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PLY18_ARATH
ID   PLY18_ARATH             Reviewed;         408 AA.
AC   Q9C5M8; O23667; Q8LAW7; Q9SB71;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Probable pectate lyase 18;
DE            EC=4.2.2.2;
DE   AltName: Full=Pectate lyase A10;
DE   Flags: Precursor;
GN   OrderedLocusNames=At4g24780; ORFNames=F22K18.20;
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 [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-298, 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   -!- 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=AAM65103.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA22985.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79388.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL035356; CAA22985.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161562; CAB79388.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84955.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84956.1; -; Genomic_DNA.
DR   EMBL; AF360140; AAK25850.1; -; mRNA.
DR   EMBL; AY087561; AAM65103.1; ALT_INIT; mRNA.
DR   EMBL; U83621; AAB69761.1; -; Genomic_DNA.
DR   PIR; T05556; T05556.
DR   RefSeq; NP_001190827.1; NM_001203898.1.
DR   RefSeq; NP_567707.1; NM_118611.3.
DR   AlphaFoldDB; Q9C5M8; -.
DR   SMR; Q9C5M8; -.
DR   BioGRID; 13869; 2.
DR   STRING; 3702.AT4G24780.1; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PaxDb; Q9C5M8; -.
DR   PRIDE; Q9C5M8; -.
DR   ProteomicsDB; 234733; -.
DR   EnsemblPlants; AT4G24780.1; AT4G24780.1; AT4G24780.
DR   EnsemblPlants; AT4G24780.2; AT4G24780.2; AT4G24780.
DR   GeneID; 828580; -.
DR   Gramene; AT4G24780.1; AT4G24780.1; AT4G24780.
DR   Gramene; AT4G24780.2; AT4G24780.2; AT4G24780.
DR   KEGG; ath:AT4G24780; -.
DR   Araport; AT4G24780; -.
DR   TAIR; locus:2121914; AT4G24780.
DR   eggNOG; ENOG502QQ5F; Eukaryota.
DR   HOGENOM; CLU_026608_0_1_1; -.
DR   InParanoid; Q9C5M8; -.
DR   OMA; NHFGWRT; -.
DR   OrthoDB; 924221at2759; -.
DR   PhylomeDB; Q9C5M8; -.
DR   BioCyc; ARA:AT4G24780-MON; -.
DR   UniPathway; UPA00545; UER00824.
DR   PRO; PR:Q9C5M8; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9C5M8; baseline and differential.
DR   Genevisible; Q9C5M8; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
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   GO; GO:0009624; P:response to nematode; IMP:TAIR.
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   Calcium; Glycoprotein; Lyase; Metal-binding; Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..408
FT                   /note="Probable pectate lyase 18"
FT                   /id="PRO_0000024883"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000255"
FT   BINDING         206
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        107
FT                   /note="D -> Y (in Ref. 4; AAM65103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        252
FT                   /note="H -> R (in Ref. 5; AAB69761)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271
FT                   /note="Q -> H (in Ref. 3; AAK25850)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="H -> D (in Ref. 4; AAM65103)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   408 AA;  45014 MW;  4117CB52C48E588C CRC64;
     MKMQTKKLFI TIVSFLLYAP LFLSSPVPDP ESVVEEVHKS INASVAGRRK LGYLSCTTGN
     PIDDCWRCDP HWEQHRQRLA DCAIGFGKNA IGGRDGRIYV VTDSGNDNPV SPKPGTLRHA
     VVQDEPLWII FQRDMTIQLK EELIMNSFKT IDGRGASVHI SGGPCITIQY VTNIIIHGIH
     IHDCKQGGNA MVRSSPRHFG WRTISDGDGV SIFGGSHVWV DHCSFSNCED GLIDAIMGST
     AITLSNNHMT HHDKVMLLGH SDTYSRDKNM QVTIAFNHFG EGLVQRMPRC RHGYFHVVNN
     DYTHWEMYAI GGSANPTINS QGNRFLAPNI RFSKEVTKHE DAPESEWKRW NWRSSGDLLL
     NGAFFTPSGG AASSSYAKAS SLGAKPSSLV GPLTSTSGAL NCRKGSRC
 
 
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