ID   CIAO1_HUMAN             Reviewed;         339 AA.
AC   O76071; A0MNN9; Q53FM5;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=Probable cytosolic iron-sulfur protein assembly protein CIAO1 {ECO:0000255|HAMAP-Rule:MF_03037};
DE   AltName: Full=WD repeat-containing protein 39 {ECO:0000255|HAMAP-Rule:MF_03037};
GN   Name=CIAO1 {ECO:0000255|HAMAP-Rule:MF_03037};
GN   Synonyms=CIA1 {ECO:0000303|PubMed:23891004}, WDR39;
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 [MRNA], AND INTERACTION WITH WT1.
RX   PubMed=9556563; DOI=10.1074/jbc.273.18.10880;
RA   Johnstone R.W., Wang J., Tommerup N., Vissing H., Roberts T., Shi Y.;
RT   "Ciao 1 is a novel WD40 protein that interacts with the tumor suppressor
RT   protein WT1.";
RL   J. Biol. Chem. 273:10880-10887(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=17041588; DOI=10.1038/ncb1490;
RA   Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H.;
RT   "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins
RT   and regulates histone methylation.";
RL   Nat. Cell Biol. 8:1277-1283(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA   Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA   Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA   Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA   Adams M.D.;
RT   "Genome duplications and other features in 12 Mb of DNA sequence from human
RT   chromosome 16p and 16q.";
RL   Genomics 60:295-308(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastric mucosa;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Blood, and Skin;
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   [7]
RP   CHARACTERIZATION.
RX   PubMed=10438340; DOI=10.1007/s002510050571;
RA   Johnstone R.W., Tommerup N., Hansen C., Vissing H., Shi Y.;
RT   "Structural organization, tissue expression, and chromosomal localization
RT   of Ciao 1, a functional modulator of the Wilms' tumor suppressor, WT1.";
RL   Immunogenetics 49:900-905(1999).
RN   [8]
RP   FUNCTION.
RX   PubMed=17937914; DOI=10.1016/j.str.2007.08.009;
RA   Srinivasan V., Netz D.J.A., Webert H., Mascarenhas J., Pierik A.J.,
RA   Michel H., Lill R.;
RT   "Structure of the yeast WD40 domain protein Cia1, a component acting late
RT   in iron-sulfur protein biogenesis.";
RL   Structure 15:1246-1257(2007).
RN   [9]
RP   FUNCTION, AND IDENTIFICATION IN MMXD COMPLEX.
RX   PubMed=20797633; DOI=10.1016/j.molcel.2010.07.029;
RA   Ito S., Tan L.J., Andoh D., Narita T., Seki M., Hirano Y., Narita K.,
RA   Kuraoka I., Hiraoka Y., Tanaka K.;
RT   "MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in chromosome
RT   segregation.";
RL   Mol. Cell 39:632-640(2010).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   INTERACTION WITH CIAO2A.
RX   PubMed=22683786; DOI=10.1107/s0907444912006592;
RA   Chen K.E., Richards A.A., Ariffin J.K., Ross I.L., Sweet M.J., Kellie S.,
RA   Kobe B., Martin J.L.;
RT   "The mammalian DUF59 protein Fam96a forms two distinct types of domain-
RT   swapped dimer.";
RL   Acta Crystallogr. D 68:637-648(2012).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [13]
RP   IDENTIFICATION IN THE CIA COMPLEX.
RX   PubMed=22678362; DOI=10.1126/science.1219723;
RA   Stehling O., Vashisht A.A., Mascarenhas J., Jonsson Z.O., Sharma T.,
RA   Netz D.J., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT   "MMS19 assembles iron-sulfur proteins required for DNA metabolism and
RT   genomic integrity.";
RL   Science 337:195-199(2012).
RN   [14]
RP   IDENTIFICATION IN THE CIA COMPLEX.
RX   PubMed=22678361; DOI=10.1126/science.1219664;
RA   Gari K., Leon Ortiz A.M., Borel V., Flynn H., Skehel J.M., Boulton S.J.;
RT   "MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA metabolism.";
RL   Science 337:243-245(2012).
RN   [15]
RP   FUNCTION, IDENTIFICATION IN THE CIA COMPLEX, AND INTERACTION WITH CHD1L;
RP   CIAO2A; CIAO2B; ERCC2; IREB2; MMS19 AND POLD1.
RX   PubMed=23891004; DOI=10.1016/j.cmet.2013.06.015;
RA   Stehling O., Mascarenhas J., Vashisht A.A., Sheftel A.D., Niggemeyer B.,
RA   Roesser R., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT   "Human CIA2A-FAM96A and CIA2B-FAM96B integrate iron homeostasis and
RT   maturation of different subsets of cytosolic-nuclear iron-sulfur
RT   proteins.";
RL   Cell Metab. 18:187-198(2013).
RN   [16]
RP   ERRATUM OF PUBMED:23891004.
RX   PubMed=29320706; DOI=10.1016/j.cmet.2017.12.009;
RA   Stehling O., Mascarenhas J., Vashisht A.A., Sheftel A.D., Niggemeyer B.,
RA   Roesser R., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT   "Human CIA2A-FAM96A and CIA2B-FAM96B Integrate Iron Homeostasis and
RT   Maturation of Different Subsets of Cytosolic-Nuclear Iron-Sulfur
RT   Proteins.";
RL   Cell Metab. 27:263-263(2018).
RN   [17]
RP   IDENTIFICATION IN THE CIA COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH CIAO2B AND CIAO3.
RX   PubMed=23585563; DOI=10.1074/jbc.m112.416602;
RA   Seki M., Takeda Y., Iwai K., Tanaka K.;
RT   "IOP1 protein is an external component of the human cytosolic iron-sulfur
RT   cluster assembly (CIA) machinery and functions in the MMS19 protein-
RT   dependent CIA pathway.";
RL   J. Biol. Chem. 288:16680-16689(2013).
RN   [18]
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   [19]
RP   INTERACTION WITH HSC20, ROLE OF LYR MOTIF, AND MUTAGENESIS OF
RP   87-ILE--ARG-89 AND 176-LYS--ARG-178.
RX   PubMed=29309586; DOI=10.1093/hmg/ddy004;
RA   Kim K.S., Maio N., Singh A., Rouault T.A.;
RT   "Cytosolic HSC20 integrates de novo iron-sulfur cluster biogenesis with the
RT   CIAO1-mediated transfer to recipients.";
RL   Hum. Mol. Genet. 27:837-852(2018).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   PubMed=21468892; DOI=10.1007/s13238-011-1018-1;
RA   Xu C., Min J.;
RT   "Structure and function of WD40 domain proteins.";
RL   Protein Cell 2:202-214(2011).
CC   -!- FUNCTION: Key component of the cytosolic iron-sulfur protein assembly
CC       (CIA) complex, a multiprotein complex that mediates the incorporation
CC       of iron-sulfur cluster into extramitochondrial Fe/S proteins
CC       (PubMed:17937914, PubMed:23891004). As a CIA complex component,
CC       interacts specifically with CIAO2A or CIAO2B and MMS19 to assist
CC       different branches of iron-sulfur protein assembly, depending of its
CC       interactors. The complex CIAO1:CIAO2B:MMS19 binds to and facilitates
CC       the assembly of most cytosolic-nuclear Fe/S proteins. CIAO1:CIAO2A
CC       specifically matures ACO1 and stabilizes IREB2 (PubMed:23891004). Seems
CC       to specifically modulate the transactivation activity of WT1
CC       (PubMed:9556563). As part of the mitotic spindle-associated MMXD
CC       complex it may play a role in chromosome segregation (PubMed:20797633).
CC       {ECO:0000255|HAMAP-Rule:MF_03037, ECO:0000269|PubMed:17937914,
CC       ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:23891004,
CC       ECO:0000269|PubMed:9556563}.
CC   -!- SUBUNIT: Component of the CIA complex (PubMed:22678361,
CC       PubMed:22678362, PubMed:23585563). Interacts with CIAO2A and forms a
CC       complex with CIAO2B and MMS19; the interactions with CIAO2A and CIAO2B
CC       are mutually exclusive (PubMed:22683786, PubMed:23891004,
CC       PubMed:23585563). Interacts with CHD1L, ERCC2, IREB2 and POLD1
CC       (PubMed:23891004). Component of the MMXD complex, which includes CIAO1,
CC       ERCC2, CIAO2B, MMS19 and SLC25A5 (PubMed:20797633). Interacts with WT1
CC       (PubMed:9556563). Interacts with CIAO3 (PubMed:23585563). Interacts
CC       (via LYR motif) with HSC20 (PubMed:29309586). {ECO:0000255|HAMAP-
CC       Rule:MF_03037, ECO:0000269|PubMed:20797633,
CC       ECO:0000269|PubMed:22678361, ECO:0000269|PubMed:22678362,
CC       ECO:0000269|PubMed:22683786, ECO:0000269|PubMed:23585563,
CC       ECO:0000269|PubMed:23891004, ECO:0000269|PubMed:29309586,
CC       ECO:0000269|PubMed:9556563}.
CC   -!- INTERACTION:
CC       O76071; Q3KP44: ANKRD55; NbExp=3; IntAct=EBI-725145, EBI-14493093;
CC       O76071; Q6NX55: C19orf2; NbExp=3; IntAct=EBI-725145, EBI-18333234;
CC       O76071; Q9H5X1: CIAO2A; NbExp=17; IntAct=EBI-725145, EBI-752069;
CC       O76071; Q9Y3D0: CIAO2B; NbExp=24; IntAct=EBI-725145, EBI-744045;
CC       O76071; P18074: ERCC2; NbExp=2; IntAct=EBI-725145, EBI-6380590;
CC       O76071; Q68CZ6: HAUS3; NbExp=3; IntAct=EBI-725145, EBI-2558217;
CC       O76071; P50221: MEOX1; NbExp=3; IntAct=EBI-725145, EBI-2864512;
CC       O76071; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-725145, EBI-16439278;
CC       O76071; Q96T76: MMS19; NbExp=13; IntAct=EBI-725145, EBI-1044169;
CC       O76071; Q96T76-8: MMS19; NbExp=5; IntAct=EBI-725145, EBI-10190644;
CC       O76071; O00264: PGRMC1; NbExp=5; IntAct=EBI-725145, EBI-1045534;
CC       O76071; P41220: RGS2; NbExp=3; IntAct=EBI-725145, EBI-712388;
CC       O76071; Q8WXG1: RSAD2; NbExp=2; IntAct=EBI-725145, EBI-12736320;
CC       O76071; Q15637: SF1; NbExp=3; IntAct=EBI-725145, EBI-744603;
CC       O76071; Q6ZSJ9: SHISA6; NbExp=3; IntAct=EBI-725145, EBI-12037847;
CC       O76071; Q9Y6M7: SLC4A7; NbExp=3; IntAct=EBI-725145, EBI-1044546;
CC       O76071; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-725145, EBI-3923210;
CC       O76071; O95985: TOP3B; NbExp=3; IntAct=EBI-725145, EBI-373403;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23585563}.
CC   -!- MISCELLANEOUS: 'Ciao' means 'bridge' in Chinese.
CC   -!- SIMILARITY: Belongs to the WD repeat CIA1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03037}.
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DR   EMBL; U63810; AAC24948.1; -; mRNA.
DR   EMBL; EF011618; ABK41108.1; -; mRNA.
DR   EMBL; AC004020; AAC23493.1; -; Genomic_DNA.
DR   EMBL; CR456802; CAG33083.1; -; mRNA.
DR   EMBL; AK223257; BAD96977.1; -; mRNA.
DR   EMBL; BC001395; AAH01395.1; -; mRNA.
DR   EMBL; BC032812; AAH32812.1; -; mRNA.
DR   CCDS; CCDS2019.1; -.
DR   RefSeq; NP_004795.1; NM_004804.2.
DR   PDB; 3FM0; X-ray; 1.70 A; A=1-339.
DR   PDBsum; 3FM0; -.
DR   AlphaFoldDB; O76071; -.
DR   SMR; O76071; -.
DR   BioGRID; 114791; 327.
DR   ComplexPortal; CPX-2837; CIAO1-CIAO2B-CIAO3-MMS19 cytosolic iron-sulfur protein assembly complex.
DR   ComplexPortal; CPX-2840; CIAO1-CIAO2A-CIAO3 cytosolic iron-sulfur protein assembly complex.
DR   CORUM; O76071; -.
DR   IntAct; O76071; 88.
DR   MINT; O76071; -.
DR   STRING; 9606.ENSP00000418287; -.
DR   GlyGen; O76071; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O76071; -.
DR   MetOSite; O76071; -.
DR   PhosphoSitePlus; O76071; -.
DR   SwissPalm; O76071; -.
DR   BioMuta; CIAO1; -.
DR   EPD; O76071; -.
DR   jPOST; O76071; -.
DR   MassIVE; O76071; -.
DR   MaxQB; O76071; -.
DR   PaxDb; 9606-ENSP00000418287; -.
DR   PeptideAtlas; O76071; -.
DR   ProteomicsDB; 50373; -.
DR   Pumba; O76071; -.
DR   TopDownProteomics; O76071; -.
DR   ABCD; O76071; 1 sequenced antibody.
DR   Antibodypedia; 17416; 266 antibodies from 29 providers.
DR   DNASU; 9391; -.
DR   Ensembl; ENST00000488633.2; ENSP00000418287.1; ENSG00000144021.3.
DR   GeneID; 9391; -.
DR   KEGG; hsa:9391; -.
DR   MANE-Select; ENST00000488633.2; ENSP00000418287.1; NM_004804.3; NP_004795.1.
DR   UCSC; uc002svs.4; human.
DR   AGR; HGNC:14280; -.
DR   CTD; 9391; -.
DR   DisGeNET; 9391; -.
DR   GeneCards; CIAO1; -.
DR   HGNC; HGNC:14280; CIAO1.
DR   HPA; ENSG00000144021; Low tissue specificity.
DR   MIM; 604333; gene.
DR   neXtProt; NX_O76071; -.
DR   OpenTargets; ENSG00000144021; -.
DR   PharmGKB; PA162382269; -.
DR   VEuPathDB; HostDB:ENSG00000144021; -.
DR   eggNOG; KOG0645; Eukaryota.
DR   GeneTree; ENSGT00940000158670; -.
DR   HOGENOM; CLU_000288_57_8_1; -.
DR   InParanoid; O76071; -.
DR   OMA; IREIRWS; -.
DR   OrthoDB; 5486866at2759; -.
DR   PhylomeDB; O76071; -.
DR   TreeFam; TF318181; -.
DR   PathwayCommons; O76071; -.
DR   Reactome; R-HSA-2564830; Cytosolic iron-sulfur cluster assembly.
DR   SignaLink; O76071; -.
DR   BioGRID-ORCS; 9391; 705 hits in 1170 CRISPR screens.
DR   ChiTaRS; CIAO1; human.
DR   EvolutionaryTrace; O76071; -.
DR   GeneWiki; CIAO1; -.
DR   GenomeRNAi; 9391; -.
DR   Pharos; O76071; Tbio.
DR   PRO; PR:O76071; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; O76071; Protein.
DR   Bgee; ENSG00000144021; Expressed in right adrenal gland cortex and 196 other cell types or tissues.
DR   GO; GO:0097361; C:CIA complex; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0071817; C:MMXD complex; IDA:UniProtKB.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR   GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   HAMAP; MF_03037; ciao1; 1.
DR   InterPro; IPR028608; CIAO1/Cia1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19920:SF0; CYTOSOLIC IRON-SULFUR PROTEIN ASSEMBLY PROTEIN CIAO1-RELATED; 1.
DR   PANTHER; PTHR19920; WD40 PROTEIN CIAO1; 1.
DR   Pfam; PF00400; WD40; 6.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   Genevisible; O76071; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Chromosome partition; Cytoplasm; Reference proteome; Repeat;
KW   WD repeat.
FT   CHAIN           1..339
FT                   /note="Probable cytosolic iron-sulfur protein assembly
FT                   protein CIAO1"
FT                   /id="PRO_0000051389"
FT   REPEAT          14..53
FT                   /note="WD 1"
FT   REPEAT          59..98
FT                   /note="WD 2"
FT   REPEAT          103..142
FT                   /note="WD 3"
FT   REPEAT          148..187
FT                   /note="WD 4"
FT   REPEAT          192..231
FT                   /note="WD 5"
FT   REPEAT          250..289
FT                   /note="WD 6"
FT   REPEAT          301..339
FT                   /note="WD 7"
FT   MOTIF           176..178
FT                   /note="LYR motif; required for interaction with HSC20"
FT                   /evidence="ECO:0000269|PubMed:29309586"
FT   MUTAGEN         87..89
FT                   /note="IWK->AAA: Does not affect binding to HSC20."
FT                   /evidence="ECO:0000269|PubMed:29309586"
FT   MUTAGEN         176..178
FT                   /note="LYR->AAA: Abolishes binding to HSC20."
FT                   /evidence="ECO:0000269|PubMed:29309586"
FT   CONFLICT        243
FT                   /note="C -> G (in Ref. 5; BAD96977)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..11
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          19..24
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          31..35
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          40..46
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          49..56
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          64..69
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          73..80
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          85..90
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          108..113
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          117..124
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          129..134
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          140..146
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          153..158
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          160..163
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          165..169
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          174..180
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          183..190
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          197..202
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          206..213
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          218..224
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          240..247
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          255..260
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   TURN            262..264
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          267..271
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          276..281
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          292..298
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          301..304
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          306..311
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          313..315
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          318..323
FT                   /evidence="ECO:0007829|PDB:3FM0"
FT   STRAND          328..333
FT                   /evidence="ECO:0007829|PDB:3FM0"
SQ   SEQUENCE   339 AA;  37840 MW;  63A8D8257A204FC8 CRC64;
     MKDSLVLLGR VPAHPDSRCW FLAWNPAGTL LASCGGDRRI RIWGTEGDSW ICKSVLSEGH
     QRTVRKVAWS PCGNYLASAS FDATTCIWKK NQDDFECVTT LEGHENEVKS VAWAPSGNLL
     ATCSRDKSVW VWEVDEEDEY ECVSVLNSHT QDVKHVVWHP SQELLASASY DDTVKLYREE
     EDDWVCCATL EGHESTVWSL AFDPSGQRLA SCSDDRTVRI WRQYLPGNEQ GVACSGSDPS
     WKCICTLSGF HSRTIYDIAW CQLTGALATA CGDDAIRVFQ EDPNSDPQQP TFSLTAHLHQ
     AHSQDVNCVA WNPKEPGLLA SCSDDGEVAF WKYQRPEGL
//