PLY15_ARATH
ID PLY15_ARATH Reviewed; 470 AA.
AC Q944R1; O23668; Q9SVP1;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable pectate lyase 15;
DE EC=4.2.2.2;
DE AltName: Full=Pectate lyase A11;
DE Flags: Precursor;
GN OrderedLocusNames=At4g13710; ORFNames=F18A5.100;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-361, AND TISSUE SPECIFICITY.
RX PubMed=9278171; DOI=10.1023/a:1005856531693;
RA Kulikauskas R., McCormick S.;
RT "Identification of the tobacco and Arabidopsis homologues of the pollen-
RT expressed LAT59 gene of tomato.";
RL Plant Mol. Biol. 34:809-814(1997).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q944R1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in flowers, but not in leaves.
CC {ECO:0000269|PubMed:9278171}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36835.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78413.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035528; CAB36835.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161537; CAB78413.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83315.1; -; Genomic_DNA.
DR EMBL; AF424592; AAL11586.1; -; mRNA.
DR EMBL; AY142013; AAM98277.1; -; mRNA.
DR EMBL; U83622; AAB69762.1; -; Genomic_DNA.
DR PIR; H85148; H85148.
DR PIR; T05240; T05240.
DR RefSeq; NP_567409.1; NM_117445.3. [Q944R1-1]
DR AlphaFoldDB; Q944R1; -.
DR SMR; Q944R1; -.
DR BioGRID; 12302; 1.
DR STRING; 3702.AT4G13710.1; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR PaxDb; Q944R1; -.
DR PRIDE; Q944R1; -.
DR ProteomicsDB; 234883; -. [Q944R1-1]
DR EnsemblPlants; AT4G13710.1; AT4G13710.1; AT4G13710. [Q944R1-1]
DR GeneID; 827005; -.
DR Gramene; AT4G13710.1; AT4G13710.1; AT4G13710. [Q944R1-1]
DR KEGG; ath:AT4G13710; -.
DR Araport; AT4G13710; -.
DR TAIR; locus:2005487; AT4G13710.
DR eggNOG; ENOG502QQ5F; Eukaryota.
DR InParanoid; Q944R1; -.
DR PhylomeDB; Q944R1; -.
DR BioCyc; ARA:AT4G13710-MON; -.
DR UniPathway; UPA00545; UER00824.
DR PRO; PR:Q944R1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q944R1; baseline and differential.
DR Genevisible; Q944R1; AT.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Glycoprotein; Lyase; Metal-binding;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..470
FT /note="Probable pectate lyase 15"
FT /id="PRO_0000024880"
FT ACT_SITE 348
FT /evidence="ECO:0000255"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 135..137
FT /note="HKN -> AQE (in Ref. 4; AAB69762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 51936 MW; 141373708998B95B CRC64;
MASSSQKLIS VCVAVLVVLA LTAMIFRNSE ISLSRKLKTE VIQSSNSSTM AAIRKLKTEE
FQSLNSSTMA ATRLDGEPQQ QQHAVADDPD MVADEVAKLV QMSEQNRTAR RKLGFFSCGT
GNPIDDCWRC DRNWHKNRKR LADCGIGFGR NAIGGRDGRF YIVTDPTDED VVNPKPGTLR
HAVIQEEPLW IVFKRDMVIE LKQELIMNSF KTIDARGSNV HIANGACITI QFITNVIIHG
LHIHDCKPTG NAMVRSSPSH FGWRTMADGD AVSIFGSSHI WIDHNSLSHC ADGLVDAVMG
STAITVSNNH FTHHNEVMLL GHSDSYTKDK LMQVTIAYNH FGEGLVQRMP RCRHGYFHVV
NNDYTHWEMY AIGGSAEPTI NSQGNRYAAP MDRFAKEVTK RVETDASEWK KWNWRSEGDL
LLNGAFFRPS GAGASASYGR ASSLAAKPSS MVDTITSTAG ALGCRKGRPC
