GDPD5_MOUSE
ID GDPD5_MOUSE Reviewed; 607 AA.
AC Q640M6; Q8R0T5; Q8R3N5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Glycerophosphodiester phosphodiesterase domain-containing protein 5 {ECO:0000305};
DE AltName: Full=Glycerophosphocholine phosphodiesterase GDPD5 {ECO:0000305};
DE EC=3.1.4.2 {ECO:0000269|PubMed:18667693};
DE AltName: Full=Glycerophosphodiester phosphodiesterase 2;
DE AltName: Full=Phosphoinositide phospholipase C GDPD5 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000250|UniProtKB:Q3KTM2};
GN Name=Gdpd5 {ECO:0000312|MGI:MGI:2686926};
GN Synonyms=Gde2 {ECO:0000303|PubMed:15276213};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Colon, Eye, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15276213; DOI=10.1016/j.gene.2004.04.026;
RA Nogusa Y., Fujioka Y., Komatsu R., Kato N., Yanaka N.;
RT "Isolation and characterization of two serpentine membrane proteins
RT containing glycerophosphodiester phosphodiesterase, GDE2 and GDE6.";
RL Gene 337:173-179(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=17275818; DOI=10.1016/j.febslet.2007.01.035;
RA Yanaka N., Nogusa Y., Fujioka Y., Yamashita Y., Kato N.;
RT "Involvement of membrane protein GDE2 in retinoic acid-induced neurite
RT formation in Neuro2A cells.";
RL FEBS Lett. 581:712-718(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, INDUCTION, AND ACTIVITY
RP REGULATION.
RX PubMed=18667693; DOI=10.1073/pnas.0805496105;
RA Gallazzini M., Ferraris J.D., Burg M.B.;
RT "GDPD5 is a glycerophosphocholine phosphodiesterase that osmotically
RT regulates the osmoprotective organic osmolyte GPC.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:11026-11031(2008).
CC -!- FUNCTION: Glycerophosphodiester phosphodiesterase that promotes neurite
CC formation and drives spinal motor neuron differentiation
CC (PubMed:17275818, PubMed:18667693). Mediates the cleavage of
CC glycosylphosphatidylinositol (GPI) anchor of target proteins: removes
CC the GPI-anchor of RECK, leading to release RECK from the plasma
CC membrane (By similarity). May contribute to the osmotic regulation of
CC cellular glycerophosphocholine (PubMed:18667693).
CC {ECO:0000250|UniProtKB:Q3KTM2, ECO:0000269|PubMed:17275818,
CC ECO:0000269|PubMed:18667693}.
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:0000250|UniProtKB:Q3KTM2};
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:0000269|PubMed:18667693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16062;
CC Evidence={ECO:0000305|PubMed:18667693};
CC -!- ACTIVITY REGULATION: Inhibited by high level of NaCl or urea.
CC {ECO:0000269|PubMed:18667693}.
CC -!- SUBUNIT: Interacts with PRDX1; forms a mixed-disulfide with PRDX1,
CC leading to disrupt intramolecular disulfide bond between Cys-25 and
CC Cys-571. {ECO:0000250|UniProtKB:Q3KTM2}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:17275818,
CC ECO:0000269|PubMed:18667693, ECO:0000305|PubMed:15276213}; Multi-pass
CC membrane protein {ECO:0000255}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:15276213, ECO:0000269|PubMed:17275818,
CC ECO:0000269|PubMed:18667693}. Cell projection, growth cone
CC {ECO:0000269|PubMed:17275818}.
CC -!- TISSUE SPECIFICITY: Detected in brain, lung, heart, kidney and testis.
CC {ECO:0000269|PubMed:15276213}.
CC -!- INDUCTION: Up-regulated during neuronal differentiation by retinoic
CC acid. Down regulated by high NaCl or urea (PubMed:18667693).
CC {ECO:0000269|PubMed:17275818, ECO:0000269|PubMed:18667693}.
CC -!- PTM: Intramolecular disulfide bond between Cys-25 and Cys-571 is
CC reduced by PRDX1. {ECO:0000250|UniProtKB:Q3KTM2}.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26428.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK141189; BAE24577.1; -; mRNA.
DR EMBL; AK154771; BAE32819.1; -; mRNA.
DR EMBL; BC024955; AAH24955.1; -; mRNA.
DR EMBL; BC026428; AAH26428.1; ALT_INIT; mRNA.
DR EMBL; BC082585; AAH82585.1; -; mRNA.
DR CCDS; CCDS21481.1; -.
DR RefSeq; NP_958740.2; NM_201352.2.
DR RefSeq; XP_017177670.1; XM_017322181.1.
DR AlphaFoldDB; Q640M6; -.
DR SMR; Q640M6; -.
DR STRING; 10090.ENSMUSP00000036175; -.
DR SwissLipids; SLP:000000668; -.
DR GlyGen; Q640M6; 5 sites.
DR iPTMnet; Q640M6; -.
DR PhosphoSitePlus; Q640M6; -.
DR MaxQB; Q640M6; -.
DR PaxDb; Q640M6; -.
DR PeptideAtlas; Q640M6; -.
DR PRIDE; Q640M6; -.
DR ProteomicsDB; 272951; -.
DR Antibodypedia; 45087; 152 antibodies from 27 providers.
DR Ensembl; ENSMUST00000037528; ENSMUSP00000036175; ENSMUSG00000035314.
DR GeneID; 233552; -.
DR KEGG; mmu:233552; -.
DR UCSC; uc009ilo.1; mouse.
DR CTD; 81544; -.
DR MGI; MGI:2686926; Gdpd5.
DR VEuPathDB; HostDB:ENSMUSG00000035314; -.
DR eggNOG; KOG2258; Eukaryota.
DR GeneTree; ENSGT00940000159690; -.
DR HOGENOM; CLU_024259_1_0_1; -.
DR InParanoid; Q640M6; -.
DR OMA; REPPREH; -.
DR PhylomeDB; Q640M6; -.
DR TreeFam; TF313692; -.
DR BRENDA; 3.1.4.44; 3474.
DR BRENDA; 3.1.4.46; 3474.
DR BioGRID-ORCS; 233552; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Gdpd5; mouse.
DR PRO; PR:Q640M6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q640M6; protein.
DR Bgee; ENSMUSG00000035314; Expressed in pigmented layer of retina and 236 other tissues.
DR ExpressionAtlas; Q640M6; baseline and differential.
DR Genevisible; Q640M6; MM.
DR GO; GO:0030424; C:axon; IDA:CACAO.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
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; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:CACAO.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:CACAO.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0047389; F:glycerophosphocholine phosphodiesterase activity; IDA:CACAO.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; ISO:MGI.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IMP:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IDA:CACAO.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:MGI.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:CACAO.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:CACAO.
DR GO; GO:0048505; P:regulation of timing of cell differentiation; IMP:MGI.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IMP:MGI.
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..607
FT /note="Glycerophosphodiester phosphodiesterase domain-
FT containing protein 5"
FT /id="PRO_0000251942"
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..89
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..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..496
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 228..485
FT /note="GP-PDE"
FT REGION 582..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:Q3KTM2"
FT DISULFID 25..571
FT /evidence="ECO:0000250|UniProtKB:Q3KTM2"
FT CONFLICT 399
FT /note="P -> L (in Ref. 2; AAH24955)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="E -> G (in Ref. 2; AAH26428)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 68890 MW; 3FF90C40A866E992 CRC64;
MVRHQPLQYY EPQLCLSCLT GIYGCRWKRY QRSHDDTTPW ERLWFLLLVC TFSLTLTWLY
FWWGVHNDYD EFNWYLYNRM GYWSDWSVPI LVTSAAAFTY IAGLLVLALC HIAVGQQLNL
HWIHKMGLVV ILASTVVAMS AVAQLWEDEW EVLLISLQGT APFLHIGALV AITALSWIVA
GQFARAERSS SQLTILCTFF AVVFTFYLIP LTISSPCIME KKDLGPKPAL IGHRGAPMLA
PEHTVMSFRK ALEQRLYGLQ ADITISLDGV PFLMHDTTLR RTTNVEHLFP ELARRPAAML
NWTVLQRLNA GQWFLKTDPF WTASSLSPSD HREVQNQSIC SLAELLELAK GNASLLLNLR
DPPRDHPYRG SFLNVTLEAV LRSGFPQHQV MWLFNRQRPL VRKMAPGFQQ TSGSKEAIAN
LRKGHIQKLN LRYTQVSHQE LRDYASWNLS VNLYTVNAPW LFSLLWCAGV PSVTSDNSHT
LSRVPSPLWI MPPDEYCLMW VTADLISFSL IIGIFVLQKW RLGGIRSYNP EQIMLSAAVR
RTSRDVSIMK EKLIFSEISD GVEVSDELSV CSDSSYDTYA NANSTATPVG PRNAGSRAKT
VTEQSGH
