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Reviewed, UniProtKB/Swiss-Prot P00764 (TRYP_SQUAC)

Last modified June 16, 2009. Version 67. 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
OrganismSqualus acanthias (Spiny dogfish)
Taxonomic identifier7797 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiSqualeaHypnosqualeaSqualiformesSqualoideiSqualidaeSqualus

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

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

Propeptide1 – 77Activation peptide Ref.1
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
P00764-1 [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: 1092332] [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: 11945763] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-21.

Cross-references

Sequence databases

PIRTRDFS. A00950.

3D structure databases

HSSPHSSP built from PDB template 1EZX based on UniProtKB P00760.
ModBaseSearch...

Phylogenomic databases

HOVERGENP00764.

Enzyme and pathway databases

BRENDA3.4.21.4. 981.

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 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: June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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