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Protein

Trypsin-1

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+Note: Binds 1 Ca2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei60 – 601Charge relay system
Metal bindingi72 – 721Calcium
Metal bindingi74 – 741Calcium; via carbonyl oxygen
Metal bindingi77 – 771Calcium; via carbonyl oxygen
Metal bindingi82 – 821Calcium
Active sitei104 – 1041Charge relay system
Sitei190 – 1901Required for specificityBy similarity
Active sitei196 – 1961Charge relay system

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Digestion

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

MEROPSiS01.125.

Names & Taxonomyi

Protein namesi
Recommended name:
Trypsin-1 (EC:3.4.21.4)
Alternative name(s):
Trypsin I
OrganismiSalmo salar (Atlantic salmon)
Taxonomic identifieri8030 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiProtacanthopterygiiSalmoniformesSalmonidaeSalmoninaeSalmo

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence AnalysisAdd
BLAST
Propeptidei16 – 205Activation peptidePRO_0000028225
Chaini21 – 242222Trypsin-1PRO_0000028226Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 156
Disulfide bondi45 ↔ 61
Disulfide bondi129 ↔ 229
Disulfide bondi136 ↔ 202
Disulfide bondi167 ↔ 181
Disulfide bondi192 ↔ 216

Keywords - PTMi

Disulfide bond, Zymogen

Interactioni

Protein-protein interaction databases

MINTiMINT-88002.

Structurei

Secondary structure

1
242
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni29 – 346Combined sources
Beta strandi35 – 5117Combined sources
Beta strandi54 – 574Combined sources
Helixi59 – 613Combined sources
Beta strandi67 – 715Combined sources
Beta strandi83 – 9210Combined sources
Turni98 – 1014Combined sources
Beta strandi106 – 1127Combined sources
Beta strandi117 – 1193Combined sources
Beta strandi135 – 1428Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi155 – 1617Combined sources
Helixi164 – 1707Combined sources
Turni172 – 1743Combined sources
Beta strandi179 – 1835Combined sources
Turni193 – 1975Combined sources
Beta strandi199 – 2024Combined sources
Beta strandi205 – 2128Combined sources
Beta strandi214 – 2174Combined sources
Beta strandi223 – 2275Combined sources
Helixi228 – 2314Combined sources
Helixi232 – 2409Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP35031.
SMRiP35031. Positions 21-242.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35031.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 240220Peptidase 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: Complete.

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

P35031-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISLVFVLLI GAAFATEDDK IVGGYECKAY SQTHQVSLNS GYHFCGGSLV
60 70 80 90 100
NENWVVSAAH CYKSRVEVRL GEHNIKVTEG SEQFISSSRV IRHPNYSSYN
110 120 130 140 150
IDNDIMLIKL SKPATLNTYV QPVALPTSCA PAGTMCTVSG WGNTMSSTAD
160 170 180 190 200
SNKLQCLNIP ILSYSDCNNS YPGMITNAMF CAGYLEGGKD SCQGDSGGPV
210 220 230 240
VCNGELQGVV SWGYGCAEPG NPGVYAKVCI FNDWLTSTMA SY
Length:242
Mass (Da):25,958
Last modified:February 1, 1994 - v1
Checksum:i43F5642498067E5A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331T → A in trypsins IA/IB.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70075 mRNA. Translation: CAA49680.1.
X70071 mRNA. Translation: CAA49676.1.
X70072 mRNA. Translation: CAA49677.1.
PIRiS66659. S31776.
S66660. S31775.
RefSeqiNP_001117183.1. NM_001123711.1.
NP_001119704.1. NM_001126232.1.
UniGeneiSsa.38456.
Ssa.628.

Genome annotation databases

GeneIDi100137021.
100137022.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70075 mRNA. Translation: CAA49680.1.
X70071 mRNA. Translation: CAA49676.1.
X70072 mRNA. Translation: CAA49677.1.
PIRiS66659. S31776.
S66660. S31775.
RefSeqiNP_001117183.1. NM_001123711.1.
NP_001119704.1. NM_001126232.1.
UniGeneiSsa.38456.
Ssa.628.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP35031.
SMRiP35031. Positions 21-242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-88002.

Protein family/group databases

MEROPSiS01.125.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100137021.
100137022.

Organism-specific databases

CTDi100137021.
100137022.

Phylogenomic databases

HOVERGENiHBG013304.

Miscellaneous databases

EvolutionaryTraceiP35031.
PROiP35031.

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(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).

Entry informationi

Entry nameiTRY1_SALSA
AccessioniPrimary (citable) accession number: P35031
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 29, 2015
This is version 105 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.