KDM1B_MOUSE
ID KDM1B_MOUSE Reviewed; 826 AA.
AC Q8CIG3; Q8C5C4; Q8CEC1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Lysine-specific histone demethylase 1B;
DE EC=1.14.99.66 {ECO:0000250|UniProtKB:Q8NB78};
DE AltName: Full=Flavin-containing amine oxidase domain-containing protein 1;
DE AltName: Full=Lysine-specific histone demethylase 2;
GN Name=Kdm1b {ECO:0000312|MGI:MGI:2145261}; Synonyms=Aof1, Lsd2;
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 [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 285-826 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cecum, and Skin;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=19407342; DOI=10.1074/jbc.m109.003087;
RA Karytinos A., Forneris F., Profumo A., Ciossani G., Battaglioli E.,
RA Binda C., Mattevi A.;
RT "A novel mammalian flavin-dependent histone demethylase.";
RL J. Biol. Chem. 284:17775-17782(2009).
RN [4]
RP FUNCTION, MUTAGENESIS OF LYS-667, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=19727073; DOI=10.1038/nature08315;
RA Ciccone D.N., Su H., Hevi S., Gay F., Lei H., Bajko J., Xu G., Li E.,
RA Chen T.;
RT "KDM1B is a histone H3K4 demethylase required to establish maternal genomic
RT imprints.";
RL Nature 461:415-418(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-253, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, and Spleen;
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: Histone demethylase that demethylates 'Lys-4' of histone H3,
CC a specific tag for epigenetic transcriptional activation, thereby
CC acting as a corepressor. Required for de novo DNA methylation of a
CC subset of imprinted genes during oogenesis. Acts by oxidizing the
CC substrate by FAD to generate the corresponding imine that is
CC subsequently hydrolyzed. Demethylates both mono- and di-methylated
CC 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-,
CC di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27',
CC mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-,
CC di- or tri-methylated 'Lys-20' of histone H4.
CC {ECO:0000269|PubMed:19407342, ECO:0000269|PubMed:19727073}.
CC -!- FUNCTION: Histone demethylase that demethylates 'Lys-4' of histone H3,
CC a specific tag for epigenetic transcriptional activation, thereby
CC acting as a corepressor. Required for de novo DNA methylation of a
CC subset of imprinted genes during oogenesis. Acts by oxidizing the
CC substrate by FAD to generate the corresponding imine that is
CC subsequently hydrolyzed. Demethylates both mono- and di-methylated
CC 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-,
CC di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27',
CC mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-,
CC di- or tri-methylated 'Lys-20' of histone H4 (PubMed:19407342,
CC PubMed:19727073). Alone, it is unable to demethylate H3K4me on
CC nucleosomes and requires the presence of GLYR1 to achieve such
CC activity, they form a multifunctional enzyme complex that modifies
CC transcribed chromatin and facilitates Pol II transcription through
CC nucleosomes (By similarity). {ECO:0000250|UniProtKB:Q8NB78,
CC ECO:0000269|PubMed:19407342, ECO:0000269|PubMed:19727073}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 A + 2 H2O + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] = 2
CC AH2 + 2 formaldehyde + L-lysyl(4)-[histone H3]; Xref=Rhea:RHEA:60244,
CC Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:61976; EC=1.14.99.66;
CC Evidence={ECO:0000250|UniProtKB:Q8NB78};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60245;
CC Evidence={ECO:0000250|UniProtKB:Q8NB78};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H2O + N(6)-methyl-L-lysyl(4)-[histone H3] = AH2 +
CC formaldehyde + L-lysyl(4)-[histone H3]; Xref=Rhea:RHEA:60256,
CC Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000250|UniProtKB:Q8NB78};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60257;
CC Evidence={ECO:0000250|UniProtKB:Q8NB78};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:19407342};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q8NB78};
CC Note=Binds 3 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q8NB78};
CC -!- ACTIVITY REGULATION: Inhibited by tranylcypromine, but not by
CC pargyline, deprenyl or rasagiline (PubMed:19407342). Histone H3K4me1
CC and H3K4me2 demethylase activity is inhibited by DNA, this inhibition
CC is released in complex with GLYR1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8NB78, ECO:0000269|PubMed:19407342}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.2 uM for mono-methylated 'Lys-4' histone H3 N-terminal peptide
CC {ECO:0000269|PubMed:19407342};
CC KM=11.3 uM for di-methylated 'Lys-4' histone H3 N-terminal peptide
CC {ECO:0000269|PubMed:19407342};
CC KM=9.0 uM for mono-methylated 'Lys-4', mono-methylated 'Lys-9'
CC histone H3 N-terminal peptide {ECO:0000269|PubMed:19407342};
CC KM=6.6 uM for di-methylated 'Lys-4', di-methylated 'Lys-9' histone H3
CC N-terminal peptide {ECO:0000269|PubMed:19407342};
CC KM=70.5 uM for mono-methylated 'Lys-4', acetylated 'Lys-9' histone H3
CC N-terminal peptide {ECO:0000269|PubMed:19407342};
CC KM=8.1 uM for mono-methylated 'Lys-4', mono-methylated 'Arg-17'
CC histone H3 N-terminal peptide {ECO:0000269|PubMed:19407342};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:19407342};
CC -!- SUBUNIT: Interacts with its cofactor GLYR1 at nucleosomes; this
CC interaction stimulates H3K4me1 and H3K4me2 demethylation. In contrast
CC to KDM1A, does not form a complex with RCOR1/CoREST.
CC {ECO:0000250|UniProtKB:Q8NB78}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19727073}. Chromosome
CC {ECO:0000250|UniProtKB:Q8NB78}. Note=Found in actively RNAPolII-
CC transcribed gene bodies. {ECO:0000250|UniProtKB:Q8NB78}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CIG3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CIG3-2; Sequence=VSP_019969;
CC Name=3;
CC IsoId=Q8CIG3-3; Sequence=VSP_019968;
CC -!- TISSUE SPECIFICITY: Expressed in growing oocytes and in intestinal
CC gland. {ECO:0000269|PubMed:19727073}.
CC -!- DISRUPTION PHENOTYPE: No effect on mouse development and oogenesis, but
CC embryos derived from oocytes from Kdm1b-deficient females die before
CC mid-gestation. {ECO:0000269|PubMed:19727073}.
CC -!- MISCELLANEOUS: Histone H3 acetylation of 'Lys-9' decreases the binding
CC of the substrate, while hyperacetylation of 'Lys-9', 'Lys-14' and 'Lys-
CC 18', phosphorylation of 'Thr3' or 'Ser-10', and methylation of 'Arg-2'
CC or 'Arg-8' abolishes its binding. Methylation of 'Lys-9' and 'Arg-17'
CC are the only two epigenetic modifications that have no significant
CC effect on catalysis. {ECO:0000269|PubMed:19407342}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC26005.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC37460.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK028553; BAC26005.1; ALT_INIT; mRNA.
DR EMBL; AK078920; BAC37460.1; ALT_FRAME; mRNA.
DR EMBL; BC023917; AAH23917.1; -; mRNA.
DR CCDS; CCDS26489.1; -. [Q8CIG3-1]
DR RefSeq; NP_758466.1; NM_172262.3. [Q8CIG3-1]
DR AlphaFoldDB; Q8CIG3; -.
DR SMR; Q8CIG3; -.
DR BioGRID; 230002; 2.
DR DIP; DIP-59111N; -.
DR STRING; 10090.ENSMUSP00000038373; -.
DR iPTMnet; Q8CIG3; -.
DR PhosphoSitePlus; Q8CIG3; -.
DR EPD; Q8CIG3; -.
DR MaxQB; Q8CIG3; -.
DR PaxDb; Q8CIG3; -.
DR PeptideAtlas; Q8CIG3; -.
DR PRIDE; Q8CIG3; -.
DR ProteomicsDB; 263515; -. [Q8CIG3-1]
DR ProteomicsDB; 263516; -. [Q8CIG3-2]
DR ProteomicsDB; 263517; -. [Q8CIG3-3]
DR Antibodypedia; 25190; 158 antibodies from 25 providers.
DR DNASU; 218214; -.
DR Ensembl; ENSMUST00000037025; ENSMUSP00000038373; ENSMUSG00000038080. [Q8CIG3-1]
DR GeneID; 218214; -.
DR KEGG; mmu:218214; -.
DR UCSC; uc007qht.3; mouse. [Q8CIG3-1]
DR UCSC; uc007qhu.3; mouse. [Q8CIG3-2]
DR UCSC; uc011yyy.2; mouse. [Q8CIG3-3]
DR CTD; 221656; -.
DR MGI; MGI:2145261; Kdm1b.
DR VEuPathDB; HostDB:ENSMUSG00000038080; -.
DR eggNOG; KOG0029; Eukaryota.
DR GeneTree; ENSGT00940000157751; -.
DR HOGENOM; CLU_007885_0_0_1; -.
DR InParanoid; Q8CIG3; -.
DR OMA; GNLEYAC; -.
DR OrthoDB; 1034142at2759; -.
DR PhylomeDB; Q8CIG3; -.
DR TreeFam; TF352593; -.
DR BRENDA; 1.14.99.66; 3474.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR BioGRID-ORCS; 218214; 7 hits in 74 CRISPR screens.
DR ChiTaRS; Kdm1b; mouse.
DR PRO; PR:Q8CIG3; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8CIG3; protein.
DR Bgee; ENSMUSG00000038080; Expressed in primary oocyte and 240 other tissues.
DR ExpressionAtlas; Q8CIG3; baseline and differential.
DR Genevisible; Q8CIG3; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0140682; F:histone H3-di/monomethyl-lysine-4 FAD-dependent demethylase activity; IDA:UniProtKB.
DR GO; GO:0032453; F:histone H3-methyl-lysine-4 demethylase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; IMP:MGI.
DR GO; GO:0034720; P:histone H3-K4 demethylation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0044030; P:regulation of DNA methylation; IMP:UniProtKB.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IMP:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR011124; Znf_CW.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF04433; SWIRM; 1.
DR Pfam; PF07496; zf-CW; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS50934; SWIRM; 1.
DR PROSITE; PS51050; ZF_CW; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Chromosome;
KW Developmental protein; FAD; Flavoprotein; Metal-binding; Nucleus;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..826
FT /note="Lysine-specific histone demethylase 1B"
FT /id="PRO_0000247337"
FT DOMAIN 281..379
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT ZN_FING 133..193
FT /note="CW-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..298
FT /note="GLYR1-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT REGION 444..473
FT /note="Histone H3-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT REGION 493..504
FT /note="Histone H3-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT REGION 544..578
FT /note="Histone H3-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT REGION 570..572
FT /note="GLYR1-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT REGION 802..818
FT /note="GLYR1-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT COMPBIAS 29..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 389..445
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78, ECO:0000255"
FT BINDING 604
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT BINDING 799
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT BINDING 807..809
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NB78"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..621
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019968"
FT VAR_SEQ 459..558
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019969"
FT MUTAGEN 667
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19727073"
SQ SEQUENCE 826 AA; 92633 MW; 02FD6FE991B1C030 CRC64;
MAASRGRSKK RSNLELSPDN LPLRSSGRQA KKKAVEIPDE DEDGSSEKKY RKCEKAGCTA
AYPVCFASAS ERCAKNGYTS RWYHLSCGEH FCNECFDHYY RSHKDGYDKY SAWKRVWTSN
GKTEPSPKAF MADQQLPYWV QCTKPECGKW RQLTKEIQLT PHMARTYRCG MKPNTITKPD
TPDHCSFPED LRVLEVSNHW WYPMLIQPPL LKDSVAAPLL SAYYPDCVGM SPSCTSTHRA
TVTAATTTTG SASPGEMEPS KAAPSSLVLG MNRYFQPFYQ PNECGKALCV RPDVMELDEL
YEFPEYSRDP TMYLALRNLI LALWYTNCKE ALTPQKCIPH IIVRGLVRIR CVQEVERILY
FMTRKGLINT GVLTVAAGQH LLPKHYHNKS VLVVGAGPAG LAAARQLHNF GMKVTVLEAK
DRIGGRVWDD KSFKGVVVGR GPQIVNGCIN NPVALMCEQL GISMRKLGER CDLIQEGGRI
TDPTVDKRMD FHFNALLDVV SEWRKDKTLL QDVPLGEKIE EIYRAFVKES GIQFSELEGQ
VLQFHLSNLE YACGSSLHQV SARSWDHNEF FAQFAGDHTL LTPGYSTIIE KLAEGLDIRL
KSPVQSIDYT GDEVQVTTTD GMGHSAQKVL VTVPLAILQR GAIQFNPPLS EKKMKAINSL
GAGIIEKIAL QFPYRFWDSK VQGADFFGHV PPSASQRGLF AVFYDMDSQQ SVLMSVITGE
AVASLRTMDD KQVLQQCMGI LRELFKEQEI PEPTKYFVTR WSTEPWIQMA YSFVKTFGSG
EAYDIIAEEI QGTVFFAGEA TNRHFPQTVT GAYLSGVREA SKIAAF
