ID   KCAB1_MOUSE             Reviewed;         401 AA.
AC   P63143; P97380; Q61763; Q63277; Q91WM5;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   02-SEP-2026, entry version 152.
DE   RecName: Full=Voltage-gated potassium channel subunit beta-1;
DE            EC=1.1.1.- {ECO:0000250|UniProtKB:P63144};
DE   AltName: Full=K(+) channel subunit beta-1;
DE   AltName: Full=Kv-beta-1;
GN   Name=Kcnab1 {ECO:0000312|MGI:MGI:109155}; Synonyms=Kvb1;
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], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=Swiss Webster; TISSUE=Hippocampus;
RX   PubMed=9468385;
RX   DOI=10.1002/(sici)1097-4695(19980205)34:2<135::aid-neu4>3.3.co;2-q;
RA   Butler D.M., Ono J.K., Chang T., McCaman R.E., Barish M.E.;
RT   "Mouse brain potassium channel beta1 subunit mRNA: cloning and distribution
RT   during development.";
RL   J. Neurobiol. 34:135-150(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=8824288; DOI=10.1074/jbc.271.42.26341;
RA   Fink M., Duprat F., Lesage F., Heurteaux C., Romey G., Barhanin J.,
RA   Lazdunski M.;
RT   "A new K+ channel beta subunit to specifically enhance Kv2.2 (CDRK)
RT   expression.";
RL   J. Biol. Chem. 271:26341-26348(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RA   Metzler M., Repp R., Kreuder J., Borkhardt A., Koschinski A., Lampert F.,
RA   Dreyer F., Repp H.;
RT   "Expression of a potassium channel beta-subunit in mouse fibroblasts.";
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
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   [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
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   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=10454353; DOI=10.1101/lm.5.4.257;
RA   Giese K.P., Storm J.F., Reuter D., Fedorov N.B., Shao L.R., Leicher T.,
RA   Pongs O., Silva A.J.;
RT   "Reduced K+ channel inactivation, spike broadening, and after-
RT   hyperpolarization in Kvbeta1.1-deficient mice with impaired learning.";
RL   Learn. Memory 5:257-273(1998).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=14511342; DOI=10.1046/j.1460-9568.2003.02889.x;
RA   Need A.C., Irvine E.E., Giese K.P.;
RT   "Learning and memory impairments in Kv beta 1.1-null mutants are rescued by
RT   environmental enrichment or ageing.";
RL   Eur. J. Neurosci. 18:1640-1644(2003).
RN   [9]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15530391; DOI=10.1016/j.cub.2004.10.021;
RA   Murphy G.G., Fedorov N.B., Giese K.P., Ohno M., Friedman E., Chen R.,
RA   Silva A.J.;
RT   "Increased neuronal excitability, synaptic plasticity, and learning in aged
RT   Kvbeta1.1 knockout mice.";
RL   Curr. Biol. 14:1907-1915(2004).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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: Regulatory subunit of the voltage-gated potassium (Kv) Shaker
CC       channels composed of pore-forming and potassium-conducting alpha
CC       subunits and of regulatory beta subunits (PubMed:10454353). The beta-
CC       1/KCNAB1 cytoplasmic subunit mediates closure of delayed rectifier
CC       potassium channels by physically obstructing the pore via its N-
CC       terminal domain and increases the speed of channel closure for other
CC       family members. Promotes the inactivation of KCNA1, KCNA2, KCNA4, KCNA5
CC       and KCNA6 alpha subunit-containing channels (By similarity). Displays
CC       nicotinamide adenine dinucleotide phosphate (NADPH)-dependent
CC       aldoketoreductase activity by catalyzing the NADPH-dependent reduction
CC       of a variety of endogenous aldehydes and ketones (By similarity). The
CC       binding of NADPH is required for efficient down-regulation of potassium
CC       channel activity (By similarity). Oxidation of the bound NADPH
CC       restrains N-terminal domain from blocking the channel, thereby
CC       decreasing N-type inactivation of potassium channel activity (By
CC       similarity). {ECO:0000250|UniProtKB:P63144,
CC       ECO:0000250|UniProtKB:Q14722, ECO:0000269|PubMed:10454353}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NADP(+) = an aldehyde + NADPH + H(+);
CC         Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P63144};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15939;
CC         Evidence={ECO:0000250|UniProtKB:P63144};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NADP(+) = a ketone + NADPH + H(+);
CC         Xref=Rhea:RHEA:19257, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P63144};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19259;
CC         Evidence={ECO:0000250|UniProtKB:P63144};
CC   -!- SUBUNIT: Homotetramer (By similarity). Interaction with tetrameric
CC       potassium channel alpha subunits gives rise to a heterooctamer
CC       (Probable). Identified in potassium channel complexes containing KCNA1,
CC       KCNA2, KCNA4, KCNA5, KCNA6, KCNAB1 and KCNAB2 (By similarity). Part of
CC       a complex containing KCNA1, KCNA4 and LGI1; interaction with LGI1
CC       inhibits down-regulation of KCNA1 channel activity (By similarity).
CC       Interacts with the dimer formed by GNB1 and GNG2; this enhances KCNA1
CC       binding (By similarity). Interacts with SQSTM (By similarity).
CC       {ECO:0000250|UniProtKB:P63144, ECO:0000250|UniProtKB:Q14722,
CC       ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14722}.
CC       Membrane {ECO:0000250|UniProtKB:P63144}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P63144}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P63144}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q14722}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q14722}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q14722}. Note=Recruited to the cytoplasmic side
CC       of the cell membrane via its interaction with pore-forming potassium
CC       channel alpha subunits. {ECO:0000250|UniProtKB:Q14722}.
CC   -!- TISSUE SPECIFICITY: Detected in brain, in hippocampus and striatum (at
CC       protein level) (PubMed:10454353). Predominantly expressed in brain
CC       (PubMed:10454353, PubMed:8824288, PubMed:9468385). No expression found
CC       in heart, skeletal muscle or kidney. In the late embryonic and early
CC       neonatal brain, highly expressed in hippocampus, cerebral cortex,
CC       caudate putamen, colliculus and cerebellum (PubMed:10454353,
CC       PubMed:9468385). {ECO:0000269|PubMed:10454353,
CC       ECO:0000269|PubMed:8824288, ECO:0000269|PubMed:9468385}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from embryonic day 16. Expressed
CC       throughout embryonic development, in neonate and in adult.
CC       {ECO:0000269|PubMed:9468385}.
CC   -!- DOMAIN: The N-terminal domain of the beta subunit mediates closure of
CC       delayed rectifier potassium channels by physically obstructing the
CC       pore. {ECO:0000250|UniProtKB:P63144}.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice show subtle defects in learning
CC       (PubMed:10454353). Such learning impairments are not detectable in
CC       older mice and are not observed when mice are kept in a stimulating
CC       environment (PubMed:14511342, PubMed:15530391).
CC       {ECO:0000269|PubMed:10454353, ECO:0000269|PubMed:14511342,
CC       ECO:0000269|PubMed:15530391}.
CC   -!- SIMILARITY: Belongs to the shaker potassium channel beta subunit
CC       family. {ECO:0000305}.
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DR   EMBL; AF033003; AAB87085.1; -; mRNA.
DR   EMBL; U65591; AAB37262.1; -; mRNA.
DR   EMBL; X97281; CAA65936.1; -; mRNA.
DR   EMBL; AK138467; BAE23670.1; -; mRNA.
DR   EMBL; CH466547; EDL15543.1; -; Genomic_DNA.
DR   EMBL; BC014701; AAH14701.1; -; mRNA.
DR   CCDS; CCDS38447.1; -.
DR   RefSeq; NP_034727.3; NM_010597.6.
DR   AlphaFoldDB; P63143; -.
DR   SMR; P63143; -.
DR   BioGRID; 200883; 9.
DR   FunCoup; P63143; 186.
DR   IntAct; P63143; 4.
DR   MINT; P63143; -.
DR   STRING; 10090.ENSMUSP00000047480; -.
DR   GlyGen; P63143; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P63143; -.
DR   PhosphoSitePlus; P63143; -.
DR   SwissPalm; P63143; -.
DR   jPOST; P63143; -.
DR   PaxDb; 10090-ENSMUSP00000047480; -.
DR   PeptideAtlas; P63143; -.
DR   ProteomicsDB; 301755; -.
DR   Pumba; P63143; -.
DR   ABCD; P63143; 3 sequenced antibodies.
DR   Antibodypedia; 18386; 432 antibodies from 34 providers.
DR   DNASU; 16497; -.
DR   Ensembl; ENSMUST00000049230.11; ENSMUSP00000047480.9; ENSMUSG00000027827.18.
DR   GeneID; 16497; -.
DR   KEGG; mmu:16497; -.
DR   UCSC; uc008pkj.2; mouse.
DR   AGR; MGI:109155; -.
DR   CTD; 7881; -.
DR   MGI; MGI:109155; Kcnab1.
DR   VEuPathDB; HostDB:ENSMUSG00000027827; -.
DR   eggNOG; KOG1575; Eukaryota.
DR   GeneTree; ENSGT00940000156760; -.
DR   HOGENOM; CLU_023205_2_0_1; -.
DR   InParanoid; P63143; -.
DR   OMA; MWAGPYG; -.
DR   PhylomeDB; P63143; -.
DR   Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR   BioGRID-ORCS; 16497; 2 hits in 76 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:P63143; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P63143; protein.
DR   Bgee; ENSMUSG00000027827; Expressed in caudate-putamen and 173 other cell types or tissues.
DR   ExpressionAtlas; P63143; baseline and differential.
DR   GO; GO:0030424; C:axon; ISO:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0032839; C:dendrite cytoplasm; ISO:GO_Central.
DR   GO; GO:0044224; C:juxtaparanode region of axon; ISO:GO_Central.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISO:GO_Central.
DR   GO; GO:0043204; C:perikaryon; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0034705; C:potassium channel complex; ISS:UniProtKB.
DR   GO; GO:1990635; C:proximal dendrite; ISO:GO_Central.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:GO_Central.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR   GO; GO:0004090; F:carbonyl reductase (NADPH) activity; ISS:UniProtKB.
DR   GO; GO:0140678; F:molecular function inhibitor activity; ISO:GO_Central.
DR   GO; GO:0070402; F:NADPH binding; ISS:UniProtKB.
DR   GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:GO_Central.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:GO_Central.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0007611; P:learning or memory; IMP:MGI.
DR   GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISO:GO_Central.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR   GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISO:GO_Central.
DR   CDD; cd19159; AKR_KCAB1B_AKR6A3-like; 1.
DR   FunFam; 3.20.20.100:FF:000001; voltage-gated potassium channel subunit beta-2 isoform X2; 1.
DR   Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR   InterPro; IPR005983; K_chnl_volt-dep_bsu_KCNAB.
DR   InterPro; IPR005399; K_chnl_volt-dep_bsu_KCNAB-rel.
DR   InterPro; IPR005400; K_chnl_volt-dep_bsu_KCNAB1.
DR   InterPro; IPR036812; NAD(P)_OxRdtase_dom_sf.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   NCBIfam; TIGR01293; Kv_beta; 1.
DR   PANTHER; PTHR43150; HYPERKINETIC, ISOFORM M; 1.
DR   PANTHER; PTHR43150:SF7; VOLTAGE-GATED POTASSIUM CHANNEL SUBUNIT BETA-1; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PRINTS; PR01578; KCNAB1CHANEL.
DR   PRINTS; PR01577; KCNABCHANNEL.
DR   SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Ion transport; Membrane; NADP; Oxidoreductase;
KW   Potassium; Potassium transport; Reference proteome; Transport.
FT   CHAIN           1..401
FT                   /note="Voltage-gated potassium channel subunit beta-1"
FT                   /id="PRO_0000148740"
FT   ACT_SITE        124
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         90
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         91
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         97
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         119
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         192
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         222
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         223
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         248
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         277
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         278
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         279
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         280
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         281
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         282
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         288
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         298
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         357
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         359
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         363
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         366
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   BINDING         367
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P62483"
FT   CONFLICT        28
FT                   /note="N -> T (in Ref. 1; AAB87085 and 3; CAA65936)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="H -> D (in Ref. 2; AAB37262)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        175
FT                   /note="K -> N (in Ref. 3; CAA65936)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191
FT                   /note="A -> S (in Ref. 2; AAB37262)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        282
FT                   /note="C -> Y (in Ref. 2; AAB37262)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        329
FT                   /note="I -> F (in Ref. 2; AAB37262)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        349
FT                   /note="E -> D (in Ref. 2; AAB37262)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   401 AA;  44723 MW;  09F7860DCD3728B6 CRC64;
     MQVSIACTEH NLKSRNGEDR LLSKQSSNAP NVVNAARAKF RTVAIIARSL GTFTPQHHIS
     LKESTAKQTG MKYRNLGKSG LRVSCLGLGT WVTFGGQISD EVAERLMTIA YESGVNLFDT
     AEVYAAGKAE VILGSIIKKK GWRRSSLVIT TKLYWGGKAE TERGLSRKHI IEGLKGSLQR
     LQLEYVDVVF ANRPDSNTPM EEIVRAMTHV INQGMAMYWG TSRWSAMEIM EAYSVARQFN
     MIPPVCEQAE YHLFQREKVE VQLPELYHKI GVGAMTWSPL ACGIISGKYG NGVPESSRAS
     LKCYQWLKER IVSEEGRKQQ NKLKDLSPIA ERLGCTLPQL AVAWCLRNEG VSSVLLGSST
     PEQLIENLGA IQVLPKMTSH VVNEIDNILR NKPYSKKDYR S
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