ID   NDUA9_HUMAN             Reviewed;         377 AA.
AC   Q16795; Q14076; Q2NKX0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial;
DE   AltName: Full=Complex I-39kD;
DE            Short=CI-39kD;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 39 kDa subunit;
DE   Flags: Precursor;
GN   Name=NDUFA9; Synonyms=NDUFS2L;
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].
RA   Loeffen J.L.C.M., Smeets R.J.P., Triepels R., Ruitenbeek W.,
RA   Smeitink J.A.M., van den Heuvel L.;
RT   "39 kDa subunit of NADH-ubiquinone oxidoreductase.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon, Muscle, and Skeletal muscle;
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RC   TISSUE=Blood;
RX   PubMed=8012384; DOI=10.1038/ng0394-236;
RA   Cross S.H., Charlton J.A., Nan X., Bird A.P.;
RT   "Purification of CpG islands using a methylated DNA binding column.";
RL   Nat. Genet. 6:236-244(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-377.
RC   TISSUE=Liver;
RX   PubMed=8486360; DOI=10.1006/geno.1993.1161;
RA   Baens M., Chaffanet M., Cassiman J.-J., van den Berghe H., Marynen P.;
RT   "Construction and evaluation of a hncDNA library of human 12p transcribed
RT   sequences derived from a somatic cell hybrid.";
RL   Genomics 16:214-218(1993).
RN   [5]
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   [6]
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   [7]
RP   INTERACTION WITH BLOC1S1, AND ACETYLATION.
RX   PubMed=22309213; DOI=10.1042/bj20120118;
RA   Scott I., Webster B.R., Li J.H., Sack M.N.;
RT   "Identification of a molecular component of the mitochondrial acetyl
RT   transferase program; a novel role for GCN5L1.";
RL   Biochem. J. 443:655-661(2012).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
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   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   [11]
RP   INVOLVEMENT IN MC1DN26, VARIANT MC1DN26 PRO-321, AND FUNCTION.
RX   PubMed=22114105; DOI=10.1136/jmedgenet-2011-100466;
RA   van den Bosch B.J., Gerards M., Sluiter W., Stegmann A.P., Jongen E.L.,
RA   Hellebrekers D.M., Oegema R., Lambrichs E.H., Prokisch H., Danhauser K.,
RA   Schoonderwoerd K., de Coo I.F., Smeets H.J.;
RT   "Defective NDUFA9 as a novel cause of neonatally fatal complex I disease.";
RL   J. Med. Genet. 49:10-15(2012).
RN   [12]
RP   ACETYLATION, AND INTERACTION WITH CLOCK.
RX   PubMed=28985504; DOI=10.1016/j.molcel.2017.09.008;
RA   Lin R., Mo Y., Zha H., Qu Z., Xie P., Zhu Z.J., Xu Y., Xiong Y., Guan K.L.;
RT   "CLOCK acetylates ASS1 to drive circadian rhythm of ureagenesis.";
RL   Mol. Cell 68:198-209(2017).
RN   [13]
RP   FUNCTION, INVOLVEMENT IN MC1DN26, VARIANTS MC1DN26 PRO-321 AND CYS-360, AND
RP   CHARACTERIZATION OF VARIANTS MC1DN26 PRO-321 AND CYS-360.
RX   PubMed=28671271; DOI=10.1111/cge.13089;
RA   Baertling F., Sanchez-Caballero L., van den Brand M.A.M., Fung C.W.,
RA   Chan S.H., Wong V.C., Hellebrekers D.M.E., de Coo I.F.M., Smeitink J.A.M.,
RA   Rodenburg R.J.T., Nijtmans L.G.J.;
RT   "NDUFA9 point mutations cause a variable mitochondrial complex I assembly
RT   defect.";
RL   Clin. Genet. 93:111-118(2018).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RAB5IF.
RX   PubMed=31536960; DOI=10.1016/j.isci.2019.08.057;
RA   Moutaoufik M.T., Malty R., Amin S., Zhang Q., Phanse S., Gagarinova A.,
RA   Zilocchi M., Hoell L., Minic Z., Gagarinova M., Aoki H., Stockwell J.,
RA   Jessulat M., Goebels F., Broderick K., Scott N.E., Vlasblom J., Musso G.,
RA   Prasad B., Lamantea E., Garavaglia B., Rajput A., Murayama K., Okazaki Y.,
RA   Foster L.J., Bader G.D., Cayabyab F.S., Babu M.;
RT   "Rewiring of the Human Mitochondrial Interactome during Neuronal
RT   Reprogramming Reveals Regulators of the Respirasome and Neurogenesis.";
RL   IScience 19:1114-1132(2019).
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. Required for proper complex I assembly
CC       (PubMed:28671271). 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:22114105,
CC       ECO:0000269|PubMed:27626371, ECO:0000269|PubMed:28671271}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC       Note=Binds 1 FAD per subunit.;
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits. This a
CC       component of the hydrophobic protein fraction (PubMed:12611891,
CC       PubMed:27626371). Interacts with BLOC1S1 (PubMed:22309213). Interacts
CC       with SLC2A4 (By similarity). Interacts with CLOCK (PubMed:28985504).
CC       Interacts with RAB5IF (PubMed:31536960). {ECO:0000250|UniProtKB:Q5BK63,
CC       ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:22309213,
CC       ECO:0000269|PubMed:27626371, ECO:0000269|PubMed:28985504,
CC       ECO:0000269|PubMed:31536960}.
CC   -!- INTERACTION:
CC       Q16795; P78537: BLOC1S1; NbExp=3; IntAct=EBI-1045087, EBI-348630;
CC       Q16795; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1045087, EBI-3867333;
CC       Q16795; P42858: HTT; NbExp=7; IntAct=EBI-1045087, EBI-466029;
CC       Q16795; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-1045087, EBI-11962084;
CC       Q16795; Q8NC60: NOA1; NbExp=2; IntAct=EBI-1045087, EBI-717871;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000305|PubMed:12611891}.
CC   -!- PTM: Acetylated on lysine residues. BLOC1S1 is required for acetylation
CC       (PubMed:22309213). Acetylated by CLOCK in a circadian manner
CC       (PubMed:28985504). {ECO:0000269|PubMed:22309213,
CC       ECO:0000269|PubMed:28985504}.
CC   -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 26 (MC1DN26)
CC       [MIM:618247]: 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. MC1DN26 transmission pattern is consistent with
CC       autosomal recessive inheritance. {ECO:0000269|PubMed:22114105,
CC       ECO:0000269|PubMed:28671271}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the complex I NDUFA9 subunit family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA54099.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF050641; AAD42055.1; -; mRNA.
DR   EMBL; BC009311; AAH09311.1; -; mRNA.
DR   EMBL; BC015837; AAH15837.1; -; mRNA.
DR   EMBL; BC111546; AAI11547.1; -; mRNA.
DR   EMBL; X76665; CAA54099.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; L04490; AAA36350.1; -; mRNA.
DR   CCDS; CCDS8532.1; -.
DR   PIR; I37258; I37258.
DR   RefSeq; NP_004993.1; NM_005002.4.
DR   PDB; 5XTB; EM; 3.40 A; J=40-376.
DR   PDB; 5XTD; EM; 3.70 A; J=40-376.
DR   PDB; 5XTH; EM; 3.90 A; J=40-376.
DR   PDB; 5XTI; EM; 17.40 A; BJ/J=40-376.
DR   PDBsum; 5XTB; -.
DR   PDBsum; 5XTD; -.
DR   PDBsum; 5XTH; -.
DR   PDBsum; 5XTI; -.
DR   AlphaFoldDB; Q16795; -.
DR   SMR; Q16795; -.
DR   BioGRID; 110784; 337.
DR   ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR   CORUM; Q16795; -.
DR   DIP; DIP-38526N; -.
DR   IntAct; Q16795; 95.
DR   MINT; Q16795; -.
DR   STRING; 9606.ENSP00000266544; -.
DR   BindingDB; Q16795; -.
DR   ChEMBL; CHEMBL2363065; -.
DR   DrugBank; DB03147; Flavin adenine dinucleotide.
DR   DrugBank; DB00157; NADH.
DR   DrugCentral; Q16795; -.
DR   CarbonylDB; Q16795; -.
DR   GlyGen; Q16795; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q16795; -.
DR   PhosphoSitePlus; Q16795; -.
DR   SwissPalm; Q16795; -.
DR   BioMuta; NDUFA9; -.
DR   DMDM; 2833280; -.
DR   EPD; Q16795; -.
DR   jPOST; Q16795; -.
DR   MassIVE; Q16795; -.
DR   MaxQB; Q16795; -.
DR   PaxDb; 9606-ENSP00000266544; -.
DR   PeptideAtlas; Q16795; -.
DR   ProteomicsDB; 61072; -.
DR   Pumba; Q16795; -.
DR   TopDownProteomics; Q16795; -.
DR   Antibodypedia; 22301; 308 antibodies from 29 providers.
DR   DNASU; 4704; -.
DR   Ensembl; ENST00000266544.10; ENSP00000266544.5; ENSG00000139180.11.
DR   GeneID; 4704; -.
DR   KEGG; hsa:4704; -.
DR   MANE-Select; ENST00000266544.10; ENSP00000266544.5; NM_005002.5; NP_004993.1.
DR   UCSC; uc001qnc.4; human.
DR   AGR; HGNC:7693; -.
DR   CTD; 4704; -.
DR   DisGeNET; 4704; -.
DR   GeneCards; NDUFA9; -.
DR   HGNC; HGNC:7693; NDUFA9.
DR   HPA; ENSG00000139180; Low tissue specificity.
DR   MalaCards; NDUFA9; -.
DR   MIM; 603834; gene.
DR   MIM; 618247; phenotype.
DR   neXtProt; NX_Q16795; -.
DR   OpenTargets; ENSG00000139180; -.
DR   PharmGKB; PA31499; -.
DR   VEuPathDB; HostDB:ENSG00000139180; -.
DR   eggNOG; KOG2865; Eukaryota.
DR   GeneTree; ENSGT00390000006865; -.
DR   HOGENOM; CLU_007383_6_4_1; -.
DR   InParanoid; Q16795; -.
DR   OMA; EDQFFNR; -.
DR   OrthoDB; 141210at2759; -.
DR   PhylomeDB; Q16795; -.
DR   TreeFam; TF105961; -.
DR   BioCyc; MetaCyc:HS06589-MONOMER; -.
DR   PathwayCommons; Q16795; -.
DR   Reactome; R-HSA-611105; Respiratory electron transport.
DR   Reactome; R-HSA-6799198; Complex I biogenesis.
DR   SignaLink; Q16795; -.
DR   SIGNOR; Q16795; -.
DR   BioGRID-ORCS; 4704; 185 hits in 1172 CRISPR screens.
DR   ChiTaRS; NDUFA9; human.
DR   GeneWiki; NDUFA9; -.
DR   GenomeRNAi; 4704; -.
DR   Pharos; Q16795; Tclin.
DR   PRO; PR:Q16795; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q16795; Protein.
DR   Bgee; ENSG00000139180; Expressed in apex of heart and 205 other cell types or tissues.
DR   ExpressionAtlas; Q16795; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR   GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; NAS:UniProtKB.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IMP:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR   GO; GO:0009060; P:aerobic respiration; NAS:ComplexPortal.
DR   GO; GO:0007623; P:circadian rhythm; IDA:UniProtKB.
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; NAS:ComplexPortal.
DR   GO; GO:0006814; P:sodium ion transport; NAS:UniProtKB.
DR   GO; GO:1901006; P:ubiquinone-6 biosynthetic process; IBA:GO_Central.
DR   CDD; cd05271; NDUFA9_like_SDR_a; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR12126:SF10; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 9, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12126; NADH-UBIQUINONE OXIDOREDUCTASE 39 KDA SUBUNIT-RELATED; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   Genevisible; Q16795; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Disease variant; Electron transport; FAD;
KW   Flavoprotein; Mitochondrion; Primary mitochondrial disease;
KW   Reference proteome; Respiratory chain; Transit peptide; Transport.
FT   TRANSIT         1..35
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           36..377
FT                   /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT                   subunit 9, mitochondrial"
FT                   /id="PRO_0000019992"
FT   MOD_RES         175
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DC69"
FT   MOD_RES         189
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DC69"
FT   MOD_RES         370
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DC69"
FT   VARIANT         321
FT                   /note="R -> P (in MC1DN26; loss of function in complex I
FT                   assembly; accumulation of several low and high molecular
FT                   weight assembly intermediates is observed in patient
FT                   fibroblasts; dbSNP:rs199592341)"
FT                   /evidence="ECO:0000269|PubMed:22114105,
FT                   ECO:0000269|PubMed:28671271"
FT                   /id="VAR_078936"
FT   VARIANT         360
FT                   /note="R -> C (in MC1DN26; loss of function in complex I
FT                   assembly; accumulation of several low and high molecular
FT                   weight assembly intermediates is observed in patient
FT                   fibroblasts; dbSNP:rs3210083)"
FT                   /evidence="ECO:0000269|PubMed:28671271"
FT                   /id="VAR_081457"
FT   STRAND          43..51
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   TURN            59..62
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           64..75
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          79..84
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           89..97
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           100..102
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          103..107
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           114..119
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   TURN            120..122
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           141..144
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           147..159
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          162..167
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           179..194
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           212..223
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          225..229
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   TURN            230..233
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           242..254
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           273..284
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          290..293
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           295..305
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           316..323
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           335..337
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           345..347
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           349..353
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   TURN            354..356
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           359..362
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           367..369
FT                   /evidence="ECO:0007829|PDB:5XTB"
SQ   SEQUENCE   377 AA;  42510 MW;  66A1CC7FCE86DD0E CRC64;
     MAAAAQSRVV RVLSMSRSAI TAIATSVCHG PPCRQLHHAL MPHGKGGRSS VSGIVATVFG
     ATGFLGRYVV NHLGRMGSQV IIPYRCDKYD IMHLRPMGDL GQLLFLEWDA RDKDSIRRVV
     QHSNVVINLI GRDWETKNFD FEDVFVKIPQ AIAQLSKEAG VEKFIHVSHL NANIKSSSRY
     LRNKAVGEKV VRDAFPEAII VKPSDIFGRE DRFLNSFASM HRFGPIPLGS LGWKTVKQPV
     YVVDVSKGIV NAVKDPDANG KSFAFVGPSR YLLFHLVKYI FAVAHRLFLP FPLPLFAYRW
     VARVFEISPF EPWITRDKVE RMHITDMKLP HLPGLEDLGI QATPLELKAI EVLRRHRTYR
     WLSAEIEDVK PAKTVNI
//