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P07478 (TRY2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 134. 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.

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.
IPIIPI00815665.
PIRB25852.
RefSeqNP_002761.1. NM_002770.2.
UniGeneHs.449281.
Hs.726742.
Hs.728780.

3D structure databases

ProteinModelPortalP07478.
ModBaseSearch...

Protein-protein interaction databases

STRING9606.ENSP00000308720.

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.
GeneCardsGC07Pg41870.
HGNCHGNC:9483. PRSS2.
MIM601564. gene.
neXtProtNX_P07478.
Orphanet676. Hereditary chronic pancreatitis.
PharmGKBPA33833.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidP07478.
KOK01312.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_6900. Immune System.

Gene expression databases

BgeeP07478.
CleanExHS_PRSS2.
GenevestigatorP07478.
GermOnlineENSG00000204982. Homo sapiens.

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. Pept_Ser_Cys. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP07478.
ChEMBLCHEMBL3159.
GenomeRNAi5645.
NextBio21930.
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: May 1, 2013
This is version 134 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

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 polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families