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 03-AUG-2022, entry version 98.
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; Q32KU2; -.
DR Ensembl; ENSBTAT00000024541; ENSBTAP00000024541; ENSBTAG00000018442.
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; 1314811at2759; -.
DR TreeFam; TF331065; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000018442; Expressed in spermatid and 14 other tissues.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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; -; 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 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; 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