ID ITR3_CYCPE Reviewed; 29 AA. AC P83394; P83392; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 22-JUL-2008, entry version 41. DE RecName: Full=Trypsin inhibitor 3; DE AltName: Full=Trypsin inhibitor III; DE AltName: Full=CyPTI-III; DE Contains: DE RecName: Full=Trypsin inhibitor 1; DE AltName: Full=Trypsin inhibitor I; DE AltName: Full=CyPTI-I; OS Cyclanthera pedata (Achocha) (Caihua). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Cucurbitales; Cucurbitaceae; Cyclanthera. OX NCBI_TaxID=198836; RN [1] RP PROTEIN SEQUENCE, AND REACTIVE SITE. RC TISSUE=Seed; RX PubMed=14515156; RA Polanowski A., Wilimowska-Pelc A., Kowalska J., Grybel J., Zelazko M., RA Wilusz T.; RT "Non-conventional affinity chromatography of serine proteinases and RT their inhibitors."; RL Acta Biochim. Pol. 50:765-773(2003). CC -!- FUNCTION: Inhibits trypsin. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot' CC structurally defines this protein as a knottin (By similarity). CC -!- SIMILARITY: Belongs to the protease inhibitor I7 (squash-type CC serine protease inhibitor) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR HSSP; P01074; 1CTI. DR InterPro; IPR000737; Prot_inh_squash. DR Pfam; PF00299; Squash; 1. DR PRINTS; PR00293; SQUASHINHBTR. DR ProDom; PD003401; Prot_inh_squash; 1. DR SMART; SM00286; PTI; 1. DR PROSITE; PS00286; SQUASH_INHIBITOR; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Knottin; Protease inhibitor; Secreted; KW Serine protease inhibitor. FT PEPTIDE 1 29 Trypsin inhibitor 3. FT /FTId=PRO_0000033204. FT PEPTIDE 2 29 Trypsin inhibitor 1. FT /FTId=PRO_0000033205. FT SITE 5 6 Reactive bond. FT DISULFID 3 20 By similarity. FT DISULFID 10 22 By similarity. FT DISULFID 16 28 By similarity. SQ SEQUENCE 29 AA; 3195 MW; D5FEFF8A5FEDCC2F CRC64; RICPRILMEC KADSDCLAQC ICEESGFCG //