PCY1A_CRIGR
ID PCY1A_CRIGR Reviewed; 367 AA.
AC P49584;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Choline-phosphate cytidylyltransferase A;
DE EC=2.7.7.15 {ECO:0000269|PubMed:8185307};
DE AltName: Full=CCT-alpha;
DE AltName: Full=CTP:phosphocholine cytidylyltransferase A;
DE Short=CCT A;
DE Short=CT A;
DE AltName: Full=Phosphorylcholine transferase A;
GN Name=PCYT1A; Synonyms=CTPCT, PCYT1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-140, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION, ACTIVITY REGULATION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Ovary;
RX PubMed=8185307; DOI=10.1006/abbi.1994.1215;
RA Sweitzer T.D., Kent C.;
RT "Expression of wild-type and mutant rat liver CTP: phosphocholine
RT cytidylyltransferase in a cytidylyltransferase-deficient Chinese hamster
RT ovary cell line.";
RL Arch. Biochem. Biophys. 311:107-116(1994).
CC -!- FUNCTION: Catalyzes the key rate-limiting step in the CDP-choline
CC pathway for phosphatidylcholine biosynthesis.
CC {ECO:0000269|PubMed:8185307}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H(+) + phosphocholine = CDP-choline + diphosphate;
CC Xref=Rhea:RHEA:18997, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:58779, ChEBI:CHEBI:295975;
CC EC=2.7.7.15; Evidence={ECO:0000269|PubMed:8185307};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18998;
CC Evidence={ECO:0000269|PubMed:8185307};
CC -!- ACTIVITY REGULATION: By phosphorylation (By similarity). Activated by
CC N-methylethanolamine (PubMed:8185307). {ECO:0000250,
CC ECO:0000269|PubMed:8185307}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.47 uM for CTP {ECO:0000269|PubMed:8185307};
CC KM=0.43 uM for phosphocholine {ECO:0000269|PubMed:8185307};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 1/2.
CC {ECO:0000269|PubMed:8185307}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P19836}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P19836}. Membrane
CC {ECO:0000250|UniProtKB:P19836}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P19836}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P49585}. Nucleus {ECO:0000269|PubMed:8185307}.
CC Note=It can interconvert between an inactive cytosolic form and an
CC active membrane-bound form. {ECO:0000250|UniProtKB:P19836}.
CC -!- PTM: Phosphorylated (PubMed:8185307). The serine residues of the C-
CC terminus are phosphorylated (By similarity). The inactive soluble form
CC is stabilized by phosphorylation, the active membrane bound form is
CC promoted by anionic lipids or diacylglycerol, and is stabilized by
CC dephosphorylation (By similarity). {ECO:0000250|UniProtKB:P19836,
CC ECO:0000269|PubMed:8185307}.
CC -!- PTM: Monoubiquitinated by the SCF(FBXL2) complex, leading to
CC proteasomal degradation. {ECO:0000250|UniProtKB:P49586}.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR EMBL; L13244; AAA21305.1; -; mRNA.
DR PIR; S44385; S44385.
DR RefSeq; NP_001233666.1; NM_001246737.1.
DR AlphaFoldDB; P49584; -.
DR SMR; P49584; -.
DR STRING; 10029.NP_001233666.1; -.
DR GeneID; 100689303; -.
DR KEGG; cge:100689303; -.
DR CTD; 5130; -.
DR eggNOG; KOG2804; Eukaryota.
DR OrthoDB; 1172502at2759; -.
DR UniPathway; UPA00753; UER00739.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006657; P:CDP-choline pathway; IDA:UniProtKB.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:UniProtKB.
DR CDD; cd02174; CCT; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR041723; CCT.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR045049; Pcy1-like.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR10739; PTHR10739; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Nucleotidyltransferase; Nucleus;
KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein; Repeat;
KW Transferase; Ubl conjugation.
FT CHAIN 1..367
FT /note="Choline-phosphate cytidylyltransferase A"
FT /id="PRO_0000208452"
FT REPEAT 319..324
FT /note="1"
FT REPEAT 329..333
FT /note="2; approximate"
FT REPEAT 343..348
FT /note="3"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..287
FT /note="Amphipathic"
FT /evidence="ECO:0000255"
FT REGION 256..288
FT /note="3 X 11 AA approximate tandem repeats"
FT REGION 313..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..348
FT /note="3 X repeats"
FT COMPBIAS 7..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 84..92
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 122
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 168..169
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 173
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 196..200
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P49585"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49585"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49585"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49585"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49586"
FT MOD_RES 325
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49586"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49585"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49585"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49585"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49585"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49585"
FT MOD_RES 358
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49586"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT VARIANT 140
FT /note="R -> H (in MT58 cell line)"
FT /evidence="ECO:0000269|PubMed:8185307"
SQ SEQUENCE 367 AA; 41717 MW; 9851F3EBF5ECE43C CRC64;
MDAQSSAKVN SRKRRKEASS PNGATEEDGI PSKVQHCSVG LRQPAPFSDE IEVDFSKPYV
RVTMEEACRG TPCERPVRVY ADGIFDLFHS GHARALMQAK NLFPNTYPIV GVCSDELTHN
FKGFTVMNEN ERYDAVQHCR YVDEVVRNAP WTLTPEFLAE HRIDFVAHDD IPYSSAGSDD
VYKHIKEAGM FAPTQRTEGI STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKKY
HLQERVDKVK KKVKDVEEKS KEFVQKVEER SIDLIQTWEE KSREFIGSFL EMFGPEGALK
HMLKEGKGRM LQAISPRQSP SSSPTHERSP SPSFRWPFSG KTSPSSSPAS LSRHKAVTCD
ISEDEED
