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Protein

Trypsin inhibitor A

Gene

KTI3

Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Inhibition of trypsin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei87 – 882Reactive bond for trypsin

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI03.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Trypsin inhibitor A
Alternative name(s):
Kunitz-type trypsin inhibitor A
Gene namesi
Name:KTI3
OrganismiGlycine max (Soybean) (Glycine hispida)
Taxonomic identifieri3847 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja
Proteomesi
  • UP000008827 Componenti: Unplaced

Pathology & Biotechi

Protein family/group databases

Allergomei1144. Gly m TI.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24243 PublicationsAdd
BLAST
Chaini25 – 205181Trypsin inhibitor APRO_0000016889Add
BLAST
Propeptidei206 – 21611PRO_0000016890Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi63 ↔ 1101 Publication
Disulfide bondi160 ↔ 1691 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

DIPiDIP-6101N.
MINTiMINT-1531958.
STRINGi3847.GLYMA08G45531.1.

Structurei

Secondary structure

1
216
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni30 – 323Combined sources
Beta strandi39 – 479Combined sources
Beta strandi53 – 564Combined sources
Beta strandi66 – 694Combined sources
Beta strandi80 – 834Combined sources
Beta strandi85 – 873Combined sources
Beta strandi97 – 1015Combined sources
Helixi108 – 1103Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi126 – 1305Combined sources
Beta strandi135 – 1373Combined sources
Beta strandi140 – 1467Combined sources
Beta strandi148 – 1525Combined sources
Beta strandi155 – 1617Combined sources
Beta strandi170 – 1767Combined sources
Turni178 – 1803Combined sources
Beta strandi183 – 1875Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi194 – 1996Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AVUX-ray2.30A25-205[»]
1AVWX-ray1.75B25-201[»]
1AVXX-ray1.90B25-201[»]
1BA7X-ray2.50A/B25-205[»]
ProteinModelPortaliP01070.
SMRiP01070. Positions 25-201.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01070.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiP01070.

Family and domain databases

InterProiIPR011065. Kunitz_inhibitor_ST1-like.
IPR002160. Prot_inh_Kunz-lg.
[Graphical view]
PfamiPF00197. Kunitz_legume. 1 hit.
[Graphical view]
PRINTSiPR00291. KUNITZINHBTR.
SMARTiSM00452. STI. 1 hit.
[Graphical view]
SUPFAMiSSF50386. SSF50386. 1 hit.
PROSITEiPS00283. SOYBEAN_KUNITZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01070-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSTIFFLFL FCAFTTSYLP SAIADFVLDN EGNPLENGGT YYILSDITAF
60 70 80 90 100
GGIRAAPTGN ERCPLTVVQS RNELDKGIGT IISSPYRIRF IAEGHPLSLK
110 120 130 140 150
FDSFAVIMLC VGIPTEWSVV EDLPEGPAVK IGENKDAMDG WFRLERVSDD
160 170 180 190 200
EFNNYKLVFC PQQAEDDKCG DIGISIDHDD GTRRLVVSKN KPLVVQFQKL
210
DKESLAKKNH GLSRSE
Length:216
Mass (Da):24,005
Last modified:May 1, 1992 - v2
Checksum:i1251FE0DE46CCA96
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251D → S AA sequence (PubMed:8318586).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti79 – 791G → E in variant C.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S45092 mRNA. Translation: AAB23464.1.
PIRiJQ0968.
RefSeqiNP_001238611.1. NM_001251682.1.
UniGeneiGma.29257.
Gma.37001.
Gma.37101.
Gma.51651.

Genome annotation databases

GeneIDi547831.
KEGGigmx:547831.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S45092 mRNA. Translation: AAB23464.1.
PIRiJQ0968.
RefSeqiNP_001238611.1. NM_001251682.1.
UniGeneiGma.29257.
Gma.37001.
Gma.37101.
Gma.51651.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AVUX-ray2.30A25-205[»]
1AVWX-ray1.75B25-201[»]
1AVXX-ray1.90B25-201[»]
1BA7X-ray2.50A/B25-205[»]
ProteinModelPortaliP01070.
SMRiP01070. Positions 25-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6101N.
MINTiMINT-1531958.
STRINGi3847.GLYMA08G45531.1.

Protein family/group databases

Allergomei1144. Gly m TI.
MEROPSiI03.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi547831.
KEGGigmx:547831.

Phylogenomic databases

InParanoidiP01070.

Miscellaneous databases

EvolutionaryTraceiP01070.

Family and domain databases

InterProiIPR011065. Kunitz_inhibitor_ST1-like.
IPR002160. Prot_inh_Kunz-lg.
[Graphical view]
PfamiPF00197. Kunitz_legume. 1 hit.
[Graphical view]
PRINTSiPR00291. KUNITZINHBTR.
SMARTiSM00452. STI. 1 hit.
[Graphical view]
SUPFAMiSSF50386. SSF50386. 1 hit.
PROSITEiPS00283. SOYBEAN_KUNITZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A frameshift mutation prevents Kunitz trypsin inhibitor mRNA accumulation in soybean embryos."
    Jofuku K.D., Schipper R.D., Goldberg R.B.
    Plant Cell 1:427-435(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Studies on soybean trypsin inhibitors. 3. Amino-acid sequences of the carboxyl-terminal region and the complete amino-acid sequence of soybean trypsin inhibitor (Kunitz)."
    Koide T., Ikenaka T.
    Eur. J. Biochem. 32:417-431(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-205 (VARIANT A).
  3. "Comparative study on amino acid sequences of Kunitz-type soybean trypsin inhibitors, Tia, Tib, and Tic."
    Kim S.-H., Hara S., Hase S., Ikenaka T., Toda H., Kitamura K., Kaizuma N.
    J. Biochem. 98:435-448(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-205 (VARIANT C), SEQUENCE REVISION (VARIANT A).
    Strain: cv. Raiden.
  4. "Isolation and characterization of a 54-kilodalton precursor of caltrin, the calcium transport inhibitor protein from seminal vesicles of the rat."
    Coronel C.E., Novella M.L., Winnica D.E., Lardy H.A.
    Biol. Reprod. 48:1326-1333(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-56.
  5. "The amino acid sequences around the disulfide bonds of soybean trypsin inhibitor."
    Brown J.R., Lerman N., Bohak Z.
    Biochem. Biophys. Res. Commun. 23:561-565(1966) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  6. "The reactive site of trypsin inhibitors."
    Ozawa K., Laskowski M. Jr.
    J. Biol. Chem. 241:3955-3961(1966) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITORY SITE.
  7. "Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-A resolution."
    Sweet R.M., Wright H.T., Janin J., Chothia C.H., Blow D.M.
    Biochemistry 13:4212-4228(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
  8. "Structure of the Kunitz-type soybean trypsin inhibitor (STI): implication for the interactions between members of the STI family and tissue-plasminogen activator."
    de Meester P., Brick P., Lloyd L.F., Blow D.M., Onesti S.
    Acta Crystallogr. D 54:589-597(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  9. "Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator."
    Song H.K., Suh S.W.
    J. Mol. Biol. 275:347-363(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiITRA_SOYBN
AccessioniPrimary (citable) accession number: P01070
Secondary accession number(s): Q9QV66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 1, 1992
Last modified: May 11, 2016
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The sequence of variant A is shown.
Electrophoresis identifies three genetically distinct variants, A, B, and C, that are inherited as codominant alleles.

Caution

PubMed:8318586 sequence was originally thought to be rat caltrin. A number of peptide fragments were derived from a trypsin digest of caltrin and soybean trypsin inhibitor was used to stop the digestion. It appears that some of the inhibitor was also digested and sequenced.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.