PRS42_MOUSE
ID PRS42_MOUSE Reviewed; 335 AA.
AC Q8VIF2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Serine protease 42 {ECO:0000305};
DE EC=3.4.21.-;
DE AltName: Full=Testis serine protease 2;
DE Flags: Precursor;
GN Name=Prss42 {ECO:0000312|MGI:MGI:2665280};
GN Synonyms=Tessp2 {ECO:0000303|PubMed:23536369};
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP FUNCTION, DEVELOPMENTAL STAGE, AND TOPOLOGY.
RX PubMed=23536369; DOI=10.1095/biolreprod.112.106328;
RA Yoneda R., Takahashi T., Matsui H., Takano N., Hasebe Y., Ogiwara K.,
RA Kimura A.P.;
RT "Three testis-specific paralogous serine proteases play different roles in
RT murine spermatogenesis and are involved in germ cell survival during
RT meiosis.";
RL Biol. Reprod. 88:118-118(2013).
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: Plays a role in spermatogenesis. Involved in germ cell
CC survival during meiosis. {ECO:0000269|PubMed:23536369}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23536369}. Cell
CC membrane {ECO:0000269|PubMed:23536369}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:23536369}.
CC -!- TISSUE SPECIFICITY: Testis-specific (PubMed:23536369). Mainly detected
CC in round spermatids at all the eminiferous epithelial stages (at
CC protein level) (PubMed:23536369). {ECO:0000269|PubMed:23536369}.
CC -!- DEVELOPMENTAL STAGE: In testis, expressed at all stages from the late
CC pachytene primary spermatocyte to the secondary spermatocyte. Not
CC detected at day 7 after birth. Expression is detected at day 14 and
CC increases dramatically at day 21 and reach a peak at day 28 to remain
CC high until day 56. {ECO:0000269|PubMed:23536369}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AB052292; BAB78735.1; -; mRNA.
DR EMBL; BC060984; AAH60984.1; -; mRNA.
DR CCDS; CCDS23572.1; -.
DR RefSeq; NP_694739.1; NM_153099.1.
DR AlphaFoldDB; Q8VIF2; -.
DR SMR; Q8VIF2; -.
DR STRING; 10090.ENSMUSP00000041088; -.
DR MEROPS; S01.317; -.
DR GlyGen; Q8VIF2; 3 sites.
DR PhosphoSitePlus; Q8VIF2; -.
DR PaxDb; Q8VIF2; -.
DR PRIDE; Q8VIF2; -.
DR ProteomicsDB; 291677; -.
DR DNASU; 235628; -.
DR Ensembl; ENSMUST00000035715; ENSMUSP00000041088; ENSMUSG00000044664.
DR GeneID; 235628; -.
DR KEGG; mmu:235628; -.
DR UCSC; uc009rus.1; mouse.
DR CTD; 235628; -.
DR MGI; MGI:2665280; Prss42.
DR VEuPathDB; HostDB:ENSMUSG00000044664; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000163134; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q8VIF2; -.
DR OMA; CEYNDTW; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q8VIF2; -.
DR TreeFam; TF351676; -.
DR BioGRID-ORCS; 235628; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Prss42; mouse.
DR PRO; PR:Q8VIF2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8VIF2; protein.
DR Bgee; ENSMUSG00000044664; Expressed in spermatocyte and 5 other tissues.
DR Genevisible; Q8VIF2; MM.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
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:0007281; P:germ cell development; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IDA:MGI.
DR CDD; cd00190; Tryp_SPc; 1.
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 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 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Differentiation; Disulfide bond; Glycoprotein;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Protease; Reference proteome;
KW Serine protease; Signal; Spermatogenesis.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..335
FT /note="Serine protease 42"
FT /id="PRO_0000349279"
FT DOMAIN 79..315
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 119
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 165
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 267
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 199..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 232..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 263..291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 335 AA; 36683 MW; E8FC667DC9427EFC CRC64;
MASGGGSLGL IVFLLLLQPK PCEAWAAASV LSTSGFPSGF SEAPRDNPPP PTRVRMSKAT
TRSPFMNFSL VCGQPFMKIM GGVDAEEGKW PWQVSVRVRH MHVCGGSLIN SQWVLTAAHC
IYSRIQYNVK VGDRSVYRQN TSLVIPIKTI FVHPKFSTTI VVKNDIALLK LQHPVNFTTN
IYPVCIPSES FPVKAGTKCW VTGWGKLVPG APDVPTEILQ EVDQNVILYE ECNEMLKKAT
SSSVDLVKRG MVCGYKERGK DACQGDSGGP MSCEFENKWV QVGVVSWGIS CGRKGYPGVY
TDVAFYSKWL IAVVNQADCL HPVVFLVLLL CSLTS
