CDIPT_MOUSE
ID CDIPT_MOUSE Reviewed; 213 AA.
AC Q8VDP6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, 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:0000250|UniProtKB:O14735, ECO:0000250|UniProtKB:P70500};
DE AltName: Full=Phosphatidylinositol synthase;
DE Short=PI synthase;
DE Short=PtdIns synthase;
GN Name=Cdipt {ECO:0000312|MGI:MGI:105491}; Synonyms=Pis1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Testis, Thymus, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
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 [3]
RP PROTEIN SEQUENCE OF 63-73 AND 122-132, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:O14735}.
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:0000250|UniProtKB:O14735};
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:0000250|UniProtKB:O14735};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O14735};
CC Note=Divalent metal cations; Mn(2+) or Mg(2+).
CC {ECO:0000250|UniProtKB:O14735};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O14735}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O14735}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; AK076974; BAC36542.1; -; mRNA.
DR EMBL; AK079226; BAC37580.1; -; mRNA.
DR EMBL; AK089109; BAC40756.1; -; mRNA.
DR EMBL; BC021473; AAH21473.1; -; mRNA.
DR EMBL; BC024413; AAH24413.1; -; mRNA.
DR CCDS; CCDS21853.1; -.
DR RefSeq; NP_080914.1; NM_026638.3.
DR AlphaFoldDB; Q8VDP6; -.
DR SMR; Q8VDP6; -.
DR BioGRID; 206858; 10.
DR IntAct; Q8VDP6; 1.
DR MINT; Q8VDP6; -.
DR STRING; 10090.ENSMUSP00000032920; -.
DR ChEMBL; CHEMBL2176; -.
DR iPTMnet; Q8VDP6; -.
DR PhosphoSitePlus; Q8VDP6; -.
DR SwissPalm; Q8VDP6; -.
DR EPD; Q8VDP6; -.
DR jPOST; Q8VDP6; -.
DR MaxQB; Q8VDP6; -.
DR PaxDb; Q8VDP6; -.
DR PeptideAtlas; Q8VDP6; -.
DR PRIDE; Q8VDP6; -.
DR ProteomicsDB; 281286; -.
DR Antibodypedia; 26862; 69 antibodies from 16 providers.
DR DNASU; 52858; -.
DR Ensembl; ENSMUST00000032920; ENSMUSP00000032920; ENSMUSG00000030682.
DR GeneID; 52858; -.
DR KEGG; mmu:52858; -.
DR UCSC; uc009jtv.2; mouse.
DR CTD; 10423; -.
DR MGI; MGI:105491; Cdipt.
DR VEuPathDB; HostDB:ENSMUSG00000030682; -.
DR eggNOG; KOG3240; Eukaryota.
DR GeneTree; ENSGT00940000154169; -.
DR HOGENOM; CLU_067602_2_0_1; -.
DR InParanoid; Q8VDP6; -.
DR OMA; AQTYSEN; -.
DR OrthoDB; 1615564at2759; -.
DR PhylomeDB; Q8VDP6; -.
DR TreeFam; TF314603; -.
DR Reactome; R-MMU-1483226; Synthesis of PI.
DR BioGRID-ORCS; 52858; 28 hits in 75 CRISPR screens.
DR ChiTaRS; Cdipt; mouse.
DR PRO; PR:Q8VDP6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8VDP6; protein.
DR Bgee; ENSMUSG00000030682; Expressed in paneth cell and 264 other tissues.
DR ExpressionAtlas; Q8VDP6; baseline and differential.
DR Genevisible; Q8VDP6; MM.
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; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0003881; F:CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019992; F:diacylglycerol binding; ISO:MGI.
DR GO; GO:0030145; F:manganese ion binding; ISO:MGI.
DR GO; GO:0046341; P:CDP-diacylglycerol metabolic process; ISO:MGI.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISS:UniProtKB.
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; Direct protein sequencing; Endoplasmic reticulum;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..213
FT /note="CDP-diacylglycerol--inositol 3-
FT phosphatidyltransferase"
FT /id="PRO_0000056803"
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; 23599 MW; 93D9F4E60CD13BB2 CRC64;
MPEENIFLFV PNLIGYARIV FAIISFYFMP CCPFTASSFY LLSGLLDAFD GHAARALNQG
TRFGAMLDML TDRCATMCLL VNLALLYPRA TLLFQLSMSL DVASHWLHLH SSVVRGSESH
KMIDLSGNPV LRIYYTSRPA LFTLCAGNEL FYCLLYLFNF SEGPLVGSVG LFRMGLWVTA
PIALLKSVIS VIHLITAARN MAALDAADRA KKK
