PRS45_MOUSE
ID PRS45_MOUSE Reviewed; 317 AA.
AC Q8K4I7; Q3KNK7; Q8K4D1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Inactive serine protease 45 {ECO:0000305};
DE AltName: Full=Inactive testis serine protease 5;
DE AltName: Full=Trypsin-like protease p98;
DE Flags: Precursor;
GN Name=Prss45 {ECO:0000312|MGI:MGI:3605764}; Synonyms=Tessp5;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=ICR; TISSUE=Testis;
RA Jinn C.L., Luo C.-W., Ou C.-M., Chen Y.-H.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 MRNA] (ISOFORM 2).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K4I7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K4I7-2; Sequence=VSP_035356;
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: In contrast to other members of the family, lacks the
CC conserved Ser at position 243 which is replaced by a Pro residue,
CC suggesting it is inactive. {ECO:0000305}.
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DR EMBL; AF392062; AAM97837.1; -; mRNA.
DR EMBL; AF453931; AAM97842.1; -; Genomic_DNA.
DR EMBL; AK077121; BAC36624.1; -; mRNA.
DR EMBL; BC107230; AAI07231.1; -; mRNA.
DR EMBL; BC107231; AAI07232.1; -; mRNA.
DR CCDS; CCDS23575.1; -. [Q8K4I7-1]
DR RefSeq; NP_694812.1; NM_153172.1. [Q8K4I7-1]
DR AlphaFoldDB; Q8K4I7; -.
DR SMR; Q8K4I7; -.
DR STRING; 10090.ENSMUSP00000011391; -.
DR MEROPS; S01.968; -.
DR GlyGen; Q8K4I7; 3 sites.
DR PaxDb; Q8K4I7; -.
DR PRIDE; Q8K4I7; -.
DR ProteomicsDB; 291750; -. [Q8K4I7-1]
DR ProteomicsDB; 291751; -. [Q8K4I7-2]
DR Antibodypedia; 53159; 29 antibodies from 10 providers.
DR DNASU; 260408; -.
DR Ensembl; ENSMUST00000011391; ENSMUSP00000011391; ENSMUSG00000047257. [Q8K4I7-1]
DR Ensembl; ENSMUST00000146794; ENSMUSP00000120471; ENSMUSG00000047257. [Q8K4I7-2]
DR GeneID; 260408; -.
DR KEGG; mmu:260408; -.
DR UCSC; uc009ruw.1; mouse. [Q8K4I7-1]
DR UCSC; uc009rux.1; mouse. [Q8K4I7-2]
DR CTD; 260408; -.
DR MGI; MGI:3605764; Prss45.
DR VEuPathDB; HostDB:ENSMUSG00000047257; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000161932; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q8K4I7; -.
DR OMA; PWEVSLQ; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q8K4I7; -.
DR TreeFam; TF351676; -.
DR BioGRID-ORCS; 260408; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8K4I7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8K4I7; protein.
DR Bgee; ENSMUSG00000047257; Expressed in spermatocyte and 4 other tissues.
DR Genevisible; Q8K4I7; MM.
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; -; 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 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.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..317
FT /note="Inactive serine protease 45"
FT /id="PRO_0000349308"
FT DOMAIN 44..291
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 172..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 207..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 239..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 36..44
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035356"
FT CONFLICT 168
FT /note="V -> I (in Ref. 1; AAM97842 and 3; AAI07232/
FT AAI07231)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 35723 MW; E061C160668B4DEC CRC64;
MATSLRGLDA GPGSLRRWIL ICFAALLLLP PRPNLGYNEN YTEPVCGTPW WPDNLEESHH
WPWEASLQIE DKHVCGGALI DRSWVVSAAH CIQGNKEYSV MLGSSTLHPN GSSWTLKIPV
GDIIIHPKYW GRNFIRSDIA LLCLETPVTF NKYVQPICLP EHNFNFKVGT KCWVTGWGQV
KQHSSAQLTP APELWEAEVF IIDNKNCDSI FHKKTLYPQV VPLIRKNMIC TTNYGEDLCY
GDPGGPLACE IDGRWILAGV FSWEKACATV PNLSVYTRIT KYTIWIKDQV SHGAQLGPCR
TSWLLLLPWL LQLPVSL