ID ACON_BOVIN Reviewed; 780 AA. AC P20004; Q3SZZ1; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 4. DT 27-MAR-2024, entry version 186. DE RecName: Full=Aconitate hydratase, mitochondrial; DE Short=Aconitase; DE EC=4.2.1.3; DE AltName: Full=Citrate hydro-lyase; DE Flags: Precursor; GN Name=ACO2; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Heart; RA Xu N., Liu W., Woldegiogis G., Sun X.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP PRELIMINARY PROTEIN SEQUENCE OF 28-780. RC TISSUE=Heart; RX PubMed=3372519; DOI=10.1016/s0021-9258(18)68459-5; RA Plank D.W., Howard J.B.; RT "Identification of the reactive sulfhydryl and sequences of cysteinyl- RT tryptic peptides from beef heart aconitase."; RL J. Biol. Chem. 263:8184-8189(1988). RN [4] RP PROTEIN SEQUENCE OF 118-139 AND 439-457, AND CHARACTERIZATION OF RP IRON-SULFUR CLUSTERS. RC TISSUE=Heart; RX PubMed=2511202; DOI=10.1016/s0021-9258(19)47074-9; RA Plank D.W., Kennedy M.C., Beinert H., Howard J.B.; RT "Cysteine labeling studies of beef heart aconitase containing a 4Fe, a RT cubane 3Fe, or a linear 3Fe cluster."; RL J. Biol. Chem. 264:20385-20393(1989). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-779 IN COMPLEX WITH IRON-SULFUR RP AND THE SUBSTRATE ANALOG NITROISOCITRATE, COFACTOR, AND REACTION MECHANISM. RX PubMed=1547214; DOI=10.1021/bi00125a014; RA Lauble H., Kennedy M.C., Beinert H., Stout C.D.; RT "Crystal structures of aconitase with isocitrate and nitroisocitrate RT bound."; RL Biochemistry 31:2735-2748(1992). CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis- CC aconitate. {ECO:0000250|UniProtKB:P19414}. CC -!- CATALYTIC ACTIVITY: CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; CC Evidence={ECO:0000250|UniProtKB:P19414}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000269|PubMed:1547214}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. Binding of a [3Fe-4S] CC cluster leads to an inactive enzyme. {ECO:0000269|PubMed:1547214}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate CC from oxaloacetate: step 2/2. {ECO:0000250|UniProtKB:P19414}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1547214}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}. CC -!- PTM: Forms covalent cross-links mediated by transglutaminase TGM2, CC between a glutamine and the epsilon-amino group of a lysine residue, CC forming homopolymers and heteropolymers. CC {ECO:0000250|UniProtKB:Q9ER34}. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. CC {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; Z49931; CAA90177.1; -; mRNA. DR EMBL; BC102642; AAI02643.1; -; mRNA. DR PIR; S57528; S57528. DR RefSeq; NP_776402.1; NM_173977.3. DR PDB; 1ACO; X-ray; 2.05 A; A=29-779. DR PDB; 1AMI; X-ray; 2.00 A; A=28-780. DR PDB; 1AMJ; X-ray; 2.00 A; A=28-780. DR PDB; 1C96; X-ray; 1.81 A; A=29-779. DR PDB; 1C97; X-ray; 1.98 A; A=29-779. DR PDB; 1FGH; X-ray; 2.05 A; A=29-779. DR PDB; 1NIS; X-ray; 2.05 A; A=29-779. DR PDB; 1NIT; X-ray; 2.05 A; A=29-779. DR PDB; 8ACN; X-ray; 2.00 A; A=29-780. DR PDBsum; 1ACO; -. DR PDBsum; 1AMI; -. DR PDBsum; 1AMJ; -. DR PDBsum; 1C96; -. DR PDBsum; 1C97; -. DR PDBsum; 1FGH; -. DR PDBsum; 1NIS; -. DR PDBsum; 1NIT; -. DR PDBsum; 8ACN; -. DR AlphaFoldDB; P20004; -. DR SMR; P20004; -. DR IntAct; P20004; 1. DR STRING; 9913.ENSBTAP00000008431; -. DR PaxDb; 9913-ENSBTAP00000008431; -. DR PeptideAtlas; P20004; -. DR Ensembl; ENSBTAT00000008431.5; ENSBTAP00000008431.4; ENSBTAG00000006429.5. DR GeneID; 280976; -. DR KEGG; bta:280976; -. DR CTD; 50; -. DR VEuPathDB; HostDB:ENSBTAG00000006429; -. DR VGNC; VGNC:25546; ACO2. DR eggNOG; KOG0453; Eukaryota. DR GeneTree; ENSGT00940000154892; -. DR HOGENOM; CLU_006714_2_2_1; -. DR InParanoid; P20004; -. DR OMA; NTHAFVA; -. DR OrthoDB; 3266779at2759; -. DR TreeFam; TF300627; -. DR Reactome; R-BTA-71403; Citric acid cycle (TCA cycle). DR UniPathway; UPA00223; UER00718. DR EvolutionaryTrace; P20004; -. DR Proteomes; UP000009136; Chromosome 5. DR Bgee; ENSBTAG00000006429; Expressed in corpus luteum and 107 other cell types or tissues. DR ExpressionAtlas; P20004; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IDA:CAFA. DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IDA:CAFA. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:CAFA. DR GO; GO:0003994; F:aconitate hydratase activity; IDA:CAFA. DR GO; GO:0008198; F:ferrous iron binding; IDA:CAFA. DR GO; GO:0005506; F:iron ion binding; ISS:AgBase. DR GO; GO:0006101; P:citrate metabolic process; IDA:CAFA. DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:AgBase. DR CDD; cd01578; AcnA_Mitochon_Swivel; 1. DR CDD; cd01584; AcnA_Mitochondrial; 1. DR Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1. DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2. DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1. DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3. DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR018136; Aconitase_4Fe-4S_BS. DR InterPro; IPR036008; Aconitase_4Fe-4S_dom. DR InterPro; IPR015932; Aconitase_dom2. DR InterPro; IPR006248; Aconitase_mito-like. DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl. DR NCBIfam; TIGR01340; aconitase_mito; 1. DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1. DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 1. DR Pfam; PF00330; Aconitase; 1. DR Pfam; PF00694; Aconitase_C; 1. DR PRINTS; PR00415; ACONITASE. DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1. DR SUPFAM; SSF52016; LeuD/IlvD-like; 1. DR PROSITE; PS00450; ACONITASE_1; 1. DR PROSITE; PS01244; ACONITASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Acetylation; Direct protein sequencing; Iron; KW Iron-sulfur; Lyase; Metal-binding; Mitochondrion; Phosphoprotein; KW Reference proteome; Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1..27 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 28..780 FT /note="Aconitate hydratase, mitochondrial" FT /id="PRO_0000000540" FT REGION 524..560 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 545..560 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 99 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:1547214, FT ECO:0007744|PDB:8ACN" FT BINDING 192..194 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:1547214, FT ECO:0007744|PDB:8ACN" FT BINDING 385 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:1547214, FT ECO:0000269|PubMed:3372519, ECO:0007744|PDB:8ACN" FT BINDING 448 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:1547214, FT ECO:0000269|PubMed:3372519, ECO:0007744|PDB:8ACN" FT BINDING 451 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:1547214, FT ECO:0000269|PubMed:3372519, ECO:0007744|PDB:8ACN" FT BINDING 474 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:1547214, FT ECO:0007744|PDB:8ACN" FT BINDING 479 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:1547214, FT ECO:0007744|PDB:8ACN" FT BINDING 607 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:1547214, FT ECO:0007744|PDB:8ACN" FT BINDING 670..671 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:1547214, FT ECO:0007744|PDB:8ACN" FT MOD_RES 31 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 50 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 50 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 138 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 138 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 144 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 144 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 233 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 233 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 411 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 517 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 517 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 523 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 523 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 549 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 559 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99798" FT MOD_RES 573 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99798" FT MOD_RES 573 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 591 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 605 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99798" FT MOD_RES 605 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 628 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 670 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 689 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 723 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 723 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 730 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 730 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 736 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT MOD_RES 743 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99KI0" FT CONFLICT 40 FT /note="N -> H (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 53 FT /note="N -> D (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 99 FT /note="Q -> R (in Ref. 1; CAA90177)" FT /evidence="ECO:0000305" FT CONFLICT 179 FT /note="E -> G (in Ref. 2; AAI02643)" FT /evidence="ECO:0000305" FT CONFLICT 217 FT /note="M -> T (in Ref. 1; CAA90177)" FT /evidence="ECO:0000305" FT CONFLICT 409 FT /note="Q -> K (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 435 FT /note="I -> V (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 555 FT /note="Q -> R (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 577 FT /note="R -> K (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 624 FT /note="V -> S (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 627 FT /note="G -> R (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 652 FT /note="K -> Q (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 674 FT /note="A -> S (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 680 FT /note="H -> F (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 727 FT /note="K -> Q (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 33..35 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 38..42 FT /evidence="ECO:0007829|PDB:1C97" FT HELIX 45..59 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 65..71 FT /evidence="ECO:0007829|PDB:1C96" FT TURN 77..79 FT /evidence="ECO:0007829|PDB:1C96" FT TURN 84..86 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 88..91 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 94..99 FT /evidence="ECO:0007829|PDB:1C96" FT TURN 100..102 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 103..113 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 122..125 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 136..146 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 148..161 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 164..166 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 173..180 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 187..192 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 195..201 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 204..207 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 210..218 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 222..225 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 228..236 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 244..255 FT /evidence="ECO:0007829|PDB:1C96" FT TURN 256..262 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 263..269 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 270..274 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 277..286 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 287..290 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 293..296 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 301..309 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 313..321 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 323..325 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 335..341 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 352..354 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 358..360 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 361..371 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 376..383 FT /evidence="ECO:0007829|PDB:1C96" FT TURN 384..386 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 390..404 FT /evidence="ECO:0007829|PDB:1C96" FT TURN 405..407 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 411..416 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 421..429 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 432..438 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 441..443 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 449..452 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 466..473 FT /evidence="ECO:0007829|PDB:1C96" FT TURN 477..481 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 486..490 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 493..502 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 504..506 FT /evidence="ECO:0007829|PDB:1AMI" FT TURN 509..511 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 513..515 FT /evidence="ECO:0007829|PDB:1C97" FT STRAND 521..523 FT /evidence="ECO:0007829|PDB:1C97" FT TURN 549..551 FT /evidence="ECO:0007829|PDB:1C97" FT STRAND 563..565 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 579..588 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 594..597 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 601..606 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 610..613 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 614..616 FT /evidence="ECO:0007829|PDB:1C96" FT TURN 618..620 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 621..623 FT /evidence="ECO:0007829|PDB:1C96" FT TURN 624..626 FT /evidence="ECO:0007829|PDB:1C96" FT TURN 635..637 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 643..652 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 657..660 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 663..665 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 673..680 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 683..689 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 693..701 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 705..711 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 712..717 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 723..727 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 729..731 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 738..743 FT /evidence="ECO:0007829|PDB:1C96" FT STRAND 749..755 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 760..768 FT /evidence="ECO:0007829|PDB:1C96" FT HELIX 771..778 FT /evidence="ECO:0007829|PDB:1C96" SQ SEQUENCE 780 AA; 85359 MW; 91EB21B3923F16C5 CRC64; MAPYSLLVSR LQKALGARQY HVASVLCQRA KVAMSHFEPN EYIRYDLLEK NINIVRKRLN RPLTLSEKIV YGHLDDPANQ EIERGKTYLR LRPDRVAMQD ATAQMAMLQF ISSGLPKVAV PSTIHCDHLI EAQLGGEKDL RRAKDINQEV YNFLATAGAK YGVGFWRPGS GIIHQIILEN YAYPGVLLIG TDSHTPNGGG LGGICIGVGG ADAVDVMAGI PWELKCPKVI GVKLTGSLSG WTSPKDVILK VAGILTVKGG TGAIVEYHGP GVDSISCTGM ATICNMGAEI GATTSVFPYN HRMKKYLSKT GRADIANLAD EFKDHLVPDS GCHYDQLIEI NLSELKPHIN GPFTPDLAHP VAEVGSVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA KQALAHGLQC KSQFTITPGS EQIRATIERD GYAQILRDVG GIVLANACGP CIGQWDRKDI KKGEKNTIVT SYNRNFTGRN DANPETHAFV TSPEIVTALA IAGTLKFNPE TDFLTGKDGK KFKLEAPDAD ELPRAEFDPG QDTYQHPPKD SSGQQVDVSP TSQRLQLLEP FDKWDGRDLE DLQILIKVKG KCTTDHISAA GPWLKFRGHL DNISNNLLIG AINVENGKAN SVRNAVTQEF GPVPDTARYY KKHGIRWVVI GDENYGEGSS REHAALEPRH LGGRAIITKS FARIHETNLK KQGLLPLTFA DPADYNKIHP VDKLTIKGLK DFAPGKPLTC IIKHPNGTQE TILLNHTFNE TQIEWFRAGS ALNRMKELQK //