GPDL6_ARATH
ID GPDL6_ARATH Reviewed; 753 AA.
AC Q9FGT9;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Glycerophosphodiester phosphodiesterase GDPDL6 {ECO:0000305};
DE EC=3.1.4.46 {ECO:0000250|UniProtKB:Q7Y208};
DE AltName: Full=Glycerophosphodiester phosphodiesterase-like 6 {ECO:0000303|PubMed:21323773};
DE Short=ATGDPDL6 {ECO:0000303|PubMed:21323773};
DE AltName: Full=Glycerophosphodiesterase-like 5 {ECO:0000303|PubMed:18718934};
DE AltName: Full=Protein SHV3-LIKE 4 {ECO:0000303|PubMed:18718934};
DE Flags: Precursor;
GN Name=GDPDL6 {ECO:0000303|PubMed:21323773};
GN Synonyms=GDPL5 {ECO:0000303|PubMed:18718934},
GN SVL4 {ECO:0000303|PubMed:18718934};
GN OrderedLocusNames=At5g58050 {ECO:0000312|Araport:AT5G58050};
GN ORFNames=K21L19.4 {ECO:0000312|EMBL:BAB10996.1};
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].
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 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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; AB024029; BAB10996.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96991.1; -; Genomic_DNA.
DR EMBL; AY074302; AAL66999.1; -; mRNA.
DR EMBL; BT001948; AAN71947.1; -; mRNA.
DR RefSeq; NP_200613.2; NM_125190.4.
DR AlphaFoldDB; Q9FGT9; -.
DR SMR; Q9FGT9; -.
DR BioGRID; 21161; 28.
DR IntAct; Q9FGT9; 28.
DR STRING; 3702.AT5G58050.1; -.
DR iPTMnet; Q9FGT9; -.
DR PaxDb; Q9FGT9; -.
DR PRIDE; Q9FGT9; -.
DR ProteomicsDB; 248509; -.
DR EnsemblPlants; AT5G58050.1; AT5G58050.1; AT5G58050.
DR GeneID; 835917; -.
DR Gramene; AT5G58050.1; AT5G58050.1; AT5G58050.
DR KEGG; ath:AT5G58050; -.
DR Araport; AT5G58050; -.
DR TAIR; locus:2155816; AT5G58050.
DR eggNOG; KOG2258; Eukaryota.
DR HOGENOM; CLU_010414_0_1_1; -.
DR InParanoid; Q9FGT9; -.
DR OMA; DYIWPTD; -.
DR OrthoDB; 210274at2759; -.
DR PhylomeDB; Q9FGT9; -.
DR PRO; PR:Q9FGT9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGT9; baseline and differential.
DR Genevisible; Q9FGT9; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 2.
DR SUPFAM; SSF51695; SSF51695; 2.
DR PROSITE; PS51704; GP_PDE; 2.
PE 2: Evidence at transcript level;
KW Glycerol metabolism; Glycoprotein; Hydrolase; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..753
FT /note="Glycerophosphodiester phosphodiesterase GDPDL6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430616"
FT TRANSMEM 731..751
FT /note="Helical"
FT /evidence="ECO:0000255"
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 REGION 707..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 516
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 715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 753 AA; 80902 MW; 32364202A2F81657 CRC64;
MLRFFILFSL FLHSSVAAPK TPAAAAAVPA KKWLTLNGQE PAVVARGGFS GLFPESSISA
NDLAIGTSSP GFTMLCNLQM TKDGVGLCLS DIRLDNATTI SSVFPKAQKT YKVNGQDLKG
WFVIDYDADT IFNKVTLVQN IFSRPSIFDG QMSVSAVEDV LGTKPPKFWL SVQYDAFYME
HKLSPAEYLR SLRFRGINVI SSPEIGFLKS IGMDAGRAKT KLIFEFKDPE AVEPTTNKKY
SEIQQNLAAI KAFASGVLVP KDYIWPIDSA KYLKPATTFV ADAHKAGLEV YASGFANDLR
TSFNYSYDPS AEYLQFVDNG QFSVDGVITD FPPTASQSIT CFSHQNGNLP KAGHALVITH
NGASGDYPGC TDLAYQKAID DGADIIDCSV QMSKDGIAFC HDAADLSAST TARTTFMSRA
TSVPEIQPTN GIFSFDLTWA EIQSVKPQIE NPFTATGFQR NPANKNAGKF TTLADFLELG
KAKAVTGVLI NIQNAAYLAS KKGLGVVDVV KSALTNSTLD KQSTQKVLIQ SDDSSVLSSF
EAVPPYTRVL SIDKEIGDAP KTSIEEIKKH ADAVNLLRTS LITVSQSFAT GKTNVVEEMH
KANISVYVSV LRNEYIAIAF DYFSDPTIEL ATFIAGRGVD GVITEFPATA TRYLRSPCSD
LNKDQPYAIL PADAGALLTV ADKEAQLPAI PPNPPLDAKD VIDPPLPPVA KLASNGTEGG
PPQTPPRSGT VAIAANLSLS LLAMMALGLL YTA
