(data stored in SCRATCH zone)

SWISSPROT: GPDL3_ARATH

ID   GPDL3_ARATH             Reviewed;         759 AA.
AC   Q9SZ11; Q93ZT1;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 3.
DT   11-DEC-2019, entry version 126.
DE   RecName: Full=Glycerophosphodiester phosphodiesterase GDPDL3 {ECO:0000305};
DE            EC=3.1.4.46 {ECO:0000250|UniProtKB:Q7Y208};
DE   AltName: Full=Glycerophosphodiester phosphodiesterase-like 3 {ECO:0000303|PubMed:21323773};
DE            Short=ATGDPDL3 {ECO:0000303|PubMed:21323773};
DE   AltName: Full=Glycerophosphodiesterase-like 2 {ECO:0000303|PubMed:18718934};
DE   AltName: Full=Protein MUTANT ROOT HAIR 5 {ECO:0000303|PubMed:16367956};
DE   AltName: Full=Protein SHAVEN 3 {ECO:0000303|PubMed:18718934};
DE   Flags: Precursor;
GN   Name=GDPDL3 {ECO:0000303|PubMed:21323773};
GN   Synonyms=GPDL2 {ECO:0000303|PubMed:18718934},
GN   MRH5 {ECO:0000303|PubMed:16367956}, SHV3 {ECO:0000303|PubMed:18718934};
GN   OrderedLocusNames=At4g26690; ORFNames=F10M23.30;
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   DISRUPTION PHENOTYPE.
RX   PubMed=16367956; DOI=10.1111/j.1365-313x.2005.02609.x;
RA   Jones M.A., Raymond M.J., Smirnoff N.;
RT   "Analysis of the root-hair morphogenesis transcriptome reveals the
RT   molecular identity of six genes with roles in root-hair development in
RT   Arabidopsis.";
RL   Plant J. 45:83-100(2006).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=18718934; DOI=10.1093/pcp/pcn120;
RA   Hayashi S., Ishii T., Matsunaga T., Tominaga R., Kuromori T., Wada T.,
RA   Shinozaki K., Hirayama T.;
RT   "The glycerophosphoryl diester phosphodiesterase-like proteins SHV3 and its
RT   homologs play important roles in cell wall organization.";
RL   Plant Cell Physiol. 49:1522-1535(2008).
RN   [6]
RP   TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=21323773; DOI=10.1111/j.1365-313x.2011.04538.x;
RA   Cheng Y., Zhou W., El Sheery N.I., Peters C., Li M., Wang X., Huang J.;
RT   "Characterization of the Arabidopsis glycerophosphodiester
RT   phosphodiesterase (GDPD) family reveals a role of the plastid-localized
RT   AtGDPD1 in maintaining cellular phosphate homeostasis under phosphate
RT   starvation.";
RL   Plant J. 66:781-795(2011).
CC   -!- FUNCTION: Involved in primary cell wall organization. Required for the
CC       accumulation of crystalline cellulose. {ECO:0000269|PubMed:18718934}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a sn-glycero-3-phosphoester + H2O = an alcohol + H(+) + sn-
CC         glycerol 3-phosphate; Xref=Rhea:RHEA:12969, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:57597,
CC         ChEBI:CHEBI:83408; EC=3.1.4.46;
CC         Evidence={ECO:0000250|UniProtKB:Q7Y208};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18718934};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, shoots, rosette and cauline
CC       leaves, stems, flowers and siliques. {ECO:0000269|PubMed:18718934,
CC       ECO:0000269|PubMed:21323773}.
CC   -!- DISRUPTION PHENOTYPE: Defective in root hair formation
CC       (PubMed:16367956, PubMed:18718934). This phenotype is partially
CC       suppressed by application of exogenous borate (PubMed:18718934).
CC       {ECO:0000269|PubMed:16367956, ECO:0000269|PubMed:18718934}.
CC   -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB36515.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79524.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AL035440; CAB36515.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161565; CAB79524.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85238.1; -; Genomic_DNA.
DR   EMBL; AY056280; AAL07129.1; -; mRNA.
DR   PIR; T04792; T04792.
DR   RefSeq; NP_567755.1; NM_118803.5.
DR   SMR; Q9SZ11; -.
DR   STRING; 3702.AT4G26690.1; -.
DR   PaxDb; Q9SZ11; -.
DR   PRIDE; Q9SZ11; -.
DR   EnsemblPlants; AT4G26690.1; AT4G26690.1; AT4G26690.
DR   GeneID; 828776; -.
DR   Gramene; AT4G26690.1; AT4G26690.1; AT4G26690.
DR   KEGG; ath:AT4G26690; -.
DR   Araport; AT4G26690; -.
DR   TAIR; locus:2116377; AT4G26690.
DR   eggNOG; KOG2258; Eukaryota.
DR   eggNOG; COG0584; LUCA.
DR   HOGENOM; HOG000239205; -.
DR   InParanoid; Q9SZ11; -.
DR   OMA; YKLNSCM; -.
DR   OrthoDB; 211520at2759; -.
DR   PRO; PR:Q9SZ11; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SZ11; baseline and differential.
DR   Genevisible; Q9SZ11; AT.
DR   GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IBA:GO_Central.
DR   GO; GO:0009932; P:cell tip growth; IMP:TAIR.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0010442; P:guard cell morphogenesis; IGI:TAIR.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   GO; GO:0052541; P:plant-type cell wall cellulose metabolic process; IGI:TAIR.
DR   GO; GO:0010053; P:root epidermal cell differentiation; IMP:TAIR.
DR   GO; GO:0048765; P:root hair cell differentiation; IMP:TAIR.
DR   GO; GO:0010026; P:trichome differentiation; IGI:TAIR.
DR   Gene3D; 3.20.20.190; -; 2.
DR   InterPro; IPR030395; GP_PDE_dom.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   Pfam; PF03009; GDPD; 1.
DR   SUPFAM; SSF51695; SSF51695; 2.
DR   PROSITE; PS51704; GP_PDE; 2.
PE   2: Evidence at transcript level;
DR   PRODOM; Q9SZ11.
DR   SWISS-2DPAGE; Q9SZ11.
KW   Cell membrane; Cell wall biogenesis/degradation; Glycerol metabolism;
KW   Glycoprotein; Hydrolase; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..759
FT                   /note="Glycerophosphodiester phosphodiesterase GDPDL3"
FT                   /id="PRO_0000012599"
FT   TOPO_DOM        28..738
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        739..759
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          44..344
FT                   /note="GP-PDE 1"
FT   DOMAIN          360..661
FT                   /note="GP-PDE 2"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        413
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        424
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        488
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        540
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        647
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        148
FT                   /note="E -> K (in Ref. 3; AAL07129)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   759 AA;  82562 MW;  C20B45292AD1B068 CRC64;
     MRGLLRASSL LLCGVILIQL LAAQIHAQSK KPKSPWPTLT GDPPLVIARG GFSGLFPDSS
     YDAYNFAILT SVPDAVLWCD VQLTKDALGI CFPDLTMRNS SSIEAVYPTR QKSYPVNGVP
     TSGWFTIDFS LKDLKDVNLI RGILSRSEKF DGNSNPIMTV QSVSTQMKPS FFWLNVQHDA
     FYAQHNLSMS SFLVAASKTV LIDFISSPEV NFFKKIAGRF GRNGPSLVFR FLGQDEFEPT
     TNRTYGSILS NLTFVKTFAS GILVPKSYIL PLDDQQYLLP HTSLVQDAHK AGLEVFVSGF
     ANDIDIAHDY SFDPVSEYLS FVDNGNFSVD GVLSDFPITA SASLDCFSHV GRNATKQVDF
     LVITKDGASG DYPGCTDLAY KKAIKDGADV IDCSVQLSSD GTPFCLSSID LGNSTTVSLT
     AFRNRSTTVP ELGSLGAIYT FSLTWAEIQT LTPAISNPYR VTSLFRNPKQ KNAGKLFSLS
     DFLSLAKNST SLSGVLISVE NAAYLREEQG LDVVKAVLDT LTQTGYSNST ATKVMIQSTN
     SSVLVDFKKQ SQYETVYKVE ENIRDILDSA IEDIKKFADA VVIQKLSVFP VAQSFITTQT
     NVVEKLQKSQ LPVYVELFQN EFLSQPYDFF ADATVEINSY ITGAGINGTI TEFPFTAARY
     KRNLCLGRKE TIPYMAPAQP GALLTLVSPT AFPPAEAPNP VFTDADVTEP PLPPVTAKAP
     TSSPGTPSTN AQAPSGQTRI TLSLLLSVFA MVLASLLLL
//

If you have problems or comments...

PBIL Back to PBIL home page