ID   CHKA_MOUSE              Reviewed;         453 AA.
AC   O54804; G5E853; Q8BPL3; Q8BPW6; Q9CXP3; Q9QX56;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 3.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Choline kinase alpha;
DE            Short=CK;
DE            EC=2.7.1.32 {ECO:0000250|UniProtKB:P35790};
DE   AltName: Full=CHETK-alpha;
DE   AltName: Full=Ethanolamine kinase;
DE            Short=EK;
DE            EC=2.7.1.82 {ECO:0000250|UniProtKB:P35790};
GN   Name=Chka; Synonyms=Chk;
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] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC   STRAIN=Swiss Webster / NIH;
RX   PubMed=9714798; DOI=10.1016/s0005-2760(98)00062-9;
RA   Aoyama C., Nakashima K., Ishidate K.;
RT   "Molecular cloning of mouse choline kinase and choline/ethanolamine kinase:
RT   their sequence comparison to the respective rat homologs.";
RL   Biochim. Biophys. Acta 1393:179-185(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RC   STRAIN=129/Sv; TISSUE=Liver;
RX   PubMed=10706593;
RA   Aoyama C., Yamazaki N., Terada H., Ishidate K.;
RT   "Structure and characterization of the genes for murine
RT   choline/ethanolamine kinase isozymes alpha and beta.";
RL   J. Lipid Res. 41:452-464(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-371 (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-150 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Limb;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-168 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic eye, Embryonic head, and Eye;
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   [7]
RP   SUBUNIT.
RX   PubMed=16490392; DOI=10.1016/j.bbalip.2006.01.005;
RA   Liao H., Aoyama C., Ishidate K., Teraoka H.;
RT   "Deletion and alanine mutation analyses for the formation of active
RT   homo- or hetero-dimer complexes of mouse choline kinase-alpha and -beta.";
RL   Biochim. Biophys. Acta 1761:111-120(2006).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=18029352; DOI=10.1074/jbc.m708766200;
RA   Wu G., Aoyama C., Young S.G., Vance D.E.;
RT   "Early embryonic lethality caused by disruption of the gene for choline
RT   kinase alpha, the first enzyme in phosphatidylcholine biosynthesis.";
RL   J. Biol. Chem. 283:1456-1462(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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: Plays a key role in phospholipid biosynthesis by catalyzing
CC       the phosphorylation of free choline to phosphocholine, the first step
CC       in phosphatidylcholine biosynthesis. Also phosphorylates ethanolamine,
CC       thereby contributing to phosphatidylethanolamine biosynthesis. Has
CC       higher activity with choline. May contribute to tumor cell growth.
CC       {ECO:0000250|UniProtKB:P35790}.
CC   -!- FUNCTION: [Isoform 1]: This isoform plays a key role in lipolysis of
CC       lipid droplets following glucose deprivation (By similarity). In
CC       response to glucose deprivation, phosphorylated by AMPK, promoting
CC       localization to lipid droplets (By similarity). Phosphorylation is
CC       followed by acetylation by KAT5, leading to dissociation of the
CC       homodimer into a monomer (By similarity). Monomeric CHKA isoform 1 is
CC       converted into a tyrosine-protein kinase, which phosphorylates lipid
CC       droplet structural proteins PLIN2 and PLIN3, leading to lipolysis of
CC       lipid droplets (By similarity). {ECO:0000250|UniProtKB:P35790}.
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:P35790};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12838;
CC         Evidence={ECO:0000250|UniProtKB:P35790};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + ethanolamine = ADP + H(+) + phosphoethanolamine;
CC         Xref=Rhea:RHEA:13069, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57603, ChEBI:CHEBI:58190, ChEBI:CHEBI:456216;
CC         EC=2.7.1.82; Evidence={ECO:0000250|UniProtKB:P35790};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13070;
CC         Evidence={ECO:0000250|UniProtKB:P35790};
CC   -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:P35790};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10597;
CC         Evidence={ECO:0000250|UniProtKB:P35790};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC       phosphocholine from choline: step 1/1. {ECO:0000250|UniProtKB:P35790}.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.
CC       {ECO:0000250|UniProtKB:P35790}.
CC   -!- SUBUNIT: Homodimer (PubMed:16490392). Heterodimer with CHKB
CC       (PubMed:16490392). {ECO:0000269|PubMed:16490392}.
CC   -!- SUBUNIT: [Isoform 1]: Monomer; acetylation by KAT5 promotes
CC       dissociation of the homodimer and monomerization.
CC       {ECO:0000250|UniProtKB:P35790}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P35790}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Lipid droplet
CC       {ECO:0000250|UniProtKB:P35790}. Note=Isoform 1 localizes to lipid
CC       droplets following phosphorylation by AMPK.
CC       {ECO:0000250|UniProtKB:P35790}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=CHETK-alpha2 {ECO:0000303|PubMed:10706593}, CHKalpha2
CC       {ECO:0000303|PubMed:10706593};
CC         IsoId=O54804-1; Sequence=Displayed;
CC       Name=2; Synonyms=CHETK-alpha1 {ECO:0000303|PubMed:10706593}, CHKalpha1
CC       {ECO:0000303|PubMed:10706593};
CC         IsoId=O54804-2; Sequence=VSP_009684;
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously with the highest level in
CC       testis. {ECO:0000269|PubMed:9714798}.
CC   -!- PTM: [Isoform 1]: Phosphorylated at Ser-275 by AMPK in response to
CC       glucose deprivation, leading to localization to lipid droplets.
CC       {ECO:0000250|UniProtKB:P35790}.
CC   -!- PTM: [Isoform 1]: Acetylated by KAT5 at Lys-243 following
CC       phosphorylation by AMPK, leading to monomerization and conversion into
CC       a tyrosine-protein kinase. {ECO:0000250|UniProtKB:P35790}.
CC   -!- DISRUPTION PHENOTYPE: Death at an early embryonic stage. Embryos die
CC       after 3 to 5 days of development. {ECO:0000269|PubMed:18029352}.
CC   -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH56758.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC       Sequence=BAA88154.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAB29191.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC       Sequence=BAC34841.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC       Sequence=BAC35539.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AB011002; BAA24898.1; -; mRNA.
DR   EMBL; AB030621; BAA88153.1; -; Genomic_DNA.
DR   EMBL; AB030621; BAA88154.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC133523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466612; EDL32956.1; -; Genomic_DNA.
DR   EMBL; BC056758; AAH56758.1; ALT_SEQ; mRNA.
DR   EMBL; BC060218; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK014174; BAB29191.1; ALT_SEQ; mRNA.
DR   EMBL; AK052056; BAC34841.1; ALT_SEQ; mRNA.
DR   EMBL; AK053818; BAC35539.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS29400.1; -. [O54804-2]
DR   CCDS; CCDS70913.1; -. [O54804-1]
DR   RefSeq; NP_001258425.1; NM_001271496.1. [O54804-1]
DR   RefSeq; NP_038518.2; NM_013490.4. [O54804-2]
DR   AlphaFoldDB; O54804; -.
DR   SMR; O54804; -.
DR   BioGRID; 198701; 1.
DR   STRING; 10090.ENSMUSP00000025760; -.
DR   iPTMnet; O54804; -.
DR   PhosphoSitePlus; O54804; -.
DR   EPD; O54804; -.
DR   MaxQB; O54804; -.
DR   PaxDb; 10090-ENSMUSP00000071933; -.
DR   PeptideAtlas; O54804; -.
DR   ProteomicsDB; 281669; -. [O54804-1]
DR   ProteomicsDB; 281670; -. [O54804-2]
DR   Pumba; O54804; -.
DR   Antibodypedia; 16639; 252 antibodies from 29 providers.
DR   DNASU; 12660; -.
DR   Ensembl; ENSMUST00000025760.13; ENSMUSP00000025760.7; ENSMUSG00000024843.16. [O54804-1]
DR   Ensembl; ENSMUST00000072055.13; ENSMUSP00000071933.7; ENSMUSG00000024843.16. [O54804-2]
DR   GeneID; 12660; -.
DR   KEGG; mmu:12660; -.
DR   UCSC; uc008fxg.2; mouse. [O54804-2]
DR   UCSC; uc008fxh.2; mouse. [O54804-1]
DR   AGR; MGI:107760; -.
DR   CTD; 1119; -.
DR   MGI; MGI:107760; Chka.
DR   VEuPathDB; HostDB:ENSMUSG00000024843; -.
DR   eggNOG; KOG2686; Eukaryota.
DR   GeneTree; ENSGT00950000182939; -.
DR   HOGENOM; CLU_012712_2_1_1; -.
DR   InParanoid; O54804; -.
DR   OMA; IETSIDY; -.
DR   OrthoDB; 144299at2759; -.
DR   PhylomeDB; O54804; -.
DR   TreeFam; TF313549; -.
DR   Reactome; R-MMU-1483191; Synthesis of PC.
DR   Reactome; R-MMU-1483213; Synthesis of PE.
DR   UniPathway; UPA00558; UER00741.
DR   UniPathway; UPA00753; UER00737.
DR   BioGRID-ORCS; 12660; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Chka; mouse.
DR   PRO; PR:O54804; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; O54804; Protein.
DR   Bgee; ENSMUSG00000024843; Expressed in prostate gland ventral lobe and 256 other cell types or tissues.
DR   ExpressionAtlas; O54804; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISO:MGI.
DR   GO; GO:0033265; F:choline binding; ISO:MGI.
DR   GO; GO:0004103; F:choline kinase activity; IDA:MGI.
DR   GO; GO:0004104; F:cholinesterase activity; IDA:MGI.
DR   GO; GO:0004305; F:ethanolamine kinase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:0006657; P:CDP-choline pathway; IBA:GO_Central.
DR   GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR   GO; GO:0019695; P:choline metabolic process; ISO:MGI.
DR   GO; GO:0006580; P:ethanolamine metabolic process; ISO:MGI.
DR   GO; GO:1905691; P:lipid droplet disassembly; ISS:UniProtKB.
DR   GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:MGI.
DR   GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05156; ChoK_euk; 1.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   PANTHER; PTHR22603:SF36; CHOLINE KINASE ALPHA; 1.
DR   PANTHER; PTHR22603; CHOLINE/ETHANOALAMINE KINASE; 1.
DR   Pfam; PF01633; Choline_kinase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   Genevisible; O54804; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW   Lipid biosynthesis; Lipid droplet; Lipid metabolism; Nucleotide-binding;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..453
FT                   /note="Choline kinase alpha"
FT                   /id="PRO_0000206220"
FT   REGION          22..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..77
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         113..119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P35790"
FT   BINDING         115..117
FT                   /ligand="phosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:295975"
FT                   /evidence="ECO:0000250|UniProtKB:P35790"
FT   BINDING         142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P35790"
FT   BINDING         203..209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P35790"
FT   BINDING         304
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P35790"
FT   BINDING         326
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P35790"
FT   MOD_RES         71
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01134"
FT   MOD_RES         243
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P35790"
FT   MOD_RES         275
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35790"
FT   VAR_SEQ         151..168
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9714798"
FT                   /id="VSP_009684"
FT   CONFLICT        193
FT                   /note="F -> Y (in Ref. 1; BAA24898 and 2;
FT                   BAA88154/BAA88153)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   453 AA;  51985 MW;  66042FEE92C333D4 CRC64;
     MKTKFCTGGE AEPSPLGLLL SCGGNAAPTP GVGQQRDAAG ELESKQLGGR TQPLALPPPP
     PPPLPLPPPP SPPLADEQPE PRTRRRAYLW CKEFLPGAWR GLREDQFHIS VIRGGLSNML
     FQCSLPDSIA SVGDEPRKVL LRLYGAILKM RSCNKEGSEQ AQNENEFQGA EAMVLESVMF
     AILAERSLGP KLFGIFPQGR LEQFIPSRRL DTEELRLPDI SAEIAEKMAT FHGMKMPFNK
     EPKWLFGTME KYLNQVLRLK FSREARVQQL HKILSYNLPL ELENLRSLLQ YTRSPVVFCH
     NDCQEGNILL LEGQENSERR KLMLIDFEYS SYNYRGFDIG NHFCEWMYDY TYEKYPFFRA
     NIQKYPSRKQ QLHFISSYLT TFQNDFESLS SEEQFATKED MLLEVNRFAL ASHFLWGLWS
     IVQAKISSIE FGYMEYAQAR FEAYFDQKRK LGV
//