ID FDX2_HUMAN Reviewed; 183 AA. AC Q6P4F2; B7Z6L7; Q8N8B8; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2024, sequence version 3. DT 02-SEP-2026, entry version 166. DE RecName: Full=Ferredoxin-2, mitochondrial {ECO:0000303|PubMed:20547883}; DE AltName: Full=Adrenodoxin-like protein; DE AltName: Full=Ferredoxin-1-like protein; DE Flags: Precursor; GN Name=FDX2 {ECO:0000312|HGNC:HGNC:30546}; Synonyms=FDX1L; 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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Small intestine; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 [4] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=20547883; DOI=10.1073/pnas.1004250107; RA Sheftel A.D., Stehling O., Pierik A.J., Elsasser H.P., Muhlenhoff U., RA Webert H., Hobler A., Hannemann F., Bernhardt R., Lill R.; RT "Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct RT roles in steroidogenesis, heme, and Fe/S cluster biosynthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 107:11775-11780(2010). RN [5] 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 [6] RP SUBUNIT, AND FUNCTION. RX PubMed=28001042; DOI=10.1021/acs.biochem.6b00447; RA Cai K., Tonelli M., Frederick R.O., Markley J.L.; RT "Human Mitochondrial Ferredoxin 1 (FDX1) and Ferredoxin 2 (FDX2) Both Bind RT Cysteine Desulfurase and Donate Electrons for Iron-Sulfur Cluster RT Biosynthesis."; RL Biochemistry 56:487-499(2017). RN [7] RP INTERACTION WITH NFS1. RX PubMed=29097656; DOI=10.1038/s41467-017-01497-1; RA Boniecki M.T., Freibert S.A., Muhlenhoff U., Lill R., Cygler M.; RT "Structure and functional dynamics of the mitochondrial Fe/S cluster RT synthesis complex."; RL Nat. Commun. 8:1287-1287(2017). RN [8] RP FUNCTION. RX PubMed=38425362; DOI=10.1038/s41929-023-01087-z; RA Nicoll C.R., Alvigini L., Gottinger A., Cecchini D., Mannucci B., RA Corana F., Mascotti M.L., Mattevi A.; RT "In vitro construction of the COQ metabolon unveils the molecular RT determinants of coenzyme Q biosynthesis."; RL Nat. Catal. 7:148-160(2024). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 66-171 IN COMPLEX WITH RP IRON-SULFUR (2FE-2S), AND COFACTOR. RA Webert H., Hobler A., Sheftel A.D., Molik S., Maestre-Reyna M., RA Essen L.-O., Vorniscescu D., Keusgen M., Hannemann F., Bernhardt R., RA Lill R.; RT "Structure and functional studies on human mitochondrial ferredoxins."; RL Submitted (JAN-2011) to the PDB data bank. RN [10] RP INVOLVEMENT IN MEOAL, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=24281368; DOI=10.1038/ejhg.2013.269; RA Spiegel R., Saada A., Halvardson J., Soiferman D., Shaag A., Edvardson S., RA Horovitz Y., Khayat M., Shalev S.A., Feuk L., Elpeleg O.; RT "Deleterious mutation in FDX1L gene is associated with a novel RT mitochondrial muscle myopathy."; RL Eur. J. Hum. Genet. 22:902-906(2014). RN [11] RP INVOLVEMENT IN MEOAL, VARIANT MEOAL LEU-141, CHARACTERIZATION OF VARIANT RP MEOAL LEU-141, AND TISSUE SPECIFICITY. RX PubMed=30010796; DOI=10.1093/brain/awy172; RA Gurgel-Giannetti J., Lynch D.S., Paiva A.R.B., Lucato L.T., Yamamoto G., RA Thomsen C., Basu S., Freua F., Giannetti A.V., de Assis B.D.R., RA Ribeiro M.D.O., Barcelos I., Sayao Souza K., Monti F., Melo U.S., RA Amorim S., Silva L.G.L., Macedo-Souza L.I., Vianna-Morgante A.M., RA Hirano M., Van der Knaap M.S., Lill R., Vainzof M., Oldfors A., Houlden H., RA Kok F.; RT "A novel complex neurological phenotype due to a homozygous mutation in RT FDX2."; RL Brain 141:2289-2298(2018). CC -!- FUNCTION: Electron donor, of the core iron-sulfur cluster (ISC) CC assembly complex, that acts to reduce the persulfide into sulfide CC during [2Fe-2S] clusters assembly on the scaffolding protein ISCU CC (PubMed:28001042). The core iron-sulfur cluster (ISC) assembly complex CC is involved in the de novo synthesis of a [2Fe-2S] cluster, the first CC step of the mitochondrial iron-sulfur protein biogenesis (By CC similarity). This process is initiated by the cysteine desulfurase CC complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is CC delivered on the scaffold protein ISCU in a FXN-dependent manner (By CC similarity). Then this complex is stabilized by FDX2 which provides CC reducing equivalents to accomplish the [2Fe-2S] cluster assembly (By CC similarity). Finally, the [2Fe-2S] cluster is transferred from ISCU to CC chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity). CC Essential for coenzyme Q biosynthesis: together with FDXR, transfers CC the electrons required for the hydroxylation reaction performed by COQ6 CC (PubMed:38425362). {ECO:0000250|UniProtKB:Q9H1K1, CC ECO:0000269|PubMed:28001042, ECO:0000269|PubMed:38425362}. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000269|Ref.9, ECO:0007744|PDB:2Y5C}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|Ref.9, CC ECO:0007744|PDB:2Y5C}; CC -!- SUBUNIT: Component of the mitochondrial core iron-sulfur cluster (ISC) CC complex composed of NFS1, LYRM4, NDUFAB1, ISCU, FXN, and FDX2; this CC complex is a heterohexamer containing two copies of each monomer CC (Probable). Form a heterodimer complex with NFS1 (PubMed:29097656). CC Interacts (in both their reduced and oxidized states) with the cysteine CC desulfurase complex; this interaction stimulates cysteine desulfurase CC activity, and serves as a reductant for Fe-S cluster assembly CC (PubMed:28001042). {ECO:0000269|PubMed:28001042, CC ECO:0000269|PubMed:29097656, ECO:0000305|PubMed:29097656}. CC -!- INTERACTION: CC Q6P4F2; Q969G2: LHX4; NbExp=3; IntAct=EBI-10252800, EBI-2865388; CC Q6P4F2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-10252800, EBI-16439278; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20547883, CC ECO:0000269|PubMed:24281368}. Mitochondrion matrix CC {ECO:0000250|UniProtKB:P10109}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q6P4F2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6P4F2-2; Sequence=VSP_056826; CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in testis, CC kidney and brain (at protein level) (PubMed:20547883). Expressed in CC muscle (at protein level) (PubMed:24281368, PubMed:30010796). Expressed CC in fibroblasts (at protein level) (PubMed:24281368). CC {ECO:0000269|PubMed:20547883, ECO:0000269|PubMed:24281368, CC ECO:0000269|PubMed:30010796}. CC -!- DISEASE: Mitochondrial myopathy, episodic, with optic atrophy and CC reversible leukoencephalopathy (MEOAL) [MIM:251900]: An autosomal CC recessive neuromuscular disorder characterized by childhood onset of CC recurrent episodes of proximal weakness and myalgia often precipitated CC by exercise, infections or low temperature. Additional features are CC optic atrophy, axonal polyneuropathy, and reversible or partially CC reversible leukoencephalopathy. {ECO:0000269|PubMed:24281368, CC ECO:0000269|PubMed:30010796}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC04929.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAH13303.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AK097022; BAC04929.1; ALT_INIT; mRNA. DR EMBL; AK300568; BAH13303.1; ALT_INIT; mRNA. DR EMBL; AC011511; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC063460; AAH63460.1; -; mRNA. DR CCDS; CCDS32905.3; -. [Q6P4F2-1] DR RefSeq; NP_001384335.1; NM_001397406.1. [Q6P4F2-1] DR PDB; 2Y5C; X-ray; 1.70 A; A/B=66-171. DR PDB; 8RMC; EM; 2.26 A; I=66-183. DR PDB; 8RMD; EM; 2.52 A; I=66-183. DR PDB; 8RMF; EM; 2.33 A; I=65-183. DR PDB; 8RMG; EM; 2.46 A; I=65-183. DR AlphaFoldDB; Q6P4F2; -. DR EMDB; EMD-19356; -. DR EMDB; EMD-19357; -. DR EMDB; EMD-19360; -. DR EMDB; EMD-19361; -. DR SMR; Q6P4F2; -. DR ComplexPortal; CPX-5641; Mitochondrial NIAUFX iron-sulfur cluster assembly complex. DR FunCoup; Q6P4F2; 1162. DR IntAct; Q6P4F2; 4. DR STRING; 9606.ENSP00000377311; -. DR PhosphoSitePlus; Q6P4F2; -. DR BioMuta; FDX2; -. DR DMDM; 74749111; -. DR jPOST; Q6P4F2; -. DR MassIVE; Q6P4F2; -. DR PaxDb; 9606-ENSP00000377311; -. DR PeptideAtlas; Q6P4F2; -. DR ProteomicsDB; 66974; -. [Q6P4F2-1] DR ProteomicsDB; 72397; -. DR Pumba; Q6P4F2; -. DR Antibodypedia; 76687; 6 antibodies from 5 providers. DR DNASU; 112812; -. DR Ensembl; ENST00000393708.3; ENSP00000377311.5; ENSG00000267673.7. [Q6P4F2-1] DR Ensembl; ENST00000452032.6; ENSP00000408510.3; ENSG00000167807.15. [Q6P4F2-2] DR GeneID; 112812; -. DR KEGG; hsa:112812; -. DR MANE-Select; ENST00000393708.3; ENSP00000377311.5; NM_001397406.1; NP_001384335.1. DR UCSC; uc002mny.2; human. [Q6P4F2-1] DR AGR; HGNC:30546; -. DR ClinPGx; PA162388212; -. DR CTD; 112812; -. DR DisGeNET; 112812; -. DR GeneCards; FDX2; -. DR HGNC; HGNC:30546; FDX2. DR HPA; ENSG00000267673; Low tissue specificity. DR MalaCards; FDX2; -. DR MIM; 251900; phenotype. DR MIM; 614585; gene. DR OpenTargets; ENSG00000267673; -. DR VEuPathDB; HostDB:ENSG00000267673; -. DR eggNOG; KOG3309; Eukaryota. DR GeneTree; ENSGT00940000161143; -. DR HOGENOM; CLU_082632_0_2_1; -. DR InParanoid; Q6P4F2; -. DR OrthoDB; 268593at2759; -. DR PAN-GO; Q6P4F2; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q6P4F2; -. DR PathwayCommons; Q6P4F2; -. DR Reactome; R-HSA-1362409; Mitochondrial iron-sulfur cluster biogenesis. DR Reactome; R-HSA-196108; Pregnenolone biosynthesis. DR Reactome; R-HSA-211976; Endogenous sterols. DR Reactome; R-HSA-2395516; Electron transport from NADPH to Ferredoxin. DR Reactome; R-HSA-5579026; Defective CYP11A1 causes AICSR. DR SignaLink; Q6P4F2; -. DR Agora; ENSG00000267673; -. DR BioGRID-ORCS; 112812; 490 hits in 1177 CRISPR screens. DR ChiTaRS; FDX1L; human. DR EvolutionaryTrace; Q6P4F2; -. DR GenomeRNAi; 112812; -. DR Pharos; Q6P4F2; Tdark. DR PRO; PR:Q6P4F2; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q6P4F2; protein. DR Bgee; ENSG00000267673; Expressed in prefrontal cortex and 102 other cell types or tissues. DR ExpressionAtlas; Q6P4F2; baseline and differential. DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; NAS:ComplexPortal. DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProt. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro. DR GO; GO:0009055; F:electron transfer activity; IDA:UniProt. DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IDA:UniProtKB. DR GO; GO:0044572; P:[4Fe-4S] cluster assembly; IDA:UniProtKB. DR GO; GO:0016226; P:iron-sulfur cluster assembly; NAS:ComplexPortal. DR GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro. DR GO; GO:0006744; P:ubiquinone biosynthetic process; IDA:UniProt. DR CDD; cd00207; fer2; 1. DR FunFam; 3.10.20.30:FF:000013; Adrenodoxin, mitochondrial; 1. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR001055; Adrenodoxin-like. DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS. DR InterPro; IPR012675; Beta-grasp_dom_sf. DR PANTHER; PTHR23426:SF65; FERREDOXIN-2, MITOCHONDRIAL; 1. DR PANTHER; PTHR23426; FERREDOXIN/ADRENODOXIN; 1. DR Pfam; PF00111; Fer2; 1. DR PRINTS; PR00355; ADRENODOXIN. DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS00814; ADX; 1. DR PDBsum; 2Y5C; -. DR PDBsum; 8RMC; -. DR PDBsum; 8RMD; -. DR PDBsum; 8RMF; -. DR PDBsum; 8RMG; -. PE 1: Evidence at protein level; KW 2Fe-2S; 3D-structure; Alternative splicing; Disease variant; KW Electron transport; Iron; Iron-sulfur; Metal-binding; Mitochondrion; KW Primary mitochondrial disease; Proteomics identification; KW Reference proteome; Transit peptide; Transport. FT TRANSIT 1..52 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 53..183 FT /note="Ferredoxin-2, mitochondrial" FT /id="PRO_0000325952" FT DOMAIN 68..170 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT REGION 45..65 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 105 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465, FT ECO:0000269|Ref.9, ECO:0007744|PDB:2Y5C" FT BINDING 111 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465, FT ECO:0000269|Ref.9, ECO:0007744|PDB:2Y5C" FT BINDING 114 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465, FT ECO:0000269|Ref.9, ECO:0007744|PDB:2Y5C" FT BINDING 151 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465, FT ECO:0000269|Ref.9, ECO:0007744|PDB:2Y5C" FT VAR_SEQ 133..183 FT /note="EDDMLDMAPLLQENSRLGCQIVLTPELEGAEFTLPKITRNFYVDGHVPKPH FT -> RTRGWAARLC (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056826" FT VARIANT 141 FT /note="P -> L (in MEOAL; strongly reduced protein FT expression in muscle in affected homozygous patients FT compared to control individuals; dbSNP:rs888630930)" FT /evidence="ECO:0000269|PubMed:30010796" FT /id="VAR_082100" FT CONFLICT 4 FT /note="S -> T (in Ref. 1; BAH13303)" FT /evidence="ECO:0000305" FT STRAND 67..73 FT /evidence="ECO:0007829|PDB:2Y5C" FT STRAND 79..85 FT /evidence="ECO:0007829|PDB:2Y5C" FT HELIX 90..96 FT /evidence="ECO:0007829|PDB:2Y5C" FT STRAND 106..110 FT /evidence="ECO:0007829|PDB:2Y5C" FT STRAND 115..118 FT /evidence="ECO:0007829|PDB:2Y5C" FT HELIX 120..123 FT /evidence="ECO:0007829|PDB:2Y5C" FT HELIX 127..130 FT /evidence="ECO:0007829|PDB:2Y5C" FT HELIX 131..138 FT /evidence="ECO:0007829|PDB:2Y5C" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:8RMF" FT STRAND 147..149 FT /evidence="ECO:0007829|PDB:2Y5C" FT HELIX 150..152 FT /evidence="ECO:0007829|PDB:2Y5C" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:2Y5C" FT STRAND 163..165 FT /evidence="ECO:0007829|PDB:2Y5C" FT HELIX 180..182 FT /evidence="ECO:0007829|PDB:8RMC" SQ SEQUENCE 183 AA; 19521 MW; 2B5F37C0061C65EF CRC64; MAASMARGGV SARVLLQAAR GTWWNRPGGT SGSGEGVALG TTRKFQATGS RPAGEEDAGG PERPGDVVNV VFVDRSGQRI PVSGRVGDNV LHLAQRHGVD LEGACEASLA CSTCHVYVSE DHLDLLPPPE EREDDMLDMA PLLQENSRLG CQIVLTPELE GAEFTLPKIT RNFYVDGHVP KPH //