UniProtKB - P07477 (TRY1_HUMAN)
Protein
Trypsin-1
Gene
PRSS1
Organism
Homo sapiens (Human)
Status
Functioni
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.1 Publication
Caution
Tyr-154 was proposed to be phosphorylated (PubMed:8683601) but it has been shown (PubMed:17087724) to be sulfated instead. Phosphate and sulfate groups are similar in mass and size, and this can lead to erroneous interpretation of the results.2 Publications
Catalytic activityi
- Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa. EC:3.4.21.4
Cofactori
Ca2+Note: Binds 1 Ca2+ ion per subunit.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 63 | Charge relay system | 1 | |
Metal bindingi | 75 | Calcium | 1 | |
Metal bindingi | 77 | Calcium; via carbonyl oxygen | 1 | |
Metal bindingi | 80 | Calcium; via carbonyl oxygen | 1 | |
Metal bindingi | 85 | Calcium | 1 | |
Active sitei | 107 | Charge relay system | 1 | |
Sitei | 194 | Required for specificityBy similarity | 1 | |
Active sitei | 200 | Charge relay system | 1 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- serine-type endopeptidase activity Source: GO_Central
GO - Biological processi
- cobalamin metabolic process Source: Reactome
- digestion Source: UniProtKB-KW
- extracellular matrix disassembly Source: Reactome
- proteolysis Source: GO_Central
Keywordsi
Molecular function | Hydrolase, Protease, Serine protease |
Biological process | Digestion |
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
PathwayCommonsi | P07477 |
Reactomei | R-HSA-1592389, Activation of Matrix Metalloproteinases R-HSA-196741, Cobalamin (Cbl, vitamin B12) transport and metabolism |
Protein family/group databases
MEROPSi | S01.127 |
Names & Taxonomyi
Protein namesi | Recommended name: Trypsin-1 (EC:3.4.21.4)Alternative name(s): Beta-trypsin Cationic trypsinogen Serine protease 1 Trypsin I Cleaved into the following 2 chains: |
Gene namesi | Name:PRSS1 Synonyms:TRP1, TRY1, TRYP1 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:9475, PRSS1 |
MIMi | 276000, gene |
neXtProti | NX_P07477 |
VEuPathDBi | HostDB:ENSG00000204983.12 |
Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- blood microparticle Source: UniProtKB
- extracellular region Source: Reactome
- extracellular space Source: GO_Central
Other locations
- collagen-containing extracellular matrix Source: BHF-UCL
Keywords - Cellular componenti
SecretedPathology & Biotechi
Involvement in diseasei
Pancreatitis, hereditary (PCTT)11 Publications
Disease susceptibility is associated with variants affecting the gene represented in this entry.
Disease descriptionA disease characterized by pancreas inflammation, permanent destruction of the pancreatic parenchyma, maldigestion, and severe abdominal pain attacks.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_011693 | 16 | A → V in PCTT; disrupts signal sequence cleavage site. 1 PublicationCorresponds to variant dbSNP:rs202003805EnsemblClinVar. | 1 | |
Natural variantiVAR_011652 | 22 | D → G in PCTT; increased rate of activation. 1 PublicationCorresponds to variant dbSNP:rs397507442Ensembl. | 1 | |
Natural variantiVAR_011653 | 23 | K → R in PCTT; increased rate of activation. 1 PublicationCorresponds to variant dbSNP:rs111033567EnsemblClinVar. | 1 | |
Natural variantiVAR_006720 | 29 | N → I in PCTT. 4 PublicationsCorresponds to variant dbSNP:rs111033566EnsemblClinVar. | 1 | |
Natural variantiVAR_012712 | 29 | N → T in PCTT. 1 PublicationCorresponds to variant dbSNP:rs111033566EnsemblClinVar. | 1 | |
Natural variantiVAR_037908 | 54 | N → S in PCTT; associated with Ile-29; the double mutant shows increased autocatalytic activation which is solely due to the Ile-29 mutation. 1 PublicationCorresponds to variant dbSNP:rs144422014EnsemblClinVar. | 1 | |
Natural variantiVAR_037909 | 79 | E → K in PCTT; Lys-79 trypsin activates anionic trypsinogen PRSS2 2-fold while the common pancreatitis-associated mutants His-122 or Ile-29 have no such effect. 1 PublicationCorresponds to variant dbSNP:rs111033564EnsemblClinVar. | 1 | |
Natural variantiVAR_011654 | 104 | L → P in PCTT. 1 PublicationCorresponds to variant dbSNP:rs1554499091EnsemblClinVar. | 1 | |
Natural variantiVAR_011655 | 116 | R → C in PCTT. 1 PublicationCorresponds to variant dbSNP:rs387906698EnsemblClinVar. | 1 | |
Natural variantiVAR_012713 | 122 | R → C in PCTT; suppresses an autocleavage site. 1 PublicationCorresponds to variant dbSNP:rs111033568EnsemblClinVar. | 1 | |
Natural variantiVAR_006721 | 122 | R → H in PCTT; 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. 5 PublicationsCorresponds to variant dbSNP:rs267606982EnsemblClinVar. | 1 | |
Natural variantiVAR_011656 | 139 | C → F in PCTT. 1 Publication | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 154 | Y → F: Lack of sulfation. 1 Publication | 1 |
Keywords - Diseasei
Disease variantOrganism-specific databases
DisGeNETi | 5644 |
GeneReviewsi | PRSS1 |
MalaCardsi | PRSS1 |
MIMi | 167800, phenotype |
OpenTargetsi | ENSG00000204983 |
Orphaneti | 676, Hereditary chronic pancreatitis 64740, NON RARE IN EUROPE: Recurrent acute pancreatitis |
PharmGKBi | PA33828 |
Miscellaneous databases
Pharosi | P07477, Tclin |
Chemistry databases
ChEMBLi | CHEMBL209 |
DrugBanki | DB02665, (1R,2S)-2-Phenylcyclopropanaminium DB03417, (2S,3R)-2-[[4-(Tert-butylcarbamoyl)piperazine-1-carbonyl]amino]-6-(diaminomethylideneamino)-3-formylhexanoic acid DB06850, (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexylamino)ethanoyl)pyrrolidine-2-carboxamide DB07091, (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexyloxy)ethanoyl)pyrrolidine-2-carboxamide DB06845, (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentylamino)ethanoyl)pyrrolidine-2-carboxamide DB07088, (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentyloxy)ethanoyl)pyrrolidine-2-carboxamide DB07131, (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclohexylpropanoyl)pyrrolidine-2-carboxamide DB07095, (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclopentylpropanoyl)pyrrolidine-2-carboxamide DB04793, 1,4:3,6-Dianhydro-2-O-(3-carbamimidoylphenyl)-5-O-(4-carbamimidoylphenyl)-D-glucitol DB03337, 1-(2-Amidinophenyl)-3-(Phenoxyphenyl)Urea DB04336, 1-(4-Amidinophenyl)-3-(4-Chlorophenyl)Urea DB08420, 1-{[1-(2-AMINO-3-PHENYL-PROPIONYL)-PYRROLIDINE-2-CARBONYL]-AMINO}-2-(3-CYANO-PHENYL)-ETHANEBORONIC ACID DB04790, 2,5-bis-O-{3-[amino(imino)methyl]phenyl}-1,4:3,6-dianhydro-D-glucitol DB04792, 2,5-O,O-BIS-{4',4''-AMIDINOPHENYL}-1,4:3,6-DIANHYDRO-D-SORBITOL DB01905, 2-(2-Hydroxy-5-Methoxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine DB02463, 2-(2-Hydroxy-Phenyl)-1h-Indole-5-Carboxamidine DB02287, 2-(2-hydroxy-phenyl)-3H-benzoimidazole-5-carboxamidine DB08184, 2-(2-METHYLPHENYL)-1H-INDOLE-5-CARBOXIMIDAMIDE DB06918, 2-(2-METHYLPHENYL)-1H-INDOLE-6-CARBOXIMIDAMIDE DB06923, 2-(3-METHYLPHENYL)-1H-INDOLE-5-CARBOXIMIDAMIDE DB08254, 2-Naphthalenesulfonic acid DB04791, 2-O-(4'-AMIDINOPHENYL)-5-O-(3''-AMIDINOPHENYL)-1,4:3,6-DIANHYDRO-D-SORBITOL DB01725, 2-{2-hydroxy-[1,1'-biphenyl]-3-yl}-1H-1,3-benzodiazole-5-carboximidamide DB01665, 2H-Benzimidazol-2-amine DB03374, 3,5-Diiodotyrosine DB04410, 3-Phenylpropylamine DB07229, 3-{5-[AMINO(IMINIO)METHYL]-1H-INDOL-2-YL}-5-METHOXY-1,1'-BIPHENYL-2-OLATE DB07368, 4-(METHYLSULFONYL)BENZENECARBOXIMIDAMIDE DB03243, 4-Fluorobenzylamine DB03136, 4-Iodobenzo[B]Thiophene-2-Carboxamidine DB04311, 4-Phenylbutylamine DB04654, 4-PIPERIDIN-4-YLBUTANAL DB02354, 4-{[1-Methyl-5-(2-Methyl-Benzoimidazol-1-Ylmethyl)-1h-Benzoimidazol-2-Ylmethyl]-Amino}-Benzamidine DB01939, 5-Amidino-Benzimidazole DB07491, 5-amino-2,4,6-tribromobenzene-1,3-dicarboxylic acid DB03865, 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine DB06855, 6-fluoro-2-(2-hydroxy-3-isobutoxy-phenyl)-1H-benzoimidazole-5-carboxamidine DB04107, [(1-{2[(4-Carbamimidoyl-Phenylamino)-Methyl]-1-Methyl-1h-Benzoimidazol-5-Yl}-Cyclopropyl)-Pyridin-2-Yl-Methyleneaminooxy]-Acetic Acid Ethyl Ester DB01836, [4-(6-Chloro-Naphthalene-2-Sulfonyl)-Piperazin-1-Yl]-(3,4,5,6-Tetrahydro-2h-[1,4']Bipyridinyl-4-Yl)-Methanone DB02269, [4-({[5-Benzyloxy-1-(3-Carbamimidoyl-Benzyl)-1h-Indole-2-Carbonyl]-Amino}-Methyl)-Phenyl]-Trimethyl-Ammonium DB08763, [N-(BENZYLOXYCARBONYL)AMINO](4-AMIDINOPHENYL)METHANE-PHOSPHONATE DB03081, [N-[N-(4-Methoxy-2,3,6-trimethylphenylsulfonyl)-L-aspartyl]-D-(4-amidino-phenylalanyl)]-piperidine DB04391, Aeruginosin 98-B DB02435, Aminomethylcyclohexane DB02045, Amylamine DB06692, Aprotinin DB03127, Benzamidine DB04446, Benzo[B]Thiophene-2-Carboxamidine DB02464, Benzylamine DB03213, Bis(5-Amidino-2-Benzimidazolyl)Methane Ketone DB04301, Bis(5-Amidino-2-Benzimidazolyl)Methane Ketone Hydrate DB01876, Bis(5-Amidino-2-Benzimidazolyl)Methanone DB01705, Bis(5-Amidino-Benzimidazolyl)Methane DB03443, bis(5-amidino-benzimidazolyl)methanone zinc DB02081, Bis-Benzamidine DB13729, Camostat DB02288, CRA-9334 DB03173, CRA_10433 DB02526, CRA_10655 DB04470, CRA_10656 DB02366, CRA_10762 DB02989, CRA_10972 DB01771, CRA_10991 DB03555, CRA_11092 DB03643, CRA_1144 DB02063, CRA_16847 DB02084, CRA_17312 DB01741, CRA_17693 DB03016, CRA_1801 DB02875, CRA_1802 DB04246, CRA_23653 DB03159, CRA_8696 DB04215, CRA_9076 DB04563, CRA_9678 DB03595, CRA_9785 DB04269, Cyclotheonamide A DB06840, diethyl [(1R)-1,5-diaminopentyl]boronate DB03608, Diminazene DB12831, Gabexate DB01767, Hemi-Babim DB04442, Imino[2-(2-oxo-1,2-dihydro-3-pyridinyl)-1H-benzimidazol-5-yl]methanaminium DB07985, METHYL 4-(AMINOIMINOMETHYL)-BETA-[3- INH (AMINOIMINO)PHENYL]BENZENE PENTANOATE DB01805, Monoisopropylphosphorylserine DB04125, N-Alpha-(2-Naphthylsulfonyl)-N(3-Amidino-L-Phenylalaninyl)-4-Acetyl-Piperazine DB01745, N-Alpha-(2-Naphthylsulfonyl)-N(3-Amidino-L-Phenylalaninyl)Isopipecolinic Acid Methyl Ester DB04238, N-Alpha-(2-Naphthylsulfonyl)-N-(3-Amidino-L-Phenylalaninyl)-D-Pipecolinic Acid DB06853, N-cycloheptylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide DB06858, N-cyclooctylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide DB12598, Nafamostat DB01737, Nalpha-(2-Naphthylsulfonylglycyl)-3-Amidino-D,L-Phenylalanine-Isopropylester DB04325, Phenethylamine DB03976, Phosphorylisopropane DB04424, RPR128515 DB02744, RPR131247 DB03251, RWJ-51084 DB02812, RWJ-56423 DB03876, Thieno[2,3-B]Pyridine-2-Carboxamidine DB04008, Zinc;[amino-[2-[[5-[amino(azaniumylidene)methyl]benzimidazol-1-id-2-yl]methyl]benzimidazol-1-id-5-yl]methylidene]azanium DB04432, ZK-805623 DB02112, Zk-806450 DB03373, ZK-806711 |
DrugCentrali | P07477 |
GuidetoPHARMACOLOGYi | 2397 |
Genetic variation databases
BioMutai | PRSS1 |
DMDMi | 136408 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 15 | 2 PublicationsAdd BLAST | 15 | |
PropeptideiPRO_0000028197 | 16 – 23 | Activation peptide | 8 | |
ChainiPRO_0000028198 | 24 – 247 | Trypsin-1Add BLAST | 224 | |
ChainiPRO_0000313570 | 24 – 122 | Alpha-trypsin chain 1Add BLAST | 99 | |
ChainiPRO_0000313571 | 123 – 247 | Alpha-trypsin chain 2Add BLAST | 125 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 30 ↔ 160 | |||
Disulfide bondi | 48 ↔ 64 | |||
Disulfide bondi | 139 ↔ 206 | |||
Modified residuei | 154 | Sulfotyrosine2 Publications | 1 | |
Disulfide bondi | 171 ↔ 185 | |||
Disulfide bondi | 196 ↔ 220 |
Post-translational modificationi
Occurs in a single-chain form and a two-chain form, produced by proteolytic cleavage after Arg-122.
Sulfation at Tyr-154 increases selectivity towards basic versus apolar residues at the P2' position of inhibitors that bind in a substrate-like fashion. Although the increase in selectivity is relatively small, it may facilitate digestion of a broader range of dietary proteins.1 Publication
Keywords - PTMi
Disulfide bond, Sulfation, ZymogenProteomic databases
EPDi | P07477 |
jPOSTi | P07477 |
MassIVEi | P07477 |
PaxDbi | P07477 |
PeptideAtlasi | P07477 |
PRIDEi | P07477 |
ProteomicsDBi | 52006 |
PTM databases
iPTMneti | P07477 |
PhosphoSitePlusi | P07477 |
Expressioni
Gene expression databases
Bgeei | ENSG00000204983, Expressed in body of pancreas and 115 other tissues |
ExpressionAtlasi | P07477, baseline and differential |
Genevisiblei | P07477, HS |
Organism-specific databases
HPAi | ENSG00000204983, Tissue enriched (pancreas) |
Interactioni
Protein-protein interaction databases
BioGRIDi | 111626, 38 interactors |
IntActi | P07477, 15 interactors |
MINTi | P07477 |
STRINGi | 9606.ENSP00000308720 |
Chemistry databases
BindingDBi | P07477 |
Miscellaneous databases
RNActi | P07477, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P07477 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P07477 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 24 – 244 | Peptidase S1PROSITE-ProRule annotationAdd BLAST | 221 |
Sequence similaritiesi
Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | KOG3627, Eukaryota |
GeneTreei | ENSGT00990000203555 |
InParanoidi | P07477 |
OrthoDBi | 1314811at2759 |
PhylomeDBi | P07477 |
TreeFami | TF331065 |
Family and domain databases
CDDi | cd00190, Tryp_SPc, 1 hit |
Gene3Di | 2.40.10.10, 2 hits |
InterProi | View protein in InterPro IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR001314, Peptidase_S1A IPR001254, Trypsin_dom IPR018114, TRYPSIN_HIS IPR033116, TRYPSIN_SER |
Pfami | View protein in Pfam PF00089, Trypsin, 1 hit |
PRINTSi | PR00722, CHYMOTRYPSIN |
SMARTi | View protein in SMART SM00020, Tryp_SPc, 1 hit |
SUPFAMi | SSF50494, SSF50494, 1 hit |
PROSITEi | View protein in PROSITE PS50240, TRYPSIN_DOM, 1 hit PS00134, TRYPSIN_HIS, 1 hit PS00135, TRYPSIN_SER, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All
P07477-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MNPLLILTFV AAALAAPFDD DDKIVGGYNC EENSVPYQVS LNSGYHFCGG
60 70 80 90 100
SLINEQWVVS AGHCYKSRIQ VRLGEHNIEV LEGNEQFINA AKIIRHPQYD
110 120 130 140 150
RKTLNNDIML IKLSSRAVIN ARVSTISLPT APPATGTKCL ISGWGNTASS
160 170 180 190 200
GADYPDELQC LDAPVLSQAK CEASYPGKIT SNMFCVGFLE GGKDSCQGDS
210 220 230 240
GGPVVCNGQL QGVVSWGDGC AQKNKPGVYT KVYNYVKWIK NTIAANS
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA6XGL3 | A6XGL3_HUMAN | Protease serine 1 | PRSS1 | 237 | Annotation score: | ||
E7EQ64 | E7EQ64_HUMAN | Trypsin-1 | PRSS1 | 261 | Annotation score: | ||
H0Y8D1 | H0Y8D1_HUMAN | Trypsin-1 | PRSS1 | 142 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 4 | L → F in AAI28227 (PubMed:15489334).Curated | 1 |
Mass spectrometryi
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_011693 | 16 | A → V in PCTT; disrupts signal sequence cleavage site. 1 PublicationCorresponds to variant dbSNP:rs202003805EnsemblClinVar. | 1 | |
Natural variantiVAR_011652 | 22 | D → G in PCTT; increased rate of activation. 1 PublicationCorresponds to variant dbSNP:rs397507442Ensembl. | 1 | |
Natural variantiVAR_011653 | 23 | K → R in PCTT; increased rate of activation. 1 PublicationCorresponds to variant dbSNP:rs111033567EnsemblClinVar. | 1 | |
Natural variantiVAR_006720 | 29 | N → I in PCTT. 4 PublicationsCorresponds to variant dbSNP:rs111033566EnsemblClinVar. | 1 | |
Natural variantiVAR_012712 | 29 | N → T in PCTT. 1 PublicationCorresponds to variant dbSNP:rs111033566EnsemblClinVar. | 1 | |
Natural variantiVAR_037908 | 54 | N → S in PCTT; associated with Ile-29; the double mutant shows increased autocatalytic activation which is solely due to the Ile-29 mutation. 1 PublicationCorresponds to variant dbSNP:rs144422014EnsemblClinVar. | 1 | |
Natural variantiVAR_037909 | 79 | E → K in PCTT; Lys-79 trypsin activates anionic trypsinogen PRSS2 2-fold while the common pancreatitis-associated mutants His-122 or Ile-29 have no such effect. 1 PublicationCorresponds to variant dbSNP:rs111033564EnsemblClinVar. | 1 | |
Natural variantiVAR_011654 | 104 | L → P in PCTT. 1 PublicationCorresponds to variant dbSNP:rs1554499091EnsemblClinVar. | 1 | |
Natural variantiVAR_011655 | 116 | R → C in PCTT. 1 PublicationCorresponds to variant dbSNP:rs387906698EnsemblClinVar. | 1 | |
Natural variantiVAR_012713 | 122 | R → C in PCTT; suppresses an autocleavage site. 1 PublicationCorresponds to variant dbSNP:rs111033568EnsemblClinVar. | 1 | |
Natural variantiVAR_006721 | 122 | R → H in PCTT; 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. 5 PublicationsCorresponds to variant dbSNP:rs267606982EnsemblClinVar. | 1 | |
Natural variantiVAR_036299 | 137 | T → M in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs117497341EnsemblClinVar. | 1 | |
Natural variantiVAR_011656 | 139 | C → F in PCTT. 1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M22612 mRNA Translation: AAA61231.1 L36092 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 |
CCDSi | CCDS5872.1 |
PIRi | A25852 S50020 S50021 |
RefSeqi | NP_002760.1, NM_002769.4 |
Genome annotation databases
Ensembli | ENST00000311737; ENSP00000308720; ENSG00000204983 ENST00000616256; ENSP00000479217; ENSG00000274247 |
GeneIDi | 5644 |
KEGGi | hsa:5644 |
UCSCi | uc003wak.3, human |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M22612 mRNA Translation: AAA61231.1 L36092 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 |
CCDSi | CCDS5872.1 |
PIRi | A25852 S50020 S50021 |
RefSeqi | NP_002760.1, NM_002769.4 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
4WWY | X-ray | 1.70 | A/B | 24-247 | [»] | |
4WXV | X-ray | 2.10 | A/B | 24-247 | [»] | |
SMRi | P07477 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 111626, 38 interactors |
IntActi | P07477, 15 interactors |
MINTi | P07477 |
STRINGi | 9606.ENSP00000308720 |
Chemistry databases
BindingDBi | P07477 |
ChEMBLi | CHEMBL209 |
DrugBanki | DB02665, (1R,2S)-2-Phenylcyclopropanaminium DB03417, (2S,3R)-2-[[4-(Tert-butylcarbamoyl)piperazine-1-carbonyl]amino]-6-(diaminomethylideneamino)-3-formylhexanoic acid DB06850, (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexylamino)ethanoyl)pyrrolidine-2-carboxamide DB07091, (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexyloxy)ethanoyl)pyrrolidine-2-carboxamide DB06845, (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentylamino)ethanoyl)pyrrolidine-2-carboxamide DB07088, (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentyloxy)ethanoyl)pyrrolidine-2-carboxamide DB07131, (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclohexylpropanoyl)pyrrolidine-2-carboxamide DB07095, (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclopentylpropanoyl)pyrrolidine-2-carboxamide DB04793, 1,4:3,6-Dianhydro-2-O-(3-carbamimidoylphenyl)-5-O-(4-carbamimidoylphenyl)-D-glucitol DB03337, 1-(2-Amidinophenyl)-3-(Phenoxyphenyl)Urea DB04336, 1-(4-Amidinophenyl)-3-(4-Chlorophenyl)Urea DB08420, 1-{[1-(2-AMINO-3-PHENYL-PROPIONYL)-PYRROLIDINE-2-CARBONYL]-AMINO}-2-(3-CYANO-PHENYL)-ETHANEBORONIC ACID DB04790, 2,5-bis-O-{3-[amino(imino)methyl]phenyl}-1,4:3,6-dianhydro-D-glucitol DB04792, 2,5-O,O-BIS-{4',4''-AMIDINOPHENYL}-1,4:3,6-DIANHYDRO-D-SORBITOL DB01905, 2-(2-Hydroxy-5-Methoxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine DB02463, 2-(2-Hydroxy-Phenyl)-1h-Indole-5-Carboxamidine DB02287, 2-(2-hydroxy-phenyl)-3H-benzoimidazole-5-carboxamidine DB08184, 2-(2-METHYLPHENYL)-1H-INDOLE-5-CARBOXIMIDAMIDE DB06918, 2-(2-METHYLPHENYL)-1H-INDOLE-6-CARBOXIMIDAMIDE DB06923, 2-(3-METHYLPHENYL)-1H-INDOLE-5-CARBOXIMIDAMIDE DB08254, 2-Naphthalenesulfonic acid DB04791, 2-O-(4'-AMIDINOPHENYL)-5-O-(3''-AMIDINOPHENYL)-1,4:3,6-DIANHYDRO-D-SORBITOL DB01725, 2-{2-hydroxy-[1,1'-biphenyl]-3-yl}-1H-1,3-benzodiazole-5-carboximidamide DB01665, 2H-Benzimidazol-2-amine DB03374, 3,5-Diiodotyrosine DB04410, 3-Phenylpropylamine DB07229, 3-{5-[AMINO(IMINIO)METHYL]-1H-INDOL-2-YL}-5-METHOXY-1,1'-BIPHENYL-2-OLATE DB07368, 4-(METHYLSULFONYL)BENZENECARBOXIMIDAMIDE DB03243, 4-Fluorobenzylamine DB03136, 4-Iodobenzo[B]Thiophene-2-Carboxamidine DB04311, 4-Phenylbutylamine DB04654, 4-PIPERIDIN-4-YLBUTANAL DB02354, 4-{[1-Methyl-5-(2-Methyl-Benzoimidazol-1-Ylmethyl)-1h-Benzoimidazol-2-Ylmethyl]-Amino}-Benzamidine DB01939, 5-Amidino-Benzimidazole DB07491, 5-amino-2,4,6-tribromobenzene-1,3-dicarboxylic acid DB03865, 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine DB06855, 6-fluoro-2-(2-hydroxy-3-isobutoxy-phenyl)-1H-benzoimidazole-5-carboxamidine DB04107, [(1-{2[(4-Carbamimidoyl-Phenylamino)-Methyl]-1-Methyl-1h-Benzoimidazol-5-Yl}-Cyclopropyl)-Pyridin-2-Yl-Methyleneaminooxy]-Acetic Acid Ethyl Ester DB01836, [4-(6-Chloro-Naphthalene-2-Sulfonyl)-Piperazin-1-Yl]-(3,4,5,6-Tetrahydro-2h-[1,4']Bipyridinyl-4-Yl)-Methanone DB02269, [4-({[5-Benzyloxy-1-(3-Carbamimidoyl-Benzyl)-1h-Indole-2-Carbonyl]-Amino}-Methyl)-Phenyl]-Trimethyl-Ammonium DB08763, [N-(BENZYLOXYCARBONYL)AMINO](4-AMIDINOPHENYL)METHANE-PHOSPHONATE DB03081, [N-[N-(4-Methoxy-2,3,6-trimethylphenylsulfonyl)-L-aspartyl]-D-(4-amidino-phenylalanyl)]-piperidine DB04391, Aeruginosin 98-B DB02435, Aminomethylcyclohexane DB02045, Amylamine DB06692, Aprotinin DB03127, Benzamidine DB04446, Benzo[B]Thiophene-2-Carboxamidine DB02464, Benzylamine DB03213, Bis(5-Amidino-2-Benzimidazolyl)Methane Ketone DB04301, Bis(5-Amidino-2-Benzimidazolyl)Methane Ketone Hydrate DB01876, Bis(5-Amidino-2-Benzimidazolyl)Methanone DB01705, Bis(5-Amidino-Benzimidazolyl)Methane DB03443, bis(5-amidino-benzimidazolyl)methanone zinc DB02081, Bis-Benzamidine DB13729, Camostat DB02288, CRA-9334 DB03173, CRA_10433 DB02526, CRA_10655 DB04470, CRA_10656 DB02366, CRA_10762 DB02989, CRA_10972 DB01771, CRA_10991 DB03555, CRA_11092 DB03643, CRA_1144 DB02063, CRA_16847 DB02084, CRA_17312 DB01741, CRA_17693 DB03016, CRA_1801 DB02875, CRA_1802 DB04246, CRA_23653 DB03159, CRA_8696 DB04215, CRA_9076 DB04563, CRA_9678 DB03595, CRA_9785 DB04269, Cyclotheonamide A DB06840, diethyl [(1R)-1,5-diaminopentyl]boronate DB03608, Diminazene DB12831, Gabexate DB01767, Hemi-Babim DB04442, Imino[2-(2-oxo-1,2-dihydro-3-pyridinyl)-1H-benzimidazol-5-yl]methanaminium DB07985, METHYL 4-(AMINOIMINOMETHYL)-BETA-[3- INH (AMINOIMINO)PHENYL]BENZENE PENTANOATE DB01805, Monoisopropylphosphorylserine DB04125, N-Alpha-(2-Naphthylsulfonyl)-N(3-Amidino-L-Phenylalaninyl)-4-Acetyl-Piperazine DB01745, N-Alpha-(2-Naphthylsulfonyl)-N(3-Amidino-L-Phenylalaninyl)Isopipecolinic Acid Methyl Ester DB04238, N-Alpha-(2-Naphthylsulfonyl)-N-(3-Amidino-L-Phenylalaninyl)-D-Pipecolinic Acid DB06853, N-cycloheptylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide DB06858, N-cyclooctylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide DB12598, Nafamostat DB01737, Nalpha-(2-Naphthylsulfonylglycyl)-3-Amidino-D,L-Phenylalanine-Isopropylester DB04325, Phenethylamine DB03976, Phosphorylisopropane DB04424, RPR128515 DB02744, RPR131247 DB03251, RWJ-51084 DB02812, RWJ-56423 DB03876, Thieno[2,3-B]Pyridine-2-Carboxamidine DB04008, Zinc;[amino-[2-[[5-[amino(azaniumylidene)methyl]benzimidazol-1-id-2-yl]methyl]benzimidazol-1-id-5-yl]methylidene]azanium DB04432, ZK-805623 DB02112, Zk-806450 DB03373, ZK-806711 |
DrugCentrali | P07477 |
GuidetoPHARMACOLOGYi | 2397 |
Protein family/group databases
MEROPSi | S01.127 |
PTM databases
iPTMneti | P07477 |
PhosphoSitePlusi | P07477 |
Genetic variation databases
BioMutai | PRSS1 |
DMDMi | 136408 |
Proteomic databases
EPDi | P07477 |
jPOSTi | P07477 |
MassIVEi | P07477 |
PaxDbi | P07477 |
PeptideAtlasi | P07477 |
PRIDEi | P07477 |
ProteomicsDBi | 52006 |
Protocols and materials databases
Antibodypediai | 18375, 534 antibodies |
Genome annotation databases
Ensembli | ENST00000311737; ENSP00000308720; ENSG00000204983 ENST00000616256; ENSP00000479217; ENSG00000274247 |
GeneIDi | 5644 |
KEGGi | hsa:5644 |
UCSCi | uc003wak.3, human |
Organism-specific databases
CTDi | 5644 |
DisGeNETi | 5644 |
GeneCardsi | PRSS1 |
GeneReviewsi | PRSS1 |
HGNCi | HGNC:9475, PRSS1 |
HPAi | ENSG00000204983, Tissue enriched (pancreas) |
MalaCardsi | PRSS1 |
MIMi | 167800, phenotype 276000, gene |
neXtProti | NX_P07477 |
OpenTargetsi | ENSG00000204983 |
Orphaneti | 676, Hereditary chronic pancreatitis 64740, NON RARE IN EUROPE: Recurrent acute pancreatitis |
PharmGKBi | PA33828 |
VEuPathDBi | HostDB:ENSG00000204983.12 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3627, Eukaryota |
GeneTreei | ENSGT00990000203555 |
InParanoidi | P07477 |
OrthoDBi | 1314811at2759 |
PhylomeDBi | P07477 |
TreeFami | TF331065 |
Enzyme and pathway databases
PathwayCommonsi | P07477 |
Reactomei | R-HSA-1592389, Activation of Matrix Metalloproteinases R-HSA-196741, Cobalamin (Cbl, vitamin B12) transport and metabolism |
Miscellaneous databases
BioGRID-ORCSi | 5644, 4 hits in 970 CRISPR screens |
ChiTaRSi | PRSS1, human |
EvolutionaryTracei | P07477 |
GeneWikii | Trypsin_1 |
GenomeRNAii | 5644 |
Pharosi | P07477, Tclin |
PROi | PR:P07477 |
RNActi | P07477, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000204983, Expressed in body of pancreas and 115 other tissues |
ExpressionAtlasi | P07477, baseline and differential |
Genevisiblei | P07477, HS |
Family and domain databases
CDDi | cd00190, Tryp_SPc, 1 hit |
Gene3Di | 2.40.10.10, 2 hits |
InterProi | View protein in InterPro IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR001314, Peptidase_S1A IPR001254, Trypsin_dom IPR018114, TRYPSIN_HIS IPR033116, TRYPSIN_SER |
Pfami | View protein in Pfam PF00089, Trypsin, 1 hit |
PRINTSi | PR00722, CHYMOTRYPSIN |
SMARTi | View protein in SMART SM00020, Tryp_SPc, 1 hit |
SUPFAMi | SSF50494, SSF50494, 1 hit |
PROSITEi | View protein in PROSITE PS50240, TRYPSIN_DOM, 1 hit PS00134, TRYPSIN_HIS, 1 hit PS00135, TRYPSIN_SER, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TRY1_HUMAN | |
Accessioni | P07477Primary (citable) accession number: P07477 Secondary accession number(s): A1A509 Q9HAN7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1988 |
Last sequence update: | April 1, 1988 | |
Last modified: | April 7, 2021 | |
This is version 218 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - Human chromosome 7
Human chromosome 7: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families