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P06871 (TRY1_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 95. 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 attributes

Sequence length246 AA.
Sequence statusComplete.
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
   Technical termComplete proteome
Reference proteome
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 peptide1 – 1515
Propeptide16 – 238Activation peptide
PRO_0000028191
Chain24 – 246223Cationic trypsin
PRO_0000028192

Regions

Domain24 – 244221Peptidase S1

Sites

Active site631Charge relay system By similarity
Active site1071Charge relay system By similarity
Active site2001Charge relay system By similarity
Metal binding751Calcium By similarity
Metal binding771Calcium; via carbonyl oxygen By similarity
Metal binding801Calcium; via carbonyl oxygen By similarity
Metal binding851Calcium By similarity
Site1941Required for specificity By similarity

Amino acid modifications

Disulfide bond30 ↔ 160 By similarity
Disulfide bond48 ↔ 64 By similarity
Disulfide bond132 ↔ 233 By similarity
Disulfide bond139 ↔ 206 By similarity
Disulfide bond171 ↔ 185 By similarity
Disulfide bond196 ↔ 220 By similarity

Sequences

Sequence LengthMass (Da)Tools
P06871 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: E9E5A1DE2391BBBB

FASTA24626,170
        10         20         30         40         50         60 
MKTFIFLALL GATVAFPIDD DDKIVGGYTC SRNSVPYQVS LNSGYHFCGG SLINSQWVVS 

        70         80         90        100        110        120 
AAHCYKSRIQ VRLGEYNIAV SEGGEQFINA AKIIRHPRYN ANTIDNDIML IKLSSPATLN 

       130        140        150        160        170        180 
SRVSAIALPK SCPAAGTQCL ISGWGNTQSI GQNYPDVLQC LKAPILSDSV CRNAYPGQIS 

       190        200        210        220        230        240 
SNMMCLGYME GGKDSCQGDS GGPVVCNGEL QGVVSWGAGC AQKGKPGVSP KVCKYVSWIQ 


QTIAAN 

« Hide

References

[1]"Differential regulation of trypsinogen mRNA translation: full-length mRNA sequences encoding two oppositely charged trypsinogen isoenzymes in the dog pancreas."
Pinsky S.D., Laforge K.S., Scheele G.
Mol. Cell. Biol. 5:2669-2676(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11590 mRNA. Translation: AAA30900.1.
PIRTRDGC. B26273.

3D structure databases

ProteinModelPortalP06871.
SMRP06871. Positions 24-246.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000005682.

Protein family/group databases

MEROPSS01.151.

Proteomic databases

PaxDbP06871.
PRIDEP06871.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidP06871.

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 nameTRY1_CANFA
AccessionPrimary (citable) accession number: P06871
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 13, 2013
This is version 95 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