GenomeNet

Database: UniProt
Entry: P07477
LinkDB: P07477
Original site: P07477 
ID   TRY1_HUMAN              Reviewed;         247 AA.
AC   P07477; A1A509; A6NJ71; B2R5I5; Q5NV57; Q7M4N3; Q7M4N4; Q92955; Q9HAN4;
AC   Q9HAN5; Q9HAN6; Q9HAN7;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   02-JUN-2021, entry version 219.
DE   RecName: Full=Trypsin-1;
DE            EC=3.4.21.4;
DE   AltName: Full=Beta-trypsin;
DE   AltName: Full=Cationic trypsinogen;
DE   AltName: Full=Serine protease 1;
DE   AltName: Full=Trypsin I;
DE   Contains:
DE     RecName: Full=Alpha-trypsin chain 1;
DE   Contains:
DE     RecName: Full=Alpha-trypsin chain 2;
DE   Flags: Precursor;
GN   Name=PRSS1; Synonyms=TRP1, TRY1, TRYP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3011602; DOI=10.1016/0378-1119(86)90111-3;
RA   Emi M., Nakamura Y., Ogawa M., Yamamoto T., Nishide T., Mori T.,
RA   Matsubara K.;
RT   "Cloning, characterization and nucleotide sequences of two cDNAs encoding
RT   human pancreatic trypsinogens.";
RL   Gene 41:305-310(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8650574; DOI=10.1126/science.272.5269.1755;
RA   Rowen L., Koop B.F., Hood L.;
RT   "The complete 685-kilobase DNA sequence of the human beta T cell receptor
RT   locus.";
RL   Science 272:1755-1762(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-67, AND VARIANT PCTT GLY-22.
RX   PubMed=10930381; DOI=10.1053/gast.2000.9312;
RA   Teich N., Ockenga J., Hoffmeister A., Manns M., Mossner J., Keim V.;
RT   "Chronic pancreatitis associated with an activation peptide mutation that
RT   facilitates trypsin activation.";
RL   Gastroenterology 119:461-465(2000).
RN   [9]
RP   PROTEIN SEQUENCE OF 16-43 AND 123-142, FUNCTION, AND POST-TRANSLATIONAL
RP   PROCESSING.
RC   TISSUE=Gastric adenocarcinoma;
RX   PubMed=7945238; DOI=10.1042/bj3030187;
RA   Koshikawa N., Yasumitsu H., Nagashima Y., Umeda M., Miyazaki K.;
RT   "Identification of one- and two-chain forms of trypsinogen 1 produced by a
RT   human gastric adenocarcinoma cell line.";
RL   Biochem. J. 303:187-190(1994).
RN   [10]
RP   PROTEIN SEQUENCE OF 16-43.
RX   PubMed=2598466; DOI=10.1016/0009-8981(89)90254-4;
RA   Kimland M., Russick C., Marks W.H., Borgstroem A.;
RT   "Immunoreactive anionic and cationic trypsin in human serum.";
RL   Clin. Chim. Acta 184:31-46(1989).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-151, AND VARIANT PCTT HIS-122.
RX   PubMed=8841182; DOI=10.1038/ng1096-141;
RA   Whitcomb D.C., Gorry M.C., Preston R.A., Furey W., Sossenheimer M.J.,
RA   Ulrich C.D., Martin S.P., Gates L.K. Jr., Amann S.T., Toskes P.P.,
RA   Liddle R., McGrath K., Uomo G., Post J.C., Ehrlich G.D.;
RT   "Hereditary pancreatitis is caused by a mutation in the cationic
RT   trypsinogen gene.";
RL   Nat. Genet. 14:141-145(1996).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-151, AND VARIANTS PCTT ILE-29;
RP   PRO-104; CYS-116; HIS-122 AND PHE-139.
RX   PubMed=11866271; DOI=10.1111/j.1572-0241.2002.05467.x;
RA   Teich N., Bauer N., Mossner J., Keim V.;
RT   "Mutational screening of patients with nonalcoholic chronic pancreatitis:
RT   identification of further trypsinogen variants.";
RL   Am. J. Gastroenterol. 97:341-346(2002).
RN   [13]
RP   PROTEIN SEQUENCE OF 73-92, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Brain, and Cajal-Retzius cell;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [14]
RP   SULFATION AT TYR-154, AND MUTAGENESIS OF TYR-154.
RX   PubMed=17087724; DOI=10.1111/j.1742-4658.2006.05501.x;
RA   Sahin-Toth M., Kukor Z., Nemoda Z.;
RT   "Human cationic trypsinogen is sulfated on Tyr154.";
RL   FEBS J. 273:5044-5050(2006).
RN   [15]
RP   SULFATION AT TYR-154.
RX   PubMed=25010489; DOI=10.1371/journal.pone.0102063;
RA   Szabo A., Salameh M.A., Ludwig M., Radisky E.S., Sahin-Toth M.;
RT   "Tyrosine sulfation of human trypsin steers S2' subsite selectivity towards
RT   basic amino acids.";
RL   PLoS ONE 9:E102063-E102063(2014).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND MASS SPECTROMETRY.
RX   PubMed=8683601; DOI=10.1006/jmbi.1996.0376;
RA   Gaboriaud C., Serre L., Guy-Crotte O., Forest E., Fontecilla-Camps J.-C.;
RT   "Crystal structure of human trypsin 1: unexpected phosphorylation of
RT   Tyr151.";
RL   J. Mol. Biol. 259:995-1010(1996).
RN   [17]
RP   VARIANTS PCTT ILE-29 AND HIS-122.
RX   PubMed=9322498; DOI=10.1053/gast.1997.v113.pm9322498;
RA   Gorry M.C., Gabbaizedeh D., Furey W., Gates L.K. Jr., Preston R.A.,
RA   Aston C.E., Zhang Y., Ulrich C., Ehrlich G.D., Whitcomb D.C.;
RT   "Mutations in the cationic trypsinogen gene are associated with recurrent
RT   acute and chronic pancreatitis.";
RL   Gastroenterology 113:1063-1068(1997).
RN   [18]
RP   VARIANT PCTT ILE-29.
RX   PubMed=9633818;
RX   DOI=10.1002/(sici)1098-1004(1998)12:1<39::aid-humu6>3.0.co;2-p;
RA   Teich N., Mossner J., Keim V.;
RT   "Mutations of the cationic trypsinogen in hereditary pancreatitis.";
RL   Hum. Mutat. 12:39-43(1998).
RN   [19]
RP   VARIANTS PCTT VAL-16 AND HIS-122.
RX   PubMed=10381903; DOI=10.1016/s0016-5085(99)70543-3;
RA   Witt H., Luck W., Becker M.;
RT   "A signal peptide cleavage site mutation in the cationic trypsinogen gene
RT   is strongly associated with chronic pancreatitis.";
RL   Gastroenterology 117:7-10(1999).
RN   [20]
RP   VARIANT PCTT ARG-23.
RX   PubMed=10204851;
RA   Ferec C., Raguenes O., Salomon R., Roche C., Bernard J.P., Guillot M.,
RA   Quere I., Faure C., Mercier B., Audrezet M.-P., Guillausseau P.J.,
RA   Dupont C., Munnich A., Bignon J.D., Le Bodic L.;
RT   "Mutations in the cationic trypsinogen gene and evidence for genetic
RT   heterogeneity in hereditary pancreatitis.";
RL   J. Med. Genet. 36:228-232(1999).
RN   [21]
RP   VARIANT PCTT HIS-122.
RX   PubMed=11073545; DOI=10.1136/jmg.37.11.e36;
RA   Chen J.-M., Raguenes O., Ferec C., Deprez P.H., Verellen-Dumoulin C.;
RT   "A CGC>CAT gene conversion-like event resulting in the R122H mutation in
RT   the cationic trypsinogen gene and its implication in the genotyping of
RT   pancreatitis.";
RL   J. Med. Genet. 37:E36-E36(2000).
RN   [22]
RP   VARIANTS PCTT THR-29 AND CYS-122.
RX   PubMed=11788572; DOI=10.1136/gut.50.2.271;
RA   Pfutzer R., Myers E., Applebaum-Shapiro S., Finch R., Ellis I.,
RA   Neoptolemos J., Kant J.A., Whitcomb D.C.;
RT   "Novel cationic trypsinogen (PRSS1) N29T and R122C mutations cause
RT   autosomal dominant hereditary pancreatitis.";
RL   Gut 50:271-272(2002).
RN   [23]
RP   VARIANT PCTT LYS-79, AND CHARACTERIZATION OF VARIANT PCTT LYS-79.
RX   PubMed=14695529; DOI=10.1002/humu.10285;
RA   Teich N., Le Marechal C., Kukor Z., Caca K., Witzigmann H., Chen J.-M.,
RA   Toth M., Moessner J., Keim V., Ferec C., Sahin-Toth M.;
RT   "Interaction between trypsinogen isoforms in genetically determined
RT   pancreatitis: mutation E79K in cationic trypsin (PRSS1) causes increased
RT   transactivation of anionic trypsinogen (PRSS2).";
RL   Hum. Mutat. 23:22-31(2004).
RN   [24]
RP   VARIANTS PCTT ILE-29 AND SER-54, AND CHARACTERIZATION OF VARIANTS PCTT
RP   ILE-29 AND SER-54.
RX   PubMed=15776435; DOI=10.1002/humu.20148;
RA   Teich N., Nemoda Z., Koehler H., Heinritz W., Moessner J., Keim V.,
RA   Sahin-Toth M.;
RT   "Gene conversion between functional trypsinogen genes PRSS1 and PRSS2
RT   associated with chronic pancreatitis in a six-year-old girl.";
RL   Hum. Mutat. 25:343-347(2005).
RN   [25]
RP   VARIANT [LARGE SCALE ANALYSIS] MET-137.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Has activity against the synthetic substrates Boc-Phe-Ser-
CC       Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-
CC       Mec. The single-chain form is more active than the two-chain form
CC       against all of these substrates. {ECO:0000269|PubMed:7945238}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC       Note=Binds 1 Ca(2+) ion per subunit.;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- PTM: Occurs in a single-chain form and a two-chain form, produced by
CC       proteolytic cleavage after Arg-122.
CC   -!- PTM: Sulfation at Tyr-154 increases selectivity towards basic versus
CC       apolar residues at the P2' position of inhibitors that bind in a
CC       substrate-like fashion. Although the increase in selectivity is
CC       relatively small, it may facilitate digestion of a broader range of
CC       dietary proteins. {ECO:0000269|PubMed:25010489}.
CC   -!- MASS SPECTROMETRY: [Trypsin-1]: Mass=24348; Mass_error=2;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:8683601};
CC   -!- DISEASE: Pancreatitis, hereditary (PCTT) [MIM:167800]: A disease
CC       characterized by pancreas inflammation, permanent destruction of the
CC       pancreatic parenchyma, maldigestion, and severe abdominal pain attacks.
CC       {ECO:0000269|PubMed:10204851, ECO:0000269|PubMed:10381903,
CC       ECO:0000269|PubMed:10930381, ECO:0000269|PubMed:11073545,
CC       ECO:0000269|PubMed:11788572, ECO:0000269|PubMed:11866271,
CC       ECO:0000269|PubMed:14695529, ECO:0000269|PubMed:15776435,
CC       ECO:0000269|PubMed:8841182, ECO:0000269|PubMed:9322498,
CC       ECO:0000269|PubMed:9633818}. Note=Disease susceptibility is associated
CC       with variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   -!- CAUTION: Tyr-154 was proposed to be phosphorylated (PubMed:8683601) but
CC       it has been shown (PubMed:17087724) to be sulfated instead. Phosphate
CC       and sulfate groups are similar in mass and size, and this can lead to
CC       erroneous interpretation of the results. {ECO:0000305|PubMed:17087724,
CC       ECO:0000305|PubMed:8683601}.
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DR   EMBL; M22612; AAA61231.1; -; mRNA.
DR   EMBL; L36092; AAC80207.1; -; Genomic_DNA.
DR   EMBL; AK312199; BAG35132.1; -; mRNA.
DR   EMBL; AC231380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH236959; EAL23773.1; -; Genomic_DNA.
DR   EMBL; CH471198; EAW51925.1; -; Genomic_DNA.
DR   EMBL; BC128226; AAI28227.1; -; mRNA.
DR   EMBL; AF314534; AAG30943.1; -; Genomic_DNA.
DR   EMBL; U70137; AAC50728.1; -; Genomic_DNA.
DR   EMBL; AF315309; AAG30947.1; -; Genomic_DNA.
DR   EMBL; AF315310; AAG30948.1; -; Genomic_DNA.
DR   EMBL; AF315311; AAG30949.1; -; Genomic_DNA.
DR   CCDS; CCDS5872.1; -.
DR   PIR; A25852; A25852.
DR   PIR; S50020; S50020.
DR   PIR; S50021; S50021.
DR   RefSeq; NP_002760.1; NM_002769.4.
DR   PDB; 1FXY; X-ray; 2.15 A; A=127-247.
DR   PDB; 1TRN; X-ray; 2.20 A; A/B=24-247.
DR   PDB; 2RA3; X-ray; 1.46 A; A/B=24-247.
DR   PDB; 4WWY; X-ray; 1.70 A; A/B=24-247.
DR   PDB; 4WXV; X-ray; 2.10 A; A/B=24-247.
DR   PDBsum; 1FXY; -.
DR   PDBsum; 1TRN; -.
DR   PDBsum; 2RA3; -.
DR   PDBsum; 4WWY; -.
DR   PDBsum; 4WXV; -.
DR   SMR; P07477; -.
DR   BioGRID; 111626; 38.
DR   IntAct; P07477; 16.
DR   MINT; P07477; -.
DR   STRING; 9606.ENSP00000308720; -.
DR   BindingDB; P07477; -.
DR   ChEMBL; CHEMBL209; -.
DR   DrugBank; DB02665; (1R,2S)-2-Phenylcyclopropanaminium.
DR   DrugBank; DB03417; (2S,3R)-2-[[4-(Tert-butylcarbamoyl)piperazine-1-carbonyl]amino]-6-(diaminomethylideneamino)-3-formylhexanoic acid.
DR   DrugBank; DB06850; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexylamino)ethanoyl)pyrrolidine-2-carboxamide.
DR   DrugBank; DB07091; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexyloxy)ethanoyl)pyrrolidine-2-carboxamide.
DR   DrugBank; DB06845; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentylamino)ethanoyl)pyrrolidine-2-carboxamide.
DR   DrugBank; DB07088; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentyloxy)ethanoyl)pyrrolidine-2-carboxamide.
DR   DrugBank; DB07131; (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclohexylpropanoyl)pyrrolidine-2-carboxamide.
DR   DrugBank; DB07095; (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclopentylpropanoyl)pyrrolidine-2-carboxamide.
DR   DrugBank; DB04793; 1,4:3,6-Dianhydro-2-O-(3-carbamimidoylphenyl)-5-O-(4-carbamimidoylphenyl)-D-glucitol.
DR   DrugBank; DB03337; 1-(2-Amidinophenyl)-3-(Phenoxyphenyl)Urea.
DR   DrugBank; DB04336; 1-(4-Amidinophenyl)-3-(4-Chlorophenyl)Urea.
DR   DrugBank; DB08420; 1-{[1-(2-AMINO-3-PHENYL-PROPIONYL)-PYRROLIDINE-2-CARBONYL]-AMINO}-2-(3-CYANO-PHENYL)-ETHANEBORONIC ACID.
DR   DrugBank; DB04790; 2,5-bis-O-{3-[amino(imino)methyl]phenyl}-1,4:3,6-dianhydro-D-glucitol.
DR   DrugBank; DB04792; 2,5-O,O-BIS-{4',4''-AMIDINOPHENYL}-1,4:3,6-DIANHYDRO-D-SORBITOL.
DR   DrugBank; DB01905; 2-(2-Hydroxy-5-Methoxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine.
DR   DrugBank; DB02463; 2-(2-Hydroxy-Phenyl)-1h-Indole-5-Carboxamidine.
DR   DrugBank; DB02287; 2-(2-hydroxy-phenyl)-3H-benzoimidazole-5-carboxamidine.
DR   DrugBank; DB08184; 2-(2-METHYLPHENYL)-1H-INDOLE-5-CARBOXIMIDAMIDE.
DR   DrugBank; DB06918; 2-(2-METHYLPHENYL)-1H-INDOLE-6-CARBOXIMIDAMIDE.
DR   DrugBank; DB06923; 2-(3-METHYLPHENYL)-1H-INDOLE-5-CARBOXIMIDAMIDE.
DR   DrugBank; DB08254; 2-Naphthalenesulfonic acid.
DR   DrugBank; DB04791; 2-O-(4'-AMIDINOPHENYL)-5-O-(3''-AMIDINOPHENYL)-1,4:3,6-DIANHYDRO-D-SORBITOL.
DR   DrugBank; DB01725; 2-{2-hydroxy-[1,1'-biphenyl]-3-yl}-1H-1,3-benzodiazole-5-carboximidamide.
DR   DrugBank; DB01665; 2H-Benzimidazol-2-amine.
DR   DrugBank; DB03374; 3,5-Diiodotyrosine.
DR   DrugBank; DB04410; 3-Phenylpropylamine.
DR   DrugBank; DB07229; 3-{5-[AMINO(IMINIO)METHYL]-1H-INDOL-2-YL}-5-METHOXY-1,1'-BIPHENYL-2-OLATE.
DR   DrugBank; DB07368; 4-(METHYLSULFONYL)BENZENECARBOXIMIDAMIDE.
DR   DrugBank; DB03243; 4-Fluorobenzylamine.
DR   DrugBank; DB03136; 4-Iodobenzo[B]Thiophene-2-Carboxamidine.
DR   DrugBank; DB04311; 4-Phenylbutylamine.
DR   DrugBank; DB04654; 4-PIPERIDIN-4-YLBUTANAL.
DR   DrugBank; DB02354; 4-{[1-Methyl-5-(2-Methyl-Benzoimidazol-1-Ylmethyl)-1h-Benzoimidazol-2-Ylmethyl]-Amino}-Benzamidine.
DR   DrugBank; DB01939; 5-Amidino-Benzimidazole.
DR   DrugBank; DB07491; 5-amino-2,4,6-tribromobenzene-1,3-dicarboxylic acid.
DR   DrugBank; DB03865; 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine.
DR   DrugBank; DB06855; 6-fluoro-2-(2-hydroxy-3-isobutoxy-phenyl)-1H-benzoimidazole-5-carboxamidine.
DR   DrugBank; DB04107; [(1-{2[(4-Carbamimidoyl-Phenylamino)-Methyl]-1-Methyl-1h-Benzoimidazol-5-Yl}-Cyclopropyl)-Pyridin-2-Yl-Methyleneaminooxy]-Acetic Acid Ethyl Ester.
DR   DrugBank; DB01836; [4-(6-Chloro-Naphthalene-2-Sulfonyl)-Piperazin-1-Yl]-(3,4,5,6-Tetrahydro-2h-[1,4']Bipyridinyl-4-Yl)-Methanone.
DR   DrugBank; DB02269; [4-({[5-Benzyloxy-1-(3-Carbamimidoyl-Benzyl)-1h-Indole-2-Carbonyl]-Amino}-Methyl)-Phenyl]-Trimethyl-Ammonium.
DR   DrugBank; DB08763; [N-(BENZYLOXYCARBONYL)AMINO](4-AMIDINOPHENYL)METHANE-PHOSPHONATE.
DR   DrugBank; DB03081; [N-[N-(4-Methoxy-2,3,6-trimethylphenylsulfonyl)-L-aspartyl]-D-(4-amidino-phenylalanyl)]-piperidine.
DR   DrugBank; DB04391; Aeruginosin 98-B.
DR   DrugBank; DB02435; Aminomethylcyclohexane.
DR   DrugBank; DB02045; Amylamine.
DR   DrugBank; DB06692; Aprotinin.
DR   DrugBank; DB03127; Benzamidine.
DR   DrugBank; DB04446; Benzo[B]Thiophene-2-Carboxamidine.
DR   DrugBank; DB02464; Benzylamine.
DR   DrugBank; DB03213; Bis(5-Amidino-2-Benzimidazolyl)Methane Ketone.
DR   DrugBank; DB04301; Bis(5-Amidino-2-Benzimidazolyl)Methane Ketone Hydrate.
DR   DrugBank; DB01876; Bis(5-Amidino-2-Benzimidazolyl)Methanone.
DR   DrugBank; DB01705; Bis(5-Amidino-Benzimidazolyl)Methane.
DR   DrugBank; DB03443; bis(5-amidino-benzimidazolyl)methanone zinc.
DR   DrugBank; DB02081; Bis-Benzamidine.
DR   DrugBank; DB13729; Camostat.
DR   DrugBank; DB02288; CRA-9334.
DR   DrugBank; DB03173; CRA_10433.
DR   DrugBank; DB02526; CRA_10655.
DR   DrugBank; DB04470; CRA_10656.
DR   DrugBank; DB02366; CRA_10762.
DR   DrugBank; DB02989; CRA_10972.
DR   DrugBank; DB01771; CRA_10991.
DR   DrugBank; DB03555; CRA_11092.
DR   DrugBank; DB03643; CRA_1144.
DR   DrugBank; DB02063; CRA_16847.
DR   DrugBank; DB02084; CRA_17312.
DR   DrugBank; DB01741; CRA_17693.
DR   DrugBank; DB03016; CRA_1801.
DR   DrugBank; DB02875; CRA_1802.
DR   DrugBank; DB04246; CRA_23653.
DR   DrugBank; DB03159; CRA_8696.
DR   DrugBank; DB04215; CRA_9076.
DR   DrugBank; DB04563; CRA_9678.
DR   DrugBank; DB03595; CRA_9785.
DR   DrugBank; DB04269; Cyclotheonamide A.
DR   DrugBank; DB06840; diethyl [(1R)-1,5-diaminopentyl]boronate.
DR   DrugBank; DB03608; Diminazene.
DR   DrugBank; DB12831; Gabexate.
DR   DrugBank; DB01767; Hemi-Babim.
DR   DrugBank; DB04442; Imino[2-(2-oxo-1,2-dihydro-3-pyridinyl)-1H-benzimidazol-5-yl]methanaminium.
DR   DrugBank; DB07985; METHYL 4-(AMINOIMINOMETHYL)-BETA-[3- INH (AMINOIMINO)PHENYL]BENZENE PENTANOATE.
DR   DrugBank; DB01805; Monoisopropylphosphorylserine.
DR   DrugBank; DB04125; N-Alpha-(2-Naphthylsulfonyl)-N(3-Amidino-L-Phenylalaninyl)-4-Acetyl-Piperazine.
DR   DrugBank; DB01745; N-Alpha-(2-Naphthylsulfonyl)-N(3-Amidino-L-Phenylalaninyl)Isopipecolinic Acid Methyl Ester.
DR   DrugBank; DB04238; N-Alpha-(2-Naphthylsulfonyl)-N-(3-Amidino-L-Phenylalaninyl)-D-Pipecolinic Acid.
DR   DrugBank; DB06853; N-cycloheptylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide.
DR   DrugBank; DB06858; N-cyclooctylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide.
DR   DrugBank; DB12598; Nafamostat.
DR   DrugBank; DB01737; Nalpha-(2-Naphthylsulfonylglycyl)-3-Amidino-D,L-Phenylalanine-Isopropylester.
DR   DrugBank; DB04325; Phenethylamine.
DR   DrugBank; DB03976; Phosphorylisopropane.
DR   DrugBank; DB04424; RPR128515.
DR   DrugBank; DB02744; RPR131247.
DR   DrugBank; DB03251; RWJ-51084.
DR   DrugBank; DB02812; RWJ-56423.
DR   DrugBank; DB03876; Thieno[2,3-B]Pyridine-2-Carboxamidine.
DR   DrugBank; DB04008; Zinc;[amino-[2-[[5-[amino(azaniumylidene)methyl]benzimidazol-1-id-2-yl]methyl]benzimidazol-1-id-5-yl]methylidene]azanium.
DR   DrugBank; DB04432; ZK-805623.
DR   DrugBank; DB02112; Zk-806450.
DR   DrugBank; DB03373; ZK-806711.
DR   DrugCentral; P07477; -.
DR   GuidetoPHARMACOLOGY; 2397; -.
DR   MEROPS; S01.127; -.
DR   iPTMnet; P07477; -.
DR   PhosphoSitePlus; P07477; -.
DR   BioMuta; PRSS1; -.
DR   DMDM; 136408; -.
DR   EPD; P07477; -.
DR   jPOST; P07477; -.
DR   MassIVE; P07477; -.
DR   PaxDb; P07477; -.
DR   PeptideAtlas; P07477; -.
DR   PRIDE; P07477; -.
DR   ProteomicsDB; 52006; -.
DR   Antibodypedia; 18375; 534 antibodies.
DR   DNASU; 5644; -.
DR   Ensembl; ENST00000311737; ENSP00000308720; ENSG00000204983.
DR   Ensembl; ENST00000616256; ENSP00000479217; ENSG00000274247.
DR   GeneID; 5644; -.
DR   KEGG; hsa:5644; -.
DR   UCSC; uc003wak.3; human.
DR   CTD; 5644; -.
DR   DisGeNET; 5644; -.
DR   GeneCards; PRSS1; -.
DR   GeneReviews; PRSS1; -.
DR   HGNC; HGNC:9475; PRSS1.
DR   HPA; ENSG00000204983; Tissue enriched (pancreas).
DR   MalaCards; PRSS1; -.
DR   MIM; 167800; phenotype.
DR   MIM; 276000; gene.
DR   neXtProt; NX_P07477; -.
DR   OpenTargets; ENSG00000204983; -.
DR   Orphanet; 676; Hereditary chronic pancreatitis.
DR   Orphanet; 64740; NON RARE IN EUROPE: Recurrent acute pancreatitis.
DR   PharmGKB; PA33828; -.
DR   VEuPathDB; HostDB:ENSG00000204983.12; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00990000203555; -.
DR   InParanoid; P07477; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; P07477; -.
DR   TreeFam; TF331065; -.
DR   PathwayCommons; P07477; -.
DR   Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
DR   Reactome; R-HSA-196741; Cobalamin (Cbl, vitamin B12) transport and metabolism.
DR   SIGNOR; P07477; -.
DR   BioGRID-ORCS; 5644; 4 hits in 970 CRISPR screens.
DR   ChiTaRS; PRSS1; human.
DR   EvolutionaryTrace; P07477; -.
DR   GeneWiki; Trypsin_1; -.
DR   GenomeRNAi; 5644; -.
DR   Pharos; P07477; Tclin.
DR   PRO; PR:P07477; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P07477; protein.
DR   Bgee; ENSG00000204983; Expressed in body of pancreas and 116 other tissues.
DR   ExpressionAtlas; P07477; baseline and differential.
DR   Genevisible; P07477; HS.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0009235; P:cobalamin metabolic process; TAS:Reactome.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
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   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   1: Evidence at protein level;
KW   3D-structure; Calcium; Digestion; Direct protein sequencing;
KW   Disease variant; Disulfide bond; Hydrolase; Metal-binding; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Sulfation; Zymogen.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000269|PubMed:2598466,
FT                   ECO:0000269|PubMed:7945238"
FT   PROPEP          16..23
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028197"
FT   CHAIN           24..247
FT                   /note="Trypsin-1"
FT                   /id="PRO_0000028198"
FT   CHAIN           24..122
FT                   /note="Alpha-trypsin chain 1"
FT                   /id="PRO_0000313570"
FT   CHAIN           123..247
FT                   /note="Alpha-trypsin chain 2"
FT                   /id="PRO_0000313571"
FT   DOMAIN          24..244
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        63
FT                   /note="Charge relay system"
FT   ACT_SITE        107
FT                   /note="Charge relay system"
FT   ACT_SITE        200
FT                   /note="Charge relay system"
FT   METAL           75
FT                   /note="Calcium"
FT   METAL           77
FT                   /note="Calcium; via carbonyl oxygen"
FT   METAL           80
FT                   /note="Calcium; via carbonyl oxygen"
FT   METAL           85
FT                   /note="Calcium"
FT   SITE            194
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         154
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000305|PubMed:17087724,
FT                   ECO:0000305|PubMed:25010489"
FT   DISULFID        30..160
FT   DISULFID        48..64
FT   DISULFID        139..206
FT   DISULFID        171..185
FT   DISULFID        196..220
FT   VARIANT         16
FT                   /note="A -> V (in PCTT; disrupts signal sequence cleavage
FT                   site; dbSNP:rs202003805)"
FT                   /evidence="ECO:0000269|PubMed:10381903"
FT                   /id="VAR_011693"
FT   VARIANT         22
FT                   /note="D -> G (in PCTT; increased rate of activation;
FT                   dbSNP:rs397507442)"
FT                   /evidence="ECO:0000269|PubMed:10930381"
FT                   /id="VAR_011652"
FT   VARIANT         23
FT                   /note="K -> R (in PCTT; increased rate of activation;
FT                   dbSNP:rs111033567)"
FT                   /evidence="ECO:0000269|PubMed:10204851"
FT                   /id="VAR_011653"
FT   VARIANT         29
FT                   /note="N -> I (in PCTT; dbSNP:rs111033566)"
FT                   /evidence="ECO:0000269|PubMed:11866271,
FT                   ECO:0000269|PubMed:15776435, ECO:0000269|PubMed:9322498,
FT                   ECO:0000269|PubMed:9633818"
FT                   /id="VAR_006720"
FT   VARIANT         29
FT                   /note="N -> T (in PCTT; dbSNP:rs111033566)"
FT                   /evidence="ECO:0000269|PubMed:11788572"
FT                   /id="VAR_012712"
FT   VARIANT         54
FT                   /note="N -> S (in PCTT; associated with Ile-29; the double
FT                   mutant shows increased autocatalytic activation which is
FT                   solely due to the Ile-29 mutation; dbSNP:rs144422014)"
FT                   /evidence="ECO:0000269|PubMed:15776435"
FT                   /id="VAR_037908"
FT   VARIANT         79
FT                   /note="E -> K (in PCTT; Lys-79 trypsin activates anionic
FT                   trypsinogen PRSS2 2-fold while the common pancreatitis-
FT                   associated mutants His-122 or Ile-29 have no such effect;
FT                   dbSNP:rs111033564)"
FT                   /evidence="ECO:0000269|PubMed:14695529"
FT                   /id="VAR_037909"
FT   VARIANT         104
FT                   /note="L -> P (in PCTT; dbSNP:rs1554499091)"
FT                   /evidence="ECO:0000269|PubMed:11866271"
FT                   /id="VAR_011654"
FT   VARIANT         116
FT                   /note="R -> C (in PCTT; dbSNP:rs387906698)"
FT                   /evidence="ECO:0000269|PubMed:11866271"
FT                   /id="VAR_011655"
FT   VARIANT         122
FT                   /note="R -> C (in PCTT; suppresses an autocleavage site;
FT                   dbSNP:rs111033568)"
FT                   /evidence="ECO:0000269|PubMed:11788572"
FT                   /id="VAR_012713"
FT   VARIANT         122
FT                   /note="R -> H (in PCTT; suppresses an autocleavage site
FT                   which is probably part of a fail-safe mechanism by which
FT                   trypsin, which is activated within the pancreas, may be
FT                   inactivated; loss of this cleavage site would permit
FT                   autodigestion resulting in pancreatitis;
FT                   dbSNP:rs267606982)"
FT                   /evidence="ECO:0000269|PubMed:10381903,
FT                   ECO:0000269|PubMed:11073545, ECO:0000269|PubMed:11866271,
FT                   ECO:0000269|PubMed:8841182, ECO:0000269|PubMed:9322498"
FT                   /id="VAR_006721"
FT   VARIANT         137
FT                   /note="T -> M (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs117497341)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036299"
FT   VARIANT         139
FT                   /note="C -> F (in PCTT)"
FT                   /evidence="ECO:0000269|PubMed:11866271"
FT                   /id="VAR_011656"
FT   MUTAGEN         154
FT                   /note="Y->F: Lack of sulfation."
FT                   /evidence="ECO:0000269|PubMed:17087724"
FT   CONFLICT        4
FT                   /note="L -> F (in Ref. 7; AAI28227)"
FT                   /evidence="ECO:0000305"
FT   STRAND          38..54
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   STRAND          57..60
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   STRAND          70..74
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:1FXY"
FT   STRAND          86..95
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   TURN            101..103
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   STRAND          109..115
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   STRAND          120..122
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   STRAND          138..144
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   STRAND          159..165
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   HELIX           168..174
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   TURN            176..178
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   STRAND          183..187
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   STRAND          192..194
FT                   /evidence="ECO:0007829|PDB:1TRN"
FT   STRAND          203..206
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   STRAND          209..216
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   STRAND          218..222
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   STRAND          227..231
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   HELIX           232..235
FT                   /evidence="ECO:0007829|PDB:2RA3"
FT   HELIX           236..245
FT                   /evidence="ECO:0007829|PDB:2RA3"
SQ   SEQUENCE   247 AA;  26558 MW;  DD49A487B8062813 CRC64;
     MNPLLILTFV AAALAAPFDD DDKIVGGYNC EENSVPYQVS LNSGYHFCGG SLINEQWVVS
     AGHCYKSRIQ VRLGEHNIEV LEGNEQFINA AKIIRHPQYD RKTLNNDIML IKLSSRAVIN
     ARVSTISLPT APPATGTKCL ISGWGNTASS GADYPDELQC LDAPVLSQAK CEASYPGKIT
     SNMFCVGFLE GGKDSCQGDS GGPVVCNGQL QGVVSWGDGC AQKNKPGVYT KVYNYVKWIK
     NTIAANS
//
DBGET integrated database retrieval system