Reviewed, UniProtKB/Swiss-Prot P07477 (TRY1_HUMAN)

Names and origin

Protein names

Recommended name:
    Trypsin-1
    EC=3.4.21.4
Alternative name(s):
    Trypsin I
    Cationic trypsinogen
    Serine protease 1
    Beta-trypsin
Cleaved into the following 2 chains:
    1- Recommended name:
            Alpha-trypsin chain 1
    2- Recommended name:
            Alpha-trypsin chain 2

Gene names

Name:	PRSS1
Synonyms:	TRP1, TRY1, TRYP1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	247 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has activity against the synthetic substrates Boc-Phe-Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-Mec. The single-chain form is more active than the two-chain form against all of these substrates. Ref.9
Catalytic activity	Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Cofactor	Binds 1 calcium ion per subunit.
Subcellular location	Secreted › extracellular space.
Post-translational modification	Occurs in a single-chain form and a two-chain form, produced by proteolytic cleavage after Arg-122.
Involvement in disease	Defects in PRSS1 are a cause of hereditary pancreatitis (HPC) [MIM:167800]; also known as chronic pancreatitis (CP). HPC is an autosomal dominant disease characterized by the presence of calculi in pancreatic ducts. It causes severe abdominal pain attacks. Ref.8 Ref.11 Ref.12 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.
Caution	Tyr-154 was proposed to be phosphorylated (Ref.15) but it has been shown (Ref.14) to be sulfated instead. Phosphate and sulfate groups are similar in mass and size, and this can lead to erroneous interpretation of the results.
Mass spectrometry	Molecular mass is 24348±2 Da from positions 24 - 247. Determined by ESI. Ref.15

Ontologies

Keywords
Biological process	Digestion
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Sulfation Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	digestion Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct serine-type endopeptidase activity Ref.11 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB2	P62993	1	EBI-1222902,EBI-401755

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 15

15

Ref.9 Ref.10

Propeptide

16 – 23

8

Activation peptide

PRO_0000028197

Chain

24 – 247

224

Trypsin-1

PRO_0000028198

Chain

24 – 122

99

Alpha-trypsin chain 1

PRO_0000313570

Chain

123 – 247

125

Alpha-trypsin chain 2

PRO_0000313571

Regions

Domain

24 – 244

221

Peptidase S1

Sites

Active site

63

1

Charge relay system

Active site

107

1

Charge relay system

Active site

200

1

Charge relay system

Metal binding

75

1

Calcium

Metal binding

77

1

Calcium; via carbonyl oxygen

Metal binding

80

1

Calcium; via carbonyl oxygen

Metal binding

85

1

Calcium

Site

194

1

Required for specificity By similarity

Amino acid modifications

Modified residue

154

1

Sulfotyrosine Ref.14

Disulfide bond

30 ↔ 160

Disulfide bond

48 ↔ 64

Disulfide bond

139 ↔ 206

Disulfide bond

171 ↔ 185

Disulfide bond

196 ↔ 220

Natural variations

Natural variant

16

1

A → V in HPC; disrupts signal sequence cleavage site. Ref.18

VAR_011693

Natural variant

22

1

D → G in HPC; increased rate of activation. Ref.8

VAR_011652

Natural variant

23

1

K → R in HPC; increased rate of activation. Ref.19

VAR_011653

Natural variant

29

1

N → I in HPC. Ref.12 Ref.16 Ref.17 Ref.23

VAR_006720

Natural variant

29

1

N → T in HPC. Ref.21

VAR_012712

Natural variant

54

1

N → S in HPC; associated with Ile-29; the double mutant shows increased autocatalytic activation which is solely due to the Ile-29 mutation. Ref.23

VAR_037908

Natural variant

79

1

E → K in HPC; Lys-79 trypsin activates anionic trypsinogen PRSS2 2-fold while the common pancreatitis-associated mutants His-122 or Ile-29 have no such effect. dbSNP rs28934902. Ref.22

VAR_037909

Natural variant

104

1

L → P in HPC. Ref.12

VAR_011654

Natural variant

116

1

R → C in HPC. Ref.12

VAR_011655

Natural variant

122

1

R → C in HPC; suppresses an autocleavage site. Ref.21

VAR_012713

Natural variant

122

1

R → H in HPC; suppresses an autocleavage site which is probably part of a fail-safe mechanism by which trypsin, which is activated within the pancreas, may be inactivated; loss of this cleavage site would permit autodigestion resulting in pancreatitis. Ref.11 Ref.12 Ref.16 Ref.18 Ref.20

VAR_006721

Natural variant

137

1

T → M in a colorectal cancer sample; somatic mutation. Ref.24

VAR_036299

Natural variant

139

1

C → F in HPC. Ref.12

VAR_011656

Experimental info

Mutagenesis

154

1

Y → F: Lack of sulfation. Ref.14

Sequence conflict

4

1

L → F in AAI28227. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

247

Helix Strand Turn

Details...

Beta strand

38 – 54

17

Beta strand

57 – 60

4

Helix

62 – 64

3

Beta strand

70 – 74

5

Beta strand

86 – 95

10

Turn

101 – 103

3

Beta strand

109 – 115

7

Beta strand

120 – 122

3

Beta strand

138 – 144

7

Beta strand

149 – 151

3

Beta strand

159 – 165

7

Helix

168 – 174

7

Turn

176 – 178

3

Beta strand

183 – 187

5

Beta strand

203 – 206

4

Beta strand

209 – 216

8

Beta strand

218 – 222

5

Beta strand

227 – 231

5

Helix

232 – 235

4

Helix

236 – 245

10

Sequences

	Sequence		Length	Mass (Da)
	P07477-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: DD49A487B8062813	FASTA	247	26,558
	10 20 30 40 50 60 MNPLLILTFV AAALAAPFDD DDKIVGGYNC EENSVPYQVS LNSGYHFCGG SLINEQWVVS 70 80 90 100 110 120 AGHCYKSRIQ VRLGEHNIEV LEGNEQFINA AKIIRHPQYD RKTLNNDIML IKLSSRAVIN 130 140 150 160 170 180 ARVSTISLPT APPATGTKCL ISGWGNTASS GADYPDELQC LDAPVLSQAK CEASYPGKIT 190 200 210 220 230 240 SNMFCVGFLE GGKDSCQGDS GGPVVCNGQL QGVVSWGDGC AQKNKPGVYT KVYNYVKWIK NTIAANS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, characterization and nucleotide sequences of two cDNAs encoding human pancreatic trypsinogens." Emi M., Nakamura Y., Ogawa M., Yamamoto T., Nishide T., Mori T., Matsubara K. Gene 41:305-310(1986) [PubMed: 3011602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The complete 685-kilobase DNA sequence of the human beta T cell receptor locus." Rowen L., Koop B.F., Hood L. Science 272:1755-1762(1996) [PubMed: 8650574] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
[4]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed: 12690205] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"Chronic pancreatitis associated with an activation peptide mutation that facilitates trypsin activation." Teich N., Ockenga J., Hoffmeister A., Manns M., Mossner J., Keim V. Gastroenterology 119:461-465(2000) [PubMed: 10930381] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-67, VARIANT HPC GLY-22.
[9]	"Identification of one- and two-chain forms of trypsinogen 1 produced by a human gastric adenocarcinoma cell line." Koshikawa N., Yasumitsu H., Nagashima Y., Umeda M., Miyazaki K. Biochem. J. 303:187-190(1994) [PubMed: 7945238] [Abstract] Cited for: PROTEIN SEQUENCE OF 16-43 AND 123-142, FUNCTION, POST-TRANSLATIONAL PROCESSING. Tissue: Gastric adenocarcinoma.
[10]	"Immunoreactive anionic and cationic trypsin in human serum." Kimland M., Russick C., Marks W.H., Borgstroem A. Clin. Chim. Acta 184:31-46(1989) [PubMed: 2598466] [Abstract] Cited for: PROTEIN SEQUENCE OF 16-43.
[11]	"Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene." Whitcomb D.C., Gorry M.C., Preston R.A., Furey W., Sossenheimer M.J., Ulrich C.D., Martin S.P., Gates L.K. Jr., Amann S.T., Toskes P.P., Liddle R., McGrath K., Uomo G., Post J.C., Ehrlich G.D. Nat. Genet. 14:141-145(1996) [PubMed: 8841182] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-151, VARIANT HPC HIS-122.
[12]	"Mutational screening of patients with nonalcoholic chronic pancreatitis: identification of further trypsinogen variants." Teich N., Bauer N., Mossner J., Keim V. Am. J. Gastroenterol. 97:341-346(2002) [PubMed: 11866271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-151, VARIANTS HPC ILE-29; PRO-104; CYS-116; HIS-122 AND PHE-139.
[13]	Lubec G., Afjehi-Sadat L. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 73-92, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[14]	"Human cationic trypsinogen is sulfated on Tyr154." Sahin-Toth M., Kukor Z., Nemoda Z. FEBS J. 273:5044-5050(2006) [PubMed: 17087724] [Abstract] Cited for: SULFATION AT TYR-154, MUTAGENESIS OF TYR-154.
[15]	"Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151." Gaboriaud C., Serre L., Guy-Crotte O., Forest E., Fontecilla-Camps J.-C. J. Mol. Biol. 259:995-1010(1996) [PubMed: 8683601] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), MASS SPECTROMETRY.
[16]	"Mutations in the cationic trypsinogen gene are associated with recurrent acute and chronic pancreatitis." Gorry M.C., Gabbaizedeh D., Furey W., Gates L.K. Jr., Preston R.A., Aston C.E., Zhang Y., Ulrich C., Ehrlich G.D., Whitcomb D.C. Gastroenterology 113:1063-1068(1997) [PubMed: 9322498] [Abstract] Cited for: VARIANTS HPC ILE-29 AND HIS-122.
[17]	"Mutations of the cationic trypsinogen in hereditary pancreatitis." Teich N., Mossner J., Keim V. Hum. Mutat. 12:39-43(1998) [PubMed: 9633818] [Abstract] Cited for: VARIANT HPC ILE-29.
[18]	"A signal peptide cleavage site mutation in the cationic trypsinogen gene is strongly associated with chronic pancreatitis." Witt H., Luck W., Becker M. Gastroenterology 117:7-10(1999) [PubMed: 10381903] [Abstract] Cited for: VARIANTS HPC VAL-16 AND HIS-122.
[19]	"Mutations in the cationic trypsinogen gene and evidence for genetic heterogeneity in hereditary pancreatitis." Ferec C., Raguenes O., Salomon R., Roche C., Bernard J.P., Guillot M., Quere I., Faure C., Mercier B., Audrezet M.-P., Guillausseau P.J., Dupont C., Munnich A., Bignon J.D., Le Bodic L. J. Med. Genet. 36:228-232(1999) [PubMed: 10204851] [Abstract] Cited for: VARIANT HPC ARG-23.
[20]	"A CGC>CAT gene conversion-like event resulting in the R122H mutation in the cationic trypsinogen gene and its implication in the genotyping of pancreatitis." Chen J.-M., Raguenes O., Ferec C., Deprez P.H., Verellen-Dumoulin C. J. Med. Genet. 37:E36-E36(2000) [PubMed: 11073545] [Abstract] Cited for: VARIANT HPC HIS-122.
[21]	"Novel cationic trypsinogen (PRSS1) N29T and R122C mutations cause autosomal dominant hereditary pancreatitis." Pfutzer R., Myers E., Applebaum-Shapiro S., Finch R., Ellis I., Neoptolemos J., Kant J.A., Whitcomb D.C. Gut 50:271-272(2002) [PubMed: 11788572] [Abstract] Cited for: VARIANTS HPC THR-29 AND CYS-122.
[22]	"Interaction between trypsinogen isoforms in genetically determined pancreatitis: mutation E79K in cationic trypsin (PRSS1) causes increased transactivation of anionic trypsinogen (PRSS2)." Teich N., Le Marechal C., Kukor Z., Caca K., Witzigmann H., Chen J.-M., Toth M., Moessner J., Keim V., Ferec C., Sahin-Toth M. Hum. Mutat. 23:22-31(2004) [PubMed: 14695529] [Abstract] Cited for: VARIANT HPC LYS-79, CHARACTERIZATION OF VARIANT HPC LYS-79.
[23]	"Gene conversion between functional trypsinogen genes PRSS1 and PRSS2 associated with chronic pancreatitis in a six-year-old girl." Teich N., Nemoda Z., Koehler H., Heinritz W., Moessner J., Keim V., Sahin-Toth M. Hum. Mutat. 25:343-347(2005) [PubMed: 15776435] [Abstract] Cited for: VARIANTS HPC ILE-29 AND SER-54, CHARACTERIZATION OF VARIANTS HPC ILE-29 AND SER-54.
[24]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-137.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M22612 mRNA. Translation: AAA61231.1.
U66061 Genomic DNA. Translation: AAC80207.1.
AK312199 mRNA. Translation: BAG35132.1.
AC231380 Genomic DNA. No translation available.
CH236959 Genomic DNA. Translation: EAL23773.1.
CH471198 Genomic DNA. Translation: EAW51925.1.
BC128226 mRNA. Translation: AAI28227.1.
AF314534 Genomic DNA. Translation: AAG30943.1.
U70137 Genomic DNA. Translation: AAC50728.1.
AF315309 Genomic DNA. Translation: AAG30947.1.
AF315310 Genomic DNA. Translation: AAG30948.1.
AF315311 Genomic DNA. Translation: AAG30949.1.

IPI

IPI00011694.

PIR

A25852.
S50020.
S50021.

RefSeq

NP_002760.1.

UniGene

Hs.622865

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FXY	X-ray	2.15	A	127-247	[»]
1TRN	X-ray	2.20	A/B	24-247	[»]
2RA3	X-ray	1.46	A/B	24-247	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P07477. 3 interactions.

STRING

P07477.

Protein family/group databases

MEROPS

S01.127.

Proteomic databases

PeptideAtlas

P07477.

PRIDE

P07477.

Genome annotation databases

Ensembl

ENST00000311737; ENSP00000308720; ENSG00000204983; Homo sapiens. [Genome view]

GeneID

5644.

KEGG

hsa:5644.

UCSC

uc003wak.2. human.

Organism-specific databases

CTD

5644.

GeneCards

GC07P142136.
GC07P142137.

HGNC

HGNC:9475. PRSS1.

MIM

167800. phenotype.
276000. gene+phenotype.

Orphanet

676. Hereditary chronic pancreatitis.

PharmGKB

PA33828.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P07477.

InParanoid

P07477.

OMA

NTIAANS.

OrthoDB

EOG9CZF11.

Enzyme and pathway databases

BRENDA

3.4.21.4. 247.

Gene expression databases

ArrayExpress

P07477.

Bgee

P07477.

Genevestigator

P07477.

GermOnline

ENSG00000173636. Homo sapiens.

Family and domain databases

InterPro

IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR009003. Ser/Cys_Pept_Trypsin-like.
[Graphical view]

Pfam

PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

SM00020. Tryp_SPc. 1 hit.
[Graphical view]

PROSITE

PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

21926.

PMAP-CutDB

P07477.

SOURCE

Search...

Entry information

Entry name

TRY1_HUMAN

Accession

Primary (citable) accession number: P07477
Secondary accession number(s): A1A509 , A6NJ71, B2R5I5, Q5NV57, Q7M4N3, Q7M4N4, Q92955, Q9HAN4, Q9HAN5, Q9HAN6, Q9HAN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	December 15, 2009
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.