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P35033 (TRY3_SALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-3

EC=3.4.21.4
Alternative name(s):
Trypsin III
OrganismSalmo salar (Atlantic salmon)
Taxonomic identifier8030 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiEuteleosteiProtacanthopterygiiSalmoniformesSalmonidaeSalmoninaeSalmo

Protein attributes

Sequence length238 AA.
Sequence statusFragment.
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
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
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 peptide‹1 – 7›7 Potential
Propeptide8 – 158Activation peptide
PRO_0000028229
Chain16 – 238223Trypsin-3
PRO_0000028230

Regions

Domain16 – 236221Peptidase S1

Sites

Active site551Charge relay system By similarity
Active site991Charge relay system By similarity
Active site1921Charge relay system By similarity
Metal binding671Calcium By similarity
Metal binding691Calcium; via carbonyl oxygen By similarity
Metal binding721Calcium; via carbonyl oxygen
Metal binding771Calcium By similarity
Site1861Required for specificity By similarity

Amino acid modifications

Disulfide bond22 ↔ 152
Disulfide bond40 ↔ 56
Disulfide bond124 ↔ 225
Disulfide bond131 ↔ 198
Disulfide bond163 ↔ 177
Disulfide bond188 ↔ 212

Experimental info

Non-terminal residue11

Secondary structure

........................................ 238
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35033 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: AE799B80E8393023

FASTA23825,389
        10         20         30         40         50         60 
FAVAFAAPID DEDDKIVGGY ECRKNSASYQ ASLQSGYHFC GGSLISSTWV VSAAHCYKSR 

        70         80         90        100        110        120 
IQVRLGEHNI AVNEGTEQFI DSVKVIMHPS YNSRNLDNDI MLIKLSKPAS LNSYVSTVAL 

       130        140        150        160        170        180 
PSSCASSGTR CLVSGWGNLS GSSSNYPDTL RCLDLPILSS SSCNSAYPGQ ITSNMFCAGF 

       190        200        210        220        230 
MEGGKDSCQG DSGGPVVCNG QLQGVVSWGY GCAQRNKPGV YTKVCNYRSW ISSTMSSN 

« Hide

References

[1]"Molecular cloning and characterization of anionic and cationic variants of trypsin from Atlantic salmon."
Male R., Lorens J.B., Smals A.O., Torrissen K.R.
Eur. J. Biochem. 232:677-685(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70074 mRNA. Translation: CAA49679.1.
PIRS31779. S66657.
UniGeneSsa.23520.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0JX-ray1.70A/B/C/D16-238[»]
ProteinModelPortalP35033.
SMRP35033. Positions 16-238.
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...

Other

EvolutionaryTraceP35033.

Entry information

Entry nameTRY3_SALSA
AccessionPrimary (citable) accession number: P35033
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 16, 2013
This is version 85 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references