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P35031 (TRY1_SALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 100. 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-1

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

Protein attributes

Sequence length242 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.

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

   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 peptide1 – 1515 Potential
Propeptide16 – 205Activation peptide
PRO_0000028225
Chain21 – 242222Trypsin-1
PRO_0000028226

Regions

Domain21 – 240220Peptidase S1

Sites

Active site601Charge relay system
Active site1041Charge relay system
Active site1961Charge relay system
Metal binding721Calcium
Metal binding741Calcium; via carbonyl oxygen
Metal binding771Calcium; via carbonyl oxygen
Metal binding821Calcium
Site1901Required for specificity By similarity

Amino acid modifications

Disulfide bond27 ↔ 156
Disulfide bond45 ↔ 61
Disulfide bond129 ↔ 229
Disulfide bond136 ↔ 202
Disulfide bond167 ↔ 181
Disulfide bond192 ↔ 216

Natural variations

Natural variant331T → A in trypsins IA/IB.

Secondary structure

.......................................... 242
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35031 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 43F5642498067E5A

FASTA24225,958
        10         20         30         40         50         60 
MISLVFVLLI GAAFATEDDK IVGGYECKAY SQTHQVSLNS GYHFCGGSLV NENWVVSAAH 

        70         80         90        100        110        120 
CYKSRVEVRL GEHNIKVTEG SEQFISSSRV IRHPNYSSYN IDNDIMLIKL SKPATLNTYV 

       130        140        150        160        170        180 
QPVALPTSCA PAGTMCTVSG WGNTMSSTAD SNKLQCLNIP ILSYSDCNNS YPGMITNAMF 

       190        200        210        220        230        240 
CAGYLEGGKD SCQGDSGGPV VCNGELQGVV SWGYGCAEPG NPGVYAKVCI FNDWLTSTMA 


SY 

« 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.
[2]"Structure determination and refinement of benzamidine-inhibited trypsin from the North Atlantic salmon (Salmo salar) at 1.82-A resolution."
Smalas A.O., Hordvik A.
Acta Crystallogr. D 49:318-330(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS).
[3]"Cold adaption of enzymes: structural comparison between salmon and bovine trypsins."
Smalas A.O., Heimstad E.S., Hordvik A., Willassen N.P., Male R.
Proteins 20:149-166(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70075 mRNA. Translation: CAA49680.1.
X70071 mRNA. Translation: CAA49676.1.
X70072 mRNA. Translation: CAA49677.1.
PIRS31776. S66659.
S31775. S66660.
RefSeqNP_001117183.1. NM_001123711.1.
NP_001119704.1. NM_001126232.1.
UniGeneSsa.38456.
Ssa.628.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BITX-ray1.83A6-242[»]
1BZXX-ray2.10E21-242[»]
1HJ8X-ray1.00A21-242[»]
1UTJX-ray1.83A1-242[»]
1UTKX-ray1.53A1-242[»]
1UTLX-ray1.70M1-242[»]
1UTMX-ray1.50A1-242[»]
2STAX-ray1.80E21-242[»]
2STBX-ray1.80E21-242[»]
2TBSX-ray1.80A21-242[»]
ProteinModelPortalP35031.
SMRP35031. Positions 21-242.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-88002.

Protein family/group databases

MEROPSS01.125.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100137021.
100137022.

Organism-specific databases

CTD100137021.
100137022.

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

EvolutionaryTraceP35031.

Entry information

Entry nameTRY1_SALSA
AccessionPrimary (citable) accession number: P35031
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 11, 2014
This is version 100 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