ID GDPD2_HUMAN Reviewed; 539 AA. AC Q9HCC8; B4DRH4; B4DVC9; Q9NXJ6; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 167. 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; ORFNames=UNQ1935/PRO4418; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Spleen; 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] (ISOFORM 1). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Caudate nucleus, Colon mucosa, and Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; 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). 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 (By similarity). {ECO:0000250}. 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 -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with CC the actin cytoskeleton. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9HCC8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9HCC8-2; Sequence=VSP_042622; CC Name=3; CC IsoId=Q9HCC8-3; Sequence=VSP_042623; 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}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA91014.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB048363; BAB13350.1; -; mRNA. DR EMBL; AY358986; AAQ89345.1; -; mRNA. DR EMBL; AK000214; BAA91014.1; ALT_FRAME; mRNA. DR EMBL; AK299255; BAG61286.1; -; mRNA. DR EMBL; AK301025; BAG62641.1; -; mRNA. DR EMBL; AK316035; BAH14406.1; -; mRNA. DR EMBL; AL139398; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC032009; AAH32009.1; -; mRNA. DR CCDS; CCDS14402.1; -. [Q9HCC8-1] DR CCDS; CCDS55437.1; -. [Q9HCC8-3] DR CCDS; CCDS55438.1; -. [Q9HCC8-2] DR RefSeq; NP_001164662.1; NM_001171191.1. [Q9HCC8-2] DR RefSeq; NP_001164663.1; NM_001171192.1. [Q9HCC8-3] DR RefSeq; NP_001164664.1; NM_001171193.1. [Q9HCC8-2] DR RefSeq; NP_060181.2; NM_017711.3. [Q9HCC8-1] DR AlphaFoldDB; Q9HCC8; -. DR SMR; Q9HCC8; -. DR BioGRID; 120207; 5. DR IntAct; Q9HCC8; 43. DR MINT; Q9HCC8; -. DR STRING; 9606.ENSP00000414019; -. DR GlyCosmos; Q9HCC8; 1 site, No reported glycans. DR GlyGen; Q9HCC8; 1 site. DR iPTMnet; Q9HCC8; -. DR PhosphoSitePlus; Q9HCC8; -. DR BioMuta; GDPD2; -. DR DMDM; 74752794; -. DR EPD; Q9HCC8; -. DR jPOST; Q9HCC8; -. DR MassIVE; Q9HCC8; -. DR PaxDb; 9606-ENSP00000414019; -. DR PeptideAtlas; Q9HCC8; -. DR ProteomicsDB; 81668; -. [Q9HCC8-1] DR ProteomicsDB; 81669; -. [Q9HCC8-2] DR ProteomicsDB; 81670; -. [Q9HCC8-3] DR Antibodypedia; 27419; 156 antibodies from 21 providers. DR DNASU; 54857; -. DR Ensembl; ENST00000374382.4; ENSP00000363503.3; ENSG00000130055.14. [Q9HCC8-1] DR Ensembl; ENST00000453994.6; ENSP00000414019.2; ENSG00000130055.14. [Q9HCC8-3] DR Ensembl; ENST00000536730.5; ENSP00000445982.1; ENSG00000130055.14. [Q9HCC8-2] DR Ensembl; ENST00000538649.5; ENSP00000444601.1; ENSG00000130055.14. [Q9HCC8-2] DR GeneID; 54857; -. DR KEGG; hsa:54857; -. DR MANE-Select; ENST00000374382.4; ENSP00000363503.3; NM_017711.4; NP_060181.2. DR UCSC; uc004dyh.4; human. [Q9HCC8-1] DR AGR; HGNC:25974; -. DR CTD; 54857; -. DR DisGeNET; 54857; -. DR GeneCards; GDPD2; -. DR HGNC; HGNC:25974; GDPD2. DR HPA; ENSG00000130055; Group enriched (choroid plexus, intestine, lymphoid tissue, skin). DR MIM; 300940; gene. DR neXtProt; NX_Q9HCC8; -. DR OpenTargets; ENSG00000130055; -. DR PharmGKB; PA134907263; -. DR VEuPathDB; HostDB:ENSG00000130055; -. DR eggNOG; KOG2258; Eukaryota. DR GeneTree; ENSGT00940000159625; -. DR HOGENOM; CLU_024259_1_0_1; -. DR InParanoid; Q9HCC8; -. DR OMA; DPPGCCS; -. DR OrthoDB; 203377at2759; -. DR PhylomeDB; Q9HCC8; -. DR TreeFam; TF313692; -. DR BRENDA; 3.1.4.46; 2681. DR BRENDA; 4.6.1.14; 2681. DR PathwayCommons; Q9HCC8; -. DR SignaLink; Q9HCC8; -. DR BioGRID-ORCS; 54857; 20 hits in 773 CRISPR screens. DR ChiTaRS; GDPD2; human. DR GenomeRNAi; 54857; -. DR Pharos; Q9HCC8; Tbio. DR PRO; PR:Q9HCC8; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q9HCC8; Protein. DR Bgee; ENSG00000130055; Expressed in spleen and 128 other cell types or tissues. DR GO; GO:0005884; C:actin filament; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. 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:0007015; P:actin filament organization; IEA:Ensembl. DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl. DR CDD; cd08609; GDPD_GDE3; 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. DR Genevisible; Q9HCC8; HS. PE 2: Evidence at transcript level; KW Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton; Glycoprotein; KW Hydrolase; Membrane; Metal-binding; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..539 FT /note="Glycerophosphoinositol inositolphosphodiesterase FT GDPD2" FT /id="PRO_0000251934" FT TOPO_DOM 1..38 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 39..59 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 60..85 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 86..106 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 107..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..188 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 189..209 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 210..490 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 491..511 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 512..539 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 224..479 FT /note="GP-PDE" FT BINDING 256 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255" FT BINDING 258 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255" FT BINDING 271 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255" FT CARBOHYD 442 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..79 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042622" FT VAR_SEQ 436 FT /note="K -> KDRFLLPAQAGLKLLASSNLPASASQSAGITGLSHCPPQPPGYKHEL FT SHLAM (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042623" FT CONFLICT 418 FT /note="E -> G (in Ref. 3; BAA91014)" FT /evidence="ECO:0000305" SQ SEQUENCE 539 AA; 61729 MW; 8271C3A74766D540 CRC64; MAESPGCCSV WARCLHCLYS CHWRKCPRER MQTSKCDCIW FGLLFLTFLL SLSWLYIGLV LLNDLHNFNE FLFRRWGHWM DWSLAFLLVI SLLVTYASLL LVLALLLRLC RQPLHLHSLH KVLLLLIMLL VAAGLVGLDI QWQQEWHSLR VSLQATAPFL HIGAAAGIAL LAWPVADTFY RIHRRGPKIL LLLLFFGVVL VIYLAPLCIS SPCIMEPRDL PPKPGLVGHR GAPMLAPENT LMSLRKTAEC GATVFETDVM VSSDGVPFLM HDEHLSRTTN VASVFPTRIT AHSSDFSWTE LKRLNAGSWF LERRPFWGAK PLAGPDQKEA ESQTVPALEE LLEEAAALNL SIMFDLRRPP QNHTYYDTFV IQTLETVLNA RVPQAMVFWL PDEDRANVQR RAPGMRQIYG RQGGNRTERP QFLNLPYQDL PLLDIKALHK DNVSVNLFVV NKPWLFSLLW CAGVDSVTTN DCQLLQQMRY PIWLITPQTY LIIWVITNCV STMLLLWTFL LQRRFVKKRG KTGLETAVLL TRINNFMME //