PRS44_MOUSE
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 03-AUG-2022, entry version 111.
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, AND DEVELOPMENTAL STAGE.
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 -!- 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}.
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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 GlyGen; Q402U7; 1 site.
DR PaxDb; Q402U7; -.
DR PRIDE; Q402U7; -.
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 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; IVIHRYF; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q402U7; -.
DR TreeFam; TF351676; -.
DR BioGRID-ORCS; 73336; 1 hit in 71 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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 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
