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UniProtKB/Swiss-Prot entry P01074


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ITR1_CUCMA
Primary accession number P01074
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    January 15, 2008 (Entry version 63)
Name and origin of the protein
Protein name Trypsin inhibitor 1
Synonyms Trypsin inhibitor I
CMTI-I
ITD-I
Gene name None
From
Cucurbita maxima (Pumpkin) (Winter squash) [TaxID: 3661] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE.
TISSUE=Seed;
PubMed=6840699 [NCBI, ExPASy, EBI, Israel, Japan]
Wilusz T., Wieczorek M., Polanowski A., Denton A., Cook J., Laskowski M. Jr.;
"Amino-acid sequence of two trypsin isoinhibitors, ITD I and ITD III from squash seeds (Cucurbita maxima).";
Hoppe-Seyler's Z. Physiol. Chem. 364:93-95(1983).
[2]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1016/0014-5793(89)80486-7; PubMed=2914611 [NCBI, ExPASy, EBI, Israel, Japan]
Bode W., Greyling H.J., Huber R., Otlewski J., Wilusz T.;
"The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes.";
FEBS Lett. 242:285-292(1989).
[3]
STRUCTURE BY NMR.
DOI=10.1016/0022-2836(89)90137-X; PubMed=2614837 [NCBI, ExPASy, EBI, Israel, Japan]
Holak T.A., Gondol D., Otlewski J., Wilusz T.;
"Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamical simulated annealing.";
J. Mol. Biol. 210:635-648(1989).
[4]
STRUCTURE BY NMR.
PubMed=10716179 [NCBI, ExPASy, EBI, Israel, Japan]
Zhukov I., Jaroszewski L., Bierzynski A.;
"Conservative mutation Met8 --> Leu affects the folding process and structural stability of squash trypsin inhibitor CMTI-I.";
Protein Sci. 9:273-279(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
PIR A01313; TIPU.
3D structure databases
PDB
1CTI; NMR; -; A=1-29.[ExPASy / RCSB / EBI]
1LU0; X-ray; 1.03 A; A/B=1-29.[ExPASy / RCSB / EBI]
1PPE; X-ray; 2.00 A; I=1-29.[ExPASy / RCSB / EBI]
2CTI; NMR; -; A=1-29.[ExPASy / RCSB / EBI]
2STA; X-ray; 1.80 A; I=1-29.[ExPASy / RCSB / EBI]
2V1V; NMR; -; A=1-29.[ExPASy / RCSB / EBI]
3CTI; NMR; -; A=1-29.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1CTI; -.
1LU0; -.
1PPE; -.
2CTI; -.
2STA; -.
2V1V; -.
3CTI; -.
ModBase P01074.
Protein family/group databases
MEROPS I07.005; -.
Family and domain databases
InterPro IPR000737; Prot_inh_squash.
Graphical view of domain structure.
Pfam PF00299; Squash; 1.
Pfam graphical view of domain structure.
PRINTS PR00293; SQUASHINHBTR.
ProDom PD003401; Prot_inh_squash; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00286; PTI; 1.
SMART graphical view of domain structure.
PROSITE PS00286; SQUASH_INHIBITOR; 1.
BLOCKS P01074.
Other
LinkHub P01074; -.
ProtoNet P01074.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Knottin; Protease inhibitor; Secreted; Serine protease inhibitor.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
PEPTIDE   1   29  29     Trypsin inhibitor 1. PRO_0000044376
SITE   5    6  2     Reactive bond. 
DISULFID   3   20         
DISULFID   10   22         
DISULFID   16   28         
HELIX   13   15  3      
STRAND   26   28  3      
Sequence information
Length: 29 AA [This is the length of the unprocessed precursor] Molecular weight: 3275 Da [This is the MW of the unprocessed precursor] CRC64: CD509120BA52C01F [This is a checksum on the sequence]
        10         20 
RVCPRILMEC KKDSDCLAEC VCLEHGYCG 

P01074 in FASTA format

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