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P16049 (TRY1_GADMO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. 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
OrganismGadus morhua (Atlantic cod)
Taxonomic identifier8049 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataZeiogadariaGadariaeGadiformesGadoideiGadidaeGadus

Protein attributes

Sequence length241 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.

Subcellular location

Secretedextracellular space.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Direct 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_functionserine-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 – 1313 Potential
Propeptide14 – 196Activation peptide
PRO_0000028309
Chain20 – 241222Trypsin-1
PRO_0000028310

Regions

Domain20 – 239220Peptidase S1

Sites

Active site591Charge relay system By similarity
Active site1031Charge relay system By similarity
Active site1951Charge relay system By similarity
Site1891Required for specificity By similarity

Amino acid modifications

Disulfide bond26 ↔ 155 By similarity
Disulfide bond44 ↔ 60 By similarity
Disulfide bond128 ↔ 228 By similarity
Disulfide bond135 ↔ 201 By similarity
Disulfide bond166 ↔ 180 By similarity
Disulfide bond191 ↔ 215 By similarity

Experimental info

Sequence conflict251E → Q AA sequence Ref.2
Sequence conflict27 – 282TK → EA AA sequence Ref.2
Sequence conflict431F → Y AA sequence Ref.2
Sequence conflict49 – 524VSKD → IN AA sequence Ref.2

Secondary structure

....................................... 241
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16049 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 44EC9A0106AD1A68

FASTA24125,941
        10         20         30         40         50         60 
MKSLIFVLLL GAVFAEEDKI VGGYECTKHS QAHQVSLNSG YHFCGGSLVS KDWVVSAAHC 

        70         80         90        100        110        120 
YKSVLRVRLG EHHIRVNEGT EQYISSSSVI RHPNYSSYNI NNDIMLIKLT KPATLNQYVH 

       130        140        150        160        170        180 
AVALPTECAA DATMCTVSGW GNTMSSVADG DKLQCLSLPI LSHADCANSY PGMITQSMFC 

       190        200        210        220        230        240 
AGYLEGGKDS CQGDSGGPVV CNGVLQGVVS WGYGCAERDH PGVYAKVCVL SGWVRDTMAN 


Y 

« Hide

References

[1]"Isolation and characterization of cDNAs from Atlantic cod encoding two different forms of trypsinogen."
Gudmundsdottir A., Gudmundsdottir E., Oskarsson S., Bjarnason J.B., Eakin A.E., Craik C.S.
Eur. J. Biochem. 217:1091-1097(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pyloric caecum.
[2]"Purification and characterization of trypsin from the poikilotherm Gadus morhua."
Asgeirsson B., Fox J.W., Bjarnason J.B.
Eur. J. Biochem. 180:85-94(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-58.
Tissue: Pyloric caecum.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X76886 mRNA. Translation: CAA54214.1.
PIRS39047.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EEKX-ray1.85A20-239[»]
ProteinModelPortalP16049.
SMRP16049. Positions 20-239.
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...

Other

EvolutionaryTraceP16049.

Entry information

Entry nameTRY1_GADMO
AccessionPrimary (citable) accession number: P16049
Secondary accession number(s): Q91040, Q92156
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 81 of the entry and version 2 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