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P19799

- TRY1_XENLA

UniProt

P19799 - TRY1_XENLA

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Protein

Trypsin

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Cofactori

Ca2+By similarityNote: Binds 1 Ca(2+) ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei60 – 601Charge relay systemBy similarity
Metal bindingi72 – 721CalciumBy similarity
Metal bindingi74 – 741Calcium; via carbonyl oxygenBy similarity
Metal bindingi82 – 821CalciumBy similarity
Active sitei104 – 1041Charge relay systemBy similarity
Sitei191 – 1911Required for specificityBy similarity
Active sitei197 – 1971Charge 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 (EC:3.4.21.4)
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515By similarityAdd
BLAST
Propeptidei16 – 205Activation peptidePRO_0000028233
Chaini21 – 243223TrypsinPRO_0000028234Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 157PROSITE-ProRule annotation
Disulfide bondi45 ↔ 61PROSITE-ProRule annotation
Disulfide bondi129 ↔ 230PROSITE-ProRule annotation
Disulfide bondi136 ↔ 203PROSITE-ProRule annotation
Disulfide bondi168 ↔ 182PROSITE-ProRule annotation
Disulfide bondi193 ↔ 217PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Zymogen

Structurei

3D structure databases

ProteinModelPortaliP19799.
SMRiP19799. Positions 21-243.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 241221Peptidase 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.

P19799-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKFLLLCVLL GAAAAFDDDK IIGGATCAKS SVPYIVSLNS GYHFCGGSLI
60 70 80 90 100
TNQWVVSAAH CYKASIQVRL GEHNIALSEG TEQFISSSKV IRHSGYNSYT
110 120 130 140 150
LDNDIMLIKL SSPASLNAAV NTVPLPSGCS AAGTSCLISG WGNTLSNGSN
160 170 180 190 200
YPDLLQCLNA PILTNAQCNS AYPGEITANM ICVGYMEGGK DSCQGDSGGP
210 220 230 240
VVCNGQLQGV VSWGYGCAMR NYPGVYTKVC NYNAWIQNTI AAN
Length:243
Mass (Da):25,492
Last modified:February 1, 1991 - v1
Checksum:iC5B8345A8B3F8031
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53458 mRNA. Translation: CAA37538.1.
PIRiA35871.
UniGeneiXl.119.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53458 mRNA. Translation: CAA37538.1 .
PIRi A35871.
UniGenei Xl.119.

3D structure databases

ProteinModelPortali P19799.
SMRi P19799. Positions 21-243.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S01.126.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG013304.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Developmental and thyroid hormone-dependent regulation of pancreatic genes in Xenopus laevis."
    Shi Y.B., Brown D.D.
    Genes Dev. 4:1107-1113(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pancreas.

Entry informationi

Entry nameiTRY1_XENLA
AccessioniPrimary (citable) accession number: P19799
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 26, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3