NDC1_ARATH
ID NDC1_ARATH Reviewed; 519 AA.
AC Q8GXR9; F4KCG9; Q6KC19; Q93ZN8; Q9C5A3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Alternative NAD(P)H-ubiquinone oxidoreductase C1, chloroplastic/mitochondrial {ECO:0000303|PubMed:15333756};
DE EC=1.6.5.9 {ECO:0000269|PubMed:21844348};
DE AltName: Full=Alternative NADH dehydrogenase NDC1 {ECO:0000303|PubMed:15333756};
DE AltName: Full=Demethylphylloquinone reductase NDC1 {ECO:0000303|PubMed:26023160};
DE EC=1.6.5.12 {ECO:0000269|PubMed:21844348, ECO:0000269|PubMed:26023160};
DE AltName: Full=NADH:ubiquinone reductase (non-electrogenic) NDC1 {ECO:0000303|PubMed:12972666};
DE Flags: Precursor;
GN Name=NDC1 {ECO:0000303|PubMed:15333756};
GN OrderedLocusNames=At5g08740 {ECO:0000312|Araport:AT5G08740};
GN ORFNames=T2K12.12 {ECO:0000312|EMBL:CAC35879.1}, T2K12_90;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 440-519 (ISOFORM 1), AND INDUCTION BY
RP LIGHT.
RX PubMed=15333756; DOI=10.1104/pp.104.046698;
RA Escobar M.A., Franklin K.A., Svensson A.S., Salter M.G., Whitelam G.C.,
RA Rasmusson A.G.;
RT "Light regulation of the Arabidopsis respiratory chain. Multiple discrete
RT photoreceptor responses contribute to induction of type II NAD(P)H
RT dehydrogenase genes.";
RL Plant Physiol. 136:2710-2721(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND ALTERNATIVE
RP SPLICING.
RX PubMed=12972666; DOI=10.1104/pp.103.024208;
RA Michalecka A.M., Svensson A.S., Johansson F.I., Agius S.C., Johanson U.,
RA Brennicke A., Binder S., Rasmusson A.G.;
RT "Arabidopsis genes encoding mitochondrial type II NAD(P)H dehydrogenases
RT have different evolutionary origin and show distinct responses to light.";
RL Plant Physiol. 133:642-652(2003).
RN [7]
RP REVIEW.
RX PubMed=15725055; DOI=10.1146/annurev.arplant.55.031903.141720;
RA Rasmusson A.G., Soole K.L., Elthon T.E.;
RT "Alternative NAD(P)H dehydrogenases of plant mitochondria.";
RL Annu. Rev. Plant Biol. 55:23-39(2004).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16258072; DOI=10.1093/pcp/pci221;
RA Elhafez D., Murcha M.W., Clifton R., Soole K.L., Day D.A., Whelan J.;
RT "Characterization of mitochondrial alternative NAD(P)H dehydrogenases in
RT Arabidopsis: intraorganelle location and expression.";
RL Plant Cell Physiol. 47:43-54(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=16461379; DOI=10.1104/pp.105.076083;
RA Ytterberg A.J., Peltier J.-B., van Wijk K.J.;
RT "Protein profiling of plastoglobules in chloroplasts and chromoplasts. A
RT surprising site for differential accumulation of metabolic enzymes.";
RL Plant Physiol. 140:984-997(2006).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=18703057; DOI=10.1016/j.febslet.2008.07.061;
RA Carrie C., Murcha M.W., Kuehn K., Duncan O., Barthet M., Smith P.M.,
RA Eubel H., Meyer E., Day D.A., Millar A.H., Whelan J.;
RT "Type II NAD(P)H dehydrogenases are targeted to mitochondria and
RT chloroplasts or peroxisomes in Arabidopsis thaliana.";
RL FEBS Lett. 582:3073-3079(2008).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INDUCTION BY LIGHT,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21844348; DOI=10.1073/pnas.1104790108;
RA Eugeni Piller L., Besagni C., Ksas B., Rumeau D., Brehelin C., Glauser G.,
RA Kessler F., Havaux M.;
RT "Chloroplast lipid droplet type II NAD(P)H quinone oxidoreductase is
RT essential for prenylquinone metabolism and vitamin K1 accumulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:14354-14359(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=22274653; DOI=10.1104/pp.111.193144;
RA Lundquist P.K., Poliakov A., Bhuiyan N.H., Zybailov B., Sun Q.,
RA van Wijk K.J.;
RT "The functional network of the Arabidopsis plastoglobule proteome based on
RT quantitative proteomics and genome-wide coexpression analysis.";
RL Plant Physiol. 158:1172-1192(2012).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=23841539; DOI=10.1186/1471-2229-13-100;
RA Xu L., Law S.R., Murcha M.W., Whelan J., Carrie C.;
RT "The dual targeting ability of type II NAD(P)H dehydrogenases arose early
RT in land plant evolution.";
RL BMC Plant Biol. 13:100-100(2013).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Col-2;
RX PubMed=25018761; DOI=10.3389/fpls.2014.00298;
RA Eugeni Piller L., Glauser G., Kessler F., Besagni C.;
RT "Role of plastoglobules in metabolite repair in the tocopherol redox
RT cycle.";
RL Front. Plant Sci. 5:298-298(2014).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26023160; DOI=10.1105/tpc.15.00103;
RA Fatihi A., Latimer S., Schmollinger S., Block A., Dussault P.H.,
RA Vermaas W.F., Merchant S.S., Basset G.J.;
RT "A dedicated type II NADPH dehydrogenase performs the penultimate step in
RT the biosynthesis of vitamin K1 in Synechocystis and Arabidopsis.";
RL Plant Cell 27:1730-1741(2015).
CC -!- FUNCTION: Bifunctional oxidoreductase ables to act both on prenyl
CC naphthoquinones and on prenyl benzoquinones (PubMed:21844348,
CC PubMed:26023160). May serve a respiratory function (PubMed:12972666).
CC Involved in an electron flow toward the plastoglobule plastoquinone
CC pool (PubMed:21844348, PubMed:25018761). Required for plastochromanol-8
CC accumulation and for phylloquinone (vitamin K1) production
CC (PubMed:21844348, PubMed:25018761). Probably not directly involved in
CC cyclic or chlororespiratory electron flows under standard growth
CC conditions, but participates in the redox metabolism of plastoquinone-9
CC and the tocophrol recycling-intermediate alpha-tocopherol quinone
CC (PubMed:21844348, PubMed:25018761). Catalyzes the penultimate step in
CC the biosynthesis of vitamin K1 (PubMed:26023160).
CC {ECO:0000269|PubMed:12972666, ECO:0000269|PubMed:21844348,
CC ECO:0000269|PubMed:25018761, ECO:0000269|PubMed:26023160}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9;
CC Evidence={ECO:0000269|PubMed:21844348};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + H(+) + NADH = a ubiquinol + NAD(+);
CC Xref=Rhea:RHEA:23152, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:21844348};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=demethylphylloquinone + H(+) + NADPH = demethylphylloquinol +
CC NADP(+); Xref=Rhea:RHEA:47744, ChEBI:CHEBI:15378, ChEBI:CHEBI:31087,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87844; EC=1.6.5.12;
CC Evidence={ECO:0000269|PubMed:21844348, ECO:0000269|PubMed:26023160};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:26023160};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by dicumarol.
CC {ECO:0000269|PubMed:26023160}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9 uM for decyl-plastoquinone {ECO:0000269|PubMed:21844348};
CC KM=20 uM for menadione {ECO:0000269|PubMed:26023160};
CC Vmax=46 umol/min/mg enzyme toward decyl-plastoquinone
CC {ECO:0000269|PubMed:21844348};
CC Note=kcat is 0.44 sec(-1) for menadione.
CC {ECO:0000269|PubMed:26023160};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12972666,
CC ECO:0000269|PubMed:18703057, ECO:0000269|PubMed:21844348,
CC ECO:0000269|PubMed:23841539}. Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16258072}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16258072}; Matrix side
CC {ECO:0000269|PubMed:16258072}. Plastid, chloroplast
CC {ECO:0000269|PubMed:18703057, ECO:0000269|PubMed:21844348,
CC ECO:0000269|PubMed:23841539}. Plastid, chloroplast, plastoglobule
CC {ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:21844348,
CC ECO:0000269|PubMed:22274653, ECO:0000269|PubMed:25018761}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8GXR9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GXR9-2; Sequence=VSP_025063, VSP_025064, VSP_025065,
CC VSP_025066;
CC -!- TISSUE SPECIFICITY: Flowers, roots, leaves and stems.
CC {ECO:0000269|PubMed:12972666}.
CC -!- INDUCTION: Up-regulated by high-light. {ECO:0000269|PubMed:15333756,
CC ECO:0000269|PubMed:21844348}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:21844348,
CC PubMed:25018761). Increased photosensitivity to high light
CC (PubMed:26023160). {ECO:0000269|PubMed:21844348,
CC ECO:0000269|PubMed:25018761, ECO:0000269|PubMed:26023160}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC42708.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC35879.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL590346; CAC35879.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91343.1; -; Genomic_DNA.
DR EMBL; AK118078; BAC42708.1; ALT_SEQ; mRNA.
DR EMBL; AY056424; AAL08280.1; -; mRNA.
DR EMBL; AY127949; AAM91048.1; -; mRNA.
DR EMBL; AJ715502; CAG29362.1; -; Genomic_DNA.
DR RefSeq; NP_568205.6; NM_120955.8.
DR AlphaFoldDB; Q8GXR9; -.
DR SMR; Q8GXR9; -.
DR STRING; 3702.AT5G08740.1; -.
DR SwissLipids; SLP:000001504; -.
DR PaxDb; Q8GXR9; -.
DR PeptideAtlas; Q8GXR9; -.
DR PRIDE; Q8GXR9; -.
DR ProteomicsDB; 236812; -. [Q8GXR9-1]
DR GeneID; 830775; -.
DR KEGG; ath:AT5G08740; -.
DR Araport; AT5G08740; -.
DR eggNOG; KOG2495; Eukaryota.
DR HOGENOM; CLU_021377_2_0_1; -.
DR InParanoid; Q8GXR9; -.
DR OrthoDB; 1463391at2759; -.
DR PhylomeDB; Q8GXR9; -.
DR BioCyc; ARA:AT5G08740-MON; -.
DR BioCyc; MetaCyc:MON-19499; -.
DR BRENDA; 1.6.5.12; 399.
DR SABIO-RK; Q8GXR9; -.
DR PRO; PR:Q8GXR9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GXR9; baseline and differential.
DR Genevisible; Q8GXR9; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0010287; C:plastoglobule; IDA:UniProtKB.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IBA:GO_Central.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0019646; P:aerobic electron transport chain; IBA:GO_Central.
DR GO; GO:0071482; P:cellular response to light stimulus; IEP:UniProtKB.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IBA:GO_Central.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; FAD; Flavoprotein; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; NAD; NADP; Oxidoreductase;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 53..519
FT /note="Alternative NAD(P)H-ubiquinone oxidoreductase C1,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000286517"
FT BINDING 82..118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 246..282
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..170
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_025063"
FT VAR_SEQ 171..195
FT /note="VNGSEISVTGGTVLLESGFKIEYDW -> MGLRFLLLEEPSCSKAVLKSNTI
FT AR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_025064"
FT VAR_SEQ 415..427
FT /note="AFQEADFTGWNIW -> RKKATKYEHIHVL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_025065"
FT VAR_SEQ 428..519
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_025066"
FT CONFLICT 404
FT /note="N -> H (in Ref. 3; BAC42708)"
FT /evidence="ECO:0000305"
FT CONFLICT 487..497
FT /note="EHRFKVGISWF -> QHLFMVRISCL (in Ref. 1; CAC35879)"
FT /evidence="ECO:0000305"
FT CONFLICT 491..493
FT /note="KVG -> MVR (in Ref. 2; AED91343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 56916 MW; 97FD4B42AE522EB1 CRC64;
MAVLSSVSSL IPFSYGATRL TSKASLASRT SGFNLSSRWN STRNSPMLYL SRAVTNNSGT
TEISDNETAP RTYSWPDNKR PRVCILGGGF GGLYTALRLE SLVWPEDKKP QVVLVDQSER
FVFKPMLYEL LSGEVDVWEI APRFSDLLTN TGIQFLRDRV KTLLPCDHLG VNGSEISVTG
GTVLLESGFK IEYDWLVLAL GAESKLDVVP GAMELAFPFY TLEDAIRVNE KLSKLERKNF
KDGSAIKVAV VGCGYAGVEL AATISERLQD RGIVQSINVS KNILTSAPDG NREAAMKVLT
SRKVQLLLGY LVQSIKRASN LEEDEGYFLE LQPAERGLES QIIEADIVLW TVGAKPLLTK
LEPSGPNVLP LNARGQAETD ETLRVKGHPR IFALGDSSSL RDSNGKILPT TAQVAFQEAD
FTGWNIWAAI NNRPLLPFRF QNLGEMMTLG RYDAAISPSF IEGLTLEGPI GHAARKLAYL
IRLPTDEHRF KVGISWFAKS AVDSIALLQS NLTKVLSGS
