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Protein

Trypsin-3

Gene
N/A
Organism
Salmo salar (Atlantic salmon)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei55 – 551Charge relay systemBy similarity
Metal bindingi67 – 671CalciumBy similarity
Metal bindingi69 – 691Calcium; via carbonyl oxygenBy similarity
Metal bindingi72 – 721Calcium; via carbonyl oxygen
Metal bindingi77 – 771CalciumBy similarity
Active sitei99 – 991Charge relay systemBy similarity
Sitei186 – 1861Required for specificityBy similarity
Active sitei192 – 1921Charge relay systemBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. digestion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Digestion

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

MEROPSiS01.126.

Names & Taxonomyi

Protein namesi
Recommended name:
Trypsin-3 (EC:3.4.21.4)
Alternative name(s):
Trypsin III
OrganismiSalmo salar (Atlantic salmon)
Taxonomic identifieri8030 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiProtacanthopterygiiSalmoniformesSalmonidaeSalmoninaeSalmo

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 7›7Sequence Analysis
Propeptidei8 – 158Activation peptidePRO_0000028229
Chaini16 – 238223Trypsin-3PRO_0000028230Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi22 ↔ 152
Disulfide bondi40 ↔ 56
Disulfide bondi124 ↔ 225
Disulfide bondi131 ↔ 198
Disulfide bondi163 ↔ 177
Disulfide bondi188 ↔ 212

Keywords - PTMi

Disulfide bond, Zymogen

Structurei

Secondary structure

1
238
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni26 – 294Combined sources
Beta strandi30 – 356Combined sources
Beta strandi38 – 5215Combined sources
Helixi54 – 563Combined sources
Beta strandi62 – 665Combined sources
Beta strandi68 – 725Combined sources
Beta strandi78 – 8710Combined sources
Turni93 – 964Combined sources
Beta strandi101 – 1077Combined sources
Beta strandi130 – 1378Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi151 – 1577Combined sources
Helixi160 – 1667Combined sources
Turni168 – 1703Combined sources
Beta strandi175 – 1795Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi201 – 2088Combined sources
Beta strandi210 – 2134Combined sources
Beta strandi219 – 2235Combined sources
Helixi224 – 2274Combined sources
Helixi228 – 23710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0JX-ray1.70A/B/C/D16-238[»]
ProteinModelPortaliP35033.
SMRiP35033. Positions 16-238.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35033.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 236221Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG013304.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35033-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
FAVAFAAPID DEDDKIVGGY ECRKNSASYQ ASLQSGYHFC GGSLISSTWV
60 70 80 90 100
VSAAHCYKSR IQVRLGEHNI AVNEGTEQFI DSVKVIMHPS YNSRNLDNDI
110 120 130 140 150
MLIKLSKPAS LNSYVSTVAL PSSCASSGTR CLVSGWGNLS GSSSNYPDTL
160 170 180 190 200
RCLDLPILSS SSCNSAYPGQ ITSNMFCAGF MEGGKDSCQG DSGGPVVCNG
210 220 230
QLQGVVSWGY GCAQRNKPGV YTKVCNYRSW ISSTMSSN
Length:238
Mass (Da):25,389
Last modified:January 31, 1994 - v1
Checksum:iAE799B80E8393023
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70074 mRNA. Translation: CAA49679.1.
PIRiS66657. S31779.
UniGeneiSsa.23520.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70074 mRNA. Translation: CAA49679.1.
PIRiS66657. S31779.
UniGeneiSsa.23520.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0JX-ray1.70A/B/C/D16-238[»]
ProteinModelPortaliP35033.
SMRiP35033. Positions 16-238.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.126.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG013304.

Miscellaneous databases

EvolutionaryTraceiP35033.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pancreas.

Entry informationi

Entry nameiTRY3_SALSA
AccessioniPrimary (citable) accession number: P35033
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1994
Last sequence update: January 31, 1994
Last modified: March 3, 2015
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.