ID   PRS39_MOUSE             Reviewed;         367 AA.
AC   O70169; Q80YD5;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Inactive serine protease 39;
DE   AltName: Full=Inactive testicular serine protease 1;
DE   Flags: Precursor;
GN   Name=Prss39; Synonyms=Tesp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Testis;
RX   PubMed=9588171; DOI=10.1006/bbrc.1998.8501;
RA   Kohno N., Yamagata K., Yamada S., Kashiwabara S., Sakai Y., Baba T.;
RT   "Two novel testicular serine proteases, TESP1 and TESP2, are present in the
RT   mouse sperm acrosome.";
RL   Biochem. Biophys. Res. Commun. 245:658-665(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play an important role in the sperm/egg interaction;
CC       released during the acrosome reaction. {ECO:0000269|PubMed:9588171}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC       {ECO:0000269|PubMed:9588171}. Secreted {ECO:0000269|PubMed:9588171}.
CC   -!- TISSUE SPECIFICITY: Expressed in testis. More specifically, abundantly
CC       expressed in the haploid round spermatid. {ECO:0000269|PubMed:9588171}.
CC   -!- MISCELLANEOUS: There appears to be no human ortholog of this protein.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   -!- CAUTION: In contrast to other members of the family, lacks the
CC       conserved Asp at position 158, which is replaced by an Asn residue,
CC       suggesting it is inactive. {ECO:0000305}.
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DR   EMBL; BC049616; AAH49616.2; -; mRNA.
DR   EMBL; BC115665; AAI15666.1; -; mRNA.
DR   EMBL; BC115666; AAI15667.1; -; mRNA.
DR   EMBL; AB008910; BAA26132.1; -; mRNA.
DR   CCDS; CCDS14868.1; -.
DR   PIR; JE0104; JE0104.
DR   RefSeq; NP_033381.1; NM_009355.2.
DR   AlphaFoldDB; O70169; -.
DR   SMR; O70169; -.
DR   STRING; 10090.ENSMUSP00000027299; -.
DR   MEROPS; S01.985; -.
DR   SwissPalm; O70169; -.
DR   PaxDb; 10090-ENSMUSP00000027299; -.
DR   ProteomicsDB; 291676; -.
DR   DNASU; 21755; -.
DR   Ensembl; ENSMUST00000027299.10; ENSMUSP00000027299.4; ENSMUSG00000026125.10.
DR   GeneID; 21755; -.
DR   KEGG; mmu:21755; -.
DR   UCSC; uc007aov.1; mouse.
DR   AGR; MGI:1270856; -.
DR   CTD; 21755; -.
DR   MGI; MGI:1270856; Prss39.
DR   VEuPathDB; HostDB:ENSMUSG00000026125; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000157345; -.
DR   HOGENOM; CLU_006842_0_4_1; -.
DR   InParanoid; O70169; -.
DR   OMA; CFQKSHE; -.
DR   OrthoDB; 4629979at2759; -.
DR   PhylomeDB; O70169; -.
DR   TreeFam; TF351692; -.
DR   BioGRID-ORCS; 21755; 2 hits in 76 CRISPR screens.
DR   PRO; PR:O70169; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; O70169; Protein.
DR   Bgee; ENSMUSG00000026125; Expressed in seminiferous tubule of testis and 7 other cell types or tissues.
DR   ExpressionAtlas; O70169; baseline and differential.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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   PANTHER; PTHR24253:SF42; PROTEASE, SERINE 47; 1.
DR   PANTHER; PTHR24253; TRANSMEMBRANE PROTEASE SERINE; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   Genevisible; O70169; MM.
PE   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; Disulfide bond; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..367
FT                   /note="Inactive serine protease 39"
FT                   /id="PRO_0000344981"
FT   DOMAIN          68..312
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        93..109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        192..269
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        225..248
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        259..287
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   367 AA;  40766 MW;  029833E3253CF954 CRC64;
     MWGSRAQQSG PDRGGACLLA AFLLCFSLLH AQDYTPSQTP PPTSNTSLKP RGRVQKELCG
     KTKFQGKIYG GQIAKAERWP WQASLIFRGR HICGAVLIDK TWLLSAAHCF QRSLTPSDYR
     ILLGYNQLSN PSNYSRQMTV NKVILHEDYS KLSRLEKNIV LIQLHHPVIY STHIFPACVP
     DGTTKVSPNN LCWISGWGML SADKFLQAPF PLLDAEVSLI DEEECTTFFQ TPEVSITEYD
     VIKDDVLCAG DLTNQKSSCR GDSGGPLVCF LNSFWYVVGL ANWNGACLEP IHSPNIFTKV
     SYFSDWIKQK KANTPAADVS SAPLEEMASS LRGWGNYSAG ITLKPRISTT LLSSQALLLQ
     SIWLRIL
//