ID CYCA_PETHY Reviewed; 79 AA. AC B3EWH5; DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 1. DT 16-OCT-2013, entry version 3. DE RecName: Full=Cyclotide phyb-A; DE Flags: Precursor; OS Petunia hybrida (Petunia). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia. OX NCBI_TaxID=4102; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Flower; RX DOI=10.1016/j.plantsci.2007.07.011; RA Shimamura K., Ishimizu T., Nishimura K., Matsubara K., Kodama H., RA Watanabe H., Hase S., Ando T.; RT "Analysis of expressed sequence tags from Petunia flowers."; RL Plant Sci. 173:495-500(2007). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-79. RC TISSUE=Root; RX PubMed=21143680; DOI=10.1111/j.1365-313X.2010.04385.x; RA Breuillin F., Schramm J., Hajirezaei M., Ahkami A., Favre P., RA Druege U., Hause B., Bucher M., Kretzschmar T., Bossolini E., RA Kuhlemeier C., Martinoia E., Franken P., Scholz U., Reinhardt D.; RT "Phosphate systemically inhibits development of arbuscular mycorrhiza RT in Petunia hybrida and represses genes involved in mycorrhizal RT functioning."; RL Plant J. 64:1002-1017(2010). RN [3] RP PROTEIN SEQUENCE OF 44-73, TISSUE SPECIFICITY, DOMAIN, DISULFIDE RP BONDS, CYCLIZATION, AND MASS SPECTROMETRY. RC TISSUE=Leaf; RX PubMed=22700981; DOI=10.1074/jbc.M112.370841; RA Poth A.G., Mylne J.S., Grassl J., Lyons R.E., Millar A.H., RA Colgrave M.L., Craik D.J.; RT "Cyclotides associate with leaf vasculature and are the products of a RT novel precursor in Petunia (Solanaceae)."; RL J. Biol. Chem. 287:27033-27046(2012). CC -!- FUNCTION: Probably participates in a plant defense mechanism (By CC similarity). CC -!- TISSUE SPECIFICITY: Expressed in midvein, lamina and periphery of CC leaves (at protein level). CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot' CC structurally defines this protein as a knottin. CC -!- PTM: This is a cyclic peptide. CC -!- PTM: Contains 3 disulfide bonds. CC -!- MASS SPECTROMETRY: Mass=3068.29; Method=MALDI; Range=44-73; CC Source=PubMed:22700981; CC -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DC242826; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; FN035504; -; NOT_ANNOTATED_CDS; mRNA. DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW. DR InterPro; IPR005535; Cyclotide. DR InterPro; IPR012323; Cyclotide_bracelet_CS. DR Pfam; PF03784; Cyclotide; 1. DR SUPFAM; SSF57038; SSF57038; 1. DR PROSITE; PS51052; CYCLOTIDE; 1. DR PROSITE; PS60008; CYCLOTIDE_BRACELET; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Knottin; Plant defense. FT PROPEP 1 43 FT /FTId=PRO_0000419342. FT PEPTIDE 44 73 Cyclotide phyb-A. FT /FTId=PRO_0000419343. FT PROPEP 74 79 FT /FTId=PRO_0000419344. FT DISULFID 47 63 By similarity. FT DISULFID 51 65 By similarity. FT DISULFID 56 70 By similarity. FT CROSSLNK 44 73 Cyclopeptide (Gly-Asn). SQ SEQUENCE 79 AA; 8575 MW; A87780D3F04DA664 CRC64; MVGVNSLRSA LYLIVLILFV QLTYFSDARV MDVDLSRAFL PLTGIGCGES CVWIPCVSAA IGCSCSNKIC YRNGIIPKK //