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P19799 (TRY1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

EC=3.4.21.4
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length243 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Secretedextracellular space.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
Gene Ontology (GO)
   Biological_processdigestion

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 By similarity
Propeptide16 – 205Activation peptide
PRO_0000028233
Chain21 – 243223Trypsin
PRO_0000028234

Regions

Domain21 – 241221Peptidase S1

Sites

Active site601Charge relay system By similarity
Active site1041Charge relay system By similarity
Active site1971Charge relay system By similarity
Metal binding721Calcium By similarity
Metal binding741Calcium; via carbonyl oxygen By similarity
Metal binding821Calcium By similarity
Site1911Required for specificity By similarity

Amino acid modifications

Disulfide bond27 ↔ 157 By similarity
Disulfide bond45 ↔ 61 By similarity
Disulfide bond129 ↔ 230 By similarity
Disulfide bond136 ↔ 203 By similarity
Disulfide bond168 ↔ 182 By similarity
Disulfide bond193 ↔ 217 By similarity

Sequences

Sequence LengthMass (Da)Tools
P19799 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: C5B8345A8B3F8031

FASTA24325,492
        10         20         30         40         50         60 
MKFLLLCVLL GAAAAFDDDK IIGGATCAKS SVPYIVSLNS GYHFCGGSLI TNQWVVSAAH 

        70         80         90        100        110        120 
CYKASIQVRL GEHNIALSEG TEQFISSSKV IRHSGYNSYT LDNDIMLIKL SSPASLNAAV 

       130        140        150        160        170        180 
NTVPLPSGCS AAGTSCLISG WGNTLSNGSN YPDLLQCLNA PILTNAQCNS AYPGEITANM 

       190        200        210        220        230        240 
ICVGYMEGGK DSCQGDSGGP VVCNGQLQGV VSWGYGCAMR NYPGVYTKVC NYNAWIQNTI 


AAN 

« Hide

References

[1]"Developmental and thyroid hormone-dependent regulation of pancreatic genes in Xenopus laevis."
Shi Y.B., Brown D.D.
Genes Dev. 4:1107-1113(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53458 mRNA. Translation: CAA37538.1.
PIRA35871.
UniGeneXl.119.

3D structure databases

ProteinModelPortalP19799.
SMRP19799. Positions 21-243.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.126.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG013304.

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...

Entry information

Entry nameTRY1_XENLA
AccessionPrimary (citable) accession number: P19799
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 16, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries