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P00764 (TRYP_SQUAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. 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
OrganismSqualus acanthias (Spiny dogfish)
Taxonomic identifier7797 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiSqualimorphiiSqualiformesSqualidaeSqualus

Protein attributes

Sequence length229 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processdigestion

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

Propeptide1 – 77Activation peptide
PRO_0000028231
Chain8 – 229222Trypsin
PRO_0000028232

Regions

Domain8 – 227220Peptidase S1

Sites

Active site471Charge relay system By similarity
Active site911Charge relay system By similarity
Active site1831Charge relay system By similarity
Metal binding591Calcium By similarity
Metal binding691Calcium By similarity
Site1771Required for specificity By similarity

Amino acid modifications

Disulfide bond14 ↔ 143 By similarity
Disulfide bond32 ↔ 48 By similarity
Disulfide bond116 ↔ 216 By similarity
Disulfide bond123 ↔ 189 By similarity
Disulfide bond154 ↔ 168 By similarity
Disulfide bond179 ↔ 203 By similarity

Natural variations

Natural variant1091L → P.

Sequences

Sequence LengthMass (Da)Tools
P00764 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: E83B83C5AD72FCE4

FASTA22924,591
        10         20         30         40         50         60 
APDDDDKIVG GYECPKHAAP WTVSLNVGYH FCGGSLIAPG WVVSAAHCYQ RRIQVRLGEH 

        70         80         90        100        110        120 
DISANEGDET YIDSSMVIRH PNYSGYDLDN DIMLIKLSKP AALNRNVDLI SLPTGCAYAG 

       130        140        150        160        170        180 
EMCLISGWGN TMDGAVSGDQ LQCLDAPVLS DAECKGAYPG MITNNMMCVG YMEGGKDSCQ 

       190        200        210        220 
GDSGGPVVCN GMLQGIVSWG YGCAERDHPG VYTRVCHYVS WIHETIASV 

« Hide

References

[1]"Amino acid sequence of dogfish trypsin."
Titani K., Ericsson L.H., Neurath H., Walsh K.A.
Biochemistry 14:1358-1366(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 8-229.
[2]"Comparison of the amino terminal sequences of bovine, dogfish, and lungfish trypsinogens."
Hermodson M.A., Tye R.W., Reeck G.R., Neurath H., Walsh K.A.
FEBS Lett. 14:222-224(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-21.

Cross-references

Sequence databases

PIRTRDFS. A00950.

3D structure databases

ProteinModelPortalP00764.
SMRP00764. Positions 8-227.
ModBaseSearch...
MobiDBSearch...

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 nameTRYP_SQUAC
AccessionPrimary (citable) accession number: P00764
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 82 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