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Database: UniProt
Entry: PRS37_BOVIN
LinkDB: PRS37_BOVIN
Original site: PRS37_BOVIN 
ID   PRS37_BOVIN             Reviewed;         235 AA.
AC   Q32KU2;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   24-JAN-2024, entry version 104.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-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 Arg. {ECO:0000305}.
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DR   EMBL; BC109928; AAI09929.1; -; mRNA.
DR   RefSeq; NP_001035659.1; NM_001040569.2.
DR   AlphaFoldDB; Q32KU2; -.
DR   SMR; Q32KU2; -.
DR   STRING; 9913.ENSBTAP00000024541; -.
DR   PaxDb; 9913-ENSBTAP00000024541; -.
DR   Ensembl; ENSBTAT00000024541.3; ENSBTAP00000024541.2; ENSBTAG00000018442.3.
DR   GeneID; 540062; -.
DR   KEGG; bta:540062; -.
DR   CTD; 136242; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018442; -.
DR   VGNC; VGNC:33420; PRSS37.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000161483; -.
DR   HOGENOM; CLU_006842_7_0_1; -.
DR   InParanoid; Q32KU2; -.
DR   OMA; DKDCQKT; -.
DR   OrthoDB; 4622581at2759; -.
DR   TreeFam; TF331065; -.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000018442; Expressed in spermatid and 14 other cell types or tissues.
DR   GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0008354; P:germ cell migration; IEA:Ensembl.
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; Trypsin-like serine proteases; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001254; Trypsin_dom.
DR   PANTHER; PTHR24271:SF61; INACTIVE SERINE PROTEASE 37-RELATED; 1.
DR   PANTHER; PTHR24271; KALLIKREIN-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; Disulfide bond; Fertilization; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..235
FT                   /note="Probable inactive serine protease 37"
FT                   /id="PRO_0000326069"
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;  26316 MW;  01A4B5ACA6F0A110 CRC64;
     MKFTFCLTVL AGTFFSAHSS VQKDDPSPYL VYLKSHFNPC VGVLIKSNWV LAPAHCYLPN
     LKVMLGNLRI RIRDGTEQTI NPIQIIRYWN HSHTAPQDDL MLIRLAKPAI LNEKVQPIAL
     ATSTVKPGTI CMLSGLDWSQ NNNGRHPDLR QNLEAPVMSD TACQETEQGK SHRNSICVKF
     LKVFSRIFGE LAVATVICKN KLQGIEVGHF MGGDVGIYTN VQKYVSWIES TTKDK
//
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