CHPT1_MOUSE
ID CHPT1_MOUSE Reviewed; 398 AA.
AC Q8C025; Q6SXV1; Q8K0H2; Q91W91;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cholinephosphotransferase 1 {ECO:0000305};
DE Short=mCHPT1;
DE EC=2.7.8.2 {ECO:0000250|UniProtKB:Q8WUD6};
DE AltName: Full=Diabetic nephropathy-associated gene transcript 1;
DE AltName: Full=Diacylglycerol cholinephosphotransferase 1;
GN Name=Chpt1 {ECO:0000312|MGI:MGI:2384841}; Synonyms=Cpt1, Dn4;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=KK Obese;
RX PubMed=15254874; DOI=10.1016/j.metabol.2004.02.002;
RA Gohda T., Tanimoto M., Shiina K., Ito T., Kobayashi M., Hagiwara S.,
RA Kaneko S., Makita Y., Funabiki K., Horikoshi S., Tomino Y.;
RT "Altered mouse cholinephosphotransferase gene expression in kidneys of type
RT 2 diabetic KK/TA mouse.";
RL Metabolism 53:842-846(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=FVB/N; TISSUE=Kidney, and Salivary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, and Lung;
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 phosphatidylcholine biosynthesis from CDP-choline.
CC It thereby plays a central role in the formation and maintenance of
CC vesicular membranes. {ECO:0000250|UniProtKB:Q8WUD6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + CDP-choline = a 1,2-diacyl-sn-
CC glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:32939,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:58779, ChEBI:CHEBI:60377; EC=2.7.8.2;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32940;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC + CDP-choline = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54344,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:74965, ChEBI:CHEBI:75728;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54345;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CDP-choline =
CC 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + CMP
CC + H(+); Xref=Rhea:RHEA:54244, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:73001, ChEBI:CHEBI:75466;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54245;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycerol + CDP-choline = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphocholine + CMP + H(+);
CC Xref=Rhea:RHEA:54332, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:74963, ChEBI:CHEBI:82949;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54333;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 2/2.
CC {ECO:0000250|UniProtKB:Q8WUD6}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8WUD6}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8WUD6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8C025-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C025-2; Sequence=VSP_025991, VSP_025994;
CC Name=3;
CC IsoId=Q8C025-3; Sequence=VSP_025992, VSP_025993;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, lung, liver, spleen,
CC intestine and muscle. Down-regulated in kidney of type 2 diabetic KK/Ta
CC mice. {ECO:0000269|PubMed:15254874}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; AY445814; AAR16089.1; -; mRNA.
DR EMBL; AK032497; BAC27897.1; -; mRNA.
DR EMBL; BC016251; AAH16251.1; -; mRNA.
DR EMBL; BC031435; AAH31435.1; -; mRNA.
DR CCDS; CCDS24112.1; -. [Q8C025-1]
DR PIR; S12207; S12207.
DR RefSeq; NP_659056.3; NM_144807.3. [Q8C025-1]
DR AlphaFoldDB; Q8C025; -.
DR STRING; 10090.ENSMUSP00000112708; -.
DR iPTMnet; Q8C025; -.
DR PhosphoSitePlus; Q8C025; -.
DR jPOST; Q8C025; -.
DR MaxQB; Q8C025; -.
DR PaxDb; Q8C025; -.
DR PRIDE; Q8C025; -.
DR ProteomicsDB; 283910; -. [Q8C025-1]
DR ProteomicsDB; 283911; -. [Q8C025-2]
DR ProteomicsDB; 283912; -. [Q8C025-3]
DR Antibodypedia; 55006; 98 antibodies from 19 providers.
DR DNASU; 212862; -.
DR Ensembl; ENSMUST00000020253; ENSMUSP00000020253; ENSMUSG00000060002. [Q8C025-1]
DR Ensembl; ENSMUST00000073783; ENSMUSP00000073455; ENSMUSG00000060002. [Q8C025-2]
DR Ensembl; ENSMUST00000139109; ENSMUSP00000116413; ENSMUSG00000060002. [Q8C025-1]
DR GeneID; 212862; -.
DR KEGG; mmu:212862; -.
DR UCSC; uc007grr.2; mouse. [Q8C025-1]
DR UCSC; uc007grs.2; mouse. [Q8C025-2]
DR CTD; 56994; -.
DR MGI; MGI:2384841; Chpt1.
DR VEuPathDB; HostDB:ENSMUSG00000060002; -.
DR eggNOG; KOG2877; Eukaryota.
DR GeneTree; ENSGT00950000183117; -.
DR InParanoid; Q8C025; -.
DR OMA; MTRSELY; -.
DR PhylomeDB; Q8C025; -.
DR Reactome; R-MMU-1483191; Synthesis of PC.
DR UniPathway; UPA00753; UER00740.
DR BioGRID-ORCS; 212862; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Chpt1; mouse.
DR PRO; PR:Q8C025; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8C025; protein.
DR Bgee; ENSMUSG00000060002; Expressed in right kidney and 253 other tissues.
DR ExpressionAtlas; Q8C025; baseline and differential.
DR Genevisible; Q8C025; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004142; F:diacylglycerol cholinephosphotransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IDA:MGI.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:MGI.
DR GO; GO:0006663; P:platelet activating factor 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; IPR014472; CHOPT.
DR PANTHER; PTHR10414; PTHR10414; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF015665; CHOPT; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Golgi apparatus; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Manganese; Membrane; Metal-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WUD6"
FT CHAIN 2..398
FT /note="Cholinephosphotransferase 1"
FT /id="PRO_0000289253"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUD6"
FT VAR_SEQ 188..237
FT /note="RVDVTEIQVALVIVFMLSTFGGATMWDYTIPILEIKLKIVPVLGVVGGLI
FT -> SQEVFFRAGEMAQWVRAPDCSSEGPEFKSQQPHGGSQPSVTRSDALFWSV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025991"
FT VAR_SEQ 188..229
FT /note="RVDVTEIQVALVIVFMLSTFGGATMWDYTIPILEIKLKIVPV -> RWRTLS
FT SLSSTMPAACHHASCHNDHGLNLGTLNQLQWNVFFL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025992"
FT VAR_SEQ 230..398
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025993"
FT VAR_SEQ 238..398
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025994"
FT CONFLICT 28
FT /note="R -> W (in Ref. 3; AAH16251)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="W -> G (in Ref. 1; AAR16089)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="M -> L (in Ref. 1; AAR16089)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 44608 MW; 09DCC40C0F0D8CEF CRC64;
MAAGAGARPA PRWVKALGEP LSAAQLRRLE EHRYTAVGES LFEPPLQLYW TWLLQWIPLW
MAPNTITLIG LAINLVTTLV LIFYCPTVTE EAPYWTYLLC ALGLFIYQSL DAIDGKQARR
TNSCSPLGEL FDHGCDSLST VFMAIGASIA VRLGTHPDWL FFCSFVGMFM FYCAHWQTYV
SGVLRFGRVD VTEIQVALVI VFMLSTFGGA TMWDYTIPIL EIKLKIVPVL GVVGGLIFSC
SNYFHVILHG GVGKNGSTIA GTSVLSPGLH IGLIIILAIM IYKKSATNMF EKHPCLYTLM
FGCVFAKVAQ KLVIAHMTKS ELYLQDTVFI GPGLLFLDQY FNNFIDEYVV LWIAMVISSF
DMMIYFTSLC LQISRHLHLN IFKTSCQQAP EQVYKHID
