GPDL4_ARATH
ID GPDL4_ARATH Reviewed; 766 AA.
AC Q9FJ62; Q5XEZ7;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Glycerophosphodiester phosphodiesterase GDPDL4 {ECO:0000305};
DE EC=3.1.4.46 {ECO:0000250|UniProtKB:Q7Y208};
DE AltName: Full=Glycerophosphodiester phosphodiesterase-like 4 {ECO:0000303|PubMed:21323773};
DE Short=ATGDPDL4 {ECO:0000303|PubMed:21323773};
DE AltName: Full=Glycerophosphodiesterase-like 1 {ECO:0000303|PubMed:18718934};
DE AltName: Full=Protein SHV3-LIKE 1 {ECO:0000303|PubMed:18718934};
DE Flags: Precursor;
GN Name=GDPDL4 {ECO:0000303|PubMed:21323773};
GN Synonyms=GPDL1 {ECO:0000303|PubMed:18718934},
GN SVL1 {ECO:0000303|PubMed:18718934}; OrderedLocusNames=At5g55480;
GN ORFNames=MTE17.19;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [5]
RP FUNCTION, AND 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 [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-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: Cell membrane; Single-pass type I membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:18718934, ECO:0000269|PubMed:21323773}.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; AB015479; BAB08565.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96633.1; -; Genomic_DNA.
DR EMBL; BT015819; AAU94382.1; -; mRNA.
DR EMBL; BT020207; AAV59273.1; -; mRNA.
DR RefSeq; NP_200359.1; NM_124930.4.
DR AlphaFoldDB; Q9FJ62; -.
DR SMR; Q9FJ62; -.
DR BioGRID; 20885; 5.
DR IntAct; Q9FJ62; 1.
DR STRING; 3702.AT5G55480.1; -.
DR PaxDb; Q9FJ62; -.
DR PRIDE; Q9FJ62; -.
DR ProteomicsDB; 248469; -.
DR EnsemblPlants; AT5G55480.1; AT5G55480.1; AT5G55480.
DR GeneID; 835641; -.
DR Gramene; AT5G55480.1; AT5G55480.1; AT5G55480.
DR KEGG; ath:AT5G55480; -.
DR Araport; AT5G55480; -.
DR TAIR; locus:2173977; AT5G55480.
DR eggNOG; KOG2258; Eukaryota.
DR HOGENOM; CLU_010414_0_1_1; -.
DR InParanoid; Q9FJ62; -.
DR OMA; QYSMFYE; -.
DR OrthoDB; 211520at2759; -.
DR PhylomeDB; Q9FJ62; -.
DR PRO; PR:Q9FJ62; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJ62; baseline and differential.
DR Genevisible; Q9FJ62; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycerol metabolism;
KW Glycoprotein; Hydrolase; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..766
FT /note="Glycerophosphodiester phosphodiesterase GDPDL4"
FT /id="PRO_0000012597"
FT TOPO_DOM 36..745
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 746..766
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 50..349
FT /note="GP-PDE 1"
FT DOMAIN 365..668
FT /note="GP-PDE 2"
FT REGION 704..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 766 AA; 84165 MW; D8C6A14AD1F9ACA4 CRC64;
MINMRDNPTM HVLQASKFLF LALILIQLLS TQLFAQRSKS PWQTLTGDAP LVIARGGFSG
LLPDSSLDAY SFVSQTSVPG AVLWCDVQLT KDAIGLCFPD VKMMNASNIQ DVYPKRKTSY
LLNGVPTQDW FTIDFNFKDL TKVILKQGIL SRSAAFDGNS YGISTVKDIS TQLKPEGFWL
NVQHDAFYAQ HNLSMSSFLL SISKTVIIDY LSSPEVNFFR NIGRRFGRNG PKFVFRFLEK
DDVEVSTNQT YGSLAGNLTF LKTFASGVLV PKSYIWPIES QYLLPRTSFV QDAHKAGLEV
YASGFGNDFD LAYNYSFDPL AEYLSFMDNG DFSVDGLLSD FPLTASSAVD CFSHLGSNAS
SQVDFLVISK NGASGDYPGC TDLAYTKAIK DGADVIDCSL QMSSDGIPFC LSSINLGEST
NVVQSPFRNR STTVPEIGSL PGIYSFSLAW SEIQTLRPAI ENPYSREFTM FRNPRERSSG
KFVSLSDFLN LAKNSSSLTG VLISVENATY LREKQGLDAV KAVLDTLTEA GYSNKTTTTR
VMIQSTNSSV LIDFKKQSRY ETVYKVEETI RDILDTAIED IKKFADAVVI SKKSVFPTSE
SFTTGQTKLV ERLQKFQLPV YVEVFRNEFV SQPWDFFADA TVEINSHVTG AGINGTITEF
PLTAARYKRN SCLTRKDVPP YMIPVQPAGL LTIVSPASLP PAEAPSPVFT DADVTEPPLP
PVSARAPTTT PGPQSTGEKS PNGQTRVALS LLLSAFATVF ASLLLL
