LPIN3_MUSSP
ID LPIN3_MUSSP Reviewed; 847 AA.
AC Q7TNN8;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Phosphatidate phosphatase LPIN3 {ECO:0000250|UniProtKB:Q9BQK8};
DE EC=3.1.3.4 {ECO:0000250|UniProtKB:Q99PI4};
DE AltName: Full=Lipin-3;
GN Name=Lpin3 {ECO:0000250|UniProtKB:Q9BQK8};
OS Mus spretus (Western Mediterranean mouse) (Algerian mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10096;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Farahani P., Chiu S., Barry S.J., Schultz B.E., Butte N.F., Warden C.H.;
RT "Evidence from mouse and human studies reveal Lpin3 as a novel obesity
RT gene.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Magnesium-dependent phosphatidate phosphatase enzyme which
CC catalyzes the conversion of phosphatidic acid to diacylglycerol during
CC triglyceride, phosphatidylcholine and phosphatidylethanolamine
CC biosynthesis therefore regulates fatty acid metabolism.
CC {ECO:0000250|UniProtKB:Q99PI4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC Evidence={ECO:0000250|UniProtKB:Q99PI4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC Evidence={ECO:0000250|UniProtKB:Q99PI4};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DOMAIN: Contains 1 Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif
CC known to be essential for phosphatidate phosphatase activity.
CC {ECO:0000250}.
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, a motif known
CC to be a transcriptional binding motif. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lipin family. {ECO:0000305}.
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DR EMBL; AY135379; AAN11295.1; -; mRNA.
DR AlphaFoldDB; Q7TNN8; -.
DR SMR; Q7TNN8; -.
DR MGI; MGI:1891342; Lpin3.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IBA:GO_Central.
DR GO; GO:0009062; P:fatty acid catabolic process; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR026058; LIPIN.
DR InterPro; IPR031703; Lipin_mid.
DR InterPro; IPR007651; Lipin_N.
DR InterPro; IPR013209; LNS2.
DR InterPro; IPR031315; LNS2/PITP.
DR PANTHER; PTHR12181; PTHR12181; 1.
DR Pfam; PF16876; Lipin_mid; 1.
DR Pfam; PF04571; Lipin_N; 1.
DR Pfam; PF08235; LNS2; 1.
DR SMART; SM00775; LNS2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 2: Evidence at transcript level;
KW Fatty acid metabolism; Hydrolase; Lipid metabolism; Nucleus;
KW Phosphoprotein.
FT CHAIN 1..847
FT /note="Phosphatidate phosphatase LPIN3"
FT /id="PRO_0000209885"
FT REGION 1..108
FT /note="N-LIP"
FT /evidence="ECO:0000250"
FT REGION 97..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..788
FT /note="C-LIP"
FT /evidence="ECO:0000250"
FT MOTIF 135..144
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 640..644
FT /note="DXDXT motif"
FT MOTIF 651..655
FT /note="LXXIL motif"
FT COMPBIAS 201..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQK8"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQK8"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PI4"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQK8"
SQ SEQUENCE 847 AA; 94310 MW; 297FF5E3E7AAB7B4 CRC64;
MNYVGQLAET VFGTVKELYR GLNPATLSGG IDVLVVRQRD GSFRCSPFHV RFGKLGVLRS
REKVVDIEIN GEPVDLHMKL GDSGEAFFVQ ELDSDEEDVP PRLCTSPIPW GGLSGFPSDS
QIGTASEPEG LVITGRRKRR RRRKPRRKED VVDSSSEELE AGVESELTLL EKPTPESPSA
QEEEETSSQP KDIHPYSDGE CTPQANLSSG DLMSPKSDSE LELRSLEPSP LRAESHMQWV
WGRLPKVAKA ERPEFSLILE SMAEAICALP EEPSPSSSPS EAGVDTLSPP VLHPGVRADK
FHPAVEAHCE ETAVDSPLAA PESKETKTQN SRGAGHPPAT KSWSWTTPES HTPSGHPQVS
RGKGSLKRNQ HLGPSDIYLD DLPSLDSENV ALYFPKSEYG MGARRWSEPS NQKLLESPNL
EHIAECTLDS VDKIELSLCG GLADNRDISL EKFTQHMVSY EDLTKNPGLL DDPNLVVKIN
EKHYNWAVAA PMILSMQAFQ KNLPESTVDK LEKEKMPRKG GRWWFSWRRK DFPAEEHSSQ
REKAATRKQQ GEKTEVLSSD DDVPDSPVIL EVPPLPSSTP GYVPTYKKSL RLSSDQIRCL
NLNEGANDVV FSVTTQYQGT CRCKATIYLW NWDDKVVISD IDGTITKSDA LGHILPQLGK
DWTHQGITSL YHKIHLNGYK FLYCSARAIG MADLTKGYLQ WVSEHGCGLP KGPILLSPSS
LFSALHREVI EKKPEVFKVA CLSDIQQLFL PQRQPFHAAF GNRPNDVFAY RQVGLPESRI
FTVNPRGELI QELIKSHKST YQRLGEVVEL LFPPVVRGPS TDLASPEYSN LSYWRKPLPY
VDFEALA
