NDUA6_HUMAN
ID NDUA6_HUMAN Reviewed; 128 AA.
AC P56556; B2RE54; O43675; Q6FGW0; Q6IBT8; Q6IC39;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 4.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 {ECO:0000305};
DE AltName: Full=Complex I-B14;
DE Short=CI-B14;
DE AltName: Full=LYR motif-containing protein 6;
DE AltName: Full=NADH-ubiquinone oxidoreductase B14 subunit;
GN Name=NDUFA6 {ECO:0000312|HGNC:HGNC:7690}; Synonyms=LYRM6, NADHB14;
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].
RC TISSUE=Heart;
RX PubMed=9425316; DOI=10.1006/bbrc.1997.7707;
RA Ton C., Hwang D.M., Dempsey A.A., Liew C.-C.;
RT "Identification and primary structure of five human NADH-ubiquinone
RT oxidoreductase subunits.";
RL Biochem. Biophys. Res. Commun. 241:589-594(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-9.
RC TISSUE=Skeletal muscle;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [8]
RP IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12611891; DOI=10.1074/jbc.c300064200;
RA Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F.,
RA Ghosh S.S., Capaldi R.A.;
RT "The subunit composition of the human NADH dehydrogenase obtained by rapid
RT one-step immunopurification.";
RL J. Biol. Chem. 278:13619-13622(2003).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
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 [12]
RP FUNCTION, AND IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX.
RX PubMed=27626371; DOI=10.1038/nature19754;
RA Stroud D.A., Surgenor E.E., Formosa L.E., Reljic B., Frazier A.E.,
RA Dibley M.G., Osellame L.D., Stait T., Beilharz T.H., Thorburn D.R.,
RA Salim A., Ryan M.T.;
RT "Accessory subunits are integral for assembly and function of human
RT mitochondrial complex I.";
RL Nature 538:123-126(2016).
RN [13]
RP FUNCTION, INVOLVEMENT IN MC1DN33, AND VARIANTS MC1DN33 PRO-64 AND
RP 89-GLU--PRO-128 DEL.
RX PubMed=30245030; DOI=10.1016/j.ajhg.2018.08.013;
RA Alston C.L., Heidler J., Dibley M.G., Kremer L.S., Taylor L.S., Fratter C.,
RA French C.E., Glasgow R.I.C., Feichtinger R.G., Delon I., Pagnamenta A.T.,
RA Dolling H., Lemonde H., Aiton N., Bjoernstad A., Henneke L., Gaertner J.,
RA Thiele H., Tauchmannova K., Quaghebeur G., Houstek J., Sperl W.,
RA Raymond F.L., Prokisch H., Mayr J.A., McFarland R., Poulton J., Ryan M.T.,
RA Wittig I., Henneke M., Taylor R.W.;
RT "Bi-allelic mutations in NDUFA6 establish its role in early-onset isolated
RT mitochondrial complex I deficiency.";
RL Am. J. Hum. Genet. 103:592-601(2018).
CC -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC chain NADH dehydrogenase (Complex I), that is believed to be not
CC involved in catalysis. Required for proper complex I assembly
CC (PubMed:30245030). Complex I functions in the transfer of electrons
CC from NADH to the respiratory chain. The immediate electron acceptor for
CC the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371,
CC ECO:0000269|PubMed:30245030}.
CC -!- SUBUNIT: Mammalian complex I is composed of 45 different subunits.
CC {ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:27626371}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:12611891}; Peripheral membrane protein
CC {ECO:0000305}; Matrix side {ECO:0000305}.
CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 33 (MC1DN33)
CC [MIM:618253]: A form of mitochondrial complex I deficiency, the most
CC common biochemical signature of mitochondrial disorders, a group of
CC highly heterogeneous conditions characterized by defective oxidative
CC phosphorylation, which collectively affects 1 in 5-10000 live births.
CC Clinical disorders have variable severity, ranging from lethal neonatal
CC disease to adult-onset neurodegenerative disorders. Phenotypes include
CC macrocephaly with progressive leukodystrophy, non-specific
CC encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh
CC syndrome, Leber hereditary optic neuropathy, and some forms of
CC Parkinson disease. MC1DN33 transmission pattern is consistent with
CC autosomal recessive inheritance. {ECO:0000269|PubMed:30245030}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the complex I LYR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG30415.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF047182; AAC04267.1; -; mRNA.
DR EMBL; CR456529; CAG30415.1; ALT_INIT; mRNA.
DR EMBL; AK291874; BAF84563.1; -; mRNA.
DR EMBL; AK316562; BAG38151.1; -; mRNA.
DR EMBL; CR456714; CAG32995.1; -; mRNA.
DR EMBL; CR541997; CAG46794.1; -; mRNA.
DR EMBL; AL021878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60489.1; -; Genomic_DNA.
DR EMBL; BC002772; AAH02772.1; -; mRNA.
DR CCDS; CCDS33656.1; -.
DR PIR; JC5821; JC5821.
DR RefSeq; NP_002481.2; NM_002490.4.
DR PDB; 5XTB; EM; 3.40 A; E=16-128.
DR PDB; 5XTD; EM; 3.70 A; E=16-128.
DR PDB; 5XTH; EM; 3.90 A; E=16-128.
DR PDB; 5XTI; EM; 17.40 A; BE/E=16-128.
DR PDBsum; 5XTB; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; P56556; -.
DR SMR; P56556; -.
DR BioGRID; 110780; 145.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; P56556; -.
DR IntAct; P56556; 64.
DR MINT; P56556; -.
DR STRING; 9606.ENSP00000418842; -.
DR BindingDB; P56556; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; P56556; -.
DR iPTMnet; P56556; -.
DR PhosphoSitePlus; P56556; -.
DR BioMuta; NDUFA6; -.
DR DMDM; 298286909; -.
DR EPD; P56556; -.
DR jPOST; P56556; -.
DR MassIVE; P56556; -.
DR PaxDb; P56556; -.
DR PeptideAtlas; P56556; -.
DR PRIDE; P56556; -.
DR ProteomicsDB; 56926; -.
DR TopDownProteomics; P56556; -.
DR Antibodypedia; 45919; 119 antibodies from 22 providers.
DR DNASU; 4700; -.
DR Ensembl; ENST00000498737.8; ENSP00000418842.3; ENSG00000184983.11.
DR Ensembl; ENST00000605916.1; ENSP00000475402.1; ENSG00000272765.2.
DR Ensembl; ENST00000628740.2; ENSP00000486781.1; ENSG00000277365.3.
DR Ensembl; ENST00000630201.4; ENSP00000487431.2; ENSG00000281013.4.
DR Ensembl; ENST00000630971.2; ENSP00000487462.1; ENSG00000273397.4.
DR GeneID; 4700; -.
DR KEGG; hsa:4700; -.
DR MANE-Select; ENST00000498737.8; ENSP00000418842.3; NM_002490.6; NP_002481.3.
DR UCSC; uc003bcb.4; human.
DR CTD; 4700; -.
DR DisGeNET; 4700; -.
DR GeneCards; NDUFA6; -.
DR HGNC; HGNC:7690; NDUFA6.
DR HPA; ENSG00000184983; Low tissue specificity.
DR MalaCards; NDUFA6; -.
DR MIM; 602138; gene.
DR MIM; 618253; phenotype.
DR neXtProt; NX_P56556; -.
DR OpenTargets; ENSG00000184983; -.
DR Orphanet; 2609; Isolated complex I deficiency.
DR PharmGKB; PA31496; -.
DR VEuPathDB; HostDB:ENSG00000184983; -.
DR eggNOG; KOG3426; Eukaryota.
DR GeneTree; ENSGT00390000018898; -.
DR InParanoid; P56556; -.
DR OMA; MVINPTY; -.
DR OrthoDB; 1518948at2759; -.
DR PhylomeDB; P56556; -.
DR TreeFam; TF105625; -.
DR BioCyc; MetaCyc:HS00037-MON; -.
DR PathwayCommons; P56556; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; P56556; -.
DR SIGNOR; P56556; -.
DR BioGRID-ORCS; 4700; 298 hits in 1087 CRISPR screens.
DR ChiTaRS; NDUFA6; human.
DR GeneWiki; NDUFA6; -.
DR GenomeRNAi; 4700; -.
DR Pharos; P56556; Tclin.
DR PRO; PR:P56556; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P56556; protein.
DR Bgee; ENSG00000184983; Expressed in hindlimb stylopod muscle and 97 other tissues.
DR ExpressionAtlas; P56556; baseline and differential.
DR Genevisible; P56556; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; TAS:ProtInc.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; NAS:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR CDD; cd20266; Complex1_LYR_NDUFA6_LYRM6; 1.
DR InterPro; IPR008011; Complex1_LYR_dom.
DR InterPro; IPR045299; Complex1_LYR_NDUFA6_LYRM6.
DR InterPro; IPR016488; NADH_Ub_cplx-1_asu_su-6.
DR PANTHER; PTHR12964; PTHR12964; 1.
DR Pfam; PF05347; Complex1_LYR; 1.
DR PIRSF; PIRSF006643; NDUA6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein;
KW Primary mitochondrial disease; Reference proteome; Respiratory chain;
KW Transport.
FT CHAIN 1..128
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 6"
FT /id="PRO_0000174302"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 9
FT /note="A -> V (in dbSNP:rs1801311)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_014483"
FT VARIANT 64
FT /note="R -> P (in MC1DN33)"
FT /evidence="ECO:0000269|PubMed:30245030"
FT /id="VAR_081470"
FT VARIANT 89..128
FT /note="Missing (in MC1DN33)"
FT /evidence="ECO:0000269|PubMed:30245030"
FT /id="VAR_081471"
FT CONFLICT 6
FT /note="V -> F (in Ref. 4; CAG32995)"
FT /evidence="ECO:0000305"
FT HELIX 25..40
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:5XTB"
FT TURN 67..72
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 76..94
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:5XTB"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:5XTB"
SQ SEQUENCE 128 AA; 15137 MW; 5EE10C571A659D8B CRC64;
MAGSGVRQAT STASTFVKPI FSRDMNEAKR RVRELYRAWY REVPNTVHQF QLDITVKMGR
DKVREMFMKN AHVTDPRVVD LLVIKGKIEL EETIKVWKQR THVMRFFHET EAPRPKDFLS
KFYVGHDP
