ID PRS44_MOUSE Reviewed; 372 AA. AC Q402U7; Q924U6; DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 1. DT 08-NOV-2023, entry version 117. DE RecName: Full=Serine protease 44 {ECO:0000305}; DE EC=3.4.21.-; DE AltName: Full=Testis serine protease 4; DE Short=TESSP-4; DE AltName: Full=Testis-specific serine protease 4; DE Flags: Precursor; GN Name=Prss44 {ECO:0000312|MGI:MGI:1920586}; GN Synonyms=Tessp4 {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] (ISOFORM 1). RX PubMed=19798924; DOI=10.2108/zsj.26.294; RA Takano N., Kimura A., Takahashi T.; RT "Two distinct localization patterns of testis-specific serine protease 1 RT (TESSP1) in the seminiferous tubules of the mouse testis."; RL Zool. Sci. 26:294-300(2009). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR RP LOCATION, DEVELOPMENTAL STAGE, FUNCTION, AND CAUTION. 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 [3] 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). CC -!- FUNCTION: Lacks protease activity in vitro. CC {ECO:0000269|PubMed:23536369}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:23536369}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q402U7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q402U7-2; Sequence=VSP_041974, VSP_041975; CC -!- TISSUE SPECIFICITY: Testis-specific (PubMed:23536369). Expressed by CC primary and secondary spermatocytes (PubMed:23536369). CC {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}. CC -!- CAUTION: Lacks protease activity in vitro. CC {ECO:0000269|PubMed:23536369}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB162857; BAE19954.1; -; mRNA. DR EMBL; AB047758; BAB63919.1; -; mRNA. DR EMBL; AC139378; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS40782.1; -. [Q402U7-1] DR RefSeq; NP_683742.2; NM_148940.3. [Q402U7-1] DR AlphaFoldDB; Q402U7; -. DR SMR; Q402U7; -. DR MEROPS; S01.106; -. DR GlyCosmos; Q402U7; 1 site, No reported glycans. DR GlyGen; Q402U7; 1 site. DR PaxDb; 10090-ENSMUSP00000095948; -. DR ProteomicsDB; 291678; -. [Q402U7-1] DR ProteomicsDB; 291679; -. [Q402U7-2] DR DNASU; 73336; -. DR Ensembl; ENSMUST00000098345; ENSMUSP00000095948; ENSMUSG00000032493. [Q402U7-1] DR GeneID; 73336; -. DR KEGG; mmu:73336; -. DR UCSC; uc009rut.2; mouse. [Q402U7-1] DR UCSC; uc009ruu.2; mouse. [Q402U7-2] DR AGR; MGI:1920586; -. DR CTD; 73336; -. DR MGI; MGI:1920586; Prss44. DR VEuPathDB; HostDB:ENSMUSG00000032493; -. DR eggNOG; KOG3627; Eukaryota. DR GeneTree; ENSGT00940000162829; -. DR HOGENOM; CLU_006842_0_4_1; -. DR InParanoid; Q402U7; -. DR OMA; INARHIC; -. DR OrthoDB; 4629979at2759; -. DR PhylomeDB; Q402U7; -. DR TreeFam; TF351676; -. DR BioGRID-ORCS; 73336; 1 hit in 76 CRISPR screens. DR PRO; PR:Q402U7; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q402U7; Protein. DR Bgee; ENSMUSG00000032493; Expressed in spermatocyte and 38 other tissues. DR ExpressionAtlas; Q402U7; baseline and differential. DR Genevisible; Q402U7; MM. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central. DR GO; GO:0007281; P:germ cell development; IBA:GO_Central. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. DR GO; GO:0007283; P:spermatogenesis; 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:SF133; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 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. PE 2: Evidence at transcript level; KW Alternative splicing; Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase; KW Membrane; Protease; Reference proteome; Serine protease; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..372 FT /note="Serine protease 44" FT /id="PRO_0000413699" FT TOPO_DOM 26..351 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 352..372 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 112..345 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT REGION 31..72 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 152 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 197 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 297 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT CARBOHYD 208 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 137..153 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 231..303 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 262..283 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 293..321 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT VAR_SEQ 1..163 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:23536369" FT /id="VSP_041974" FT VAR_SEQ 334..372 FT /note="SYYRDWIIKELSRASCWKLSGFLVLSVCLVLHLAIVVAL -> ASPNDTALP FT PTHRAHCPQDCFQDPRLAKME (in isoform 2)" FT /evidence="ECO:0000303|PubMed:23536369" FT /id="VSP_041975" SQ SEQUENCE 372 AA; 41073 MW; E15BB243F3B9784A CRC64; MAFQGCDCFG LLVWLLLLQT RLGKARMVPG TPSLSPLPSE NGLDDSGVNP QERPLTGMPE TSLPRKPGDS TRPLDSMAFT PGQSFSTMSL SRQPFPTWVP PTSACGHRTA RIVGGRPAPA RKWPWQVSLQ VHKQHICGGS LISKWWVITA AHCVYGHLDY AVFMGDADLW SKRPVRIPVQ DIIVHQDFSM MRTVVHDIAL VLLAFPVNYS VNIQPVCIPE KSFLVQPGTL CWVTGWGKVL EQGRSSRILQ EIELNIIRHE KCNQILKDIM GNIFTLVQEG GVCGYNEKGG DACQGDSGGP LVCEFNKTWV QVGIVSWGLG CGRIGYPGVY TEVSYYRDWI IKELSRASCW KLSGFLVLSV CLVLHLAIVV AL //