KWL1_MAIZE
ID KWL1_MAIZE Reviewed; 198 AA.
AC A0A1D6GNR3;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Kiwellin-1 {ECO:0000305};
DE Short=ZmKWL1 {ECO:0000303|PubMed:30651637};
DE Flags: Precursor;
GN Name=KWL1 {ECO:0000303|PubMed:30651637};
GN ORFNames=ZEAMMB73_Zm00001d013945 {ECO:0000312|EMBL:AQK64854.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 33-198, DISULFIDE BONDS,
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, INTERACTION WITH USTILAGO MAYDIS CMU1, AND INDUCTION BY USTILAGO
RP MAYDIS.
RX PubMed=30651637; DOI=10.1038/s41586-018-0857-9;
RA Han X., Altegoer F., Steinchen W., Binnebesel L., Schuhmacher J.,
RA Glatter T., Giammarinaro P.I., Djamei A., Rensing S.A., Reissmann S.,
RA Kahmann R., Bange G.;
RT "A kiwellin disarms the metabolic activity of a secreted fungal virulence
RT factor.";
RL Nature 565:650-653(2019).
CC -!- FUNCTION: Specifically blocks the catalytic activity of the chorismate
CC mutase Cmu1 from the fungal pathogen Ustilago maydis. Hinders substrate
CC access to the active site of Cmu1 through intimate interactions
CC (PubMed:30651637). A structural feature specific to the fungal secreted
CC Cmu1 called extensive loop region (ELR) is required for the intimate
CC interaction (PubMed:30651637). Does not interact with its own
CC chorismate mutases (PubMed:30651637). The secreted fungal Cmu1
CC presumably affects biosynthesis of the plant immune signal salicylic
CC acid by channelling chorismate into the phenylpropanoid pathway
CC (PubMed:30651637). {ECO:0000269|PubMed:30651637}.
CC -!- SUBUNIT: Monomer (PubMed:30651637). Interacts with Cmu1 of the fungal
CC pathogen Ustilago maydis (PubMed:30651637). A structural feature
CC specific to the fungal secreted Cmu1 called extensive loop region (ELR)
CC is required for the intimate interaction (PubMed:30651637). Does not
CC interact with its own chorismate mutases (PubMed:30651637).
CC {ECO:0000269|PubMed:30651637}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:30651637}.
CC -!- INDUCTION: Induced by the fungal pathogen Ustilago maydis.
CC {ECO:0000305|PubMed:30651637}.
CC -!- SIMILARITY: Belongs to the kiwellin family. {ECO:0000305}.
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DR EMBL; CM000781; AQK64854.1; -; Genomic_DNA.
DR RefSeq; XP_008644746.1; XM_008646524.1.
DR PDB; 6FPG; X-ray; 1.80 A; D/E/H/I=33-198.
DR PDBsum; 6FPG; -.
DR AlphaFoldDB; A0A1D6GNR3; -.
DR SMR; A0A1D6GNR3; -.
DR STRING; 4577.GRMZM2G073114_P01; -.
DR EnsemblPlants; Zm00001eb221000_T001; Zm00001eb221000_P001; Zm00001eb221000.
DR GeneID; 103626138; -.
DR Gramene; Zm00001eb221000_T001; Zm00001eb221000_P001; Zm00001eb221000.
DR KEGG; zma:103626138; -.
DR OMA; NGSECCK; -.
DR OrthoDB; 1360754at2759; -.
DR SABIO-RK; A0A1D6GNR3; -.
DR Proteomes; UP000007305; Chromosome 5.
DR ExpressionAtlas; A0A1D6GNR3; baseline and differential.
DR GO; GO:0048046; C:apoplast; IDA:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:PHI-base.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0051851; P:modulation by host of symbiont process; IDA:PHI-base.
DR Gene3D; 2.40.40.10; -; 1.
DR InterPro; IPR039271; Kiwellin-like.
DR InterPro; IPR036908; RlpA-like_sf.
DR PANTHER; PTHR33191; PTHR33191; 1.
DR SUPFAM; SSF50685; SSF50685; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoplast; Disulfide bond; Glycoprotein; Plant defense;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..198
FT /note="Kiwellin-1"
FT /id="PRO_5010804478"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 42..75
FT /evidence="ECO:0000269|PubMed:30651637,
FT ECO:0007744|PDB:6FPG"
FT DISULFID 55..63
FT /evidence="ECO:0000269|PubMed:30651637,
FT ECO:0007744|PDB:6FPG"
FT DISULFID 64..157
FT /evidence="ECO:0000269|PubMed:30651637,
FT ECO:0007744|PDB:6FPG"
FT DISULFID 104..129
FT /evidence="ECO:0000269|PubMed:30651637,
FT ECO:0007744|PDB:6FPG"
FT DISULFID 151..167
FT /evidence="ECO:0000269|PubMed:30651637,
FT ECO:0007744|PDB:6FPG"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:6FPG"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6FPG"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:6FPG"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:6FPG"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:6FPG"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:6FPG"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:6FPG"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:6FPG"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:6FPG"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6FPG"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:6FPG"
SQ SEQUENCE 198 AA; 20849 MW; 48D2AA065F47716C CRC64;
MATVGGNRAL YAVVALPLLA TLLHGPMRLS HAFPYRSLLQ TCQPSGSIQG RSGNCNTENG
SECCKNGRRY TTYGCSPPVT GSTRAVLTLN SFAEGGDGGG AAACTGKFYD DSKKVVALST
GWYNGGSRCR KHIMIHAGNG NSVSALVVDE CDSTVGCDKD HNFEPPCRNN IVDGSPAVWD
ALGLNKDDGQ AQITWSDE
