CDIPT_RAT
ID CDIPT_RAT Reviewed; 213 AA.
AC P70500;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=CDP-diacylglycerol--inositol 3-phosphatidyltransferase {ECO:0000305};
DE EC=2.7.8.11 {ECO:0000269|PubMed:7998949};
DE AltName: Full=Phosphatidylinositol synthase;
DE Short=PI synthase;
DE Short=PtdIns synthase;
GN Name=Cdipt {ECO:0000312|RGD:620576}; Synonyms=Pis1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8804431; DOI=10.1016/0014-5793(96)00858-7;
RA Tanaka S., Nikawa J., Imai H., Yamashita S., Hosaka K.;
RT "Molecular cloning of rat phosphatidylinositol synthase cDNA by functional
RT complementation of the yeast Saccharomyces cerevisiae pis mutation.";
RL FEBS Lett. 393:89-92(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nikawa J., Kojima S., Syugyo M.;
RT "Exon-intron structure of rat phosphatidylinositol synthase.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
RC TISSUE=Pituitary;
RX PubMed=3032971; DOI=10.1016/s0021-9258(18)48262-2;
RA Imai A., Gershengorn M.C.;
RT "Regulation by phosphatidylinositol of rat pituitary plasma membrane and
RT endoplasmic reticulum phosphatidylinositol synthase activities. A mechanism
RT for activation of phosphoinositide resynthesis during cell stimulation.";
RL J. Biol. Chem. 262:6457-6459(1987).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=7998949; DOI=10.1042/bj3040301;
RA Monaco M.E., Feldman M., Kleinberg D.L.;
RT "Identification of rat liver phosphatidylinositol synthase as a 21 kDa
RT protein.";
RL Biochem. J. 304:301-305(1994).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC -!- FUNCTION: Catalyzes the biosynthesis of phosphatidylinositol (PtdIns)
CC as well as PtdIns:inositol exchange reaction. May thus act to reduce an
CC excessive cellular PtdIns content. The exchange activity is due to the
CC reverse reaction of PtdIns synthase and is dependent on CMP, which is
CC tightly bound to the enzyme. {ECO:0000269|PubMed:3032971,
CC ECO:0000269|PubMed:7998949}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-
CC glycero-3-phospho-(1D-myo-inositol) + CMP + H(+);
CC Xref=Rhea:RHEA:11580, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.11;
CC Evidence={ECO:0000269|PubMed:3032971, ECO:0000269|PubMed:7998949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11581;
CC Evidence={ECO:0000250|UniProtKB:O14735};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11582;
CC Evidence={ECO:0000250|UniProtKB:O14735};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:3032971, ECO:0000269|PubMed:7998949};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:3032971, ECO:0000269|PubMed:7998949};
CC Note=Divalent metal cations; Mn(2+) or Mg(2+) (PubMed:3032971).
CC According to PubMed:7998949 the cofactor is Mn(2+), while Mg(2+) is
CC much less effective. {ECO:0000269|PubMed:3032971,
CC ECO:0000269|PubMed:7998949};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:3032971}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:3032971}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level). Widely
CC expressed. Highly expressed in the brain and kidney; lower levels in
CC heart, spleen, lung, liver, skeletal muscle and testis.
CC {ECO:0000269|PubMed:7998949}.
CC -!- INDUCTION: Inhibited by PtdIns (product inhibition).
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {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; D82928; BAA11634.1; -; mRNA.
DR EMBL; AB022890; BAA82112.1; -; Genomic_DNA.
DR EMBL; BC070876; AAH70876.1; -; mRNA.
DR PIR; S74247; S74247.
DR RefSeq; NP_620254.1; NM_138899.2.
DR RefSeq; XP_006230270.1; XM_006230208.1.
DR AlphaFoldDB; P70500; -.
DR SMR; P70500; -.
DR IntAct; P70500; 1.
DR STRING; 10116.ENSRNOP00000013691; -.
DR iPTMnet; P70500; -.
DR PhosphoSitePlus; P70500; -.
DR jPOST; P70500; -.
DR PaxDb; P70500; -.
DR PRIDE; P70500; -.
DR Ensembl; ENSRNOT00000091295; ENSRNOP00000070871; ENSRNOG00000024144.
DR GeneID; 192260; -.
DR KEGG; rno:192260; -.
DR UCSC; RGD:620576; rat.
DR CTD; 10423; -.
DR RGD; 620576; Cdipt.
DR eggNOG; KOG3240; Eukaryota.
DR GeneTree; ENSGT00940000154169; -.
DR HOGENOM; CLU_067602_2_0_1; -.
DR InParanoid; P70500; -.
DR OMA; AQTYSEN; -.
DR OrthoDB; 1615564at2759; -.
DR PhylomeDB; P70500; -.
DR TreeFam; TF314603; -.
DR Reactome; R-RNO-1483226; Synthesis of PI.
DR PRO; PR:P70500; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000024144; Expressed in cerebellum and 20 other tissues.
DR Genevisible; P70500; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043178; F:alcohol binding; IPI:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IPI:RGD.
DR GO; GO:0003881; F:CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity; IDA:RGD.
DR GO; GO:0019992; F:diacylglycerol binding; IPI:RGD.
DR GO; GO:0030145; F:manganese ion binding; IDA:RGD.
DR GO; GO:0046341; P:CDP-diacylglycerol metabolic process; IDA:RGD.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IDA:RGD.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR014387; CDP_diag_ino_3_P_euk.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF000848; CDP_diag_ino_3_P; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Manganese; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..213
FT /note="CDP-diacylglycerol--inositol 3-
FT phosphatidyltransferase"
FT /id="PRO_0000056804"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 213 AA; 23613 MW; 93C7137664EAABB2 CRC64;
MPEENIFLFV PNLIGYARIV FAIISFYFMP CCPFTASSFY LLSGLLDAFD GHAARALNQG
TRFGAMLDML TDRCATMCLL VNLALLYPRA TLLFQLSMSL DVASHWLHLH SSVVRGSESH
KMIDLSGNPV LRIYYTSRPA LFTLCAGNEL FYCLLYLFNF SEGPLVGSVG LFRMGLWITA
PIALLKSIIS VIHLVTAARN MAALDAADRA KKK
