CHPT1_HUMAN
ID CHPT1_HUMAN Reviewed; 406 AA.
AC Q8WUD6; B3KQM2; Q7Z7H0; Q7Z7H1; Q7Z7H2; Q8IWQ4; Q8IWQ5; Q8WYI4; Q9NRQ6;
AC Q9NRQ7; Q9Y6M6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Cholinephosphotransferase 1 {ECO:0000305};
DE Short=hCPT1 {ECO:0000303|PubMed:10893425};
DE EC=2.7.8.2 {ECO:0000269|PubMed:10893425};
DE AltName: Full=AAPT1-like protein;
DE AltName: Full=Diacylglycerol cholinephosphotransferase 1;
GN Name=CHPT1 {ECO:0000312|HGNC:HGNC:17852}; Synonyms=CPT1; ORFNames=MSTP022;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ENZYME ACTIVITY, COFACTOR,
RP TISSUE SPECIFICITY, VARIANT SER-162, CATALYTIC ACTIVITY, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=10893425; DOI=10.1074/jbc.m005786200;
RA Henneberry A.L., Wistow G., McMaster C.R.;
RT "Cloning, genomic organization, and characterization of a human
RT cholinephosphotransferase.";
RL J. Biol. Chem. 275:29808-29815(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 70-406.
RA Zhang Q., Mao M., Fu G., Huang Q., Zhou J., Yu Y., Xu S., Shen Y.,
RA Huang Q., Wang Y., Chen Z.;
RT "Human AAPT1-like gene.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-406.
RC TISSUE=Heart;
RA Xu Y.Y., Sun L.Z., Wu Q.Y., Liu Y.Q., Liu B., Zhao B., Wang X.Y., Song L.,
RA Ye J., Sheng H., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Sun Y.H.,
RA Jiang Y.X., Zhao X.W., Liu S., Liu L.S., Ding J.F., Gao R.L., Qiang B.Q.,
RA Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 174-406.
RX PubMed=16292752; DOI=10.1002/jbt.20092;
RA Sinha Roy S., Mukherjee S., Kabir S., Rajaratnam V., Smith M., Das S.K.;
RT "Inhibition of cholinephosphotransferase activity in lung injury induced by
RT 2-chloroethyl ethyl sulfide, a mustard analog.";
RL J. Biochem. Mol. Toxicol. 19:289-297(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 235-371, TISSUE SPECIFICITY, AND VARIANT
RP SER-323.
RX PubMed=12359261; DOI=10.1016/s0006-291x(02)02332-x;
RA Ghosh A., Akech J., Mukherjee S., Das S.K.;
RT "Differential expression of cholinephosphotransferase in normal and
RT cancerous human mammary epithelial cells.";
RL Biochem. Biophys. Res. Commun. 297:1043-1048(2002).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=12221122; DOI=10.1091/mbc.01-11-0540;
RA Henneberry A.L., Wright M.M., McMaster C.R.;
RT "The major sites of cellular phospholipid synthesis and molecular
RT determinants of fatty acid and lipid head group specificity.";
RL Mol. Biol. Cell 13:3148-3161(2002).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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:0000269|PubMed:10893425}.
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:0000269|PubMed:10893425};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32940;
CC Evidence={ECO:0000305|PubMed:10893425};
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:0000269|PubMed:10893425};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54345;
CC Evidence={ECO:0000305|PubMed:10893425};
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:0000269|PubMed:10893425};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54245;
CC Evidence={ECO:0000305|PubMed:10893425};
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:0000269|PubMed:10893425};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54333;
CC Evidence={ECO:0000305|PubMed:10893425};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10893425};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10893425};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 2/2.
CC {ECO:0000269|PubMed:10893425}.
CC -!- INTERACTION:
CC Q8WUD6; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-11337856, EBI-12947623;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12221122}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12221122}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q8WUD6-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q8WUD6-2; Sequence=VSP_025989, VSP_025990;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, colon, small intestine,
CC heart, prostate and spleen. Also detected in kidney, skeletal muscle,
CC pancreas, leukocytes, ovary and thymus. Weakly expressed in the brain,
CC placenta and lung. Overexpressed in cancerous breast epithelial cell
CC lines. {ECO:0000269|PubMed:10893425, ECO:0000269|PubMed:12359261}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD44019.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL39005.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF195623; AAF87947.1; -; mRNA.
DR EMBL; AF195624; AAF87948.1; -; mRNA.
DR EMBL; AK075211; BAG52084.1; -; mRNA.
DR EMBL; CH471054; EAW97675.1; -; Genomic_DNA.
DR EMBL; BC020819; AAH20819.1; -; mRNA.
DR EMBL; BC050429; AAH50429.1; -; mRNA.
DR EMBL; AF047431; AAD44019.1; ALT_FRAME; mRNA.
DR EMBL; AF111803; AAL39005.1; ALT_INIT; mRNA.
DR EMBL; AY280609; AAP34412.1; -; mRNA.
DR EMBL; AY280610; AAP34413.1; -; mRNA.
DR EMBL; AY294627; AAP37157.1; -; mRNA.
DR EMBL; AY166717; AAN86122.1; -; mRNA.
DR EMBL; AY166718; AAN86123.1; -; mRNA.
DR CCDS; CCDS9086.1; -. [Q8WUD6-1]
DR RefSeq; NP_064629.2; NM_020244.2. [Q8WUD6-1]
DR AlphaFoldDB; Q8WUD6; -.
DR BioGRID; 121309; 65.
DR IntAct; Q8WUD6; 36.
DR MINT; Q8WUD6; -.
DR STRING; 9606.ENSP00000229266; -.
DR SwissLipids; SLP:000001750; -. [Q8WUD6-1]
DR iPTMnet; Q8WUD6; -.
DR PhosphoSitePlus; Q8WUD6; -.
DR SwissPalm; Q8WUD6; -.
DR BioMuta; CHPT1; -.
DR DMDM; 74730698; -.
DR EPD; Q8WUD6; -.
DR jPOST; Q8WUD6; -.
DR MassIVE; Q8WUD6; -.
DR MaxQB; Q8WUD6; -.
DR PaxDb; Q8WUD6; -.
DR PeptideAtlas; Q8WUD6; -.
DR PRIDE; Q8WUD6; -.
DR ProteomicsDB; 74659; -. [Q8WUD6-1]
DR ProteomicsDB; 74660; -. [Q8WUD6-2]
DR Antibodypedia; 55006; 98 antibodies from 19 providers.
DR DNASU; 56994; -.
DR Ensembl; ENST00000229266.8; ENSP00000229266.3; ENSG00000111666.11. [Q8WUD6-1]
DR Ensembl; ENST00000552351.5; ENSP00000447887.1; ENSG00000111666.11. [Q8WUD6-2]
DR GeneID; 56994; -.
DR KEGG; hsa:56994; -.
DR MANE-Select; ENST00000229266.8; ENSP00000229266.3; NM_020244.3; NP_064629.2.
DR UCSC; uc001tin.4; human. [Q8WUD6-1]
DR CTD; 56994; -.
DR DisGeNET; 56994; -.
DR GeneCards; CHPT1; -.
DR HGNC; HGNC:17852; CHPT1.
DR HPA; ENSG00000111666; Low tissue specificity.
DR MalaCards; CHPT1; -.
DR MIM; 616747; gene.
DR neXtProt; NX_Q8WUD6; -.
DR OpenTargets; ENSG00000111666; -.
DR PharmGKB; PA26477; -.
DR VEuPathDB; HostDB:ENSG00000111666; -.
DR eggNOG; KOG2877; Eukaryota.
DR GeneTree; ENSGT00950000183117; -.
DR HOGENOM; CLU_035066_1_0_1; -.
DR InParanoid; Q8WUD6; -.
DR OMA; CKEPISM; -.
DR OrthoDB; 847100at2759; -.
DR PhylomeDB; Q8WUD6; -.
DR TreeFam; TF313270; -.
DR BRENDA; 2.7.8.2; 2681.
DR PathwayCommons; Q8WUD6; -.
DR Reactome; R-HSA-1483191; Synthesis of PC.
DR SignaLink; Q8WUD6; -.
DR UniPathway; UPA00753; UER00740.
DR BioGRID-ORCS; 56994; 13 hits in 1078 CRISPR screens.
DR ChiTaRS; CHPT1; human.
DR GenomeRNAi; 56994; -.
DR Pharos; Q8WUD6; Tbio.
DR PRO; PR:Q8WUD6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8WUD6; protein.
DR Bgee; ENSG00000111666; Expressed in jejunal mucosa and 203 other tissues.
DR ExpressionAtlas; Q8WUD6; baseline and differential.
DR Genevisible; Q8WUD6; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0019992; F:diacylglycerol binding; NAS:UniProtKB.
DR GO; GO:0004142; F:diacylglycerol cholinephosphotransferase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006657; P:CDP-choline pathway; NAS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006663; P:platelet activating factor biosynthetic process; IDA:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; NAS: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:0007744|PubMed:22814378"
FT CHAIN 2..406
FT /note="Cholinephosphotransferase 1"
FT /id="PRO_0000289252"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
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:0007744|PubMed:22814378"
FT VAR_SEQ 217..218
FT /note="IP -> FS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10893425"
FT /id="VSP_025989"
FT VAR_SEQ 219..406
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10893425"
FT /id="VSP_025990"
FT VARIANT 162
FT /note="F -> S (in dbSNP:rs3205421)"
FT /evidence="ECO:0000269|PubMed:10893425"
FT /id="VAR_032612"
FT VARIANT 323
FT /note="Y -> S (in MCF-12A cell line)"
FT /evidence="ECO:0000269|PubMed:12359261"
FT /id="VAR_032613"
FT CONFLICT 86
FT /note="P -> L (in Ref. 5; AAD44019)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="S -> P (in Ref. 5; AAD44019)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="L -> P (in Ref. 5; AAD44019)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="D -> G (in Ref. 5; AAD44019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 45097 MW; AE5357C02ED40E4C CRC64;
MAAGAGAGSA PRWLRALSEP LSAAQLRRLE EHRYSAAGVS LLEPPLQLYW TWLLQWIPLW
MAPNSITLLG LAVNVVTTLV LISYCPTATE EAPYWTYLLC ALGLFIYQSL DAIDGKQARR
TNSCSPLGEL FDHGCDSLST VFMAVGASIA ARLGTYPDWF FFCSFIGMFV FYCAHWQTYV
SGMLRFGKVD VTEIQIALVI VFVLSAFGGA TMWDYTIPIL EIKLKILPVL GFLGGVIFSC
SNYFHVILHG GVGKNGSTIA GTSVLSPGLH IGLIIILAIM IYKKSATDVF EKHPCLYILM
FGCVFAKVSQ KLVVAHMTKS ELYLQDTVFL GPGLLFLDQY FNNFIDEYVV LWMAMVISSF
DMVIYFSALC LQISRHLHLN IFKTACHQAP EQVQVLSSKS HQNNMD
