PCY1B_RAT
ID PCY1B_RAT Reviewed; 369 AA.
AC Q9QZC4;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Choline-phosphate cytidylyltransferase B;
DE EC=2.7.7.15 {ECO:0000250|UniProtKB:Q9Y5K3};
DE AltName: Full=CCT-beta;
DE AltName: Full=CTP:phosphocholine cytidylyltransferase B;
DE Short=CCT B;
DE Short=CT B;
DE AltName: Full=Phosphorylcholine transferase B;
GN Name=Pcyt1b; Synonyms=Cctb;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=12114961;
RA Xiong Y., Wang Y., Liu X.L., Du Y.C.;
RT "Cloning of a gene in rat brain induced to be expressed differently by
RT AVP(4-8) with differential display PCR.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 31:509-512(1999).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-362, AND
RP IDENTIFICATION BY 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: Catalyzes the key rate-limiting step in the CDP-choline
CC pathway for phosphatidylcholine biosynthesis.
CC {ECO:0000250|UniProtKB:Q9Y5K3}.
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:0000250|UniProtKB:Q9Y5K3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18998;
CC Evidence={ECO:0000250|UniProtKB:Q9Y5K3};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 1/2.
CC {ECO:0000250|UniProtKB:Q9Y5K3}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P19836}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9Y5K3}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y5K3}.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR EMBL; AF190256; AAF04586.1; -; mRNA.
DR RefSeq; NP_775174.1; NM_173151.1.
DR AlphaFoldDB; Q9QZC4; -.
DR SMR; Q9QZC4; -.
DR BioGRID; 251926; 1.
DR STRING; 10116.ENSRNOP00000016669; -.
DR iPTMnet; Q9QZC4; -.
DR PhosphoSitePlus; Q9QZC4; -.
DR jPOST; Q9QZC4; -.
DR PaxDb; Q9QZC4; -.
DR PRIDE; Q9QZC4; -.
DR GeneID; 286936; -.
DR KEGG; rno:286936; -.
DR CTD; 9468; -.
DR RGD; 708434; Pcyt1b.
DR eggNOG; KOG2804; Eukaryota.
DR InParanoid; Q9QZC4; -.
DR OrthoDB; 1172502at2759; -.
DR PhylomeDB; Q9QZC4; -.
DR BRENDA; 2.7.7.15; 5301.
DR Reactome; R-RNO-1483191; Synthesis of PC.
DR UniPathway; UPA00753; UER00739.
DR PRO; PR:Q9QZC4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0006657; P:CDP-choline pathway; ISS:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; ISO:RGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISS:UniProtKB.
DR GO; GO:1904116; P:response to vasopressin; IEP:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
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 Cytoplasm; Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism;
KW Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..369
FT /note="Choline-phosphate cytidylyltransferase B"
FT /id="PRO_0000208457"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..361
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 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5K3"
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:Q811Q9"
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:P19836"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 345
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811Q9"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 369 AA; 41900 MW; 4F5C5D7667110E10 CRC64;
MPVVTTDAES ETGIPKSLSN EPPSETMEEI EHTCPQPRLT LTAPAPFADE SSCQCQAPHE
KLTIAQARLG TPVDRPVRVY ADGIFDLFHS GHARALMQAK TLFPNSYLLV GVCSDDLTHK
FKGFTVMNEA ERYEALRHCR YVDEVIRDAP WTLTPEFLEK HKIDFVAHDD IPYSSAGSDD
VYKHIKEAGM FVPTQRTEGI STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKKY
RFQNQVDKMK EKVKNVEERS KEFVNRVEEK SHDLIQKWEE KSREFIGNFL ELFGPDGAWK
QMFQERSSRM LQALSPKQSP VSSPTRSRSP SRSPSPTFSW LPNKTSPPSS PKAASASISS
MSEGDEDEK
