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   24-JAN-2024, entry version 137.
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   SwissPalm; Q811Q9; -.
DR   jPOST; Q811Q9; -.
DR   MaxQB; Q811Q9; -.
DR   PaxDb; 10090-ENSMUSP00000044280; -.
DR   PeptideAtlas; Q811Q9; -.
DR   ProteomicsDB; 294035; -. [Q811Q9-1]
DR   ProteomicsDB; 294036; -. [Q811Q9-2]
DR   Antibodypedia; 505; 60 antibodies from 20 providers.
DR   DNASU; 236899; -.
DR   Ensembl; ENSMUST00000045898.4; ENSMUSP00000044280.4; ENSMUSG00000035246.17. [Q811Q9-1]
DR   Ensembl; ENSMUST00000113933.9; ENSMUSP00000109566.3; ENSMUSG00000035246.17. [Q811Q9-2]
DR   GeneID; 236899; -.
DR   KEGG; mmu:236899; -.
DR   UCSC; uc009tsv.1; mouse. [Q811Q9-2]
DR   UCSC; uc009tsw.1; mouse. [Q811Q9-1]
DR   AGR; MGI:2147987; -.
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; 5474784at2759; -.
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 79 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 152 other cell types or tissues.
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; HUPs; 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   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   PANTHER; PTHR10739:SF20; CHOLINE-PHOSPHATE CYTIDYLYLTRANSFERASE B; 1.
DR   PANTHER; PTHR10739; CYTIDYLYLTRANSFERASE; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   Genevisible; Q811Q9; MM.
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
//