GDPD2_MOUSE
ID GDPD2_MOUSE Reviewed; 539 AA.
AC Q9ESM6;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Glycerophosphoinositol inositolphosphodiesterase GDPD2;
DE EC=3.1.4.43;
DE AltName: Full=Glycerophosphodiester phosphodiesterase 3;
DE AltName: Full=Glycerophosphodiester phosphodiesterase domain-containing protein 2;
DE AltName: Full=Osteoblast differentiation promoting factor;
GN Name=Gdpd2; Synonyms=Gde3, Obdpf;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Osteoblast;
RX PubMed=12933806; DOI=10.1074/jbc.m302867200;
RA Yanaka N., Imai Y., Kawai E., Akatsuka H., Wakimoto K., Nogusa Y., Kato N.,
RA Chiba H., Kotani E., Omori K., Sakurai N.;
RT "Novel membrane protein containing glycerophosphodiester phosphodiesterase
RT motif is transiently expressed during osteoblast differentiation.";
RL J. Biol. Chem. 278:43595-43602(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP 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 [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-231.
RX PubMed=19596859; DOI=10.1074/jbc.m109.035444;
RA Corda D., Kudo T., Zizza P., Iurisci C., Kawai E., Kato N., Yanaka N.,
RA Mariggio S.;
RT "The developmentally regulated osteoblast phosphodiesterase GDE3 is
RT glycerophosphoinositol-specific and modulates cell growth.";
RL J. Biol. Chem. 284:24848-24856(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Has glycerophosphoinositol inositolphosphodiesterase activity
CC and specifically hydrolyzes glycerophosphoinositol, with no activity
CC for other substrates such as glycerophosphoinositol 4-phosphate,
CC glycerophosphocholine, glycerophosphoethanolamine, and
CC glycerophosphoserine. Accelerates the program of osteoblast
CC differentiation and growth. May play a role in remodeling of the actin
CC cytoskeleton. {ECO:0000269|PubMed:12933806,
CC ECO:0000269|PubMed:19596859}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycero-3-phospho-1D-myo-inositol = 1D-myo-inositol
CC 1-phosphate + glycerol + H(+); Xref=Rhea:RHEA:14033,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:58433, ChEBI:CHEBI:58444; EC=3.1.4.43;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=97.2 mM for glycerophosphoinositol {ECO:0000269|PubMed:19596859};
CC Vmax=1.9 nmol/min/mg enzyme {ECO:0000269|PubMed:19596859};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12933806};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12933806}. Cytoplasm
CC {ECO:0000269|PubMed:12933806}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12933806}. Note=Colocalizes with the actin
CC cytoskeleton.
CC -!- TISSUE SPECIFICITY: Detected in spleen, femur and calvaria.
CC {ECO:0000269|PubMed:12933806, ECO:0000269|PubMed:15276213}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during osteoblast differentiation.
CC Detected at low levels in mature osteoblasts.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
CC -!- CAUTION: The catalytic domain of Gdpd2 is oriented extracellularly;
CC Glycerophosphoinositol is hydrolyzed in the medium of cells
CC overexpressing Gdpd2, whereas intracellular levels of
CC glycerophosphoinositol is not affected. {ECO:0000305}.
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DR EMBL; AB048364; BAB13351.1; -; mRNA.
DR EMBL; AK018634; BAB31318.1; -; mRNA.
DR EMBL; BC038274; AAH38274.1; -; mRNA.
DR CCDS; CCDS30306.1; -.
DR RefSeq; NP_001292870.1; NM_001305941.1.
DR RefSeq; NP_076097.1; NM_023608.4.
DR RefSeq; XP_006528358.1; XM_006528295.1.
DR AlphaFoldDB; Q9ESM6; -.
DR SMR; Q9ESM6; -.
DR STRING; 10090.ENSMUSP00000019503; -.
DR GlyGen; Q9ESM6; 1 site.
DR iPTMnet; Q9ESM6; -.
DR PhosphoSitePlus; Q9ESM6; -.
DR MaxQB; Q9ESM6; -.
DR PaxDb; Q9ESM6; -.
DR PeptideAtlas; Q9ESM6; -.
DR PRIDE; Q9ESM6; -.
DR ProteomicsDB; 265740; -.
DR Antibodypedia; 27419; 139 antibodies from 21 providers.
DR DNASU; 71584; -.
DR Ensembl; ENSMUST00000019503; ENSMUSP00000019503; ENSMUSG00000019359.
DR Ensembl; ENSMUST00000113744; ENSMUSP00000109373; ENSMUSG00000019359.
DR GeneID; 71584; -.
DR KEGG; mmu:71584; -.
DR UCSC; uc009twi.2; mouse.
DR CTD; 54857; -.
DR MGI; MGI:1918834; Gdpd2.
DR VEuPathDB; HostDB:ENSMUSG00000019359; -.
DR eggNOG; KOG2258; Eukaryota.
DR GeneTree; ENSGT00940000159625; -.
DR HOGENOM; CLU_024259_3_0_1; -.
DR InParanoid; Q9ESM6; -.
DR OMA; PPNHTYH; -.
DR OrthoDB; 404866at2759; -.
DR PhylomeDB; Q9ESM6; -.
DR TreeFam; TF313692; -.
DR SABIO-RK; Q9ESM6; -.
DR BioGRID-ORCS; 71584; 0 hits in 61 CRISPR screens.
DR ChiTaRS; Gdpd2; mouse.
DR PRO; PR:Q9ESM6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9ESM6; protein.
DR Bgee; ENSMUSG00000019359; Expressed in small intestine Peyer's patch and 114 other tissues.
DR Genevisible; Q9ESM6; MM.
DR GO; GO:0005884; C:actin filament; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0047394; F:glycerophosphoinositol inositolphosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090527; P:actin filament reorganization; IDA:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA: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 membrane; Cytoplasm; Cytoskeleton; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..539
FT /note="Glycerophosphoinositol inositolphosphodiesterase
FT GDPD2"
FT /id="PRO_0000251935"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..83
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..154
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..491
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..539
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 225..480
FT /note="GP-PDE"
FT BINDING 257
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 259
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 272
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 231
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19596859"
SQ SEQUENCE 539 AA; 61165 MW; B8A63DF2D6532BA2 CRC64;
MADSPGCCSI WARCLHCLYS CHWRKYPKQK MQTSKCDCIW FGLLFLTFLL SLGWLYIGLI
LLNDLHNFNE FLFRHWGHWM DWSLIVLLVV SLLVTYASLL LLLGLLLQLC GQPLHLHSLH
KVLLLLIVLL VAAGLVGLDI QWRQEWHSLR LSLQATAPFL HIGAVAGITL LAWPVADTFY
RIHPRGPKVL LLLLFFGVTL VIYLMPLLFI SSPCIMKLRD LPPKPGLVGH RGAPMLAPEN
TLMSLRKTAE CGAAVFETDV MVSSDGVPFL MHDERLSRTT NVASVFPERI SAHSSDFSWA
ELQRLNAGTW FLERQPFWGA KKLSGSDRKE AENQTIPALE ELLKEAAALN LSIMFDLRRP
PRNHTYYDTF VNQTLEAVLS ANVSQAMVLW LPDEDRANVQ QRAPRMRQIY GHQGGNWTER
PQFLNLPYQD LPALDIKALH QDNISVNLFV VNKPWLFSLL WCAGVDSVTT NACQLLQQMQ
NPLWLLPPQK YLMIWVITDC ASILLLLSIF LLRGGCAKRN RTGLETAVLL TKINNFASE
