ID   TRY5_MOUSE              Reviewed;         246 AA.
AC   Q9QUK9;
DT   03-MAY-2023, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Trypsin-5 {ECO:0000312|MGI:MGI:102756};
DE            EC=3.4.21.4 {ECO:0000269|PubMed:23814066};
DE   AltName: Full=Testicular-specific serine protease 4 {ECO:0000303|PubMed:10506205};
DE   AltName: Full=Trypsinogen 9 {ECO:0000303|PubMed:23814066};
DE            Short=T9 {ECO:0000303|PubMed:23814066};
DE   Flags: Precursor;
GN   Name=Try5 {ECO:0000312|MGI:MGI:102756};
GN   Synonyms=Tc {ECO:0000303|PubMed:10506205}, Tesp4
GN   {ECO:0000303|PubMed:10506205};
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 {ECO:0000312|EMBL:BAA85187.1};
RN   [1] {ECO:0000312|EMBL:BAA85187.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=129/SvJ {ECO:0000312|EMBL:BAA74760.1};
RC   TISSUE=Testis {ECO:0000312|EMBL:BAA85187.1};
RX   PubMed=10506205; DOI=10.1074/jbc.274.41.29426;
RA   Ohmura K., Kohno N., Kobayashi Y., Yamagata K., Sato S., Kashiwabara S.,
RA   Baba T.;
RT   "A homologue of pancreatic trypsin is localized in the acrosome of
RT   mammalian sperm and is released during acrosome reaction.";
RL   J. Biol. Chem. 274:29426-29432(1999).
RN   [2] {ECO:0000312|EMBL:AAB69057.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11160223; DOI=10.4049/jimmunol.166.3.1771;
RA   Chen F., Rowen L., Hood L., Rothenberg E.V.;
RT   "Differential transcriptional regulation of individual TCR V beta segments
RT   before gene rearrangement.";
RL   J. Immunol. 166:1771-1780(2001).
RN   [3] {ECO:0000312|EMBL:BAB25300.1, ECO:0000312|EMBL:BAE35815.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB25300.1};
RC   TISSUE=Pancreas {ECO:0000312|EMBL:BAB25300.1}, and Stomach
RC   {ECO:0000312|EMBL:BAE35815.1};
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   [4] {ECO:0000312|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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   [5] {ECO:0000312|EMBL:AAI39221.1, ECO:0000312|EMBL:AAI39224.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000312|EMBL:AAI39221.1,
RC   ECO:0000312|EMBL:AAI39224.1};
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   [6] {ECO:0007744|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN   [7] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND CLEAVAGE BY
RP   AUTOCATALYSIS.
RX   PubMed=23814066; DOI=10.1074/jbc.m113.478800;
RA   Nemeth B.C., Wartmann T., Halangk W., Sahin-Toth M.;
RT   "Autoactivation of mouse trypsinogens is regulated by chymotrypsin C via
RT   cleavage of the autolysis loop.";
RL   J. Biol. Chem. 288:24049-24062(2013).
CC   -!- FUNCTION: Serine protease capable of autoactivation.
CC       {ECO:0000269|PubMed:23814066}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC         Evidence={ECO:0000269|PubMed:23814066};
CC   -!- ACTIVITY REGULATION: Activated by autocatalytic cleavage
CC       (PubMed:23814066). Cleavage by CTRC inhibits autoactivation
CC       (PubMed:23814066). {ECO:0000269|PubMed:23814066}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC       {ECO:0000269|PubMed:10506205}.
CC   -!- TISSUE SPECIFICITY: Expressed in the heart, lung, brain, kidney, liver,
CC       epididymis, ovary and uterus. Expression in the testis is limited to
CC       round and elongating spermatids. {ECO:0000269|PubMed:10506205}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the testis from 20 days of age
CC       onwards. {ECO:0000269|PubMed:10506205}.
CC   -!- PTM: Proteolytically cleaved and activated by an autocatalytic
CC       mechanism (PubMed:23814066). Cleavage by CTRC inhibits autoactivation
CC       (PubMed:23814066). {ECO:0000269|PubMed:23814066}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; AB017031; BAA74760.1; -; Genomic_DNA.
DR   EMBL; AB009661; BAA85187.1; -; mRNA.
DR   EMBL; AE000664; AAB69057.1; -; Genomic_DNA.
DR   EMBL; AK007843; BAB25300.1; -; mRNA.
DR   EMBL; AK160484; BAE35815.1; -; mRNA.
DR   EMBL; BC139220; AAI39221.1; -; mRNA.
DR   EMBL; BC139223; AAI39224.1; -; mRNA.
DR   CCDS; CCDS20045.1; -.
DR   RefSeq; NP_001003405.1; NM_001003405.4.
DR   AlphaFoldDB; Q9QUK9; -.
DR   SMR; Q9QUK9; -.
DR   STRING; 10090.ENSMUSP00000064498; -.
DR   MEROPS; S01.057; -.
DR   MEROPS; S01.058; -.
DR   GlyGen; Q9QUK9; 1 site, 1 O-linked glycan (1 site).
DR   MaxQB; Q9QUK9; -.
DR   PaxDb; 10090-ENSMUSP00000064498; -.
DR   PeptideAtlas; Q9QUK9; -.
DR   ProteomicsDB; 339082; -.
DR   Ensembl; ENSMUST00000064324.12; ENSMUSP00000064498.6; ENSMUSG00000036938.18.
DR   GeneID; 103964; -.
DR   KEGG; mmu:103964; -.
DR   UCSC; uc009bot.2; mouse.
DR   AGR; MGI:102756; -.
DR   CTD; 103964; -.
DR   MGI; MGI:102756; Try5.
DR   VEuPathDB; HostDB:ENSMUSG00000036938; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01050000244883; -.
DR   HOGENOM; CLU_006842_7_0_1; -.
DR   InParanoid; Q9QUK9; -.
DR   OMA; HPRYSSW; -.
DR   OrthoDB; 1314811at2759; -.
DR   Reactome; R-MMU-1442490; Collagen degradation.
DR   Reactome; R-MMU-1462054; Alpha-defensins.
DR   Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-6803157; Antimicrobial peptides.
DR   BioGRID-ORCS; 103964; 6 hits in 58 CRISPR screens.
DR   ChiTaRS; Try5; mouse.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9QUK9; Protein.
DR   Bgee; ENSMUSG00000036938; Expressed in pancreas and 21 other cell types or tissues.
DR   ExpressionAtlas; Q9QUK9; baseline and differential.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:MGI.
DR   GO; GO:0008236; F:serine-type peptidase activity; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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   PANTHER; PTHR24264:SF57; TRYPSIN-2; 1.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 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   1: Evidence at protein level;
KW   Autocatalytic cleavage; Cytoplasmic vesicle; Disulfide bond; Hydrolase;
KW   Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   PROPEP          16..23
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000457720"
FT   CHAIN           24..246
FT                   /note="Trypsin-5"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5015099940"
FT   DOMAIN          24..244
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        63
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        107
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        200
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   SITE            81
FT                   /note="Cleavage; by CTRC"
FT                   /evidence="ECO:0000269|PubMed:23814066"
FT   SITE            122
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000269|PubMed:23814066"
FT   SITE            150
FT                   /note="Cleavage; by CTRC"
FT                   /evidence="ECO:0000269|PubMed:23814066"
FT   SITE            193
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000269|PubMed:23814066"
FT   DISULFID        48..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        139..206
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        171..185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        196..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   246 AA;  26277 MW;  915C92353EC42809 CRC64;
     MNSLLFLALV GAAVAFPVDD DDKIVGGYTC RENSIPYQVS LNSGYHFCGG SLINDQWVVS
     AAHCYKTRIQ VRLGEHNINV LEGNEQFVNS AKIIKHPNFN SRTLNNDIML IKLASPVTLN
     ARVATVALPS SCAPAGTQCL ISGWGNTLSF GVNNPDLLQC LDAPLLPQAD CEASYPGKIT
     NNMICVGFLE GGKDSCQGDS GGPVVCNGQL QGIVSWGYGC ALKDNPGVYT KVCNYVDWIQ
     DTIAAN
//