Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P07478 (TRY2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trypsin-2

EC=3.4.21.4
Alternative name(s):
Anionic trypsinogen
Serine protease 2
Trypsin II
Gene names
Name:PRSS2
Synonyms:TRY2, TRYP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length247 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In the ileum, may be involved in defensin processing, including DEFA5. Ref.3

Catalytic activity

Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Secretedextracellular space.

Tissue specificity

Expressed in Paneth cells, at the base of small intestinal crypts. Ref.3

Post-translational modification

Sulfated on tyrosine.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Sulfation
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcollagen catabolic process

Inferred from direct assay PubMed 12731883. Source: UniProtKB

digestion

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

positive regulation of cell adhesion

Traceable author statement PubMed 12731883. Source: UniProtKB

positive regulation of cell growth

Traceable author statement PubMed 12731883. Source: UniProtKB

proteolysis

Inferred from direct assay PubMed 12731883. Source: UniProtKB

   Cellular_componentextracellular matrix

Traceable author statement PubMed 12731883. Source: UniProtKB

extracellular region

Inferred from direct assay PubMed 12731883. Source: UniProtKB

extracellular space

Inferred from mutant phenotype PubMed 16192646. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from direct assay PubMed 12709065. Source: UniProtKB

serine-type endopeptidase activity

Inferred from direct assay PubMed 12709065PubMed 12731883. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Ref.2
Propeptide16 – 238Activation peptide
PRO_0000028199
Chain24 – 247224Trypsin-2
PRO_0000028200

Regions

Domain24 – 244221Peptidase S1

Sites

Active site631Charge relay system By similarity
Active site1071Charge relay system By similarity
Active site2001Charge relay system By similarity
Metal binding751Calcium By similarity
Metal binding771Calcium; via carbonyl oxygen By similarity
Metal binding801Calcium; via carbonyl oxygen By similarity
Metal binding851Calcium By similarity
Site1941Required for specificity By similarity

Amino acid modifications

Modified residue1541Sulfotyrosine Probable
Disulfide bond30 ↔ 160 By similarity
Disulfide bond48 ↔ 64 By similarity
Disulfide bond171 ↔ 185 By similarity
Disulfide bond196 ↔ 220 By similarity

Natural variations

Natural variant1171A → V.
Corresponds to variant rs11547028 [ dbSNP | Ensembl ].
VAR_051858

Sequences

Sequence LengthMass (Da)Tools
P07478 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 82B0F41EB8E3D5DB

FASTA24726,488
        10         20         30         40         50         60 
MNLLLILTFV AAAVAAPFDD DDKIVGGYIC EENSVPYQVS LNSGYHFCGG SLISEQWVVS 

        70         80         90        100        110        120 
AGHCYKSRIQ VRLGEHNIEV LEGNEQFINA AKIIRHPKYN SRTLDNDILL IKLSSPAVIN 

       130        140        150        160        170        180 
SRVSAISLPT APPAAGTESL ISGWGNTLSS GADYPDELQC LDAPVLSQAE CEASYPGKIT 

       190        200        210        220        230        240 
NNMFCVGFLE GGKDSCQGDS GGPVVSNGEL QGIVSWGYGC AQKNRPGVYT KVYNYVDWIK 


DTIAANS 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-49.
[3]"Paneth cell trypsin is the processing enzyme for human defensin-5."
Ghosh D., Porter E., Shen B., Lee S.K., Wilk D., Drazba J., Yadav S.P., Crabb J.W., Ganz T., Bevins C.L.
Nat. Immunol. 3:583-590(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[4]"Human cationic trypsinogen is sulfated on Tyr154."
Sahin-Toth M., Kukor Z., Nemoda Z.
FEBS J. 273:5044-5050(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27602 mRNA. Translation: AAA61232.1.
PIRB25852.
RefSeqNP_002761.1. NM_002770.2.
UniGeneHs.449281.
Hs.726742.
Hs.728780.

3D structure databases

ProteinModelPortalP07478.
SMRP07478. Positions 24-247.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111627. 1 interaction.
STRING9606.ENSP00000308720.

Chemistry

BindingDBP07478.
ChEMBLCHEMBL2096988.

Protein family/group databases

MEROPSS01.258.

PTM databases

PhosphoSiteP07478.

Polymorphism databases

DMDM136413.

Proteomic databases

PRIDEP07478.

Protocols and materials databases

DNASU5645.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000570608; ENSP00000459226; ENSG00000262739.
GeneID5645.
KEGGhsa:5645.

Organism-specific databases

CTD5645.
GeneCardsGC07P9T0974.
HGNCHGNC:9483. PRSS2.
MIM601564. gene.
neXtProtNX_P07478.
Orphanet676. Hereditary chronic pancreatitis.
PharmGKBPA33833.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidP07478.
KOK01312.
OMAHPKYSSW.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_6900. Immune System.

Gene expression databases

BgeeP07478.
CleanExHS_PRSS2.
GenevestigatorP07478.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi5645.
NextBio21930.
PROP07478.
SOURCESearch...

Entry information

Entry nameTRY2_HUMAN
AccessionPrimary (citable) accession number: P07478
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM