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 27-MAR-2024, entry version 156.
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 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 [9]
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 [10]
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. This process
CC is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1)
CC that produces persulfide which is delivered on the scaffold protein
CC ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2
CC which provides reducing equivalents to accomplish the [2Fe-2S] cluster
CC assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to
CC chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H1K1, ECO:0000269|PubMed:28001042}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|Ref.8, ECO:0007744|PDB:2Y5C};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|Ref.8,
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 an heterohexamer containing two copies of each monomer
CC (Probable). Form an 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 RefSeq; NP_001026904.2; NM_001031734.3.
DR PDB; 2Y5C; X-ray; 1.70 A; A/B=66-171.
DR PDBsum; 2Y5C; -.
DR AlphaFoldDB; Q6P4F2; -.
DR SMR; Q6P4F2; -.
DR ComplexPortal; CPX-5641; Mitochondrial NIAUFX iron-sulfur cluster assembly complex.
DR IntAct; Q6P4F2; 3.
DR STRING; 9606.ENSP00000377311; -.
DR iPTMnet; Q6P4F2; -.
DR PhosphoSitePlus; Q6P4F2; -.
DR BioMuta; FDX2; -.
DR DMDM; 74749111; -.
DR EPD; Q6P4F2; -.
DR jPOST; Q6P4F2; -.
DR MassIVE; Q6P4F2; -.
DR MaxQB; Q6P4F2; -.
DR PaxDb; 9606-ENSP00000377311; -.
DR PeptideAtlas; Q6P4F2; -.
DR ProteomicsDB; 66974; -. [Q6P4F2-1]
DR ProteomicsDB; 72397; -.
DR Pumba; Q6P4F2; -.
DR Antibodypedia; 76687; 7 antibodies from 6 providers.
DR DNASU; 112812; -.
DR Ensembl; ENST00000393708.3; ENSP00000377311.5; ENSG00000267673.7. [Q6P4F2-1]
DR GeneID; 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 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 neXtProt; NX_Q6P4F2; -.
DR OpenTargets; ENSG00000267673; -.
DR PharmGKB; PA162388212; -.
DR VEuPathDB; HostDB:ENSG00000267673; -.
DR eggNOG; KOG3309; Eukaryota.
DR GeneTree; ENSGT00940000161143; -.
DR HOGENOM; CLU_082632_0_2_1; -.
DR InParanoid; Q6P4F2; -.
DR OMA; TTRRFWA; -.
DR OrthoDB; 36668at2759; -.
DR PhylomeDB; Q6P4F2; -.
DR TreeFam; TF354319; -.
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 BioGRID-ORCS; 112812; 490 hits in 1177 CRISPR screens.
DR ChiTaRS; FDX1L; human.
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 Genevisible; Q6P4F2; HS.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; NAS:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0022900; P:electron transport chain; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; NAS:ComplexPortal.
DR GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR CDD; cd00207; fer2; 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.
DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR23426:SF34; 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.
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; Reference proteome; Transit peptide;
KW 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.8, 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.8, 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.8, 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.8, 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 70..76
FT /evidence="ECO:0007829|PDB:2Y5C"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:2Y5C"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:2Y5C"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:2Y5C"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2Y5C"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:2Y5C"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:2Y5C"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:2Y5C"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:2Y5C"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:2Y5C"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2Y5C"
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
//
