PRS40_MOUSE
ID PRS40_MOUSE Reviewed; 365 AA.
AC A6H6T1; E9QL09; O70170;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Serine protease 40;
DE EC=3.4.21.-;
DE AltName: Full=Testicular serine protease 2;
DE Flags: Precursor;
GN Name=Prss40; Synonyms=Tesp2;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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}.
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DR EMBL; AB008911; BAA26133.1; -; mRNA.
DR EMBL; AC106841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC145989; AAI45990.1; -; mRNA.
DR CCDS; CCDS14870.1; -.
DR PIR; JE0105; JE0105.
DR RefSeq; NP_033382.2; NM_009356.2.
DR AlphaFoldDB; A6H6T1; -.
DR SMR; A6H6T1; -.
DR BioGRID; 204122; 4.
DR STRING; 10090.ENSMUSP00000045118; -.
DR MEROPS; S01.045; -.
DR GlyGen; A6H6T1; 1 site.
DR EPD; A6H6T1; -.
DR PaxDb; A6H6T1; -.
DR PRIDE; A6H6T1; -.
DR ProteomicsDB; 291904; -.
DR DNASU; 21756; -.
DR Ensembl; ENSMUST00000047840; ENSMUSP00000045118; ENSMUSG00000037529.
DR GeneID; 21756; -.
DR KEGG; mmu:21756; -.
DR UCSC; uc007aox.2; mouse.
DR CTD; 21756; -.
DR MGI; MGI:1270857; Prss40.
DR VEuPathDB; HostDB:ENSMUSG00000037529; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000157345; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; A6H6T1; -.
DR OMA; SWYVVGL; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; A6H6T1; -.
DR TreeFam; TF351676; -.
DR BioGRID-ORCS; 21756; 3 hits in 71 CRISPR screens.
DR PRO; PR:A6H6T1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; A6H6T1; protein.
DR Bgee; ENSMUSG00000037529; Expressed in spermatid and 13 other tissues.
DR ExpressionAtlas; A6H6T1; baseline and differential.
DR Genevisible; A6H6T1; MM.
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; -; 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 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.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..365
FT /note="Serine protease 40"
FT /id="PRO_0000344982"
FT DOMAIN 69..313
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 312..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 109
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 193..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 226..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 260..288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 4
FT /note="I -> V (in Ref. 1; BAA26133)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="G -> S (in Ref. 1; BAA26133)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="H -> PTN (in Ref. 1; BAA26133)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="S -> G (in Ref. 1; BAA26133 and 3; AAI45990)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="G -> S (in Ref. 1; BAA26133)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="D -> N (in Ref. 1; BAA26133)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="A -> T (in Ref. 1; BAA26133)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="Missing (in Ref. 1; BAA26133)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="I -> T (in Ref. 1; BAA26133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 40146 MW; E012E07D446B6429 CRC64;
MCGIRAKKSG LGGYGAGLLA ALLGVSFLSQ HAQTAEHVTN AANNTTIQIM KSTLSLSEVC
GKTKFQGKIY GGQIAGAERW PWQASLRLYG RHICGAVLID KNWVLSAAHC FQRSQEPSDY
HVMLGYTDLN SPTRYSRTMS VQKVIVHKDY NRFHTQGSDI VLLQLRSSVE YSSHILPACV
PEENIKIPKE KACWASGWGY LREDVRIPLP NELYEAELII MSNDQCKGFF PPPVPGSGRS
YYIYDDMVCA ADYDMSKSIC AGDSGGPLVC LLEGSWYVVG LTSWSSTCEE PIVSPSVFAR
VSYFDKWIKD NKKSSSNSKP GESPHHPGSP ENENPEGDNK NQGAVIKPTV CTALLLSQIL
LQQLI
