GDPD5_CHICK
ID GDPD5_CHICK Reviewed; 599 AA.
AC Q3KTM2;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Glycerophosphodiester phosphodiesterase domain-containing protein 5 {ECO:0000305};
DE AltName: Full=Glycerophosphocholine phosphodiesterase GDPD5 {ECO:0000250|UniProtKB:Q640M6};
DE EC=3.1.4.2 {ECO:0000250|UniProtKB:Q640M6};
DE AltName: Full=Glycerophosphodiester phosphodiesterase 2 {ECO:0000303|PubMed:16195461};
DE AltName: Full=Phosphoinositide phospholipase C GDPD5 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000269|PubMed:23329048};
GN Name=GDPD5; Synonyms=GDE2 {ECO:0000303|PubMed:16195461};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF HIS-275.
RX PubMed=16195461; DOI=10.1126/science.1117156;
RA Rao M., Sockanathan S.;
RT "Transmembrane protein GDE2 induces motor neuron differentiation in vivo.";
RL Science 309:2212-2215(2005).
RN [2]
RP FUNCTION, INTERACTION WITH PRDX1, ACTIVITY REGULATION, DISULFIDE BOND, AND
RP MUTAGENESIS OF CYS-15; CYS-18; CYS-25 AND CYS-576.
RX PubMed=19766572; DOI=10.1016/j.cell.2009.06.042;
RA Yan Y., Sabharwal P., Rao M., Sockanathan S.;
RT "The antioxidant enzyme Prdx1 controls neuronal differentiation by thiol-
RT redox-dependent activation of GDE2.";
RL Cell 138:1209-1221(2009).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF 236-ALA--LEU-239.
RX PubMed=23329048; DOI=10.1126/science.1231921;
RA Park S., Lee C., Sabharwal P., Zhang M., Meyers C.L., Sockanathan S.;
RT "GDE2 promotes neurogenesis by glycosylphosphatidylinositol-anchor cleavage
RT of RECK.";
RL Science 339:324-328(2013).
CC -!- FUNCTION: Glycerophosphodiester phosphodiesterase that promotes cell
CC cycle exit and drives spinal motor neuron differentiation
CC (PubMed:16195461, PubMed:19766572, PubMed:23329048). Mediates the
CC cleavage of glycosylphosphatidylinositol (GPI) anchor of target
CC proteins: removes the GPI-anchor of RECK, leading to release RECK from
CC the plasma membrane (PubMed:23329048). May contribute to the osmotic
CC regulation of cellular glycerophosphocholine (By similarity).
CC {ECO:0000250|UniProtKB:Q640M6, ECO:0000269|PubMed:16195461,
CC ECO:0000269|PubMed:19766572, ECO:0000269|PubMed:23329048}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC ChEBI:CHEBI:203600; EC=3.1.4.11;
CC Evidence={ECO:0000269|PubMed:23329048};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 3-phosphocholine = choline + H(+) + sn-
CC glycerol 3-phosphate; Xref=Rhea:RHEA:16061, ChEBI:CHEBI:15354,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:57597; EC=3.1.4.2;
CC Evidence={ECO:0000250|UniProtKB:Q640M6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16062;
CC Evidence={ECO:0000250|UniProtKB:Q640M6};
CC -!- ACTIVITY REGULATION: Activated by PRDX1 by reduction of an
CC intramolecular disulfide bond. {ECO:0000269|PubMed:19766572}.
CC -!- SUBUNIT: Interacts with PRDX1; forms a mixed-disulfide with PRDX1,
CC leading to disrupt intramolecular disulfide bond between Cys-25 and
CC Cys-576. {ECO:0000269|PubMed:19766572}.
CC -!- INTERACTION:
CC Q3KTM2; P0CB50: PRDX1; NbExp=5; IntAct=EBI-2464223, EBI-2464239;
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000250|UniProtKB:Q640M6}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q640M6}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q640M6}.
CC -!- TISSUE SPECIFICITY: Detected in mature motor neurons.
CC {ECO:0000269|PubMed:16195461}.
CC -!- DEVELOPMENTAL STAGE: Expression started in the intermediate zone of
CC spinal motor neurons as they differentiate into postmitotic motor
CC neurons. {ECO:0000269|PubMed:16195461}.
CC -!- PTM: Intramolecular disulfide bond between Cys-25 and Cys-576 is
CC reduced by PRDX1. {ECO:0000269|PubMed:19766572}.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; AY910750; AAX89036.1; -; mRNA.
DR AlphaFoldDB; Q3KTM2; -.
DR SMR; Q3KTM2; -.
DR IntAct; Q3KTM2; 3.
DR STRING; 9031.ENSGALP00000027954; -.
DR PaxDb; Q3KTM2; -.
DR VEuPathDB; HostDB:geneid_419070; -.
DR eggNOG; KOG2258; Eukaryota.
DR InParanoid; Q3KTM2; -.
DR PhylomeDB; Q3KTM2; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0047389; F:glycerophosphocholine phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IMP:MGI.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:CACAO.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR Pfam; PF03009; GDPD; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS51704; GP_PDE; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase;
KW Lipid metabolism; Membrane; Neurogenesis; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..599
FT /note="Glycerophosphodiester phosphodiesterase domain-
FT containing protein 5"
FT /id="PRO_0000387960"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..87
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..160
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..497
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..599
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 228..485
FT /note="GP-PDE"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 15..18
FT /evidence="ECO:0000269|PubMed:19766572"
FT DISULFID 25..576
FT /evidence="ECO:0000269|PubMed:19766572"
FT MUTAGEN 15
FT /note="C->S: Retains the ability to bind PRDX1; forms a
FT mixed-disulfide with PRDX1; can be reduced by PRDX1;
FT promote motor neuron differentiation as the wild type; when
FT associated with S-18."
FT /evidence="ECO:0000269|PubMed:19766572"
FT MUTAGEN 18
FT /note="C->S: Retains the ability to bind PRDX1; forms a
FT mixed-disulfide with PRDX1; can be reduced by PRDX1;
FT promote motor neuron differentiation as the wild type; when
FT associated with S-15."
FT /evidence="ECO:0000269|PubMed:19766572"
FT MUTAGEN 25
FT /note="C->S: Enhances the ability to promote motor neuron
FT differentiation. Retains the ability to bind PRDX1; loss
FT the ability to form a mixed-disulfide with PRDX1; loss the
FT ability to be reduced by PRDX1; when associated with S-
FT 576."
FT /evidence="ECO:0000269|PubMed:19766572"
FT MUTAGEN 236..239
FT /note="APML->GAHD: Catalytically inactive mutant. Abolishes
FT ability to remove the GPI-anchor of RECK."
FT /evidence="ECO:0000269|PubMed:23329048"
FT MUTAGEN 275
FT /note="H->A: Abolishes the ability to promote motor neuron
FT differentiation."
FT /evidence="ECO:0000269|PubMed:16195461"
FT MUTAGEN 576
FT /note="C->S: Enhances the ability to promote motor neuron
FT differentiation. Retains the ability to bind PRDX1; loss
FT the ability to form a mixed-disulfide with PRDX1; loss the
FT ability to be reduced by PRDX1; when associated with S-25."
FT /evidence="ECO:0000269|PubMed:19766572"
SQ SEQUENCE 599 AA; 69101 MW; 4A6A8CE259F659F3 CRC64;
MVKHQPLQYY EPQLCLSCLT GIYGCRWKRY QRSHDDTTKW ERLWFLILTS SFFLTLVWFY
FWWEVHNDYN EINWFLYNRM GYWSDWSIPI LVTTAAGFTY ITVLLILALC HIAVGQQMNL
HWLHKIGLMT TLITTVVTMS SIAQLWDDEW EMVFISLQAT APFLHIGALA AVTALSWLIA
GQFARMEKAT SQMLMVTAYL AVVVALYLVP LTISSPCIME KKALGPKPAI IGHRGAPMLA
PENTLMSFQK AVEQKIYGVQ ADVILSYDGV PFLMHDKTLR RTTNVEEVFP GRAYEHSSMF
NWTDLEMLNA GEWFLRNDPF WTAGSLSRSD YLEAANQSVC KLADMLEVIK DNTSLILNFQ
DLPPDHPYYT SYINITLKTI LASGIQQQAV MWLPDTERQL VRQIAPAFQQ TSGLKLDAER
LREKGIVKLN LRYTKVTNED VRDYMAANLS VNLYTVNEPW LYSILWCTGV PSVTSDSSHV
LRKVPFPIWL MPPDEYRLIW ITSDLISFII IVGVFIFQNY HNDQWRLGSI RTYNPEQIML
SAAVRRSSRD VKIMKEKLIF SEINNGVETT DELSLCSENG YANEMVTPTD HRDTRLRMN
