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   09-APR-2025, entry version 146.
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=sn-glycero-3-phospho-1D-myo-inositol + H2O = 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_001345436.1; NM_001358507.1.
DR   RefSeq; NP_076097.1; NM_023608.4.
DR   RefSeq; XP_006528358.1; XM_006528295.1.
DR   RefSeq; XP_036017993.1; XM_036162100.1.
DR   AlphaFoldDB; Q9ESM6; -.
DR   SMR; Q9ESM6; -.
DR   STRING; 10090.ENSMUSP00000019503; -.
DR   GlyCosmos; Q9ESM6; 1 site, No reported glycans.
DR   GlyGen; Q9ESM6; 2 sites, 2 N-linked glycans (2 sites).
DR   iPTMnet; Q9ESM6; -.
DR   PhosphoSitePlus; Q9ESM6; -.
DR   SwissPalm; Q9ESM6; -.
DR   PaxDb; 10090-ENSMUSP00000019503; -.
DR   PeptideAtlas; Q9ESM6; -.
DR   ProteomicsDB; 265740; -.
DR   Antibodypedia; 27419; 166 antibodies from 21 providers.
DR   DNASU; 71584; -.
DR   Ensembl; ENSMUST00000019503.14; ENSMUSP00000019503.8; ENSMUSG00000019359.15.
DR   Ensembl; ENSMUST00000113744.2; ENSMUSP00000109373.2; ENSMUSG00000019359.15.
DR   GeneID; 71584; -.
DR   KEGG; mmu:71584; -.
DR   UCSC; uc009twi.2; mouse.
DR   AGR; MGI:1918834; -.
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; DPPGCCS; -.
DR   OrthoDB; 1058301at2759; -.
DR   PhylomeDB; Q9ESM6; -.
DR   TreeFam; TF313692; -.
DR   SABIO-RK; Q9ESM6; -.
DR   BioGRID-ORCS; 71584; 0 hits in 64 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 116 other cell types or tissues.
DR   GO; GO:0005884; C:actin filament; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
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:0007015; P:actin filament organization; 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   FunFam; 3.20.20.190:FF:000028; Glycerophosphodiester phosphodiesterase domain-containing protein 5; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   InterPro; IPR030395; GP_PDE_dom.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   PANTHER; PTHR23344:SF1; GLYCEROPHOSPHOINOSITOL INOSITOLPHOSPHODIESTERASE GDPD2; 1.
DR   PANTHER; PTHR23344; GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE; 1.
DR   Pfam; PF03009; GDPD; 1.
DR   Pfam; PF13653; GDPD_2; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 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
//