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ITR5_SECED
ID   ITR5_SECED              Reviewed;          27 AA.
AC   P84452;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Trypsin inhibitor 5;
DE   AltName: Full=SETI-V;
DE   AltName: Full=Trypsin inhibitor V;
OS   Sechium edule (Chayote) (Sicyos edulis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Sicyoeae; Sicyos.
OX   NCBI_TaxID=184140;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Seed;
RX   PubMed=16406091; DOI=10.1016/j.phytochem.2005.11.016;
RA   Laure H.J., Faca V.M., Lzumi C., Padovan J.C., Greene L.J.;
RT   "Low molecular weight squash trypsin inhibitors from Sechium edule seeds.";
RL   Phytochemistry 67:362-370(2006).
CC   -!- FUNCTION: Inhibits trypsin. {ECO:0000269|PubMed:16406091}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=2990.5; Mass_error=0.1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16406091};
CC   -!- SIMILARITY: Belongs to the protease inhibitor I7 (squash-type serine
CC       protease inhibitor) family. {ECO:0000305}.
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DR   AlphaFoldDB; P84452; -.
DR   SMR; P84452; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000737; Prot_inh_squash.
DR   InterPro; IPR011052; Proteinase_amylase_inhib_sf.
DR   Pfam; PF00299; Squash; 1.
DR   SUPFAM; SSF57027; SSF57027; 1.
DR   PROSITE; PS00286; SQUASH_INHIBITOR; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Knottin; Protease inhibitor;
KW   Secreted; Serine protease inhibitor.
FT   PEPTIDE         1..27
FT                   /note="Trypsin inhibitor 5"
FT                   /id="PRO_0000044392"
FT   SITE            3..4
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000305"
FT   DISULFID        1..18
FT                   /evidence="ECO:0000250|UniProtKB:P12071"
FT   DISULFID        8..20
FT                   /evidence="ECO:0000250|UniProtKB:P12071"
FT   DISULFID        14..26
FT                   /evidence="ECO:0000250|UniProtKB:P12071"
SQ   SEQUENCE   27 AA;  2997 MW;  6F8F96B38BAF7139 CRC64;
     CPRILMKCKL DTDCFPTCTC RPSGFCG
 
 
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