KICH_SCHPO
ID KICH_SCHPO Reviewed; 456 AA.
AC Q10276;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Choline kinase;
DE EC=2.7.1.32 {ECO:0000250|UniProtKB:P20485};
DE AltName: Full=ATP:choline phosphotransferase;
GN ORFNames=SPAC13G7.12c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalyzes the committed step in the synthesis of
CC phosphatidylcholine by the CDP-choline pathway.
CC {ECO:0000250|UniProtKB:P20485}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + choline = ADP + H(+) + phosphocholine;
CC Xref=Rhea:RHEA:12837, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:295975, ChEBI:CHEBI:456216;
CC EC=2.7.1.32; Evidence={ECO:0000250|UniProtKB:P20485};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12838;
CC Evidence={ECO:0000250|UniProtKB:P20485};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P20485};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphocholine from choline: step 1/1. {ECO:0000250|UniProtKB:P20485}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P20485}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA93600.1; -; Genomic_DNA.
DR PIR; S67441; S67441.
DR RefSeq; NP_593714.1; NM_001019145.2.
DR AlphaFoldDB; Q10276; -.
DR SMR; Q10276; -.
DR BioGRID; 279285; 34.
DR STRING; 4896.SPAC13G7.12c.1; -.
DR MaxQB; Q10276; -.
DR PaxDb; Q10276; -.
DR EnsemblFungi; SPAC13G7.12c.1; SPAC13G7.12c.1:pep; SPAC13G7.12c.
DR GeneID; 2542839; -.
DR KEGG; spo:SPAC13G7.12c; -.
DR PomBase; SPAC13G7.12c; -.
DR VEuPathDB; FungiDB:SPAC13G7.12c; -.
DR eggNOG; KOG2686; Eukaryota.
DR HOGENOM; CLU_012712_5_1_1; -.
DR InParanoid; Q10276; -.
DR OMA; HEWTADY; -.
DR PhylomeDB; Q10276; -.
DR Reactome; R-SPO-1483191; Synthesis of PC.
DR Reactome; R-SPO-1483213; Synthesis of PE.
DR UniPathway; UPA00753; UER00737.
DR PRO; PR:Q10276; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004103; F:choline kinase activity; ISO:PomBase.
DR GO; GO:0004305; F:ethanolamine kinase activity; ISO:PomBase.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:PomBase.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISO:PomBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR007521; Choline_kin_N.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF04428; Choline_kin_N; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Nucleotide-binding; Nucleus; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..456
FT /note="Choline kinase"
FT /id="PRO_0000206225"
SQ SEQUENCE 456 AA; 52536 MW; 08284FF1FC5FA089 CRC64;
MVNFASEVDK NNAFDSAHPS RKCKGSLDCN DPDPIFRHKV LVIIHKLAIS SWNRIPLTLC
NKLHIKRISG ALTNAVYYVA PPEGYHAPKL LLRIYGPHVE LFINRQVELE NLKRLARHNI
GPYLIGEFSN GRFEQYMEST TLTCKTIRDP KLSIYVGRRL CELHNFILLH PHEVLEMPAA
WKNCLVWLPK AKAKILGRKH SLAITSEFMK TLEEDFNAYY NWFVEWSRDK KDWFGLKMVF
SHNDTQYGNL LKIKAKKRSI PLSQKHRTLV PVDFEYAGPN LCAFDLANYF AEWMADYHHP
THNYLMDRSR YPDFNARKLV YHAYVEQSAV INDLLEIEDA SLLKTDISDE LKNTFEKQIM
NLEESVRAIS PAANIGWALW GILQCLEEDD EWEDLSVSSQ VADRPEKQLV EGSTVPPIGT
SSFDYIGYSS EKFDLFYEGC AALGLNGRNR STFSYA
