKFIFYLSVL TGTFLFADSS VQKEDPAPYL VYLKSHFNPC VGVLIKPSWV LAPAHCYLPN
     LEVMLGNFKS RVRDGTEQTI NPIQIVRYWN YSDSAPQDDL MLIKLAKPAM LNPKVQPLPL
     ATTNVRPGTV CLLSGLDWSQ ENSGRHPDLR QNLEAPVMSD KECQKTEQGK SHRNSLCVKF
     VKVFSRIFGE VAVATVICKD KLQGIEVGHF MGGDVGIYTN VYKYVSWIEN TAKDK