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Voltage-gated potassium channel subunit beta-1 (EC 1.1.1.-) (K( ) channel subunit beta-1) (Kv-beta-1)

 KCAB1_HUMAN             Reviewed;         419 AA.
Q14722; A8K9H8; A8KAD4; B3KPZ4; Q13031; Q13302; Q16547; Q6PI60;
Q99869;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
20-JUN-2018, entry version 165.
RecName: Full=Voltage-gated potassium channel subunit beta-1;
EC=1.1.1.- {ECO:0000250|UniProtKB:P63144};
AltName: Full=K(+) channel subunit beta-1;
AltName: Full=Kv-beta-1;
Name=KCNAB1; Synonyms=KCNA1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KVB1.3), AND FUNCTION.
TISSUE=Heart left ventricle;
PubMed=7499366; DOI=10.1074/jbc.270.48.28531;
England S.K., Uebele V.N., Kodali J., Bennett P.B., Tamkun M.M.;
"A novel K+ channel beta-subunit (hKv beta 1.3) is produced via
alternative mRNA splicing.";
J. Biol. Chem. 270:28531-28534(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KVB1.2), FUNCTION, AND SUBUNIT.
TISSUE=Heart atrium;
PubMed=7890032; DOI=10.1016/0014-5793(95)00120-X;
Majumder K., De Biasi M., Wang Z., Wible B.A.;
"Molecular cloning and functional expression of a novel potassium
channel beta-subunit from human atrium.";
FEBS Lett. 361:13-16(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KVB1.2), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Heart left ventricle;
PubMed=7603988; DOI=10.1073/pnas.92.14.6309;
England S.K., Uebele V.N., Shear H., Kodali J., Bennett P.B.,
Tamkun M.M.;
"Characterization of a voltage-gated K+ channel beta subunit expressed
in human heart.";
Proc. Natl. Acad. Sci. U.S.A. 92:6309-6313(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KVB1.1), AND FUNCTION.
TISSUE=Hippocampus;
PubMed=7649300; DOI=10.1016/0014-5793(95)00785-8;
Mccormack K., McCormack T., Tanouye M.A., Rudy B., Stuehmer W.;
"Alternative splicing of the human Shaker K+ channel beta 1 gene and
functional expression of the beta 2 gene product.";
FEBS Lett. 370:32-36(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KVB1.1), ALTERNATIVE SPLICING,
FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Brain cortex;
PubMed=8938711; DOI=10.1016/0028-3908(96)00133-5;
Leicher T., Roeper J., Weber K., Wang X., Pongs O.;
"Structural and functional characterization of human potassium channel
subunit beta 1 (KCNA1B).";
Neuropharmacology 35:787-795(1996).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS KVB1.1; KVB1.2 AND
KVB1.3).
TISSUE=Hippocampus, Thymus, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM KVB1.1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-147 (ISOFORM KVB1.2), AND FUNCTION.
TISSUE=Heart;
PubMed=7890764; DOI=10.1074/jbc.270.11.6272;
Morales M.J., Castellino R.C., Crews A.L., Rasmusson R.L.,
Strauss H.C.;
"A novel beta subunit increases rate of inactivation of specific
voltage-gated potassium channel alpha subunits.";
J. Biol. Chem. 270:6272-6277(1995).
[10]
FUNCTION, AND DOMAIN.
PubMed=9763623; DOI=10.1111/j.1469-7793.1998.325be.x;
Accili E.A., Kuryshev Y.A., Wible B.A., Brown A.M.;
"Separable effects of human Kvbeta1.2 N- and C-termini on inactivation
and expression of human Kv1.4.";
J. Physiol. (Lond.) 512:325-336(1998).
[11]
FUNCTION.
PubMed=12077175;
Maylie B., Bissonnette E., Virk M., Adelman J.P., Maylie J.G.;
"Episodic ataxia type 1 mutations in the human Kv1.1 potassium channel
alter hKvbeta 1-induced N-type inactivation.";
J. Neurosci. 22:4786-4793(2002).
[12]
FUNCTION, AND INTERACTION WITH KCNA5.
PubMed=12130714; DOI=10.1124/jpet.102.033357;
Williams C.P., Hu N., Shen W., Mashburn A.B., Murray K.T.;
"Modulation of the human Kv1.5 channel by protein kinase C activation:
role of the Kvbeta1.2 subunit.";
J. Pharmacol. Exp. Ther. 302:545-550(2002).
[13]
FUNCTION.
PubMed=15361858; DOI=10.1038/nsmb825;
Bhalla T., Rosenthal J.J., Holmgren M., Reenan R.;
"Control of human potassium channel inactivation by editing of a small
mRNA hairpin.";
Nat. Struct. Mol. Biol. 11:950-956(2004).
[14]
FUNCTION.
PubMed=17156368; DOI=10.1111/j.1460-9568.2006.05186.x;
Imbrici P., D'Adamo M.C., Kullmann D.M., Pessia M.;
"Episodic ataxia type 1 mutations in the KCNA1 gene impair the fast
inactivation properties of the human potassium channels Kv1.4-
1.1/Kvbeta1.1 and Kv1.4-1.1/Kvbeta1.2.";
Eur. J. Neurosci. 24:3073-3083(2006).
[15]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF TYR-307 AND
ARG-316.
PubMed=17540341; DOI=10.1016/j.bbrc.2007.05.102;
Tipparaju S.M., Liu S.Q., Barski O.A., Bhatnagar A.;
"NADPH binding to beta-subunit regulates inactivation of voltage-gated
K(+) channels.";
Biochem. Biophys. Res. Commun. 359:269-276(2007).
[16]
FUNCTION, AND DOMAIN.
PubMed=19713757; DOI=10.4161/chan.3.5.9558;
Peters C.J., Vaid M., Horne A.J., Fedida D., Accili E.A.;
"The molecular basis for the actions of Kvbeta1.2 on the opening and
closing of the Kv1.2 delayed rectifier channel.";
Channels 3:314-322(2009).
-!- FUNCTION: Cytoplasmic potassium channel subunit that modulates the
characteristics of the channel-forming alpha-subunits
(PubMed:7499366, PubMed:7603988, PubMed:17156368,PubMed:17540341,
PubMed:19713757). Modulates action potentials via its effect on
the pore-forming alpha subunits (By similarity). Promotes
expression of the pore-forming alpha subunits at the cell
membrane, and thereby increases channel activity (By similarity).
Mediates closure of delayed rectifier potassium channels by
physically obstructing the pore via its N-terminal domain and
increases the speed of channel closure for other family members
(PubMed:9763623). Promotes the closure of KCNA1, KCNA2 and KCNA5
channels (PubMed:7499366, PubMed:7890032, PubMed:7603988,
PubMed:7649300, PubMed:8938711, PubMed:12077175, PubMed:12130714,
PubMed:15361858, PubMed:17540341, PubMed:19713757). Accelerates
KCNA4 channel closure (PubMed:7890032, PubMed:7649300,
PubMed:7890764, PubMed:9763623). Accelerates the closure of
heteromeric channels formed by KCNA1 and KCNA4 (PubMed:17156368).
Accelerates the closure of heteromeric channels formed by KCNA2,
KCNA5 and KCNA6 (By similarity). Isoform KvB1.2 has no effect on
KCNA1, KCNA2 or KCNB1 (PubMed:7890032, PubMed:7890764). Enhances
KCNB1 and KCNB2 channel activity (By similarity). Binds NADPH;
this is required for efficient down-regulation of potassium
channel activity (PubMed:17540341). Has NADPH-dependent
aldoketoreductase activity (By similarity). Oxidation of the bound
NADPH strongly decreases N-type inactivation of potassium channel
activity (By similarity). {ECO:0000250|UniProtKB:P63143,
ECO:0000250|UniProtKB:P63144, ECO:0000269|PubMed:12077175,
ECO:0000269|PubMed:12130714, ECO:0000269|PubMed:15361858,
ECO:0000269|PubMed:17156368, ECO:0000269|PubMed:17540341,
ECO:0000269|PubMed:19713757, ECO:0000269|PubMed:7499366,
ECO:0000269|PubMed:7603988, ECO:0000269|PubMed:7649300,
ECO:0000269|PubMed:7890032, ECO:0000269|PubMed:7890764,
ECO:0000269|PubMed:8938711, ECO:0000269|PubMed:9763623,
ECO:0000305}.
-!- SUBUNIT: Homotetramer (By similarity). Interaction with tetrameric
potassium channel alpha subunits gives rise to a heterooctamer
(Probable). Identified in potassium channel complexes containing
KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNAB1 and KCNAB2 (By
similarity). Interacts with KCNA1 (By similarity). Interacts with
the dimer formed by GNB1 and GNG2; this enhances KCNA1 binding (By
similarity). Interacts with KCNA4 (PubMed:9763623). Interacts with
KCNA5 (PubMed:12130714). Interacts with KCNB2 (By similarity).
Interacts with SQSTM1 (By similarity). Part of a complex
containing KCNA1, KCNA4 and LGI1; interaction with LGI1 inhibits
down-regulation of KCNA1 channel activity (By similarity).
{ECO:0000250|UniProtKB:P63143, ECO:0000250|UniProtKB:P63144,
ECO:0000269|PubMed:12130714, ECO:0000269|PubMed:9763623,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17540341}.
Membrane {ECO:0000250|UniProtKB:P63144}; Peripheral membrane
protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell
membrane {ECO:0000269|PubMed:17540341}; Peripheral membrane
protein {ECO:0000269|PubMed:17540341}; Cytoplasmic side
{ECO:0000269|PubMed:17540341}. Note=Recruited to the cytoplasmic
side of the cell membrane via its interaction with pore-forming
potassium channel alpha subunits. {ECO:0000269|PubMed:17540341}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=KvB1.3;
IsoId=Q14722-1; Sequence=Displayed;
Name=KvB1.1;
IsoId=Q14722-2; Sequence=VSP_001051;
Name=KvB1.2;
IsoId=Q14722-3; Sequence=VSP_001050;
Note=Ref.9 (AAC50113) sequence is in conflict in position:
16:L->S. {ECO:0000305};
-!- TISSUE SPECIFICITY: In brain, expression is most prominent in
caudate nucleus, hippocampus and thalamus. Significant expression
also detected in amygdala and subthalamic nucleus. Also expressed
in both healthy and cardiomyopathic heart. Up to four times more
abundant in left ventricle than left atrium.
{ECO:0000269|PubMed:7603988, ECO:0000269|PubMed:8938711}.
-!- DOMAIN: The N-terminal domain of the beta subunit mediates closure
of delayed rectifier potassium channels by physically obstructing
the pore. {ECO:0000269|PubMed:19713757,
ECO:0000269|PubMed:9763623}.
-!- SIMILARITY: Belongs to the shaker potassium channel beta subunit
family. {ECO:0000305}.
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EMBL; L47665; AAC41926.1; -; mRNA.
EMBL; U16953; AAC50122.1; -; mRNA.
EMBL; L39833; AAC37573.1; -; mRNA.
EMBL; U33428; AAC50953.1; -; mRNA.
EMBL; X83127; CAA58208.1; -; mRNA.
EMBL; AK057059; BAG51856.1; -; mRNA.
EMBL; AK127240; BAG54461.1; -; mRNA.
EMBL; AK292693; BAF85382.1; -; mRNA.
EMBL; AK292999; BAF85688.1; -; mRNA.
EMBL; CH471052; EAW78732.1; -; Genomic_DNA.
EMBL; CH471052; EAW78733.1; -; Genomic_DNA.
EMBL; CH471052; EAW78734.1; -; Genomic_DNA.
EMBL; BC043166; AAH43166.1; -; mRNA.
EMBL; U17968; AAC50113.1; -; mRNA.
CCDS; CCDS3174.1; -. [Q14722-1]
CCDS; CCDS3175.1; -. [Q14722-3]
CCDS; CCDS33882.1; -. [Q14722-2]
PIR; I55463; I55463.
PIR; I59393; I59393.
RefSeq; NP_001295146.1; NM_001308217.1.
RefSeq; NP_001295151.1; NM_001308222.1.
RefSeq; NP_003462.2; NM_003471.3. [Q14722-3]
RefSeq; NP_751891.1; NM_172159.3. [Q14722-2]
RefSeq; NP_751892.1; NM_172160.2. [Q14722-1]
UniGene; Hs.654519; -.
UniGene; Hs.703187; -.
DisProt; DP00090; -.
ProteinModelPortal; Q14722; -.
SMR; Q14722; -.
BioGrid; 113626; 12.
IntAct; Q14722; 2.
STRING; 9606.ENSP00000419952; -.
ChEMBL; CHEMBL5884; -.
TCDB; 8.A.5.1.1; the voltage-gated k(+) channel -subunit (kv) family.
iPTMnet; Q14722; -.
PhosphoSitePlus; Q14722; -.
BioMuta; KCNAB1; -.
DMDM; 18202500; -.
MaxQB; Q14722; -.
PaxDb; Q14722; -.
PeptideAtlas; Q14722; -.
PRIDE; Q14722; -.
ProteomicsDB; 60145; -.
ProteomicsDB; 60146; -. [Q14722-2]
ProteomicsDB; 60147; -. [Q14722-3]
DNASU; 7881; -.
Ensembl; ENST00000302490; ENSP00000305858; ENSG00000169282. [Q14722-2]
Ensembl; ENST00000471742; ENSP00000418956; ENSG00000169282. [Q14722-3]
Ensembl; ENST00000490337; ENSP00000419952; ENSG00000169282. [Q14722-1]
GeneID; 7881; -.
KEGG; hsa:7881; -.
UCSC; uc003far.3; human. [Q14722-1]
CTD; 7881; -.
DisGeNET; 7881; -.
EuPathDB; HostDB:ENSG00000169282.17; -.
GeneCards; KCNAB1; -.
HGNC; HGNC:6228; KCNAB1.
HPA; HPA044550; -.
MIM; 601141; gene.
neXtProt; NX_Q14722; -.
OpenTargets; ENSG00000169282; -.
PharmGKB; PA370; -.
eggNOG; KOG1575; Eukaryota.
eggNOG; COG0667; LUCA.
GeneTree; ENSGT00550000074567; -.
HOVERGEN; HBG052216; -.
InParanoid; Q14722; -.
KO; K04882; -.
OMA; AVSIQNP; -.
OrthoDB; EOG091G0KDN; -.
PhylomeDB; Q14722; -.
TreeFam; TF324563; -.
Reactome; R-HSA-1296072; Voltage gated Potassium channels.
ChiTaRS; KCNAB1; human.
GeneWiki; KCNAB1; -.
GenomeRNAi; 7881; -.
PRO; PR:Q14722; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000169282; -.
CleanEx; HS_KCNAB1; -.
ExpressionAtlas; Q14722; baseline and differential.
Genevisible; Q14722; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0044224; C:juxtaparanode region of axon; IEA:Ensembl.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0034705; C:potassium channel complex; IDA:UniProtKB.
GO; GO:1990635; C:proximal dendrite; IEA:Ensembl.
GO; GO:0008076; C:voltage-gated potassium channel complex; IMP:CAFA.
GO; GO:0004033; F:aldo-keto reductase (NADP) activity; ISS:UniProtKB.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0060539; P:diaphragm development; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0007611; P:learning or memory; IEA:Ensembl.
GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; IEA:Ensembl.
GO; GO:1903817; P:negative regulation of voltage-gated potassium channel activity; IMP:CAFA.
GO; GO:0055114; P:oxidation-reduction process; ISS:UniProtKB.
GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
CDD; cd06660; Aldo_ket_red; 1.
Gene3D; 3.20.20.100; -; 1.
InterPro; IPR005983; K_chnl_volt-dep_bsu_KCNAB.
InterPro; IPR005399; K_chnl_volt-dep_bsu_KCNAB-rel.
InterPro; IPR005400; K_chnl_volt-dep_bsu_KCNAB1.
InterPro; IPR023210; NADP_OxRdtase_dom.
InterPro; IPR036812; NADP_OxRdtase_dom_sf.
Pfam; PF00248; Aldo_ket_red; 1.
PRINTS; PR01578; KCNAB1CHANEL.
PRINTS; PR01577; KCNABCHANNEL.
SUPFAM; SSF51430; SSF51430; 1.
TIGRFAMs; TIGR01293; Kv_beta; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
Ion channel; Ion transport; Membrane; NADP; Oxidoreductase; Potassium;
Potassium transport; Reference proteome; Transport;
Voltage-gated channel.
CHAIN 1 419 Voltage-gated potassium channel subunit
beta-1.
/FTId=PRO_0000148739.
NP_BIND 108 109 NADP. {ECO:0000250|UniProtKB:P62483}.
NP_BIND 240 241 NADP. {ECO:0000250|UniProtKB:P62483}.
NP_BIND 295 300 NADP. {ECO:0000250|UniProtKB:P62483}.
NP_BIND 375 381 NADP. {ECO:0000250|UniProtKB:P62483}.
ACT_SITE 142 142 Proton donor/acceptor.
{ECO:0000250|UniProtKB:P62483}.
BINDING 115 115 NADP. {ECO:0000250|UniProtKB:P62483}.
BINDING 137 137 NADP. {ECO:0000250|UniProtKB:P62483}.
BINDING 142 142 NADP. {ECO:0000250|UniProtKB:P62483}.
BINDING 266 266 NADP. {ECO:0000250|UniProtKB:P62483}.
BINDING 306 306 NADP. {ECO:0000250|UniProtKB:P62483}.
VAR_SEQ 1 91 MLAARTGAAGSQISEENTKLRRQSGFSVAGKDKSPKKASEN
AKDSSLSPSGESQLRARQLALLREVEMNWYLKLCDLSSEHT
TVCTTGMPH -> MQVSIACTEHNLKSRNGEDRLLSKQSST
APNVVNAARAKFRTVAIIARSLGTFTPQHHISLKESTAKQT
GMKY (in isoform KvB1.1).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7649300,
ECO:0000303|PubMed:8938711}.
/FTId=VSP_001051.
VAR_SEQ 1 91 MLAARTGAAGSQISEENTKLRRQSGFSVAGKDKSPKKASEN
AKDSSLSPSGESQLRARQLALLREVEMNWYLKLCDLSSEHT
TVCTTGMPH -> MHLYKPACADIPSPKLGLPKSSESALKC
RWHLAVTKTQPQAACKPVRPSGAAEQKYVEKFLRVHGISLQ
ETTRAETGMAY (in isoform KvB1.2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:7603988,
ECO:0000303|PubMed:7890032,
ECO:0000303|PubMed:7890764}.
/FTId=VSP_001050.
MUTAGEN 307 307 Y->F: Reduces affinity for NADPH.
{ECO:0000269|PubMed:17540341}.
MUTAGEN 316 316 R->E: Nearly abolishes NADPH binding.
{ECO:0000269|PubMed:17540341}.
CONFLICT 290 290 V -> L (in Ref. 5; CAA58208).
{ECO:0000305}.
SEQUENCE 419 AA; 46563 MW; EFFDA78568007A7A CRC64;
MLAARTGAAG SQISEENTKL RRQSGFSVAG KDKSPKKASE NAKDSSLSPS GESQLRARQL
ALLREVEMNW YLKLCDLSSE HTTVCTTGMP HRNLGKSGLR VSCLGLGTWV TFGGQISDEV
AERLMTIAYE SGVNLFDTAE VYAAGKAEVI LGSIIKKKGW RRSSLVITTK LYWGGKAETE
RGLSRKHIIE GLKGSLQRLQ LEYVDVVFAN RPDSNTPMEE IVRAMTHVIN QGMAMYWGTS
RWSAMEIMEA YSVARQFNMI PPVCEQAEYH LFQREKVEVQ LPELYHKIGV GAMTWSPLAC
GIISGKYGNG VPESSRASLK CYQWLKERIV SEEGRKQQNK LKDLSPIAER LGCTLPQLAV
AWCLRNEGVS SVLLGSSTPE QLIENLGAIQ VLPKMTSHVV NEIDNILRNK PYSKKDYRS


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