PCY2_RAT
ID PCY2_RAT Reviewed; 404 AA.
AC O88637; Q6AZ30;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Ethanolamine-phosphate cytidylyltransferase;
DE EC=2.7.7.14 {ECO:0000250|UniProtKB:Q99447};
DE AltName: Full=CTP:phosphoethanolamine cytidylyltransferase;
DE AltName: Full=Phosphorylethanolamine transferase;
GN Name=Pcyt2;
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] (ISOFORM 1).
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=10493918; DOI=10.1042/bj3430107;
RA Bladergroen B.A., Houweling M., Geelen M.J.H., van Golde L.M.G.;
RT "Cloning and expression of CTP:phosphoethanolamine cytidylyltransferase
RT cDNA from rat liver.";
RL Biochem. J. 343:107-114(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 298-319, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-360, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Phosphatidylethanolamine
CC is a dominant inner-leaflet phospholipid in cell membranes, where it
CC plays a role in membrane function by structurally stabilizing membrane-
CC anchored proteins, and participates in important cellular processes
CC such as cell division, cell fusion, blood coagulation, and apoptosis.
CC {ECO:0000250|UniProtKB:Q99447}.
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:0000250|UniProtKB:Q99447};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24593;
CC Evidence={ECO:0000250|UniProtKB:Q99447};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
CC {ECO:0000250|UniProtKB:Q99447}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O88637-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88637-2; Sequence=VSP_022116;
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR EMBL; AF080568; AAC28864.1; -; mRNA.
DR EMBL; BC078772; AAH78772.1; -; mRNA.
DR RefSeq; NP_446020.1; NM_053568.1. [O88637-1]
DR RefSeq; XP_006247997.1; XM_006247935.3. [O88637-2]
DR AlphaFoldDB; O88637; -.
DR SMR; O88637; -.
DR IntAct; O88637; 2.
DR STRING; 10116.ENSRNOP00000051835; -.
DR iPTMnet; O88637; -.
DR PhosphoSitePlus; O88637; -.
DR jPOST; O88637; -.
DR PaxDb; O88637; -.
DR PRIDE; O88637; -.
DR GeneID; 89841; -.
DR KEGG; rno:89841; -.
DR CTD; 5833; -.
DR RGD; 619970; Pcyt2.
DR VEuPathDB; HostDB:ENSRNOG00000036684; -.
DR eggNOG; KOG2803; Eukaryota.
DR HOGENOM; CLU_031246_2_2_1; -.
DR InParanoid; O88637; -.
DR OMA; VLQCKYI; -.
DR OrthoDB; 871204at2759; -.
DR PhylomeDB; O88637; -.
DR TreeFam; TF106337; -.
DR Reactome; R-RNO-1483213; Synthesis of PE.
DR UniPathway; UPA00558; UER00742.
DR PRO; PR:O88637; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000036684; Expressed in liver and 20 other tissues.
DR Genevisible; O88637; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004306; F:ethanolamine-phosphate cytidylyltransferase activity; IDA:RGD.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISS: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 Alternative splicing; Direct protein sequencing; Lipid biosynthesis;
KW Lipid metabolism; Nucleotidyltransferase; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..404
FT /note="Ethanolamine-phosphate cytidylyltransferase"
FT /id="PRO_0000208463"
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:0007744|PubMed:22673903"
FT VAR_SEQ 180..197
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022116"
SQ SEQUENCE 404 AA; 45220 MW; 4B0B6A9315B32CE3 CRC64;
MIRNGHGAGG AAGLKGPGGQ RTVRVWCDGC 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 EEPKRRGIFC QIDSGSDLTT
DLIVQRIIKN RLEYEARNQK KEAKELAFLE ALRQQEAQPR GETD
