ID   NDUB3_HUMAN             Reviewed;          98 AA.
AC   O43676; Q6IB80;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 195.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3;
DE   AltName: Full=Complex I-B12;
DE            Short=CI-B12;
DE   AltName: Full=NADH-ubiquinone oxidoreductase B12 subunit;
GN   Name=NDUFB3;
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 [MRNA].
RX   PubMed=9878551; DOI=10.1006/bbrc.1998.9786;
RA   Loeffen J.L.C.M., Triepels R.H., van den Heuvel L.P., Schuelke M.,
RA   Buskens C.A.F., Smeets R.J.P., Trijbels J.M.F., Smeitink J.A.M.;
RT   "cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase:
RT   human complex I cDNA characterization completed.";
RL   Biochem. Biophys. Res. Commun. 253:415-422(1998).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [7]
RP   IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX,
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
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   [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   INVOLVEMENT IN MC1DN25, AND VARIANTS MC1DN25 ARG-22 AND 70-GLY--HIS-98 DEL.
RX   PubMed=22499348; DOI=10.1136/jmedgenet-2012-100846;
RA   Haack T.B., Haberberger B., Frisch E.M., Wieland T., Iuso A., Gorza M.,
RA   Strecker V., Graf E., Mayr J.A., Herberg U., Hennermann J.B., Klopstock T.,
RA   Kuhn K.A., Ahting U., Sperl W., Wilichowski E., Hoffmann G.F., Tesarova M.,
RA   Hansikova H., Zeman J., Plecko B., Zeviani M., Wittig I., Strom T.M.,
RA   Schuelke M., Freisinger P., Meitinger T., Prokisch H.;
RT   "Molecular diagnosis in mitochondrial complex I deficiency using exome
RT   sequencing.";
RL   J. Med. Genet. 49:277-283(2012).
RN   [10]
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   [11]
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   [12]
RP   METHYLATION AT HIS-5; HIS-7 AND HIS-9, AND MUTAGENESIS OF 5-HIS--HIS-9.
RX   PubMed=33563959; DOI=10.1038/s41467-020-20670-7;
RA   Davydova E., Shimazu T., Schuhmacher M.K., Jakobsson M.E.,
RA   Willemen H.L.D.M., Liu T., Moen A., Ho A.Y.Y., Malecki J., Schroer L.,
RA   Pinto R., Suzuki T., Groensberg I.A., Sohtome Y., Akakabe M., Weirich S.,
RA   Kikuchi M., Olsen J.V., Dohmae N., Umehara T., Sodeoka M., Siino V.,
RA   McDonough M.A., Eijkelkamp N., Schofield C.J., Jeltsch A., Shinkai Y.,
RA   Falnes P.O.;
RT   "The methyltransferase METTL9 mediates pervasive 1-methylhistidine
RT   modification in mammalian proteomes.";
RL   Nat. Commun. 12:891-891(2021).
RN   [13]
RP   VARIANT MC1DN25 ARG-22.
RX   PubMed=27091925; DOI=10.1136/jmedgenet-2015-103576;
RA   Alston C.L., Howard C., Olahova M., Hardy S.A., He L., Murray P.G.,
RA   O'Sullivan S., Doherty G., Shield J.P., Hargreaves I.P., Monavari A.A.,
RA   Knerr I., McCarthy P., Morris A.A., Thorburn D.R., Prokisch H.,
RA   Clayton P.E., McFarland R., Hughes J., Crushell E., Taylor R.W.;
RT   "A recurrent mitochondrial p.Trp22Arg NDUFB3 variant causes a distinctive
RT   facial appearance, short stature and a mild biochemical and clinical
RT   phenotype.";
RL   J. Med. Genet. 53:634-641(2016).
CC   -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC       chain NADH dehydrogenase (Complex I), that is believed not to be
CC       involved in catalysis. 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   -!- SUBUNIT: 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}; Single-pass membrane protein
CC       {ECO:0000305}; Matrix side {ECO:0000305}.
CC   -!- PTM: Methylation at His residues by METTL9 enhances complex I-mediated
CC       mitochondrial respiration. {ECO:0000269|PubMed:33563959}.
CC   -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 25 (MC1DN25)
CC       [MIM:618246]: 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. MC1DN25 transmission pattern is consistent with
CC       autosomal recessive inheritance. {ECO:0000269|PubMed:22499348,
CC       ECO:0000269|PubMed:27091925}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the complex I NDUFB3 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AF047183; AAC04268.1; -; mRNA.
DR   EMBL; AF035839; AAC15590.1; -; mRNA.
DR   EMBL; CR456924; CAG33205.1; -; mRNA.
DR   EMBL; AC007272; AAX88972.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70233.1; -; Genomic_DNA.
DR   EMBL; BC018183; AAH18183.1; -; mRNA.
DR   CCDS; CCDS2336.1; -.
DR   PIR; JC5822; JC5822.
DR   RefSeq; NP_001244031.1; NM_001257102.2.
DR   RefSeq; NP_002482.1; NM_002491.3.
DR   RefSeq; XP_011509532.1; XM_011511230.4.
DR   RefSeq; XP_047300444.1; XM_047444488.1.
DR   RefSeq; XP_054198228.1; XM_054342253.1.
DR   RefSeq; XP_054198229.1; XM_054342254.1.
DR   PDB; 5XTC; EM; 3.70 A; Z=10-89.
DR   PDB; 5XTD; EM; 3.70 A; Z=10-89.
DR   PDB; 5XTH; EM; 3.90 A; Z=10-89.
DR   PDB; 5XTI; EM; 17.40 A; BZ/Z=10-89.
DR   PDB; 9CWT; EM; 3.44 A; Z=1-98.
DR   PDB; 9I4I; EM; 2.63 A; Z=1-98.
DR   PDB; 9TI4; EM; 2.66 A; Z=10-92.
DR   AlphaFoldDB; O43676; -.
DR   EMDB; EMD-45974; -.
DR   EMDB; EMD-52619; -.
DR   SMR; O43676; -.
DR   BioGRID; 110789; 118.
DR   ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR   CORUM; O43676; -.
DR   FunCoup; O43676; 562.
DR   IntAct; O43676; 101.
DR   MINT; O43676; -.
DR   NDEx; IQUERY-CP-NDUFB3; 3 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000407336; -.
DR   BindingDB; O43676; -.
DR   ChEMBL; CHEMBL2363065; -.
DR   DrugBank; DB00157; NADH.
DR   DrugCentral; O43676; -.
DR   iPTMnet; O43676; -.
DR   PhosphoSitePlus; O43676; -.
DR   BioMuta; NDUFB3; -.
DR   jPOST; O43676; -.
DR   MassIVE; O43676; -.
DR   PaxDb; 9606-ENSP00000407336; -.
DR   PeptideAtlas; O43676; -.
DR   ProteomicsDB; 49104; -.
DR   Pumba; O43676; -.
DR   TopDownProteomics; O43676; -.
DR   Antibodypedia; 34135; 137 antibodies from 28 providers.
DR   DNASU; 4709; -.
DR   Ensembl; ENST00000237889.9; ENSP00000237889.4; ENSG00000119013.11.
DR   Ensembl; ENST00000433898.5; ENSP00000410600.1; ENSG00000119013.11.
DR   Ensembl; ENST00000450023.6; ENSP00000401834.2; ENSG00000119013.11.
DR   Ensembl; ENST00000454214.1; ENSP00000407336.1; ENSG00000119013.11.
DR   Ensembl; ENST00000682325.1; ENSP00000507925.1; ENSG00000119013.11.
DR   Ensembl; ENST00000684175.1; ENSP00000508132.1; ENSG00000119013.11.
DR   Ensembl; ENST00000684420.1; ENSP00000508208.1; ENSG00000119013.11.
DR   Ensembl; ENST00000878930.1; ENSP00000548989.1; ENSG00000119013.11.
DR   Ensembl; ENST00000878931.1; ENSP00000548990.1; ENSG00000119013.11.
DR   Ensembl; ENST00000878932.1; ENSP00000548991.1; ENSG00000119013.11.
DR   Ensembl; ENST00000928296.1; ENSP00000598355.1; ENSG00000119013.11.
DR   Ensembl; ENST00000928297.1; ENSP00000598356.1; ENSG00000119013.11.
DR   Ensembl; ENST00000928298.1; ENSP00000598357.1; ENSG00000119013.11.
DR   Ensembl; ENST00000928299.1; ENSP00000598358.1; ENSG00000119013.11.
DR   Ensembl; ENST00000928300.1; ENSP00000598359.1; ENSG00000119013.11.
DR   Ensembl; ENST00000928301.1; ENSP00000598360.1; ENSG00000119013.11.
DR   Ensembl; ENST00000928302.1; ENSP00000598361.1; ENSG00000119013.11.
DR   Ensembl; ENST00000928303.1; ENSP00000598362.1; ENSG00000119013.11.
DR   Ensembl; ENST00000928304.1; ENSP00000598363.1; ENSG00000119013.11.
DR   Ensembl; ENST00000953983.1; ENSP00000624042.1; ENSG00000119013.11.
DR   Ensembl; ENST00000953984.1; ENSP00000624043.1; ENSG00000119013.11.
DR   GeneID; 4709; -.
DR   KEGG; hsa:4709; -.
DR   MANE-Select; ENST00000237889.9; ENSP00000237889.4; NM_002491.3; NP_002482.1.
DR   UCSC; uc002uwx.6; human.
DR   AGR; HGNC:7698; -.
DR   ClinPGx; PA31504; -.
DR   CTD; 4709; -.
DR   DisGeNET; 4709; -.
DR   GeneCards; NDUFB3; -.
DR   HGNC; HGNC:7698; NDUFB3.
DR   HPA; ENSG00000119013; Tissue enhanced (skeletal muscle, tongue).
DR   MalaCards; NDUFB3; -.
DR   MIM; 603839; gene.
DR   MIM; 618246; phenotype.
DR   OpenTargets; ENSG00000119013; -.
DR   Orphanet; 2609; Isolated complex I deficiency.
DR   VEuPathDB; HostDB:ENSG00000119013; -.
DR   eggNOG; KOG4631; Eukaryota.
DR   GeneTree; ENSGT00390000010316; -.
DR   HOGENOM; CLU_160226_1_0_1; -.
DR   InParanoid; O43676; -.
DR   OMA; YMGGFAH; -.
DR   OrthoDB; 521512at2759; -.
DR   PAN-GO; O43676; 1 GO annotation based on evolutionary models.
DR   PhylomeDB; O43676; -.
DR   BioCyc; MetaCyc:HS04271-MONOMER; -.
DR   PathwayCommons; O43676; -.
DR   Reactome; R-HSA-611105; Respiratory electron transport.
DR   Reactome; R-HSA-6799198; Complex I biogenesis.
DR   SignaLink; O43676; -.
DR   SIGNOR; O43676; -.
DR   Agora; ENSG00000119013; -.
DR   BioGRID-ORCS; 4709; 436 hits in 1068 CRISPR screens.
DR   ChiTaRS; NDUFB3; human.
DR   GenomeRNAi; 4709; -.
DR   Pharos; O43676; Tclin.
DR   PRO; PR:O43676; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; O43676; protein.
DR   Bgee; ENSG00000119013; Expressed in right atrium auricular region and 207 other cell types or tissues.
DR   ExpressionAtlas; O43676; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR   GO; GO:0005739; C:mitochondrion; HTP:FlyBase.
DR   GO; GO:0045271; C:respiratory chain complex I; IDA:UniProtKB.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; TAS:ProtInc.
DR   GO; GO:0009060; P:aerobic respiration; NAS:ComplexPortal.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; TAS:ProtInc.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; NAS:ComplexPortal.
DR   InterPro; IPR012576; NDUFB3.
DR   PANTHER; PTHR15082:SF2; NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT 3; 1.
DR   PANTHER; PTHR15082; NADH-UBIQUINONE OXIDOREDUCTASE B12 SUBUNIT; 1.
DR   Pfam; PF08122; NDUF_B12; 1.
DR   PDBsum; 5XTC; -.
DR   PDBsum; 5XTD; -.
DR   PDBsum; 5XTH; -.
DR   PDBsum; 5XTI; -.
DR   PDBsum; 9CWT; -.
DR   PDBsum; 9I4I; -.
DR   PDBsum; 9TI4; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Disease variant; Electron transport; Membrane;
KW   Methylation; Mitochondrion; Mitochondrion inner membrane;
KW   Primary mitochondrial disease; Proteomics identification;
KW   Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q02365"
FT   CHAIN           2..98
FT                   /note="NADH dehydrogenase [ubiquinone] 1 beta subcomplex
FT                   subunit 3"
FT                   /id="PRO_0000118797"
FT   TRANSMEM        66..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02365"
FT   MOD_RES         5
FT                   /note="Pros-methylhistidine"
FT                   /evidence="ECO:0000269|PubMed:33563959"
FT   MOD_RES         7
FT                   /note="Pros-methylhistidine"
FT                   /evidence="ECO:0000269|PubMed:33563959"
FT   MOD_RES         9
FT                   /note="Pros-methylhistidine"
FT                   /evidence="ECO:0000269|PubMed:33563959"
FT   MOD_RES         23
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQZ6"
FT   MOD_RES         23
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQZ6"
FT   MOD_RES         34
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQZ6"
FT   MOD_RES         34
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQZ6"
FT   VARIANT         22
FT                   /note="W -> R (in MC1DN25; dbSNP:rs142609245)"
FT                   /evidence="ECO:0000269|PubMed:22499348,
FT                   ECO:0000269|PubMed:27091925"
FT                   /id="VAR_078939"
FT   VARIANT         70..98
FT                   /note="Missing (in MC1DN25)"
FT                   /evidence="ECO:0000269|PubMed:22499348"
FT                   /id="VAR_078940"
FT   MUTAGEN         5..9
FT                   /note="HGHEH->RGHER: Abolished histidine methylation by
FT                   METTL9."
FT                   /evidence="ECO:0000269|PubMed:33563959"
FT   HELIX           16..18
FT                   /evidence="ECO:0007829|PDB:9CWT"
FT   STRAND          24..27
FT                   /evidence="ECO:0007829|PDB:9CWT"
FT   HELIX           29..38
FT                   /evidence="ECO:0007829|PDB:9CWT"
FT   HELIX           46..50
FT                   /evidence="ECO:0007829|PDB:9CWT"
FT   HELIX           55..57
FT                   /evidence="ECO:0007829|PDB:9CWT"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:9CWT"
FT   HELIX           63..67
FT                   /evidence="ECO:0007829|PDB:9CWT"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:9CWT"
FT   HELIX           71..80
FT                   /evidence="ECO:0007829|PDB:9CWT"
SQ   SEQUENCE   98 AA;  11402 MW;  1C77F0C7A4DC757F CRC64;
     MAHEHGHEHG HHKMELPDYR QWKIEGTPLE TIQKKLAAKG LRDPWGRNEA WRYMGGFAKS
     VSFSDVFFKG FKWGFAAFVV AVGAEYYLES LNKDKKHH
//