TSP50_MOUSE
ID TSP50_MOUSE Reviewed; 439 AA.
AC Q8BLH5; B2RWS9; Q8K466;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable threonine protease PRSS50;
DE EC=3.4.25.- {ECO:0000250|UniProtKB:Q9UI38};
DE AltName: Full=Serine protease 50;
DE AltName: Full=Testis-specific protease-like protein 50;
DE Flags: Precursor;
GN Name=Prss50; Synonyms=Tsp50;
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].
RC STRAIN=C57BL/6J;
RX PubMed=12140191; DOI=10.1093/hmg/11.16.1887;
RA Mitchem K.L., Hibbard E., Beyer L.A., Bosom K., Dootz G.A., Dolan D.F.,
RA Johnson K.R., Raphael Y., Kohrman D.C.;
RT "Mutation of the novel gene Tmie results in sensory cell defects in the
RT inner ear of spinner, a mouse model of human hearing loss DFNB6.";
RL Hum. Mol. Genet. 11:1887-1898(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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).
RN [4]
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be involved in proteolysis through its threonine
CC endopeptidase activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Although related to peptidase S1 family, lacks the conserved
CC active Ser residue in position 364 which is replaced by a Thr.
CC {ECO:0000305}.
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DR EMBL; AF481144; AAM89223.1; -; mRNA.
DR EMBL; AK045168; BAC32245.1; -; mRNA.
DR EMBL; AC139378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150686; AAI50687.1; -; mRNA.
DR CCDS; CCDS23577.1; -.
DR RefSeq; NP_666339.2; NM_146227.4.
DR AlphaFoldDB; Q8BLH5; -.
DR SMR; Q8BLH5; -.
DR BioGRID; 231698; 1.
DR STRING; 10090.ENSMUSP00000059668; -.
DR MEROPS; S01.993; -.
DR GlyGen; Q8BLH5; 3 sites.
DR PhosphoSitePlus; Q8BLH5; -.
DR MaxQB; Q8BLH5; -.
DR PaxDb; Q8BLH5; -.
DR PRIDE; Q8BLH5; -.
DR ProteomicsDB; 297999; -.
DR DNASU; 235631; -.
DR Ensembl; ENSMUST00000051097; ENSMUSP00000059668; ENSMUSG00000048752.
DR GeneID; 235631; -.
DR KEGG; mmu:235631; -.
DR UCSC; uc009rva.1; mouse.
DR CTD; 29122; -.
DR MGI; MGI:2447303; Prss50.
DR VEuPathDB; HostDB:ENSMUSG00000048752; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162593; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q8BLH5; -.
DR OMA; EQFCYEL; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q8BLH5; -.
DR TreeFam; TF351676; -.
DR BioGRID-ORCS; 235631; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q8BLH5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BLH5; protein.
DR Bgee; ENSMUSG00000048752; Expressed in spermatid and 21 other tissues.
DR ExpressionAtlas; Q8BLH5; baseline and differential.
DR Genevisible; Q8BLH5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
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 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.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Signal; Threonine protease; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..47
FT /evidence="ECO:0000255"
FT CHAIN 48..439
FT /note="Probable threonine protease PRSS50"
FT /id="PRO_0000415813"
FT TOPO_DOM 48..415
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 157..412
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 207
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 364
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 192..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 294..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 327..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 360..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 68
FT /note="W -> S (in Ref. 4; AAI50687)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="G -> S (in Ref. 4; AAI50687)"
FT /evidence="ECO:0000305"
FT CONFLICT 180..187
FT /note="WMVSVQAN -> GWSACRLH (in Ref. 1; AAM89223)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="I -> V (in Ref. 4; AAI50687)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 48676 MW; 7B007E62C5D8A154 CRC64;
MEPWCGAEVR GQGPQGPRVP GASRSRSRAL LLLLLLLLLL LPRRPAGERI RPRRPPRHAH
PRPPLTRWRP STGYLAAGAS PGTLSTTVPT GPGVSCGSRG ICPSGRLRLP RQAQTNQTTT
APPNSQTMAP LKTVGTLGMM DTTGSVLKTV HSSNLPFCGS SHEPDPTLRD PEAMTRRWPW
MVSVQANGSH ICAGILIASQ WVLTVAHCLS QNHVNYIVRA GSPWINQTAG TSSDVPVHRV
IINHGYQPRR YWSWVGRAHD IGLLKLKWGL KYSKYVWPIC LPGLDYVVED SSLCTVTGWG
YPRANGIWPQ FQSLQEKEVS ILNSKKCDHF YHKFSRISSL VRIINPQMIC ASDNNREEFC
YEITGEPLVC SSDGTWYLVG MMSWGPGCKK SEAPPIFLQV SYYRPWIWDR LSGEPLALPA
PSRTLLLAFL LLLILLGTL
