TRY1_HUMAN
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 03-AUG-2022, entry version 223.
DE RecName: Full=Serine protease 1 {ECO:0000312|HGNC:HGNC:9475};
DE EC=3.4.21.4;
DE AltName: Full=Anionic trypsin I {ECO:0000250|UniProtKB:P00762};
DE AltName: Full=Anionic trypsin-I {ECO:0000250|UniProtKB:P00762};
DE AltName: Full=Beta-trypsin;
DE AltName: Full=Cationic trypsinogen;
DE AltName: Full=Pretrypsinogen I {ECO:0000250|UniProtKB:P00762};
DE AltName: Full=Trypsin I {ECO:0000312|HGNC:HGNC:9475};
DE AltName: Full=Trypsin-1;
DE Contains:
DE RecName: Full=Alpha-trypsin chain 1;
DE Contains:
DE RecName: Full=Alpha-trypsin chain 2;
DE Flags: Precursor;
GN Name=PRSS1 {ECO:0000312|HGNC:HGNC:9475};
GN Synonyms=TRP1, TRY1 {ECO:0000312|HGNC:HGNC:9475}, 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 INTERACTION WITH SERPINA1.
RX PubMed=11057674; DOI=10.1038/35038119;
RA Huntington J.A., Read R.J., Carrell R.W.;
RT "Structure of a serpin-protease complex shows inhibition by deformation.";
RL Nature 407:923-926(2000).
RN [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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 -!- SUBUNIT: Interacts with SERPINA1. {ECO:0000269|PubMed:11057674}.
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: [Serine protease 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 PDB; 7QE8; X-ray; 2.90 A; A/B=24-247.
DR PDB; 7QE9; 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 PDBsum; 7QE8; -.
DR PDBsum; 7QE9; -.
DR AlphaFoldDB; P07477; -.
DR SMR; P07477; -.
DR BioGRID; 111626; 61.
DR IntAct; P07477; 17.
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; 542 antibodies from 37 providers.
DR DNASU; 5644; -.
DR Ensembl; ENST00000311737.12; ENSP00000308720.7; ENSG00000204983.15.
DR Ensembl; ENST00000616256.4; ENSP00000479217.1; ENSG00000274247.4.
DR GeneID; 5644; -.
DR KEGG; hsa:5644; -.
DR MANE-Select; ENST00000311737.12; ENSP00000308720.7; NM_002769.5; NP_002760.1.
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; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01050000244883; -.
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-9758881; Uptake of dietary cobalamins into enterocytes.
DR SignaLink; P07477; -.
DR SIGNOR; P07477; -.
DR BioGRID-ORCS; 5644; 9 hits in 1048 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 91 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: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="Serine protease 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 BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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
