TBL44_ARATH
ID TBL44_ARATH Reviewed; 402 AA.
AC Q9LUZ6; F4KGA2; Q8LEB9;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Protein PMR5;
DE AltName: Full=Powdery mildew resistance protein 5;
DE AltName: Full=Protein trichome birefringence-like 44;
GN Name=PMR5; Synonyms=TBL44; OrderedLocusNames=At5g58600; ORFNames=MZN1.6;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15584961; DOI=10.1111/j.1365-313x.2004.02264.x;
RA Vogel J.P., Raab T.K., Somerville C.R., Somerville S.C.;
RT "Mutations in PMR5 result in powdery mildew resistance and altered cell
RT wall composition.";
RL Plant J. 40:968-978(2004).
RN [7]
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=17316173; DOI=10.1111/j.1365-313x.2006.02994.x;
RA Xin Z., Mandaokar A., Chen J., Last R.L., Browse J.;
RT "Arabidopsis ESK1 encodes a novel regulator of freezing tolerance.";
RL Plant J. 49:786-799(2007).
RN [8]
RP FUNCTION.
RX PubMed=19810803; DOI=10.1094/mpmi-22-11-1331;
RA Maeda K., Houjyou Y., Komatsu T., Hori H., Kodaira T., Ishikawa A.;
RT "AGB1 and PMR5 contribute to PEN2-mediated preinvasion resistance to
RT Magnaporthe oryzae in Arabidopsis thaliana.";
RL Mol. Plant Microbe Interact. 22:1331-1340(2009).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20388664; DOI=10.1104/pp.110.153320;
RA Bischoff V., Nita S., Neumetzler L., Schindelasch D., Urbain A., Eshed R.,
RA Persson S., Delmer D., Scheible W.R.;
RT "TRICHOME BIREFRINGENCE and its homolog AT5G01360 encode plant-specific
RT DUF231 proteins required for cellulose biosynthesis in Arabidopsis.";
RL Plant Physiol. 153:590-602(2010).
RN [10]
RP 3D-STRUCTURE MODELING.
RX PubMed=20657172; DOI=10.4161/psb.5.8.12414;
RA Bischoff V., Selbig J., Scheible W.R.;
RT "Involvement of TBL/DUF231 proteins into cell wall biology.";
RL Plant Signal. Behav. 5:1057-1059(2010).
CC -!- FUNCTION: Required for nonhost resistance (NHR) during plant-microbe
CC interactions. Plants mutated in PMR5 are resistant to powdery mildew
CC species (PubMed:15584961, PubMed:19810803). May act as a bridging
CC protein that binds pectin and other cell wall polysaccharides. Probably
CC involved in maintaining esterification of pectins (By similarity). May
CC be involved in the specific O-acetylation of cell wall polymers (By
CC similarity). {ECO:0000250|UniProtKB:Q9FG35,
CC ECO:0000250|UniProtKB:Q9LY46, ECO:0000269|PubMed:15584961,
CC ECO:0000269|PubMed:19810803}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LUZ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LUZ6-2; Sequence=VSP_053700, VSP_053701;
CC -!- TISSUE SPECIFICITY: Expressed in flowers, siliques, stems and leaves.
CC {ECO:0000269|PubMed:15584961}.
CC -!- MISCELLANEOUS: Contains 2 motifs that are conserved in esterases, but
CC it is unlikely that this protein belongs to the catalytically active
CC pectin esterases. {ECO:0000305|PubMed:20657172}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
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; AB020755; BAA97330.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97074.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97075.1; -; Genomic_DNA.
DR EMBL; AK117382; BAC42051.1; -; mRNA.
DR EMBL; BT005096; AAO50629.1; -; mRNA.
DR EMBL; AY085512; AAM62736.1; -; mRNA.
DR RefSeq; NP_200668.1; NM_125247.4. [Q9LUZ6-1]
DR RefSeq; NP_974961.1; NM_203232.2. [Q9LUZ6-2]
DR AlphaFoldDB; Q9LUZ6; -.
DR SMR; Q9LUZ6; -.
DR STRING; 3702.AT5G58600.1; -.
DR PaxDb; Q9LUZ6; -.
DR PRIDE; Q9LUZ6; -.
DR ProteomicsDB; 234266; -. [Q9LUZ6-1]
DR EnsemblPlants; AT5G58600.1; AT5G58600.1; AT5G58600. [Q9LUZ6-1]
DR EnsemblPlants; AT5G58600.2; AT5G58600.2; AT5G58600. [Q9LUZ6-2]
DR GeneID; 835974; -.
DR Gramene; AT5G58600.1; AT5G58600.1; AT5G58600. [Q9LUZ6-1]
DR Gramene; AT5G58600.2; AT5G58600.2; AT5G58600. [Q9LUZ6-2]
DR KEGG; ath:AT5G58600; -.
DR Araport; AT5G58600; -.
DR TAIR; locus:2178813; AT5G58600.
DR eggNOG; ENOG502QR9P; Eukaryota.
DR HOGENOM; CLU_020953_3_0_1; -.
DR InParanoid; Q9LUZ6; -.
DR OMA; PDQSADC; -.
DR OrthoDB; 663648at2759; -.
DR PhylomeDB; Q9LUZ6; -.
DR PRO; PR:Q9LUZ6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LUZ6; baseline and differential.
DR Genevisible; Q9LUZ6; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016413; F:O-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009620; P:response to fungus; IMP:TAIR.
DR InterPro; IPR026057; PC-Esterase.
DR InterPro; IPR029981; PMR5.
DR InterPro; IPR029962; TBL.
DR InterPro; IPR025846; TBL_N.
DR PANTHER; PTHR32285; PTHR32285; 1.
DR PANTHER; PTHR32285:SF14; PTHR32285:SF14; 1.
DR Pfam; PF13839; PC-Esterase; 1.
DR Pfam; PF14416; PMR5N; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Membrane; Plant defense; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..402
FT /note="Protein PMR5"
FT /id="PRO_0000425409"
FT TRANSMEM 7..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT REGION 40..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 140..142
FT /note="GDS motif"
FT MOTIF 379..393
FT /note="DCXHWCLPGXXDXWN motif"
FT VAR_SEQ 291
FT /note="N -> K (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053700"
FT VAR_SEQ 292..402
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053701"
FT CONFLICT 20
FT /note="V -> L (in Ref. 5; AAM62736)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="N -> K (in Ref. 5; AAM62736)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 44833 MW; 4798874F20E76CB9 CRC64;
MGSLLPLLGI SVVSAIFFLV LQQPEQSSSA IILSLKKRHG SSSGSSGNQY SSSRPSAGFQ
GNRSTCSLFL GTWVRDNSYP LYKPADCPGV VEPEFDCQMY GRPDSDYLKY RWQPQNCNLP
TFNGAQFLLK MKGKTIMFAG DSLGKNQWES LICLIVSSAP STRTEMTRGL PLSTFRFLDY
GITMSFYKAP FLVDIDAVQG KRVLKLDEIS GNANAWHDAD LLIFNTGHWW SHTGSMQGWD
LIQSGNSYYQ DMDRFVAMEK ALRTWAYWVE THVDRSRTQV LFLSISPTHD NPSDWAASSS
SGSKNCYGET EPITGTAYPV SSYTDQLRSV IVEVLHGMHN PAFLLDITLL SSLRKDGHPS
VYSGLISGSQ RSRPDQSADC SHWCLPGLPD TWNQLLYTLL IY
