ID Q9R0T7_MOUSE Unreviewed; 246 AA. AC Q9R0T7; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 10-JUN-2008, entry version 59. DE Pancreatic trypsin (Trypsin 4) (Adult male stomach cDNA, RIKEN full- DE length enriched library, clone:2210008B19 product:PANCREATIC TRYPSIN DE (0910001B19RIK PROTEIN) (TRYPSINOGEN 8) homolog) (Adult male spleen DE cDNA, RIKEN full-length enriched library, clone:0910001B19 DE product:PANCREATIC TRYPSIN (0910001B19RIK PROTEIN) (TRYPSINOGEN 8) DE homolog) (Trypsinogen 8). GN Name=Try4; Synonyms=trypsinogen; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=129SVJ; RX MEDLINE=99436155; PubMed=10506205; DOI=10.1074/jbc.274.41.29426; RA Ohmura K., Kohno N., Kobayashi Y., Yamagata K., Sato S., RA Kashiwabara S., 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] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Stomach, and Spleen; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=21103195; PubMed=11160223; RA Chen F., Rowen L., Hood L., Rothenberg E.V.; RT "Differential transcriptional regulation of individual TCR V beta RT segments before gene rearrangement."; RL J. Immunol. 166:1771-1780(2001). CC -!- SIMILARITY: Belongs to the peptidase S1 family. 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; AE000664; AAB69056.1; -; Genomic_DNA. DR EMBL; BC061135; AAH61135.1; -; mRNA. DR EMBL; AB017032; BAA74761.1; -; Genomic_DNA. DR EMBL; AK003064; BAB22542.1; -; mRNA. DR EMBL; AK008667; BAB25821.1; -; mRNA. DR RefSeq; NP_035776.1; -. DR UniGene; Mm.383263; -. DR HSSP; P00763; 1SLU. DR SMR; Q9R0T7; 24-246. DR MEROPS; S01.057; -. DR Ensembl; ENSMUSG00000054106; Mus musculus. DR GeneID; 22074; -. DR KEGG; mmu:22074; -. DR MGI; MGI:102757; Try4. DR HOVERGEN; Q9R0T7; -. DR ArrayExpress; Q9R0T7; -. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR001254; Peptidase_S1_S6. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; UNKNOWN_1. DR PROSITE; PS00135; TRYPSIN_SER; 1. PE 2: Evidence at transcript level; KW Hydrolase; Protease; Serine protease. SQ SEQUENCE 246 AA; 26274 MW; B6A9F4C99079633F CRC64; MRALLFLALV GAAVAFPVDD DDKIVGGYTC RENSVPYQVS LNSGYHFCGG SLINDQWVVS AAHCYKSRIQ VRLGEHNINV LEGNEQFVNS AKIIKHPNFN SRTLNNDIML IKLASPVTLN ARVATVALPS SCAPAGTQCL ISGWGNTLSF GVNNPDLLQC LDAPLLPQAD CEASYPGKIT NNMICVGFLE GGKDSCQGDS GGPVVCNGQL QGIVSWGYGC ALKDNPGVYT KVCNYVDWIQ NTIAAN //