GPDL7_ARATH
ID GPDL7_ARATH Reviewed; 750 AA.
AC Q9LVN0; Q8GXJ8;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Glycerophosphodiester phosphodiesterase GDPDL7 {ECO:0000305};
DE EC=3.1.4.46 {ECO:0000250|UniProtKB:Q7Y208};
DE AltName: Full=Glycerophosphodiester phosphodiesterase-like 7 {ECO:0000303|PubMed:21323773};
DE Short=ATGDPDL7 {ECO:0000303|PubMed:21323773};
DE AltName: Full=Glycerophosphodiesterase-like 6 {ECO:0000303|PubMed:18718934};
DE AltName: Full=Protein SHV3-LIKE 5 {ECO:0000303|PubMed:18718934};
DE Flags: Precursor;
GN Name=GDPDL7 {ECO:0000303|PubMed:21323773};
GN Synonyms=GDPL6 {ECO:0000303|PubMed:18718934},
GN SVL5 {ECO:0000303|PubMed:18718934};
GN OrderedLocusNames=At5g58170 {ECO:0000312|Araport:AT5G58170};
GN ORFNames=MCK7.4 {ECO:0000312|EMBL:BAA96908.1};
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] OF 392-750.
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 TISSUE SPECIFICITY.
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 [5]
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a sn-glycero-3-phosphodiester + 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 -!- TISSUE SPECIFICITY: Expressed in flowers and siliques.
CC {ECO:0000269|PubMed:21323773}.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; AB019228; BAA96908.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97007.1; -; Genomic_DNA.
DR EMBL; AK118200; BAC42822.1; -; mRNA.
DR RefSeq; NP_200625.1; NM_125202.2.
DR AlphaFoldDB; Q9LVN0; -.
DR SMR; Q9LVN0; -.
DR BioGRID; 21173; 1.
DR STRING; 3702.AT5G58170.1; -.
DR PaxDb; Q9LVN0; -.
DR PRIDE; Q9LVN0; -.
DR ProteomicsDB; 248506; -.
DR EnsemblPlants; AT5G58170.1; AT5G58170.1; AT5G58170.
DR GeneID; 835929; -.
DR Gramene; AT5G58170.1; AT5G58170.1; AT5G58170.
DR KEGG; ath:AT5G58170; -.
DR Araport; AT5G58170; -.
DR TAIR; locus:2161248; AT5G58170.
DR eggNOG; KOG2258; Eukaryota.
DR HOGENOM; CLU_010414_0_1_1; -.
DR InParanoid; Q9LVN0; -.
DR OMA; MIKTFAS; -.
DR OrthoDB; 210274at2759; -.
DR PhylomeDB; Q9LVN0; -.
DR PRO; PR:Q9LVN0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LVN0; baseline and differential.
DR Genevisible; Q9LVN0; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
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;
KW Glycerol metabolism; Glycoprotein; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..750
FT /note="Glycerophosphodiester phosphodiesterase GDPDL7"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430617"
FT DOMAIN 41..339
FT /note="GP-PDE 1"
FT /evidence="ECO:0000255"
FT DOMAIN 355..654
FT /note="GP-PDE 2"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 716
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 504
FT /note="L -> I (in Ref. 3; BAC42822)"
SQ SEQUENCE 750 AA; 80038 MW; CEB5AEB682C818A5 CRC64;
MLRFIIFFSL FIHLCVAAPQ TPAAAAAVPA KKWLTLNGQE PAVVARGGFS GLFPESSASA
NDLAIGTSSP GLTMLCNLQM TKDGVGLCLS DIILDNATTI SSVFPKAQKT YKVNGQDLKG
WFVLDYDADT IFNNVTLVQN IFSRPSIFDG QMSVSAVEDV LGTKPPKFWL SVQYDAFYME
HKLSPAEYLR SLQFRGINVI SSPEIGFLKS IGMDAGRAKT KLIFEFKDPE AVEPTTNKKY
SEIQQNLAAI KAFASGVLVP KDYIWPIDSA KYLKPATTFV ADAHKAGLEV YASGFANDLR
TSFNYSYDPS AEYLQFVDNG QFSVDGVITD FPPTASQSIT CFSHQNGNLP KAGHALVITH
NGASGDYPGC TDLAYQKAVD DGADVIDCSV QMSKDGIAFC HDAADLTAST TAMTIFMSRA
TSVPEIQPTN GIFSFDLTWA EIQSVKPQIE NPFTATGFQR NPANKNAGKF ITLADFLDFS
KAKAVTGVMI NIENAAYLAS KKGLGVVDAV KSALAKSTLD KQSTQKVLIQ SDDSSVLASF
EAVPPYTRVL SIDKEIGGAP KPSVDEIKKY AEAVNLLRTS LVTVSQSFTT GKTNVVEEMH
KGNISVYVSV LRNEYISVAF DYFSDPTIEL ATFISGSGVD GVITEFPATA TRYLKSPCSD
LNKEQPYAIL PAEAGGLVVV ADKEAQPPAS APNPPLEAKD VIDPPLPPVA NLAASNATGG
AQSHPPPASG TVANAANLGL SLLAMLALGV
