PLY13_ARATH
ID PLY13_ARATH Reviewed; 501 AA.
AC Q93Z04; Q9SV40;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Probable pectate lyase 13;
DE EC=4.2.2.2;
DE AltName: Full=Powdery mildew susceptibility protein;
DE AltName: Full=Powdery mildew-resistant mutant 6;
DE Flags: Precursor;
GN Name=PMR6; OrderedLocusNames=At3g54920; ORFNames=F28P10_100;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF GLY-140 AND PRO-339.
RX PubMed=12215508; DOI=10.1105/tpc.003509;
RA Vogel J.P., Raab T.K., Schiff C., Somerville S.C.;
RT "PMR6, a pectate lyase-like gene required for powdery mildew susceptibility
RT in Arabidopsis.";
RL Plant Cell 14:2095-2106(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Susceptibility factor required for infection by most powdery
CC mildews, but not by unrelated pathogens. Exact function not known, but
CC clearly affects cell wall composition. {ECO:0000269|PubMed:12215508}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
CC oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
CC their non-reducing ends.; EC=4.2.2.2;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. Required for its activity. {ECO:0000250};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 2/5.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed equally in mature leaves, buds, flowers,
CC rosettes and roots. {ECO:0000269|PubMed:12215508}.
CC -!- DOMAIN: The C-terminal domain not found in other pectate lyase-like
CC protein is required for PMR6 function since the pmr6-2 mutation confers
CC resistance by introducing a frameshift in the mature mRNA which
CC eliminates the C-terminal domain.
CC -!- MISCELLANEOUS: Pmr6 mutations are pleiotropic, indicating that PMR6
CC plays a unique role in normal plant growth and development. The
CC increased resistance in mutants is not mediated by the constitutive
CC activation of the SA-dependent or the JA/ethylene-dependent defense
CC pathway.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41092.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF534079; AAM97687.1; -; mRNA.
DR EMBL; AL049655; CAB41092.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79313.1; -; Genomic_DNA.
DR EMBL; AY058870; AAL24257.1; -; mRNA.
DR EMBL; AY074331; AAL67027.1; -; mRNA.
DR EMBL; AY096739; AAM20373.1; -; mRNA.
DR PIR; T06728; T06728.
DR RefSeq; NP_191052.2; NM_115349.6.
DR AlphaFoldDB; Q93Z04; -.
DR SMR; Q93Z04; -.
DR BioGRID; 9973; 3.
DR STRING; 3702.AT3G54920.1; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR iPTMnet; Q93Z04; -.
DR PaxDb; Q93Z04; -.
DR PRIDE; Q93Z04; -.
DR ProteomicsDB; 234687; -.
DR EnsemblPlants; AT3G54920.1; AT3G54920.1; AT3G54920.
DR GeneID; 824657; -.
DR Gramene; AT3G54920.1; AT3G54920.1; AT3G54920.
DR KEGG; ath:AT3G54920; -.
DR Araport; AT3G54920; -.
DR TAIR; locus:2082667; AT3G54920.
DR eggNOG; ENOG502QPY9; Eukaryota.
DR HOGENOM; CLU_026608_0_0_1; -.
DR InParanoid; Q93Z04; -.
DR OMA; GEGMSSM; -.
DR OrthoDB; 924221at2759; -.
DR PhylomeDB; Q93Z04; -.
DR BioCyc; ARA:AT3G54920-MON; -.
DR UniPathway; UPA00545; UER00824.
DR PRO; PR:Q93Z04; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93Z04; baseline and differential.
DR Genevisible; Q93Z04; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030570; F:pectate lyase activity; ISS:TAIR.
DR GO; GO:0042547; P:cell wall modification involved in multidimensional cell growth; IMP:TAIR.
DR GO; GO:0098542; P:defense response to other organism; IMP:TAIR.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR018082; AmbAllergen.
DR InterPro; IPR002022; Pec_lyase.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR045032; PEL.
DR PANTHER; PTHR31683; PTHR31683; 1.
DR Pfam; PF00544; Pectate_lyase_4; 1.
DR PRINTS; PR00807; AMBALLERGEN.
DR SMART; SM00656; Amb_all; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Lyase;
KW Membrane; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..22
FT CHAIN 23..474
FT /note="Probable pectate lyase 13"
FT /id="PRO_0000024877"
FT PROPEP 475..501
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000024878"
FT REGION 55..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 297
FT /evidence="ECO:0000255"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT LIPID 474
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 140
FT /note="G->D: In pmr6-1; strong powdery mildew resistance,
FT cell walls of plants are enriched for pectins with a lower
FT degree of esterification and an alteration in the H bonding
FT environment of cellulose microfibrils."
FT /evidence="ECO:0000269|PubMed:12215508"
FT MUTAGEN 339
FT /note="P->L: In pmr6-5; strong powdery mildew resistance,
FT cell walls of plants are enriched for pectins with a lower
FT degree of esterification and an alteration in the H bonding
FT environment of cellulose microfibrils."
FT /evidence="ECO:0000269|PubMed:12215508"
SQ SEQUENCE 501 AA; 53929 MW; 9E0DE36DEF4C7ABB CRC64;
MLLQNFSNTI FLLCLFFTLL SATKPLNLTL PHQHPSPDSV ALHVIRSVNE SLARRQLSSP
SSSSSSSSSS SSSSCRTGNP IDDCWRCSDA DWSTNRQRLA DCSIGFGHGT LGGKNGKIYV
VTDSSDNNPT NPTPGTLRYG VIQEEPLWIV FSSNMLIRLK QELIINSYKT LDGRGSAVHI
TGNGCLTLQY VQHIIIHNLH IYDCKPSAGF EKRGRSDGDG ISIFGSQKIW VDHCSMSHCT
DGLIDAVMGS TAITISNNYF THHDEVMLLG HDDNYAPDTG MQVTIAFNHF GQGLVQRMPR
CRRGYIHVVN NDFTEWKMYA IGGSGNPTIN SQGNRYSAPS DPSAKEVTKR VDSKDDGEWS
NWNWRTEGDL MENGAFFVAS GEGMSSMYSK ASSVDPKAAS LVDQLTRNAG VFGGPRDDQG
QSGNSYSPYG GDGGGGGSSG GSSGGGMDVM GGTTRGSSSS SGDDSNVFQM IFGSDAPSRP
RLTLLFSLLM ISVLSLSTLL L
