PCY1B_MOUSE
ID PCY1B_MOUSE Reviewed; 369 AA.
AC Q811Q9; Q3UEW0; Q80Y63; Q811Q8; Q8BKD2; Q8C085;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Choline-phosphate cytidylyltransferase B;
DE EC=2.7.7.15 {ECO:0000269|PubMed:12842190};
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;
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 [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY (ISOFORMS
RP 1 AND 2), DEVELOPMENTAL STAGE (ISOFORMS 1 AND 2), FUNCTION (ISOFORMS 1 AND
RP 2), AND CATALYTIC ACTIVITY (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=12842190; DOI=10.1016/s1388-1981(03)00067-2;
RA Karim M., Jackson P., Jackowski S.;
RT "Gene structure, expression and identification of a new CTP:phosphocholine
RT cytidylyltransferase beta isoform.";
RL Biochim. Biophys. Acta 1633:1-12(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 18-369 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye, Medulla oblongata, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Olfactory epithelium;
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 [4]
RP FUNCTION (ISOFORM 1), TISSUE SPECIFICITY (ISOFORM 1), AND DISRUPTION
RP PHENOTYPE (ISOFORM 1).
RX PubMed=15143167; DOI=10.1128/mcb.24.11.4720-4733.2004;
RA Jackowski S., Rehg J.E., Zhang Y.-M., Wang J., Miller K., Jackson P.,
RA Karim M.A.;
RT "Disruption of CCTbeta2 expression leads to gonadal dysfunction.";
RL Mol. Cell. Biol. 24:4720-4733(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-319, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-319; SER-323;
RP SER-360 AND SER-362, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, 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: [Isoform 1]: Catalyzes the key rate-limiting step in the CDP-
CC choline pathway for phosphatidylcholine biosynthesis (PubMed:12842190).
CC Plays an important role in ovary maturation and the maintenance of
CC sperm production (PubMed:15143167). {ECO:0000269|PubMed:12842190,
CC ECO:0000269|PubMed:15143167}.
CC -!- FUNCTION: [Isoform 2]: Catalyzes the key rate-limiting step in the CDP-
CC choline pathway for phosphatidylcholine biosynthesis.
CC {ECO:0000269|PubMed:12842190}.
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:12842190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18998;
CC Evidence={ECO:0000305|PubMed:12842190};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 1/2.
CC {ECO:0000269|PubMed:12842190}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P19836}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9Y5K3}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y5K3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CCTbeta2 {ECO:0000303|PubMed:12842190};
CC IsoId=Q811Q9-1; Sequence=Displayed;
CC Name=2; Synonyms=CCTbeta3 {ECO:0000303|PubMed:12842190};
CC IsoId=Q811Q9-2; Sequence=VSP_020041, VSP_020042;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Highly expressed in brain (at protein
CC level) (PubMed:12842190). Expressed in liver (at protein level)
CC (PubMed:12842190). Expressed at lower levels in lung and gonads
CC (PubMed:15143167). {ECO:0000269|PubMed:12842190,
CC ECO:0000269|PubMed:15143167}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in brain (at protein level)
CC (PubMed:12842190). Expressed at lower levels in lung and gonads
CC (PubMed:15143167). {ECO:0000269|PubMed:12842190,
CC ECO:0000269|PubMed:15143167}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 1]: Expression is low at 7 dpc, reaches a
CC maximum at 15 dpc and decreases at 17 dpc.
CC {ECO:0000269|PubMed:12842190}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 2]: Not expressed in embryo. Expression
CC starts at 5 weeks. {ECO:0000269|PubMed:12842190}.
CC -!- DISRUPTION PHENOTYPE: Female mice lacking isoform 1 have reduced
CC fecundity due to failure in ovary maturation. Male mice lacking isoform
CC 1 have reduced fecundity due to testicular degeneration.
CC {ECO:0000269|PubMed:15143167}.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27658.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY189949; AAO39004.1; -; mRNA.
DR EMBL; AY189950; AAO39005.1; -; mRNA.
DR EMBL; AK032027; BAC27658.1; ALT_INIT; mRNA.
DR EMBL; AK053577; BAC35435.1; -; mRNA.
DR EMBL; AK149304; BAE28801.1; -; mRNA.
DR EMBL; BC048917; AAH48917.1; -; mRNA.
DR CCDS; CCDS30274.1; -. [Q811Q9-1]
DR CCDS; CCDS41061.1; -. [Q811Q9-2]
DR RefSeq; NP_808214.1; NM_177546.2. [Q811Q9-2]
DR RefSeq; NP_997593.1; NM_211138.1. [Q811Q9-1]
DR AlphaFoldDB; Q811Q9; -.
DR SMR; Q811Q9; -.
DR STRING; 10090.ENSMUSP00000044280; -.
DR iPTMnet; Q811Q9; -.
DR PhosphoSitePlus; Q811Q9; -.
DR jPOST; Q811Q9; -.
DR MaxQB; Q811Q9; -.
DR PaxDb; Q811Q9; -.
DR PeptideAtlas; Q811Q9; -.
DR PRIDE; Q811Q9; -.
DR ProteomicsDB; 294035; -. [Q811Q9-1]
DR ProteomicsDB; 294036; -. [Q811Q9-2]
DR Antibodypedia; 505; 56 antibodies from 20 providers.
DR DNASU; 236899; -.
DR Ensembl; ENSMUST00000045898; ENSMUSP00000044280; ENSMUSG00000035246. [Q811Q9-1]
DR Ensembl; ENSMUST00000113933; ENSMUSP00000109566; ENSMUSG00000035246. [Q811Q9-2]
DR GeneID; 236899; -.
DR KEGG; mmu:236899; -.
DR UCSC; uc009tsv.1; mouse. [Q811Q9-2]
DR UCSC; uc009tsw.1; mouse. [Q811Q9-1]
DR CTD; 9468; -.
DR MGI; MGI:2147987; Pcyt1b.
DR VEuPathDB; HostDB:ENSMUSG00000035246; -.
DR eggNOG; KOG2804; Eukaryota.
DR GeneTree; ENSGT00940000156040; -.
DR HOGENOM; CLU_034585_4_2_1; -.
DR InParanoid; Q811Q9; -.
DR OMA; FEDFSIC; -.
DR OrthoDB; 1172502at2759; -.
DR PhylomeDB; Q811Q9; -.
DR TreeFam; TF106336; -.
DR BRENDA; 2.7.7.15; 3474.
DR Reactome; R-MMU-1483191; Synthesis of PC.
DR UniPathway; UPA00753; UER00739.
DR BioGRID-ORCS; 236899; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Pcyt1b; mouse.
DR PRO; PR:Q811Q9; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q811Q9; protein.
DR Bgee; ENSMUSG00000035246; Expressed in animal zygote and 151 other tissues.
DR Genevisible; Q811Q9; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0006657; P:CDP-choline pathway; IDA:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
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 Alternative splicing; Cytoplasm; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Nucleotidyltransferase; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..369
FT /note="Choline-phosphate cytidylyltransferase B"
FT /id="PRO_0000247762"
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:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0000250|UniProtKB:Q9QZC4"
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:0007744|PubMed:21183079"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12842190,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_020041"
FT VAR_SEQ 25..39
FT /note="ETMEEIEHTCPQPRL -> MDKDEFSRK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12842190,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_020042"
FT CONFLICT 73
FT /note="V -> G (in Ref. 1; AAO39004/AAO39005)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="V -> I (in Ref. 2; BAE28801)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 41900 MW; 841B0E2E9EE22615 CRC64;
MPVLTTDAES ETGIPKSLSN EPPSETMEEI EHTCPQPRLT LTAPAPFADE SSCQCQAPHE
KLTVAQARLG 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
