IDH3B_HUMAN
ID IDH3B_HUMAN Reviewed; 385 AA.
AC O43837; B2RDR1; D3DVX2; D3DVX3; O95106; Q5JXS8; Q9NQ06; Q9NQ07; Q9NUZ0;
AC Q9UEX0; Q9UG99;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial;
DE AltName: Full=Isocitric dehydrogenase subunit beta;
DE AltName: Full=NAD(+)-specific ICDH subunit beta;
DE Flags: Precursor;
GN Name=IDH3B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), VARIANT VAL-3, AND
RP ALTERNATIVE SPLICING.
RC TISSUE=Heart;
RX PubMed=10601238; DOI=10.1074/jbc.274.52.36866;
RA Kim Y.-O., Koh H.-J., Kim S.-H., Jo S.-H., Huh J.-W., Jeong K.-S.,
RA Lee I.J., Song B.J., Huh T.-L.;
RT "Identification and functional characterization of a novel, tissue-specific
RT NAD+-dependent isocitrate dehydrogenase beta subunit isoform.";
RL J. Biol. Chem. 274:36866-36875(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).
RC TISSUE=Placenta, and Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Lung;
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 127-385 (ISOFORM B).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=28098230; DOI=10.1038/srep40921;
RA Ma T., Peng Y., Huang W., Ding J.;
RT "Molecular mechanism of the allosteric regulation of the alphagamma
RT heterodimer of human NAD-dependent isocitrate dehydrogenase.";
RL Sci. Rep. 7:40921-40921(2017).
RN [11]
RP FUNCTION, SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=28139779; DOI=10.1038/srep41882;
RA Ma T., Peng Y., Huang W., Liu Y., Ding J.;
RT "The beta and gamma subunits play distinct functional roles in the
RT alpha2betagamma heterotetramer of human NAD-dependent isocitrate
RT dehydrogenase.";
RL Sci. Rep. 7:41882-41882(2017).
RN [12]
RP VARIANT RP46 PRO-132.
RX PubMed=18806796; DOI=10.1038/ng.223;
RA Hartong D.T., Dange M., McGee T.L., Berson E.L., Dryja T.P., Colman R.F.;
RT "Insights from retinitis pigmentosa into the roles of isocitrate
RT dehydrogenases in the Krebs cycle.";
RL Nat. Genet. 40:1230-1234(2008).
CC -!- FUNCTION: Plays a structural role to facilitate the assembly and ensure
CC the full activity of the enzyme catalyzing the decarboxylation of
CC isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of
CC the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer
CC composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have
CC considerable basal activity but the full activity of the heterotetramer
CC (containing two subunits of IDH3A, one of IDH3B and one of IDH3G)
CC requires the assembly and cooperative function of both heterodimers.
CC {ECO:0000269|PubMed:28139779}.
CC -!- ACTIVITY REGULATION: The heterotetramer and the heterodimer composed of
CC IDH3A and IDH3G subunits can be allosterically activated by citrate
CC (CIT) or/and ADP, and the two activators can act independently or
CC synergistically. The heterodimer composed of IDH3A and IDH3B subunits
CC cannot be allosterically regulated and the allosteric regulation of the
CC heterotetramer is through the IDH3G subunit and not the IDH3B subunit.
CC The IDH3G subunit contains the allosteric site which consists of a CIT-
CC binding site and an ADP-binding site, and the binding of CIT and ADP
CC causes conformational changes at the allosteric site which are
CC transmitted to the active site in the catalytic subunit (IDH3A) through
CC a cascade of conformational changes at the heterodimer interface,
CC leading to stabilization of the isocitrate-binding at the active site
CC and thus activation of the enzyme. ATP can activate the heterotetramer
CC and the heterodimer composed of IDH3A and IDH3G subunits at low
CC concentrations but inhibits their activities at high concentrations,
CC whereas ATP exhibits only inhibitory effect on the heterodimer composed
CC of IDH3A and IDH3B subunits. {ECO:0000269|PubMed:28098230,
CC ECO:0000269|PubMed:28139779}.
CC -!- SUBUNIT: Heterooligomer of subunits alpha (IDH3A), beta (IDH3B), and
CC gamma (IDH3G) in the apparent ratio of 2:1:1. The heterodimer
CC containing one IDH3A and one IDH3B subunit and the heterodimer
CC containing one IDH3A and one IDH3G subunit assemble into a
CC heterotetramer (which contains two subunits of IDH3A, one of IDH3B and
CC one of IDH3G) and further into the heterooctamer.
CC {ECO:0000269|PubMed:28139779}.
CC -!- INTERACTION:
CC O43837-2; PRO_0000014436 [P50213]: IDH3A; NbExp=2; IntAct=EBI-725399, EBI-25820746;
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B;
CC IsoId=O43837-1; Sequence=Displayed;
CC Name=A;
CC IsoId=O43837-2; Sequence=VSP_002462;
CC Name=C;
CC IsoId=O43837-3; Sequence=VSP_041335;
CC -!- DISEASE: Retinitis pigmentosa 46 (RP46) [MIM:612572]: A retinal
CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. {ECO:0000269|PubMed:18806796}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; U49283; AAB94295.1; -; mRNA.
DR EMBL; AF023265; AAD09339.1; -; mRNA.
DR EMBL; AF023266; AAD09340.1; -; mRNA.
DR EMBL; AK001905; BAA91971.1; -; mRNA.
DR EMBL; AK315641; BAG38008.1; -; mRNA.
DR EMBL; AL049712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10579.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10580.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10582.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10583.1; -; Genomic_DNA.
DR EMBL; BC001960; AAH01960.1; -; mRNA.
DR EMBL; AL050094; CAB43266.1; -; mRNA.
DR CCDS; CCDS13031.1; -. [O43837-2]
DR CCDS; CCDS13032.1; -. [O43837-1]
DR PIR; T08743; T08743.
DR PIR; T13147; T13147.
DR RefSeq; NP_001317692.1; NM_001330763.1.
DR RefSeq; NP_008830.2; NM_006899.4. [O43837-1]
DR RefSeq; NP_777280.1; NM_174855.3. [O43837-2]
DR PDB; 6KDE; X-ray; 3.00 A; B/D=35-374.
DR PDB; 6KDF; X-ray; 3.05 A; C/D/F/H/J/L/N/P=35-374.
DR PDB; 6KDY; X-ray; 3.02 A; B/D/F/H=35-374.
DR PDB; 6KE3; X-ray; 3.31 A; B/D/F/H=35-374.
DR PDB; 7CE3; X-ray; 3.47 A; D=35-374.
DR PDBsum; 6KDE; -.
DR PDBsum; 6KDF; -.
DR PDBsum; 6KDY; -.
DR PDBsum; 6KE3; -.
DR PDBsum; 7CE3; -.
DR AlphaFoldDB; O43837; -.
DR SMR; O43837; -.
DR BioGRID; 109646; 77.
DR ComplexPortal; CPX-553; Mitochondrial isocitrate dehydrogenase complex (NAD+).
DR CORUM; O43837; -.
DR IntAct; O43837; 34.
DR MINT; O43837; -.
DR STRING; 9606.ENSP00000370223; -.
DR DrugBank; DB00157; NADH.
DR iPTMnet; O43837; -.
DR MetOSite; O43837; -.
DR PhosphoSitePlus; O43837; -.
DR BioMuta; IDH3B; -.
DR EPD; O43837; -.
DR jPOST; O43837; -.
DR MassIVE; O43837; -.
DR MaxQB; O43837; -.
DR PaxDb; O43837; -.
DR PeptideAtlas; O43837; -.
DR PRIDE; O43837; -.
DR ProteomicsDB; 49197; -. [O43837-1]
DR ProteomicsDB; 49198; -. [O43837-2]
DR ProteomicsDB; 49199; -. [O43837-3]
DR Antibodypedia; 23248; 265 antibodies from 32 providers.
DR DNASU; 3420; -.
DR Ensembl; ENST00000380843.9; ENSP00000370223.4; ENSG00000101365.21. [O43837-1]
DR Ensembl; ENST00000380851.9; ENSP00000370232.5; ENSG00000101365.21. [O43837-2]
DR GeneID; 3420; -.
DR KEGG; hsa:3420; -.
DR MANE-Select; ENST00000380843.9; ENSP00000370223.4; NM_006899.5; NP_008830.2.
DR UCSC; uc002wgp.4; human. [O43837-1]
DR CTD; 3420; -.
DR DisGeNET; 3420; -.
DR GeneCards; IDH3B; -.
DR GeneReviews; IDH3B; -.
DR HGNC; HGNC:5385; IDH3B.
DR HPA; ENSG00000101365; Low tissue specificity.
DR MalaCards; IDH3B; -.
DR MIM; 604526; gene.
DR MIM; 612572; phenotype.
DR neXtProt; NX_O43837; -.
DR OpenTargets; ENSG00000101365; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA29633; -.
DR VEuPathDB; HostDB:ENSG00000101365; -.
DR eggNOG; KOG0784; Eukaryota.
DR GeneTree; ENSGT00950000182989; -.
DR HOGENOM; CLU_031953_0_1_1; -.
DR InParanoid; O43837; -.
DR OMA; TCAHKAN; -.
DR OrthoDB; 868374at2759; -.
DR PhylomeDB; O43837; -.
DR TreeFam; TF315033; -.
DR BioCyc; MetaCyc:ENSG00000101365-MON; -.
DR BRENDA; 1.1.1.41; 2681.
DR PathwayCommons; O43837; -.
DR Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
DR SABIO-RK; O43837; -.
DR SignaLink; O43837; -.
DR SIGNOR; O43837; -.
DR BioGRID-ORCS; 3420; 21 hits in 1083 CRISPR screens.
DR ChiTaRS; IDH3B; human.
DR GeneWiki; IDH3B; -.
DR GenomeRNAi; 3420; -.
DR Pharos; O43837; Tbio.
DR PRO; PR:O43837; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O43837; protein.
DR Bgee; ENSG00000101365; Expressed in apex of heart and 206 other tissues.
DR ExpressionAtlas; O43837; baseline and differential.
DR Genevisible; O43837; HS.
DR GO; GO:0005962; C:mitochondrial isocitrate dehydrogenase complex (NAD+); IPI:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; TAS:ProtInc.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:Ensembl.
DR GO; GO:0006102; P:isocitrate metabolic process; IBA:GO_Central.
DR GO; GO:0006734; P:NADH metabolic process; IEA:Ensembl.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:ComplexPortal.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004434; Isocitrate_DH_NAD.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Disease variant;
KW Mitochondrion; Reference proteome; Retinitis pigmentosa; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 35..385
FT /note="Isocitrate dehydrogenase [NAD] subunit beta,
FT mitochondrial"
FT /id="PRO_0000014444"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..177
FT /note="MAALSGVRWLTRALVSAGNPGAWRGLSTSAAAHAASRSQAEDVRVEGSFPVT
FT MLPGDGVGPELMHAVKEVFKAAAVPVEFQEHHLSEVQNMASEEKLEQVLSSMKENKVAI
FT IGKIHTPMEYKGELASYDMRLRRKLDLFANVVHVKSLPGYMTRHNNLDLVIIREQTEGE
FT YSSLEHE -> MKMGERWSSLFPFPVSPSCCFLLTQ (in isoform C)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041335"
FT VAR_SEQ 361..385
FT /note="RDMGGYSTTTDFIKSVIGHLQTKGS -> SDMGGYATCHDFTEAVIAALPHP
FT (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10601238"
FT /id="VSP_002462"
FT VARIANT 3
FT /note="A -> V (in dbSNP:rs3178817)"
FT /evidence="ECO:0000269|PubMed:10601238"
FT /id="VAR_022660"
FT VARIANT 132
FT /note="L -> P (in RP46; dbSNP:rs137853020)"
FT /evidence="ECO:0000269|PubMed:18806796"
FT /id="VAR_054851"
FT VARIANT 166
FT /note="Q -> H (in dbSNP:rs11542741)"
FT /id="VAR_049781"
FT VARIANT 360
FT /note="T -> A (in dbSNP:rs8296)"
FT /id="VAR_056005"
FT CONFLICT 127..130
FT /note="SYDM -> RTLV (in Ref. 6; CAB43266)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="I -> V (in Ref. 2; BAA91971)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="S -> SNL (in Ref. 1; AAD09340)"
FT /evidence="ECO:0000305"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6KDE"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:6KDE"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:6KDE"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:6KDY"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:6KDE"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:6KDE"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6KDY"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:6KDY"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:6KDE"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:6KDE"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6KDE"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:6KDE"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6KDE"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:6KDF"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:6KDE"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:6KDE"
FT HELIX 191..207
FT /evidence="ECO:0007829|PDB:6KDE"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:6KDE"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:6KDE"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:6KDE"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:6KDE"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:6KDE"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:6KDE"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:6KDE"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:6KDE"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:6KDE"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:6KDE"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:6KDE"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:6KDY"
FT HELIX 323..335
FT /evidence="ECO:0007829|PDB:6KDE"
FT HELIX 339..355
FT /evidence="ECO:0007829|PDB:6KDE"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:6KDE"
FT HELIX 369..374
FT /evidence="ECO:0007829|PDB:6KDE"
SQ SEQUENCE 385 AA; 42184 MW; 7324E6CC30A68EE2 CRC64;
MAALSGVRWL TRALVSAGNP GAWRGLSTSA AAHAASRSQA EDVRVEGSFP VTMLPGDGVG
PELMHAVKEV FKAAAVPVEF QEHHLSEVQN MASEEKLEQV LSSMKENKVA IIGKIHTPME
YKGELASYDM RLRRKLDLFA NVVHVKSLPG YMTRHNNLDL VIIREQTEGE YSSLEHESAR
GVIECLKIVT RAKSQRIAKF AFDYATKKGR GKVTAVHKAN IMKLGDGLFL QCCEEVAELY
PKIKFETMII DNCCMQLVQN PYQFDVLVMP NLYGNIIDNL AAGLVGGAGV VPGESYSAEY
AVFETGARHP FAQAVGRNIA NPTAMLLSAS NMLRHLNLEY HSSMIADAVK KVIKVGKVRT
RDMGGYSTTT DFIKSVIGHL QTKGS
