Full text data of LPIN3
LPIN3
(LIPN3L)
[Confidence: low (only semi-automatic identification from reviews)]
Phosphatidate phosphatase LPIN3; 3.1.3.4 (Lipin-3; Lipin-3-like)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phosphatidate phosphatase LPIN3; 3.1.3.4 (Lipin-3; Lipin-3-like)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BQK8
ID LPIN3_HUMAN Reviewed; 851 AA.
AC Q9BQK8; B2RTT5; Q5TDB9; Q9NPY8; Q9UJE5;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-JUL-2005, sequence version 3.
DT 22-JAN-2014, entry version 80.
DE RecName: Full=Phosphatidate phosphatase LPIN3;
DE EC=3.1.3.4;
DE AltName: Full=Lipin-3;
DE AltName: Full=Lipin-3-like;
GN Name=LPIN3; Synonyms=LIPN3L;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=17158099; DOI=10.1074/jbc.M610745200;
RA Donkor J., Sariahmetoglu M., Dewald J., Brindley D.N., Reue K.;
RT "Three mammalian lipins act as phosphatidate phosphatases with
RT distinct tissue expression patterns.";
RL J. Biol. Chem. 282:3450-3457(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-159; SER-161 AND
RP SER-162, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC -!- FUNCTION: Regulates fatty acid metabolism. Magnesium-dependent
CC phosphatidate phosphatase enzyme which catalyzes the conversion of
CC phosphatidic acid to diacylglycerol during triglyceride,
CC phosphatidylcholine and phosphatidylethanolamine biosynthesis (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
CC 1,2-diacyl-sn-glycerol + phosphate.
CC -!- COFACTOR: Mg(2+) (By similarity).
CC -!- ENZYME REGULATION: Inhibited by N-ethylmaleimide (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BQK8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQK8-2; Sequence=VSP_036885;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Significant expression in intestine and other
CC regions of the gastrointestinal tract.
CC -!- DOMAIN: Contains 1 Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic
CC motif known to be essential for phosphatidate phosphatase activity
CC (By similarity).
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, a motif
CC known to be a transcriptional binding motif (By similarity).
CC -!- SIMILARITY: Belongs to the lipin family.
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; AL132654; CAI21064.1; -; Genomic_DNA.
DR EMBL; AL031667; CAI21064.1; JOINED; Genomic_DNA.
DR EMBL; AL031667; CAI42978.1; -; Genomic_DNA.
DR EMBL; AL132654; CAI42978.1; JOINED; Genomic_DNA.
DR EMBL; BC140806; AAI40807.1; -; mRNA.
DR RefSeq; NP_075047.1; NM_022896.1.
DR RefSeq; XP_005260572.1; XM_005260515.1.
DR UniGene; Hs.25897; -.
DR ProteinModelPortal; Q9BQK8; -.
DR STRING; 9606.ENSP00000362354; -.
DR PhosphoSite; Q9BQK8; -.
DR DMDM; 71153524; -.
DR PaxDb; Q9BQK8; -.
DR PRIDE; Q9BQK8; -.
DR Ensembl; ENST00000373257; ENSP00000362354; ENSG00000132793.
DR GeneID; 64900; -.
DR KEGG; hsa:64900; -.
DR UCSC; uc002xjx.3; human.
DR CTD; 64900; -.
DR GeneCards; GC20P039969; -.
DR HGNC; HGNC:14451; LPIN3.
DR MIM; 605520; gene.
DR neXtProt; NX_Q9BQK8; -.
DR PharmGKB; PA30438; -.
DR eggNOG; COG5083; -.
DR HOGENOM; HOG000230954; -.
DR HOVERGEN; HBG052338; -.
DR InParanoid; Q9BQK8; -.
DR KO; K15728; -.
DR OMA; APAMNYV; -.
DR OrthoDB; EOG7QZG8X; -.
DR Reactome; REACT_111217; Metabolism.
DR GenomeRNAi; 64900; -.
DR NextBio; 67045; -.
DR PRO; PR:Q9BQK8; -.
DR Bgee; Q9BQK8; -.
DR CleanEx; HS_LPIN3; -.
DR Genevestigator; Q9BQK8; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:Reactome.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; TAS:Reactome.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR007651; Lipin_N.
DR InterPro; IPR013209; LNS2.
DR Pfam; PF04571; Lipin_N; 1.
DR Pfam; PF08235; LNS2; 1.
DR SMART; SM00775; LNS2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Fatty acid metabolism;
KW Hydrolase; Lipid metabolism; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 851 Phosphatidate phosphatase LPIN3.
FT /FTId=PRO_0000209883.
FT REGION 1 108 N-LIP.
FT REGION 590 792 C-LIP.
FT MOTIF 141 148 Nuclear localization signal (Potential).
FT MOTIF 644 648 DXDXT motif.
FT MOTIF 655 659 LXXIL motif.
FT MOD_RES 159 159 Phosphothreonine.
FT MOD_RES 161 161 Phosphoserine.
FT MOD_RES 162 162 Phosphoserine.
FT VAR_SEQ 186 186 G -> GS (in isoform 2).
FT /FTId=VSP_036885.
FT VARIANT 679 679 Q -> H (in dbSNP:rs12625565).
FT /FTId=VAR_053489.
SQ SEQUENCE 851 AA; 93614 MW; BBDFDA0A53722625 CRC64;
MNYVGQLAET VFGTVKELYR GLNPATLSGG IDVLVVKQVD GSFRCSPFHV RFGKLGVLRS
REKVVDIELN GEPVDLHMKL GDSGEAFFVQ ELESDDEHVP PGLCTSPIPW GGLSGFPSDS
QLGTASEPEG LVMAGTASTG RRKRRRRRKP KQKEDAVATD SSPEELEAGA ESELSLPEKL
RPEPPGVQLE EKSSLQPKDI YPYSDGEWPP QASLSAGELT SPKSDSELEV RTPEPSPLRA
ESHMQWAWGR LPKVARAERP ESSVVLEGRA GATSPPRGGP STPSTSVAGG VDPLGLPIQQ
TEAGADLQPD TEDPTLVGPP LHTPETEESK TQSSGDMGLP PASKSWSWAT LEVPVPTGQP
ERVSRGKGSP KRSQHLGPSD IYLDDLPSLD SENAALYFPQ SDSGLGARRW SEPSSQKSLR
DPNPEHEPEP TLDTVDTIAL SLCGGLADSR DISLEKFNQH SVSYQDLTKN PGLLDDPNLV
VKINGKHYNW AVAAPMILSL QAFQKNLPKS TMDKLEREKM PRKGGRWWFS WRRRDFLAEE
RSAQKEKTAA KEQQGEKTEV LSSDDDAPDS PVILEIPSLP PSTPPSTPTY KKSLRLSSDQ
IRRLNLQEGA NDVVFSVTTQ YQGTCRCKAT IYLWKWDDKV VISDIDGTIT KSDALGHILP
QLGKDWTHQG ITSLYHKIQL NGYKFLYCSA RAIGMADLTK GYLQWVSEGG CSLPKGPILL
SPSSLFSALH REVIEKKPEV FKVACLSDIQ QLFLPHGQPF YAAFGNRPND VFAYRQVGLP
ESRIFTVNPR GELIQELIKN HKSTYERLGE VVELLFPPVA RGPSTDLANP EYSNFCYWRE
PLPAVDLDTL D
//
ID LPIN3_HUMAN Reviewed; 851 AA.
AC Q9BQK8; B2RTT5; Q5TDB9; Q9NPY8; Q9UJE5;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-JUL-2005, sequence version 3.
DT 22-JAN-2014, entry version 80.
DE RecName: Full=Phosphatidate phosphatase LPIN3;
DE EC=3.1.3.4;
DE AltName: Full=Lipin-3;
DE AltName: Full=Lipin-3-like;
GN Name=LPIN3; Synonyms=LIPN3L;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=17158099; DOI=10.1074/jbc.M610745200;
RA Donkor J., Sariahmetoglu M., Dewald J., Brindley D.N., Reue K.;
RT "Three mammalian lipins act as phosphatidate phosphatases with
RT distinct tissue expression patterns.";
RL J. Biol. Chem. 282:3450-3457(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-159; SER-161 AND
RP SER-162, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC -!- FUNCTION: Regulates fatty acid metabolism. Magnesium-dependent
CC phosphatidate phosphatase enzyme which catalyzes the conversion of
CC phosphatidic acid to diacylglycerol during triglyceride,
CC phosphatidylcholine and phosphatidylethanolamine biosynthesis (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
CC 1,2-diacyl-sn-glycerol + phosphate.
CC -!- COFACTOR: Mg(2+) (By similarity).
CC -!- ENZYME REGULATION: Inhibited by N-ethylmaleimide (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BQK8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQK8-2; Sequence=VSP_036885;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Significant expression in intestine and other
CC regions of the gastrointestinal tract.
CC -!- DOMAIN: Contains 1 Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic
CC motif known to be essential for phosphatidate phosphatase activity
CC (By similarity).
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, a motif
CC known to be a transcriptional binding motif (By similarity).
CC -!- SIMILARITY: Belongs to the lipin family.
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; AL132654; CAI21064.1; -; Genomic_DNA.
DR EMBL; AL031667; CAI21064.1; JOINED; Genomic_DNA.
DR EMBL; AL031667; CAI42978.1; -; Genomic_DNA.
DR EMBL; AL132654; CAI42978.1; JOINED; Genomic_DNA.
DR EMBL; BC140806; AAI40807.1; -; mRNA.
DR RefSeq; NP_075047.1; NM_022896.1.
DR RefSeq; XP_005260572.1; XM_005260515.1.
DR UniGene; Hs.25897; -.
DR ProteinModelPortal; Q9BQK8; -.
DR STRING; 9606.ENSP00000362354; -.
DR PhosphoSite; Q9BQK8; -.
DR DMDM; 71153524; -.
DR PaxDb; Q9BQK8; -.
DR PRIDE; Q9BQK8; -.
DR Ensembl; ENST00000373257; ENSP00000362354; ENSG00000132793.
DR GeneID; 64900; -.
DR KEGG; hsa:64900; -.
DR UCSC; uc002xjx.3; human.
DR CTD; 64900; -.
DR GeneCards; GC20P039969; -.
DR HGNC; HGNC:14451; LPIN3.
DR MIM; 605520; gene.
DR neXtProt; NX_Q9BQK8; -.
DR PharmGKB; PA30438; -.
DR eggNOG; COG5083; -.
DR HOGENOM; HOG000230954; -.
DR HOVERGEN; HBG052338; -.
DR InParanoid; Q9BQK8; -.
DR KO; K15728; -.
DR OMA; APAMNYV; -.
DR OrthoDB; EOG7QZG8X; -.
DR Reactome; REACT_111217; Metabolism.
DR GenomeRNAi; 64900; -.
DR NextBio; 67045; -.
DR PRO; PR:Q9BQK8; -.
DR Bgee; Q9BQK8; -.
DR CleanEx; HS_LPIN3; -.
DR Genevestigator; Q9BQK8; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:Reactome.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; TAS:Reactome.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR007651; Lipin_N.
DR InterPro; IPR013209; LNS2.
DR Pfam; PF04571; Lipin_N; 1.
DR Pfam; PF08235; LNS2; 1.
DR SMART; SM00775; LNS2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Fatty acid metabolism;
KW Hydrolase; Lipid metabolism; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 851 Phosphatidate phosphatase LPIN3.
FT /FTId=PRO_0000209883.
FT REGION 1 108 N-LIP.
FT REGION 590 792 C-LIP.
FT MOTIF 141 148 Nuclear localization signal (Potential).
FT MOTIF 644 648 DXDXT motif.
FT MOTIF 655 659 LXXIL motif.
FT MOD_RES 159 159 Phosphothreonine.
FT MOD_RES 161 161 Phosphoserine.
FT MOD_RES 162 162 Phosphoserine.
FT VAR_SEQ 186 186 G -> GS (in isoform 2).
FT /FTId=VSP_036885.
FT VARIANT 679 679 Q -> H (in dbSNP:rs12625565).
FT /FTId=VAR_053489.
SQ SEQUENCE 851 AA; 93614 MW; BBDFDA0A53722625 CRC64;
MNYVGQLAET VFGTVKELYR GLNPATLSGG IDVLVVKQVD GSFRCSPFHV RFGKLGVLRS
REKVVDIELN GEPVDLHMKL GDSGEAFFVQ ELESDDEHVP PGLCTSPIPW GGLSGFPSDS
QLGTASEPEG LVMAGTASTG RRKRRRRRKP KQKEDAVATD SSPEELEAGA ESELSLPEKL
RPEPPGVQLE EKSSLQPKDI YPYSDGEWPP QASLSAGELT SPKSDSELEV RTPEPSPLRA
ESHMQWAWGR LPKVARAERP ESSVVLEGRA GATSPPRGGP STPSTSVAGG VDPLGLPIQQ
TEAGADLQPD TEDPTLVGPP LHTPETEESK TQSSGDMGLP PASKSWSWAT LEVPVPTGQP
ERVSRGKGSP KRSQHLGPSD IYLDDLPSLD SENAALYFPQ SDSGLGARRW SEPSSQKSLR
DPNPEHEPEP TLDTVDTIAL SLCGGLADSR DISLEKFNQH SVSYQDLTKN PGLLDDPNLV
VKINGKHYNW AVAAPMILSL QAFQKNLPKS TMDKLEREKM PRKGGRWWFS WRRRDFLAEE
RSAQKEKTAA KEQQGEKTEV LSSDDDAPDS PVILEIPSLP PSTPPSTPTY KKSLRLSSDQ
IRRLNLQEGA NDVVFSVTTQ YQGTCRCKAT IYLWKWDDKV VISDIDGTIT KSDALGHILP
QLGKDWTHQG ITSLYHKIQL NGYKFLYCSA RAIGMADLTK GYLQWVSEGG CSLPKGPILL
SPSSLFSALH REVIEKKPEV FKVACLSDIQ QLFLPHGQPF YAAFGNRPND VFAYRQVGLP
ESRIFTVNPR GELIQELIKN HKSTYERLGE VVELLFPPVA RGPSTDLANP EYSNFCYWRE
PLPAVDLDTL D
//
MIM
605520
*RECORD*
*FIELD* NO
605520
*FIELD* TI
*605520 LIPIN 3
;;LPIN3
*FIELD* TX
Mice carrying mutations in the fatty liver dystrophy (fld) gene have
read morefeatures of human lipodystrophy (Reue et al., 2000). In the human,
lipodystrophy is a heterogeneous group of disorders characterized by
loss of body fat, fatty liver, hypertriglyceridemia, and insulin
resistance. Through positional cloning, Peterfy et al. (2001) isolated
the gene responsible for fatty liver dystrophy in mice and characterized
2 independent mutant alleles of the fld gene. They designated the gene
Lpin1 and named the novel nuclear protein which it encodes lipin.
Through database searches, Peterfy et al. (2001) identified several
mouse and human EST and genomic sequences with similarities to Lpin1.
These included 2 Lpin1-related mouse genes (Lpin2 and Lpin3) and 3 human
homologs (LPIN1 (605518), LPIN2 (605519), and LPIN3). Consistent with
the observed reduction of adipose tissue mass in fld mice, wildtype
Lpin1 mRNA was expressed at high levels in adipose tissue and was
induced during differentiation of 3T3-L1 preadipocytes. The results
indicated that lipin is required for normal adipose tissue development,
and provided a candidate gene for human lipodystrophy.
Using sequence databases, Peterfy et al. (2001) mapped the human LPIN3
gene to 20q. They mapped the mouse gene to chromosome 2.
*FIELD* RF
1. Peterfy, M.; Phan, J.; Xu, P.; Reue, K.: Lipodystrophy in the
fld mouse results from mutation of a new gene encoding a nuclear protein,
lipin. Nature Genet. 27: 121-124, 2001.
2. Reue, K.; Xu, P.; Wang, X.-P.; Slavin, B. G.: Adipose tissue deficiency,
glucose intolerance, and increased atherosclerosis result from mutation
in the mouse fatty liver dystrophy (fld) gene. J. Lipid Res. 41:
1067-1076, 2000.
*FIELD* CD
Victor A. McKusick: 1/2/2001
*FIELD* ED
mgross: 01/02/2001
*RECORD*
*FIELD* NO
605520
*FIELD* TI
*605520 LIPIN 3
;;LPIN3
*FIELD* TX
Mice carrying mutations in the fatty liver dystrophy (fld) gene have
read morefeatures of human lipodystrophy (Reue et al., 2000). In the human,
lipodystrophy is a heterogeneous group of disorders characterized by
loss of body fat, fatty liver, hypertriglyceridemia, and insulin
resistance. Through positional cloning, Peterfy et al. (2001) isolated
the gene responsible for fatty liver dystrophy in mice and characterized
2 independent mutant alleles of the fld gene. They designated the gene
Lpin1 and named the novel nuclear protein which it encodes lipin.
Through database searches, Peterfy et al. (2001) identified several
mouse and human EST and genomic sequences with similarities to Lpin1.
These included 2 Lpin1-related mouse genes (Lpin2 and Lpin3) and 3 human
homologs (LPIN1 (605518), LPIN2 (605519), and LPIN3). Consistent with
the observed reduction of adipose tissue mass in fld mice, wildtype
Lpin1 mRNA was expressed at high levels in adipose tissue and was
induced during differentiation of 3T3-L1 preadipocytes. The results
indicated that lipin is required for normal adipose tissue development,
and provided a candidate gene for human lipodystrophy.
Using sequence databases, Peterfy et al. (2001) mapped the human LPIN3
gene to 20q. They mapped the mouse gene to chromosome 2.
*FIELD* RF
1. Peterfy, M.; Phan, J.; Xu, P.; Reue, K.: Lipodystrophy in the
fld mouse results from mutation of a new gene encoding a nuclear protein,
lipin. Nature Genet. 27: 121-124, 2001.
2. Reue, K.; Xu, P.; Wang, X.-P.; Slavin, B. G.: Adipose tissue deficiency,
glucose intolerance, and increased atherosclerosis result from mutation
in the mouse fatty liver dystrophy (fld) gene. J. Lipid Res. 41:
1067-1076, 2000.
*FIELD* CD
Victor A. McKusick: 1/2/2001
*FIELD* ED
mgross: 01/02/2001