Full text data of GDE1
GDE1
(MIR16)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Glycerophosphodiester phosphodiesterase 1; 3.1.4.44 (Membrane-interacting protein of RGS16; RGS16-interacting membrane protein)
Glycerophosphodiester phosphodiesterase 1; 3.1.4.44 (Membrane-interacting protein of RGS16; RGS16-interacting membrane protein)
UniProt
Q9NZC3
ID GDE1_HUMAN Reviewed; 331 AA.
AC Q9NZC3; O43334; Q6PKF7; Q7KYR4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 93.
DE RecName: Full=Glycerophosphodiester phosphodiesterase 1;
DE EC=3.1.4.44;
DE AltName: Full=Membrane-interacting protein of RGS16;
DE AltName: Full=RGS16-interacting membrane protein;
GN Name=GDE1; Synonyms=MIR16;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10760272; DOI=10.1073/pnas.97.8.3999;
RA Zheng B., Chen D., Farquhar M.G.;
RT "MIR16, a putative membrane glycerophosphodiester phosphodiesterase,
RT interacts with RGS16.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3999-4004(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Duennebier F.F., Bachmann A.S.;
RT "The role of GDE1/MIR16 in G protein-coupled receptor signaling.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R.,
RA Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L.,
RA Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E.,
RA Harris P.C., Venter J.C., Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from
RT human chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell, Brain, Colon, and Kidney;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP 3D-STRUCTURE MODELING, AND INTERACTION WITH PRAF2.
RX PubMed=16472945; DOI=10.1016/j.gene.2005.11.023;
RA Bachmann A.S., Duennebier F.F., Mocz G.;
RT "Genomic organization, characterization, and molecular 3D model of
RT GDE1, a novel mammalian glycerophosphoinositol phosphodiesterase.";
RL Gene 371:144-153(2006).
CC -!- FUNCTION: Has glycerophosphoinositol phosphodiesterase activity.
CC Has little or no activity towards glycerophosphocholine. GDE1
CC activity can be modulated by G-protein signaling pathways (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: 1-(sn-glycero-3-phospho)-1D-myo-inositol +
CC H(2)O = myo-inositol + sn-glycerol 3-phosphate.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- SUBUNIT: Interacts with RGS16 (By similarity). Interacts with
CC PRAF2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; Multi-
CC pass membrane protein (By similarity). Note=Perinuclear vesicles
CC and cell membrane (By similarity).
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- PTM: N-glycosylated (By similarity).
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester
CC phosphodiesterase family.
CC -!- SIMILARITY: Contains 1 GDPD domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC05440.1; Type=Erroneous gene model prediction;
CC Sequence=AAC05803.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF212862; AAF65234.1; -; mRNA.
DR EMBL; AY463154; AAR25624.1; -; mRNA.
DR EMBL; U91321; AAC05440.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC003108; AAC05803.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC014981; AAH14981.1; -; mRNA.
DR EMBL; BC025273; AAH25273.1; -; mRNA.
DR PIR; T01371; T01371.
DR RefSeq; NP_057725.1; NM_016641.3.
DR UniGene; Hs.512607; -.
DR ProteinModelPortal; Q9NZC3; -.
DR SMR; Q9NZC3; 63-220.
DR IntAct; Q9NZC3; 3.
DR STRING; 9606.ENSP00000261386; -.
DR DMDM; 74734724; -.
DR PaxDb; Q9NZC3; -.
DR PRIDE; Q9NZC3; -.
DR DNASU; 51573; -.
DR Ensembl; ENST00000353258; ENSP00000261386; ENSG00000006007.
DR GeneID; 51573; -.
DR KEGG; hsa:51573; -.
DR UCSC; uc002dgh.3; human.
DR CTD; 51573; -.
DR GeneCards; GC16M019513; -.
DR HGNC; HGNC:29644; GDE1.
DR MIM; 605943; gene.
DR neXtProt; NX_Q9NZC3; -.
DR PharmGKB; PA162389327; -.
DR eggNOG; COG0584; -.
DR HOGENOM; HOG000006722; -.
DR HOVERGEN; HBG052946; -.
DR InParanoid; Q9NZC3; -.
DR OMA; SPFNACL; -.
DR OrthoDB; EOG72JWGZ; -.
DR BRENDA; 3.1.4.44; 2681.
DR ChiTaRS; GDE1; human.
DR GenomeRNAi; 51573; -.
DR NextBio; 55400; -.
DR PRO; PR:Q9NZC3; -.
DR ArrayExpress; Q9NZC3; -.
DR Bgee; Q9NZC3; -.
DR CleanEx; HS_GDE1; -.
DR Genevestigator; Q9NZC3; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; TAS:UniProtKB.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; TAS:UniProtKB.
DR GO; GO:0047395; F:glycerophosphoinositol glycerophosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; TAS:UniProtKB.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR004129; GlyceroP-diester-Pdiesterase.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR PANTHER; PTHR23344; PTHR23344; 1.
DR Pfam; PF03009; GDPD; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Glycoprotein; Hydrolase; Magnesium;
KW Membrane; Metal-binding; Polymorphism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 331 Glycerophosphodiester phosphodiesterase
FT 1.
FT /FTId=PRO_0000251944.
FT TOPO_DOM 1 3 Cytoplasmic (Potential).
FT TRANSMEM 4 24 Helical; (Potential).
FT TOPO_DOM 25 247 Lumenal (Potential).
FT TRANSMEM 248 268 Helical; (Potential).
FT TOPO_DOM 269 331 Cytoplasmic (Potential).
FT DOMAIN 70 325 GDPD.
FT METAL 97 97 Magnesium (Potential).
FT METAL 99 99 Magnesium (Potential).
FT METAL 174 174 Magnesium (Potential).
FT CARBOHYD 168 168 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 198 198 N-linked (GlcNAc...) (Potential).
FT VARIANT 218 218 R -> Q (in dbSNP:rs2072086).
FT /FTId=VAR_044018.
FT VARIANT 328 328 E -> K (in dbSNP:rs34137361).
FT /FTId=VAR_044019.
SQ SEQUENCE 331 AA; 37718 MW; EFE567E71DBD4AC5 CRC64;
MWLWEDQGGL LGPFSFLLLV LLLVTRSPVN ACLLTGSLFV LLRVFSFEPV PSCRALQVLK
PRDRISAIAH RGGSHDAPEN TLAAIRQAAK NGATGVELDI EFTSDGIPVL MHDNTVDRTT
DGTGRLCDLT FEQIRKLNPA ANHRLRNDFP DEKIPTLREA VAECLNHNLT IFFDVKGHAH
KATEALKKMY MEFPQLYNNS VVCSFLPEVI YKMRQTDRDV ITALTHRPWS LSHTGDGKPR
YDTFWKHFIF VMMDILLDWS MHNILWYLCG ISAFLMQKDF VSPAYLKKWS AKGIQVVGWT
VNTFDEKSYY ESHLGSSYIT DSMVEDCEPH F
//
ID GDE1_HUMAN Reviewed; 331 AA.
AC Q9NZC3; O43334; Q6PKF7; Q7KYR4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 93.
DE RecName: Full=Glycerophosphodiester phosphodiesterase 1;
DE EC=3.1.4.44;
DE AltName: Full=Membrane-interacting protein of RGS16;
DE AltName: Full=RGS16-interacting membrane protein;
GN Name=GDE1; Synonyms=MIR16;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10760272; DOI=10.1073/pnas.97.8.3999;
RA Zheng B., Chen D., Farquhar M.G.;
RT "MIR16, a putative membrane glycerophosphodiester phosphodiesterase,
RT interacts with RGS16.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3999-4004(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Duennebier F.F., Bachmann A.S.;
RT "The role of GDE1/MIR16 in G protein-coupled receptor signaling.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R.,
RA Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L.,
RA Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E.,
RA Harris P.C., Venter J.C., Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from
RT human chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell, Brain, Colon, and Kidney;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP 3D-STRUCTURE MODELING, AND INTERACTION WITH PRAF2.
RX PubMed=16472945; DOI=10.1016/j.gene.2005.11.023;
RA Bachmann A.S., Duennebier F.F., Mocz G.;
RT "Genomic organization, characterization, and molecular 3D model of
RT GDE1, a novel mammalian glycerophosphoinositol phosphodiesterase.";
RL Gene 371:144-153(2006).
CC -!- FUNCTION: Has glycerophosphoinositol phosphodiesterase activity.
CC Has little or no activity towards glycerophosphocholine. GDE1
CC activity can be modulated by G-protein signaling pathways (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: 1-(sn-glycero-3-phospho)-1D-myo-inositol +
CC H(2)O = myo-inositol + sn-glycerol 3-phosphate.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- SUBUNIT: Interacts with RGS16 (By similarity). Interacts with
CC PRAF2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; Multi-
CC pass membrane protein (By similarity). Note=Perinuclear vesicles
CC and cell membrane (By similarity).
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- PTM: N-glycosylated (By similarity).
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester
CC phosphodiesterase family.
CC -!- SIMILARITY: Contains 1 GDPD domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC05440.1; Type=Erroneous gene model prediction;
CC Sequence=AAC05803.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF212862; AAF65234.1; -; mRNA.
DR EMBL; AY463154; AAR25624.1; -; mRNA.
DR EMBL; U91321; AAC05440.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC003108; AAC05803.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC014981; AAH14981.1; -; mRNA.
DR EMBL; BC025273; AAH25273.1; -; mRNA.
DR PIR; T01371; T01371.
DR RefSeq; NP_057725.1; NM_016641.3.
DR UniGene; Hs.512607; -.
DR ProteinModelPortal; Q9NZC3; -.
DR SMR; Q9NZC3; 63-220.
DR IntAct; Q9NZC3; 3.
DR STRING; 9606.ENSP00000261386; -.
DR DMDM; 74734724; -.
DR PaxDb; Q9NZC3; -.
DR PRIDE; Q9NZC3; -.
DR DNASU; 51573; -.
DR Ensembl; ENST00000353258; ENSP00000261386; ENSG00000006007.
DR GeneID; 51573; -.
DR KEGG; hsa:51573; -.
DR UCSC; uc002dgh.3; human.
DR CTD; 51573; -.
DR GeneCards; GC16M019513; -.
DR HGNC; HGNC:29644; GDE1.
DR MIM; 605943; gene.
DR neXtProt; NX_Q9NZC3; -.
DR PharmGKB; PA162389327; -.
DR eggNOG; COG0584; -.
DR HOGENOM; HOG000006722; -.
DR HOVERGEN; HBG052946; -.
DR InParanoid; Q9NZC3; -.
DR OMA; SPFNACL; -.
DR OrthoDB; EOG72JWGZ; -.
DR BRENDA; 3.1.4.44; 2681.
DR ChiTaRS; GDE1; human.
DR GenomeRNAi; 51573; -.
DR NextBio; 55400; -.
DR PRO; PR:Q9NZC3; -.
DR ArrayExpress; Q9NZC3; -.
DR Bgee; Q9NZC3; -.
DR CleanEx; HS_GDE1; -.
DR Genevestigator; Q9NZC3; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; TAS:UniProtKB.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; TAS:UniProtKB.
DR GO; GO:0047395; F:glycerophosphoinositol glycerophosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; TAS:UniProtKB.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR004129; GlyceroP-diester-Pdiesterase.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR PANTHER; PTHR23344; PTHR23344; 1.
DR Pfam; PF03009; GDPD; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Glycoprotein; Hydrolase; Magnesium;
KW Membrane; Metal-binding; Polymorphism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 331 Glycerophosphodiester phosphodiesterase
FT 1.
FT /FTId=PRO_0000251944.
FT TOPO_DOM 1 3 Cytoplasmic (Potential).
FT TRANSMEM 4 24 Helical; (Potential).
FT TOPO_DOM 25 247 Lumenal (Potential).
FT TRANSMEM 248 268 Helical; (Potential).
FT TOPO_DOM 269 331 Cytoplasmic (Potential).
FT DOMAIN 70 325 GDPD.
FT METAL 97 97 Magnesium (Potential).
FT METAL 99 99 Magnesium (Potential).
FT METAL 174 174 Magnesium (Potential).
FT CARBOHYD 168 168 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 198 198 N-linked (GlcNAc...) (Potential).
FT VARIANT 218 218 R -> Q (in dbSNP:rs2072086).
FT /FTId=VAR_044018.
FT VARIANT 328 328 E -> K (in dbSNP:rs34137361).
FT /FTId=VAR_044019.
SQ SEQUENCE 331 AA; 37718 MW; EFE567E71DBD4AC5 CRC64;
MWLWEDQGGL LGPFSFLLLV LLLVTRSPVN ACLLTGSLFV LLRVFSFEPV PSCRALQVLK
PRDRISAIAH RGGSHDAPEN TLAAIRQAAK NGATGVELDI EFTSDGIPVL MHDNTVDRTT
DGTGRLCDLT FEQIRKLNPA ANHRLRNDFP DEKIPTLREA VAECLNHNLT IFFDVKGHAH
KATEALKKMY MEFPQLYNNS VVCSFLPEVI YKMRQTDRDV ITALTHRPWS LSHTGDGKPR
YDTFWKHFIF VMMDILLDWS MHNILWYLCG ISAFLMQKDF VSPAYLKKWS AKGIQVVGWT
VNTFDEKSYY ESHLGSSYIT DSMVEDCEPH F
//
MIM
605943
*RECORD*
*FIELD* NO
605943
*FIELD* TI
*605943 GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE 1; GDE1
;;MEMBRANE INTERACTING PROTEIN OF RGS16; MIR16;;
read moreRGS16-INTERACTING MEMBRANE PROTEIN
*FIELD* TX
CLONING
Using a yeast 2-hybrid screen to identify proteins that interact with
RGS16 (602514), Zheng et al. (2000) isolated a cDNA encoding rat Mir16.
By searching sequence databases with rat Mir16 as the probe, they
identified a cDNA encoding human MIR16 that had been reported by Loftus
et al. (1999) as part of a large-scale chromosome 16 sequencing effort.
The human MIR16 protein shares 94% amino acid similarity with rat MIR16
and also shares strong homology with bacterial glycerophosphodiester
phosphodiesterases. Northern blot analysis detected widespread
expression of a 1.8-kb Mir16 transcript in rat tissues, with highest
levels in heart, brain, liver, kidney, and testis. Similar expression
was observed for human and mouse MIR16. Using yeast 2-hybrid and GST
pull-down assays, Zheng et al. (2000) demonstrated that MIR16 interacts
with the RGS domain of RGS16 and weakly with other RGS proteins,
including RGS2 (600861). Membrane association assays and endoglycosidase
H digestion showed that MIR16 is an integral membrane glycoprotein.
Immunofluorescence and immunoelectron microscopy localized Mir16 in the
intracellular membranes in rat pituitary and on the plasma membrane in
rat liver and kidney.
MAPPING
By genomic sequence analysis, Loftus et al. (1999) mapped the GDE1 gene
to chromosome 16p.
*FIELD* RF
1. Loftus, B. J.; Kim, U.-J.; Sneddon, V. P.; Kalush, F.; Brandon,
R.; Fuhrmann, J.; Mason, T.; Crosby, M. L.; Barnstead, M.; Cronin,
L.; Mays, A. D.; Cao, Y.; Xu, R. X.; Kang, H.-L.; Mitchell, S.; Eichler,
E. E.; Harris, P. C.; Venter, J. C.; Adams, M. D.: Genome duplications
and other features in 12 Mb of DNA sequence from human chromosome
16p and 16q. Genomics 60: 295-308, 1999.
2. Zheng, B.; Chen, D.; Farquhar, M. G.: MIR16, a putative membrane
glycerophosphodiester phosphodiesterase, interacts with RGS16. Proc.
Nat. Acad. Sci. 97: 3999-4004, 2000.
*FIELD* CD
Dawn Watkins-Chow: 5/16/2001
*FIELD* ED
alopez: 02/09/2009
mgross: 5/16/2001
*RECORD*
*FIELD* NO
605943
*FIELD* TI
*605943 GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE 1; GDE1
;;MEMBRANE INTERACTING PROTEIN OF RGS16; MIR16;;
read moreRGS16-INTERACTING MEMBRANE PROTEIN
*FIELD* TX
CLONING
Using a yeast 2-hybrid screen to identify proteins that interact with
RGS16 (602514), Zheng et al. (2000) isolated a cDNA encoding rat Mir16.
By searching sequence databases with rat Mir16 as the probe, they
identified a cDNA encoding human MIR16 that had been reported by Loftus
et al. (1999) as part of a large-scale chromosome 16 sequencing effort.
The human MIR16 protein shares 94% amino acid similarity with rat MIR16
and also shares strong homology with bacterial glycerophosphodiester
phosphodiesterases. Northern blot analysis detected widespread
expression of a 1.8-kb Mir16 transcript in rat tissues, with highest
levels in heart, brain, liver, kidney, and testis. Similar expression
was observed for human and mouse MIR16. Using yeast 2-hybrid and GST
pull-down assays, Zheng et al. (2000) demonstrated that MIR16 interacts
with the RGS domain of RGS16 and weakly with other RGS proteins,
including RGS2 (600861). Membrane association assays and endoglycosidase
H digestion showed that MIR16 is an integral membrane glycoprotein.
Immunofluorescence and immunoelectron microscopy localized Mir16 in the
intracellular membranes in rat pituitary and on the plasma membrane in
rat liver and kidney.
MAPPING
By genomic sequence analysis, Loftus et al. (1999) mapped the GDE1 gene
to chromosome 16p.
*FIELD* RF
1. Loftus, B. J.; Kim, U.-J.; Sneddon, V. P.; Kalush, F.; Brandon,
R.; Fuhrmann, J.; Mason, T.; Crosby, M. L.; Barnstead, M.; Cronin,
L.; Mays, A. D.; Cao, Y.; Xu, R. X.; Kang, H.-L.; Mitchell, S.; Eichler,
E. E.; Harris, P. C.; Venter, J. C.; Adams, M. D.: Genome duplications
and other features in 12 Mb of DNA sequence from human chromosome
16p and 16q. Genomics 60: 295-308, 1999.
2. Zheng, B.; Chen, D.; Farquhar, M. G.: MIR16, a putative membrane
glycerophosphodiester phosphodiesterase, interacts with RGS16. Proc.
Nat. Acad. Sci. 97: 3999-4004, 2000.
*FIELD* CD
Dawn Watkins-Chow: 5/16/2001
*FIELD* ED
alopez: 02/09/2009
mgross: 5/16/2001