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P35032 (TRY2_SALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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-2

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

Protein attributes

Sequence length231 AA.
Sequence statusFragment.
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

   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 – 4›4 Potential
Propeptide5 – 95Activation peptide
PRO_0000028227
Chain10 – 231222Trypsin-2
PRO_0000028228

Regions

Domain10 – 229220Peptidase S1

Sites

Active site491Charge relay system By similarity
Active site931Charge relay system By similarity
Active site1851Charge relay system By similarity
Metal binding611Calcium By similarity
Metal binding631Calcium; via carbonyl oxygen By similarity
Metal binding661Calcium; via carbonyl oxygen By similarity
Metal binding711Calcium By similarity
Site1791Required for specificity By similarity

Amino acid modifications

Disulfide bond16 ↔ 145 By similarity
Disulfide bond34 ↔ 50 By similarity
Disulfide bond118 ↔ 218 By similarity
Disulfide bond125 ↔ 191 By similarity
Disulfide bond156 ↔ 170 By similarity
Disulfide bond181 ↔ 205 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P35032 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: C54A1CAFE74FAE18

FASTA23124,823
        10         20         30         40         50         60 
AAFATEDDKI VGGYECKAYS QPHQVSLNSG YHFCGGSLVN ENWVVSAAHC YQSRVEVRLG 

        70         80         90        100        110        120 
EHNIQVTEGS EQFISSSRVI RHPNYSSYNI DNDIMLIKLS KPATLNTYVQ PVALPTSCAP 

       130        140        150        160        170        180 
AGTMCTVSGW GNTMSSTADK NKLQCLNIPI LSYSDCNNSY PGMITNAMFC AGYLEGGKDS 

       190        200        210        220        230 
CQGDSGGPVV CNGELQGVVS WGYGCAEPGN PGVYAKVCIF NDWLTSTMAT Y 

« 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70073 mRNA. Translation: CAA49678.1.
PIRS31778. S66658.
UniGeneSsa.19782.

3D structure databases

ProteinModelPortalP35032.
SMRP35032. Positions 10-231.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.125.

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 nameTRY2_SALSA
AccessionPrimary (citable) accession number: P35032
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 11, 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