ID NDUS1_ARATH Reviewed; 748 AA. AC Q9FGI6; Q940B1; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 2. DT 24-JAN-2024, entry version 187. DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial; DE EC=7.1.1.2; DE AltName: Full=Protein EMBRYO DEFECTIVE 1467; DE Flags: Precursor; GN Name=EMB1467; OrderedLocusNames=At5g37510; ORFNames=MPA22.5; 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 {ECO:0000312|EMBL:BAB10668.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000305} RP GENOME REANNOTATION. 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]. 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 [4] {ECO:0000305} RP PROTEIN SEQUENCE OF 511-523. RC TISSUE=Leaf, and Stem; RX PubMed=11743114; DOI=10.1104/pp.127.4.1694; RA Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.; RT "Proteomic approach to identify novel mitochondrial proteins in RT Arabidopsis."; RL Plant Physiol. 127:1694-1710(2001). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RC STRAIN=cv. Landsberg erecta; RX PubMed=14671022; DOI=10.1105/tpc.016055; RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., RA Millar A.H.; RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights RT signaling and regulatory components, provides assessment of targeting RT prediction programs, and indicates plant-specific mitochondrial proteins."; RL Plant Cell 16:241-256(2004). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain CC NADH dehydrogenase (Complex I) that is believed to belong to the CC minimal assembly required for catalysis. Complex I functions in the CC transfer of electrons from NADH to the respiratory chain. The immediate CC electron acceptor for the enzyme is believed to be ubiquinone (By CC similarity). This is the largest subunit of complex I and it is a CC component of the iron-sulfur (IP) fragment of the enzyme. It may form CC part of the active site crevice where NADH is oxidized (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA- CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250}; CC -!- SUBUNIT: Complex I is composed of at least 49 different subunits. This CC is a component of the iron-sulfur (IP) fragment of the enzyme. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. CC Note=Matrix and cytoplasmic side of the mitochondrial inner membrane. CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences.; CC Name=1; CC IsoId=Q9FGI6-1; Sequence=Displayed; CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB10668.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB025630; BAB10668.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002688; AED94200.1; -; Genomic_DNA. DR EMBL; AY056140; AAL07219.1; -; mRNA. DR RefSeq; NP_568550.1; NM_123110.2. [Q9FGI6-1] DR RefSeq; NP_851103.1; NM_180772.2. DR PDB; 7A23; EM; 3.70 A; C=1-748. DR PDB; 7A24; EM; 3.80 A; C=1-748. DR PDB; 7AQR; EM; 2.91 A; G=1-748. DR PDB; 7AR7; EM; 3.72 A; G=57-744. DR PDB; 7AR8; EM; 3.53 A; G=1-748. DR PDB; 7ARB; EM; 3.41 A; G=1-748. DR PDB; 8BED; EM; 2.03 A; G=1-748. DR PDB; 8BPX; EM; 2.09 A; G=1-748. DR PDB; 8BQ5; EM; 2.73 A; G=1-748. DR PDB; 8BQ6; EM; 2.80 A; G=1-748. DR PDBsum; 7A23; -. DR PDBsum; 7A24; -. DR PDBsum; 7AQR; -. DR PDBsum; 7AR7; -. DR PDBsum; 7AR8; -. DR PDBsum; 7ARB; -. DR PDBsum; 8BED; -. DR PDBsum; 8BPX; -. DR PDBsum; 8BQ5; -. DR PDBsum; 8BQ6; -. DR AlphaFoldDB; Q9FGI6; -. DR EMDB; EMD-11873; -. DR EMDB; EMD-11875; -. DR EMDB; EMD-11876; -. DR EMDB; EMD-11878; -. DR EMDB; EMD-15998; -. DR EMDB; EMD-16168; -. DR EMDB; EMD-16171; -. DR EMDB; EMD-16172; -. DR SMR; Q9FGI6; -. DR BioGRID; 18980; 3. DR IntAct; Q9FGI6; 2. DR STRING; 3702.Q9FGI6; -. DR TCDB; 3.D.1.6.3; the h+ or na+-translocating nadh dehydrogenase (ndh) family. DR iPTMnet; Q9FGI6; -. DR MetOSite; Q9FGI6; -. DR PaxDb; 3702-AT5G37510-2; -. DR ProteomicsDB; 251103; -. [Q9FGI6-1] DR EnsemblPlants; AT5G37510.2; AT5G37510.2; AT5G37510. [Q9FGI6-1] DR GeneID; 833729; -. DR Gramene; AT5G37510.2; AT5G37510.2; AT5G37510. [Q9FGI6-1] DR KEGG; ath:AT5G37510; -. DR Araport; AT5G37510; -. DR TAIR; AT5G37510; EMB1467. DR eggNOG; KOG2282; Eukaryota. DR InParanoid; Q9FGI6; -. DR OrthoDB; 19999at2759; -. DR PhylomeDB; Q9FGI6; -. DR BioCyc; ARA:AT5G37510-MONOMER; -. DR BioCyc; MetaCyc:AT5G37510-MONOMER; -. DR PRO; PR:Q9FGI6; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q9FGI6; baseline and differential. DR GO; GO:0009507; C:chloroplast; HDA:TAIR. DR GO; GO:0031966; C:mitochondrial membrane; IDA:TAIR. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:TAIR. DR GO; GO:0005739; C:mitochondrion; IDA:TAIR. DR GO; GO:0009536; C:plastid; HDA:TAIR. DR GO; GO:0045271; C:respiratory chain complex I; IDA:TAIR. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR GO; GO:0009853; P:photorespiration; TAS:TAIR. DR CDD; cd00207; fer2; 1. DR CDD; cd02773; MopB_Res-Cmplx1_Nad11; 1. DR Gene3D; 3.10.20.740; -; 1. DR Gene3D; 3.30.70.20; -; 1. DR Gene3D; 3.40.50.740; -; 2. DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1. DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom. DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS. DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu. DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. DR InterPro; IPR015405; NDUFS1-like_C. DR NCBIfam; TIGR01973; NuoG; 1. DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1. DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1. DR Pfam; PF13510; Fer2_4; 1. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1. DR Pfam; PF09326; NADH_dhqG_C; 1. DR SMART; SM00929; NADH-G_4Fe-4S_3; 1. DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51839; 4FE4S_HC3; 1. DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1. DR PROSITE; PS00641; COMPLEX1_75K_1; 1. DR PROSITE; PS00642; COMPLEX1_75K_2; 1. DR PROSITE; PS00643; COMPLEX1_75K_3; 1. DR Genevisible; Q9FGI6; AT. PE 1: Evidence at protein level; KW 2Fe-2S; 3D-structure; 4Fe-4S; Alternative splicing; KW Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD; KW Oxidoreductase; Reference proteome; Respiratory chain; Transit peptide; KW Translocase; Transport; Ubiquinone. FT TRANSIT 1..33 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 34..748 FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein FT 1, mitochondrial" FT /id="PRO_0000019972" FT DOMAIN 72..150 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT DOMAIN 150..189 FT /note="4Fe-4S His(Cys)3-ligated-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT DOMAIN 287..343 FT /note="4Fe-4S Mo/W bis-MGD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT REGION 38..64 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 106 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 117 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 120 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 134 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 166 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 170 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 173 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 179 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 218 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 221 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 224 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 268 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" FT HELIX 60..62 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 73..78 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 81..86 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 91..97 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 121..124 FT /evidence="ECO:0007829|PDB:8BED" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 143..148 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 149..164 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 170..172 FT /evidence="ECO:0007829|PDB:8BED" FT TURN 174..177 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 180..187 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 209..213 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 215..217 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 223..230 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 238..242 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 243..245 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 247..249 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 251..253 FT /evidence="ECO:0007829|PDB:8BED" FT TURN 259..262 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 263..267 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 273..275 FT /evidence="ECO:0007829|PDB:8BED" FT TURN 276..280 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 288..293 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 296..299 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 302..317 FT /evidence="ECO:0007829|PDB:8BED" FT TURN 321..326 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 330..334 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 335..340 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 341..343 FT /evidence="ECO:0007829|PDB:7AQR" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 352..354 FT /evidence="ECO:0007829|PDB:7AQR" FT STRAND 356..358 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 361..372 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 377..379 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 380..384 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 390..402 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 408..413 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 422..425 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 432..436 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 438..444 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 447..450 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 452..465 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 468..474 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 483..488 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 489..497 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 501..507 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 510..517 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 518..522 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 526..539 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 550..553 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 559..565 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 572..574 FT /evidence="ECO:0007829|PDB:7AQR" FT HELIX 575..577 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 579..585 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 591..593 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 598..605 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 609..613 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 615..620 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 623..625 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 629..631 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 637..639 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 653..664 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 673..681 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 685..687 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 700..702 FT /evidence="ECO:0007829|PDB:8BED" FT STRAND 724..726 FT /evidence="ECO:0007829|PDB:7AQR" FT HELIX 729..731 FT /evidence="ECO:0007829|PDB:8BED" FT HELIX 733..741 FT /evidence="ECO:0007829|PDB:8BED" SQ SEQUENCE 748 AA; 81525 MW; C83400F148E73F44 CRC64; MGLGILASRT IRPASRLLQS QTSNFFLRTI VSKPELQSPE SAAVSEPEPP TQILPPRNPV GGARVHFSNP EDAIEVFVDG YAVKVPKGFT VLQACEVAGV DIPRFCYHSR LSIAGNCRMC LVEVEKSPKP VASCAMPALP GMKIKTDTPI AKKAREGVME FLLMNHPLDC PICDQGGECD LQDQSMAFGS DRGRFTEMKR SVVDKNLGPL VKTVMTRCIQ CTRCVRFASE VAGVQDLGIL GRGSGEEIGT YVEKLMTSEL SGNVIDICPV GALTSKPFAF KARNWELKAT ETIDVSDAVG SNIRVDSRGP EVMRIIPRLN EDINEEWISD KTRFCYDGLK RQRLSDPMIR DSDGRFKAVS WRDALAVVGD IIHQVKPDEI VGVAGQLSDA ESMMVLKDFV NRMGSDNVWC EGTAAGVDAD LRYSYLMNTS ISGLENADLF LLIGTQPRVE AAMVNARICK TVRASNAKVG YVGPPAEFNY DCKHLGTGPD TLKEIAEGRH PFCTALKNAK NPAIIVGAGL FNRTDKNAIL SSVESIAQAN NVVRPDWNGL NFLLQYAAQA AALDLGLIQQ SAKALESAKF VYLMGADDVN VDKIPKDAFV VYQGHHGDKA VYRANVILPA SAFTEKEGTY ENTEGFTQQT VPAVPTVGDA RDDWKIVRAL SEVSGVKLPY NSIEGVRSRI KSVAPNLVHT DEREPAAFGP SLKPECKEAM STTPFQTVVE NFYMTNSITR ASKIMAQCSA VLLKKPFV //