CIAO1_HUMAN
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 03-AUG-2022, entry version 191.
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=14; IntAct=EBI-725145, EBI-752069;
CC O76071; Q9Y3D0: CIAO2B; NbExp=22; IntAct=EBI-725145, EBI-744045;
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=11; 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; 202.
DR CORUM; O76071; -.
DR IntAct; O76071; 86.
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; O76071; -.
DR PeptideAtlas; O76071; -.
DR PRIDE; O76071; -.
DR ProteomicsDB; 50373; -.
DR TopDownProteomics; O76071; -.
DR ABCD; O76071; 1 sequenced antibody.
DR Antibodypedia; 17416; 245 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 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; AIWSKSS; -.
DR OrthoDB; 793298at2759; -.
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; 670 hits in 1082 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 194 other tissues.
DR Genevisible; O76071; HS.
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 Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03037; ciao1; 1.
DR InterPro; IPR028608; CIAO1/Cia1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19920; PTHR19920; 1.
DR Pfam; PF00400; WD40; 6.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
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
