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Reviewed, UniProtKB/Swiss-Prot P70059 (TRY2_XENLA)

Last modified June 16, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Trypsin
    EC=3.4.21.4
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraMesobatrachiaPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length244 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: InterPro

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium 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 – 216Activation peptide By similarity
PRO_0000028235
Chain22 – 244223Trypsin
PRO_0000028236

Regions

Domain22 – 242221Peptidase S1

Sites

Active site611Charge relay system By similarity
Active site1051Charge relay system By similarity
Active site1981Charge relay system By similarity
Metal binding731Calcium By similarity
Metal binding751Calcium; via carbonyl oxygen By similarity
Metal binding831Calcium By similarity
Site1921Required for specificity By similarity

Amino acid modifications

Disulfide bond28 ↔ 158 By similarity
Disulfide bond46 ↔ 62 By similarity
Disulfide bond130 ↔ 231 By similarity
Disulfide bond137 ↔ 204 By similarity
Disulfide bond169 ↔ 183 By similarity
Disulfide bond194 ↔ 218 By similarity

Sequences

Sequence LengthMass (Da)Tools
P70059-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: C63F29CB3300B323

FASTA24426,080
        10         20         30         40         50         60 
MKFLVILVLL GAAVAFEDDD KIVGGFTCAK NAVPYQVSLN AGYHFCGGSL INSQWVVSAA 

        70         80         90        100        110        120 
HCYKSRIQVR LGEHNIALNE GTEQFIDSQK VIKHPNYNSR NLDNDIMLIK LSTTARLSAN 

       130        140        150        160        170        180 
IQSVPLPSAC ASAGTNCLIS GWGNTLSSGT NYPDLLQCLN APILTDSQCS NSYPGEITKN 

       190        200        210        220        230        240 
MFCAGFLAGG KDSCQGDSGG PVVCNGQLQG VVSWGYGCAQ RNYPGVYTKV CNFVTWIQST 


ISSN 

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References

[1]Wang K., Lytle L., Gan L., Hood L.E.
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

U72330 mRNA. Translation: AAB17274.1.
UniGeneXl.1858

3D structure databases

HSSPHSSP built from PDB template 1EZX based on UniProtKB P00760.
SMRP70059. Positions 22-244.
ModBaseSearch...

Protein family/group databases

MEROPSS01.126.

Organism-specific databases

XenbaseXB-FEAT-5776261. prss3.

Phylogenomic databases

HOVERGENP70059.

Enzyme and pathway databases

BRENDA3.4.21.4. 648.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRY2_XENLA
AccessionPrimary (citable) accession number: P70059
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectXenopus annotation project

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents