KAB2_OLDAF
ID KAB2_OLDAF Reviewed; 210 AA.
AC P58454;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Kalata-B2;
DE Flags: Precursor;
GN Name=OAK4;
OS Oldenlandia affinis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Rubiaceae; Rubioideae; Spermacoceae;
OC Hedyotis-Oldenlandia complex; Oldenlandia.
OX NCBI_TaxID=60225;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11535828; DOI=10.1073/pnas.191366898;
RA Jennings C.V., West J., Waine C., Craik D.J., Anderson M.A.;
RT "Biosynthesis and insecticidal properties of plant cyclotides: the cyclic
RT knotted proteins from Oldenlandia affinis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10614-10619(2001).
RN [2]
RP PROTEIN SEQUENCE OF 67-95; 121-149 AND 175-203.
RX PubMed=10600388; DOI=10.1006/jmbi.1999.3383;
RA Craik D.J., Daly N.L., Bond T., Waine C.;
RT "Plant cyclotides: a unique family of cyclic and knotted proteins that
RT defines the cyclic cystine knot structural motif.";
RL J. Mol. Biol. 294:1327-1336(1999).
RN [3]
RP PROTEIN SEQUENCE OF 67-95; 121-149 AND 175-203, STRUCTURE BY NMR OF 67-95;
RP 121-149 AND 175-203, AND FUNCTION.
RX PubMed=15654741; DOI=10.1021/bi047837h;
RA Jennings C.V., Rosengren K.J., Daly N.L., Plan M.R.R., Stevens J.,
RA Scanlon M.J., Waine C., Norman D.G., Anderson M.A., Craik D.J.;
RT "Isolation, solution structure, and insecticidal activity of kalata B2, a
RT circular protein with a twist: do Mobius strips exist in nature?";
RL Biochemistry 44:851-860(2005).
RN [4]
RP PROTEIN SEQUENCE OF 67-95; 121-149 AND 175-203, MASS SPECTROMETRY, AND
RP MODIFICATION AT TRP-89; TRP-143 AND TRP-197.
RX PubMed=17534989; DOI=10.1002/cbic.200700097;
RA Plan M.R.R., Goeransson U., Clark R.J., Daly N.L., Colgrave M.L.,
RA Craik D.J.;
RT "The cyclotide fingerprint in Oldenlandia affinis: elucidation of
RT chemically modified, linear and novel macrocyclic peptides.";
RL ChemBioChem 8:1001-1011(2007).
CC -!- FUNCTION: Probably participates in a plant defense mechanism.
CC Inhibitory effect on the growth and development of larvae from
CC Helicoverpa punctigera. Has hemolytic activity. {ECO:0000255|PROSITE-
CC ProRule:PRU00395, ECO:0000269|PubMed:15654741}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC -!- PTM: Kalata-B2 is a cyclic peptide which occurs in three forms: with
CC unmodified Trp, with Trp oxidized to form N-formylkynurenine and with
CC Trp oxidized to form kynurenine. Oxidation is enhanced by exposure to
CC sunlight. {ECO:0000269|PubMed:17534989}.
CC -!- MASS SPECTROMETRY: Mass=2955.4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17534989};
CC -!- MASS SPECTROMETRY: Mass=2987.4; Method=Electrospray; Note=With N-
CC formylkynurenine.; Evidence={ECO:0000269|PubMed:17534989};
CC -!- MASS SPECTROMETRY: Mass=2959.4; Method=Electrospray; Note=With
CC kynurenine.; Evidence={ECO:0000269|PubMed:17534989};
CC -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC -!- CAUTION: The oxidation forms of Trp-89, Trp-143 and Trp-197 are subject
CC of controversy and could be the artifactual results of sample handling.
CC {ECO:0000305|PubMed:17534989}.
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; AF393828; AAL05480.1; -; mRNA.
DR PDB; 1PT4; NMR; -; A=179-206.
DR PDB; 2KCH; NMR; -; A=179-206.
DR PDBsum; 1PT4; -.
DR PDBsum; 2KCH; -.
DR AlphaFoldDB; P58454; -.
DR SMR; P58454; -.
DR EvolutionaryTrace; P58454; -.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR InterPro; IPR005535; Cyclotide.
DR InterPro; IPR012324; Cyclotide_moebius_CS.
DR InterPro; IPR036146; Cyclotide_sf.
DR Pfam; PF03784; Cyclotide; 3.
DR SUPFAM; SSF57038; SSF57038; 3.
DR PROSITE; PS51052; CYCLOTIDE; 3.
DR PROSITE; PS60009; CYCLOTIDE_MOEBIUS; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Direct protein sequencing; Disulfide bond;
KW Hemolysis; Knottin; Plant defense; Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..66
FT /id="PRO_0000006620"
FT PEPTIDE 67..95
FT /note="Kalata-B2"
FT /id="PRO_0000006621"
FT PROPEP 96..120
FT /id="PRO_0000006622"
FT PEPTIDE 121..149
FT /note="Kalata-B2"
FT /id="PRO_0000006623"
FT PROPEP 150..174
FT /id="PRO_0000006624"
FT PEPTIDE 175..203
FT /note="Kalata-B2"
FT /id="PRO_0000006625"
FT PROPEP 204..210
FT /id="PRO_0000006626"
FT DISULFID 71..85
FT DISULFID 75..87
FT DISULFID 80..92
FT DISULFID 125..139
FT DISULFID 129..141
FT DISULFID 134..146
FT DISULFID 179..193
FT DISULFID 183..195
FT DISULFID 188..200
FT CROSSLNK 67..95
FT /note="Cyclopeptide (Gly-Asp)"
FT CROSSLNK 121..149
FT /note="Cyclopeptide (Gly-Asp)"
FT CROSSLNK 175..203
FT /note="Cyclopeptide (Gly-Asp)"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1PT4"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:1PT4"
SQ SEQUENCE 210 AA; 22327 MW; C6A0D05D294A6147 CRC64;
MAKFTNCLVL SLLLAAFVGA FGAEFSEADK ATLVNDIAEN IQKEILGEVK TSETVLTMFL
KEMQLKGLPV CGETCFGGTC NTPGCSCTWP ICTRDSLPMR AGGKTSETTL HMFLKEMQLK
GLPVCGETCF GGTCNTPGCS CTWPICTRDS LPMSAGGKTS ETTLHMFLKE MQLKGLPVCG
ETCFGGTCNT PGCSCTWPIC TRDSLPLVAA
