PCY2_MOUSE
ID PCY2_MOUSE Reviewed; 404 AA.
AC Q922E4; Q99J50;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ethanolamine-phosphate cytidylyltransferase;
DE EC=2.7.7.14 {ECO:0000269|PubMed:17325045};
DE AltName: Full=CTP:phosphoethanolamine cytidylyltransferase;
DE AltName: Full=Phosphorylethanolamine transferase;
GN Name=Pcyt2;
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].
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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=17325045; DOI=10.1128/mcb.01527-06;
RA Fullerton M.D., Hakimuddin F., Bakovic M.;
RT "Developmental and metabolic effects of disruption of the mouse
RT CTP:phosphoethanolamine cytidylyltransferase gene (Pcyt2).";
RL Mol. Cell. Biol. 27:3327-3336(2007).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Ethanolamine-phosphate cytidylyltransferase that catalyzes
CC the second step in the synthesis of phosphatidylethanolamine (PE) from
CC ethanolamine via the CDP-ethanolamine pathway (PubMed:17325045).
CC Phosphatidylethanolamine is a dominant inner-leaflet phospholipid in
CC cell membranes, where it plays a role in membrane function by
CC structurally stabilizing membrane-anchored proteins, and participates
CC in important cellular processes such as cell division, cell fusion,
CC blood coagulation, and apoptosis (PubMed:17325045).
CC {ECO:0000269|PubMed:17325045, ECO:0000303|PubMed:17325045}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H(+) + phosphoethanolamine = CDP-ethanolamine +
CC diphosphate; Xref=Rhea:RHEA:24592, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57876,
CC ChEBI:CHEBI:58190; EC=2.7.7.14;
CC Evidence={ECO:0000269|PubMed:17325045};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24593;
CC Evidence={ECO:0000269|PubMed:17325045};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
CC {ECO:0000269|PubMed:17325045}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout embryos die after
CC implantation, prior to embryonic day 8.5.
CC {ECO:0000269|PubMed:17325045}.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR EMBL; BC003473; AAH03473.1; -; mRNA.
DR EMBL; BC008276; AAH08276.1; -; mRNA.
DR CCDS; CCDS25747.1; -.
DR RefSeq; NP_077191.2; NM_024229.2.
DR AlphaFoldDB; Q922E4; -.
DR SMR; Q922E4; -.
DR BioGRID; 212982; 5.
DR STRING; 10090.ENSMUSP00000026129; -.
DR iPTMnet; Q922E4; -.
DR PhosphoSitePlus; Q922E4; -.
DR SwissPalm; Q922E4; -.
DR UCD-2DPAGE; Q922E4; -.
DR EPD; Q922E4; -.
DR jPOST; Q922E4; -.
DR MaxQB; Q922E4; -.
DR PaxDb; Q922E4; -.
DR PRIDE; Q922E4; -.
DR ProteomicsDB; 287981; -.
DR Antibodypedia; 19846; 131 antibodies from 25 providers.
DR DNASU; 68671; -.
DR Ensembl; ENSMUST00000026129; ENSMUSP00000026129; ENSMUSG00000025137.
DR GeneID; 68671; -.
DR KEGG; mmu:68671; -.
DR UCSC; uc007mtp.1; mouse.
DR CTD; 5833; -.
DR MGI; MGI:1915921; Pcyt2.
DR VEuPathDB; HostDB:ENSMUSG00000025137; -.
DR eggNOG; KOG2803; Eukaryota.
DR GeneTree; ENSGT00550000075065; -.
DR InParanoid; Q922E4; -.
DR OMA; VLQCKYI; -.
DR OrthoDB; 871204at2759; -.
DR PhylomeDB; Q922E4; -.
DR TreeFam; TF106337; -.
DR BRENDA; 2.7.7.14; 3474.
DR Reactome; R-MMU-1483213; Synthesis of PE.
DR UniPathway; UPA00558; UER00742.
DR BioGRID-ORCS; 68671; 22 hits in 75 CRISPR screens.
DR ChiTaRS; Pcyt2; mouse.
DR PRO; PR:Q922E4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q922E4; protein.
DR Bgee; ENSMUSG00000025137; Expressed in left lobe of liver and 272 other tissues.
DR ExpressionAtlas; Q922E4; baseline and differential.
DR Genevisible; Q922E4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004306; F:ethanolamine-phosphate cytidylyltransferase activity; IMP:UniProtKB.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IMP:UniProtKB.
DR CDD; cd02174; CCT; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR InterPro; IPR041723; CCT.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR044608; Ect1/PCYT2.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR45780; PTHR45780; 1.
DR Pfam; PF01467; CTP_transf_like; 2.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 2.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Nucleotidyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..404
FT /note="Ethanolamine-phosphate cytidylyltransferase"
FT /id="PRO_0000208462"
FT REGION 173..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239..240
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 247..250
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 325..328
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 354..358
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99447"
FT MOD_RES 359
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99447"
FT MOD_RES 360
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88637"
FT CONFLICT 110
FT /note="C -> S (in Ref. 1; AAH03473)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 404 AA; 45235 MW; D45A76E2EB0C9327 CRC64;
MIRNGHGAAS AAGLKGPGDQ RIVRVWCDGC YDMVHYGHSN QLRQARAMGD YLIVGVHTDE
EIAKHKGPPV FTQEERYKMV QAIKWVDEVV PAAPYVTTLE TLDKHNCDFC VHGNDITLTV
DGRDTYEEVK QAGRYRECKR TQGVSTTDLV GRMLLVTKAH HSSQEMSSEY REYADSFGKP
PHPTPAGDTL SSEVSSQCPG GQSPWTGVSQ FLQTSQKIIQ FASGKEPQPG ETVIYVAGAF
DLFHIGHVDF LQEVHKLAKR PYVIAGLHFD QEVNRYKGKN YPIMNLHERT LSVLACRYVS
EVVIGAPYSV TAELLNHFKV DLVCHGKTEI VPDRDGSDPY QEPKRRGIFY QIDSGSDLTT
DLIVQRIIKN RLEYEARNQK KEAKELAFLE ATKQQEAPPG GEID
