ID FBXW8_HUMAN Reviewed; 598 AA. AC Q8N3Y1; Q9UK95; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 27-MAR-2024, entry version 185. DE RecName: Full=F-box/WD repeat-containing protein 8; DE AltName: Full=F-box and WD-40 domain-containing protein 8; DE AltName: Full=F-box only protein 29; GN Name=FBXW8; Synonyms=FBW6, FBW8, FBX29, FBXO29, FBXW6; 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] (ISOFORM 2), AND VARIANT GLN-192. RX PubMed=10531037; DOI=10.1016/s0960-9822(00)80021-4; RA Winston J.T., Koepp D.M., Zhu C., Elledge S.J., Harper J.W.; RT "A family of mammalian F-box proteins."; RL Curr. Biol. 9:1180-1182(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-192. 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 IDENTIFICATION IN SCF-LIKE COMPLEX. RX PubMed=12481031; DOI=10.1073/pnas.252646399; RA Dias D.C., Dolios G., Wang R., Pan Z.Q.; RT "CUL7: a DOC domain-containing cullin selectively binds Skp1.Fbx29 to form RT an SCF-like complex."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16601-16606(2002). RN [5] RP IDENTIFICATION IN A COMPLEX WITH CUL7; SKP1; RBX1 AND GLMN. RX PubMed=12904573; DOI=10.1073/pnas.1733908100; RA Arai T., Kasper J.S., Skaar J.R., Ali S.H., Takahashi C., DeCaprio J.A.; RT "Targeted disruption of p185/Cul7 gene results in abnormal vascular RT morphogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:9855-9860(2003). RN [6] RP INTERACTION WITH CUL7. RX PubMed=17332328; DOI=10.1158/0008-5472.can-06-3241; RA Skaar J.R., Florens L., Tsutsumi T., Arai T., Tron A., Swanson S.K., RA Washburn M.P., DeCaprio J.A.; RT "PARC and CUL7 form atypical cullin RING ligase complexes."; RL Cancer Res. 67:2006-2014(2007). RN [7] RP FUNCTION, AND INTERACTION WITH IRS1. RX PubMed=18498745; DOI=10.1016/j.molcel.2008.03.009; RA Xu X., Sarikas A., Dias-Santagata D.C., Dolios G., Lafontant P.J., RA Tsai S.C., Zhu W., Nakajima H., Nakajima H.O., Field L.J., Wang R., RA Pan Z.Q.; RT "The CUL7 E3 ubiquitin ligase targets insulin receptor substrate 1 for RT ubiquitin-dependent degradation."; RL Mol. Cell 30:403-414(2008). RN [8] RP FUNCTION, INTERACTION WITH OBSL1; CUL1; CUL2; CUL7; SKP1; CCT6B; PFDN5; RP CCT2; CCT3; CCT6A; CCT7; VBP1; CCDC8; ARF1; TRIP13; PDCD5 AND GORASP1, AND RP SUBCELLULAR LOCATION. RX PubMed=21572988; DOI=10.1371/journal.pbio.1001060; RA Litterman N., Ikeuchi Y., Gallardo G., O'Connell B.C., Sowa M.E., RA Gygi S.P., Harper J.W., Bonni A.; RT "An OBSL1-Cul7Fbxw8 ubiquitin ligase signaling mechanism regulates Golgi RT morphology and dendrite patterning."; RL PLoS Biol. 9:E1001060-E1001060(2011). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [10] RP FUNCTION, AND INTERACTION WITH CUL7 AND MAP4K1. RX PubMed=24362026; DOI=10.1074/jbc.m113.520106; RA Wang H., Chen Y., Lin P., Li L., Zhou G., Liu G., Logsdon C., Jin J., RA Abbruzzese J.L., Tan T.H., Wang H.; RT "The CUL7/F-box and WD repeat domain containing 8 (CUL7/Fbxw8) ubiquitin RT ligase promotes degradation of hematopoietic progenitor kinase 1."; RL J. Biol. Chem. 289:4009-4017(2014). RN [11] RP FUNCTION. RX PubMed=24793695; DOI=10.1016/j.molcel.2014.03.047; RA Yan J., Yan F., Li Z., Sinnott B., Cappell K.M., Yu Y., Mo J., Duncan J.A., RA Chen X., Cormier-Daire V., Whitehurst A.W., Xiong Y.; RT "The 3M complex maintains microtubule and genome integrity."; RL Mol. Cell 54:791-804(2014). CC -!- FUNCTION: Substrate-recognition component of a Cul7-RING ubiquitin- CC protein ligase complex, which mediates the ubiquitination and CC subsequent proteasomal degradation of target proteins. The Cul7- CC RING(FBXW8) complex mediates ubiquitination and consequent degradation CC of GORASP1, acting as a component of the ubiquitin ligase pathway that CC regulates Golgi morphogenesis and dendrite patterning in brain CC (PubMed:21572988). Mediates ubiquitination and degradation of IRS1 in a CC mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and CC binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2) CC (PubMed:18498745). The Cul7-RING(FBXW8) complex also mediates CC ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated CC MAP4K1/HPK1, leading to its degradation, thereby affecting cell CC proliferation and differentiation (PubMed:24362026). Associated CC component of the 3M complex, suggesting that it mediates some of 3M CC complex functions (PubMed:24793695). {ECO:0000269|PubMed:18498745, CC ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24362026, CC ECO:0000269|PubMed:24793695}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Part of a Cul7-RING ubiquitin-protein ligase complex, CC consisting of CUL7, RBX1, SKP1 and FBXW8. Interacts with GLMN isoform CC 1. Interacts with CUL7. Interacts with OBSL1, CUL1, CUL2, SKP1, CCT6B, CC PFDN5, CCT2, CCT3, CCT6A, CCT7, VBP1, CCDC8, ARF1, TRIP13, PDCD5 and CC GORASP1. Interacts with IRS1 (when phosphorylated). Interacts with CC MAP4K1/HPK1 (when autophosphorylated). Associated component of the 3M CC complex. Interacts with POUF51 (when phosphorylated on 'Ser-355') (By CC similarity). {ECO:0000250|UniProtKB:Q8BIA4, CC ECO:0000269|PubMed:12481031, ECO:0000269|PubMed:12904573, CC ECO:0000269|PubMed:17332328, ECO:0000269|PubMed:18498745, CC ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24362026}. CC -!- INTERACTION: CC Q8N3Y1; P01106: MYC; NbExp=3; IntAct=EBI-914770, EBI-447544; CC Q8N3Y1; P63208: SKP1; NbExp=2; IntAct=EBI-914770, EBI-307486; CC Q8N3Y1-2; B1WBR1: Gorasp1; Xeno; NbExp=2; IntAct=EBI-15927105, EBI-15927064; CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:21572988}. Golgi apparatus CC {ECO:0000269|PubMed:21572988}. Note=Colocalizes with CUL7 at the Golgi CC apparatus in neurons. {ECO:0000250|UniProtKB:P0DL28}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8N3Y1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N3Y1-2; Sequence=VSP_008501; CC -!- SEQUENCE CAUTION: CC Sequence=AAF03129.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF03129.1; Type=Frameshift; 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; AF176707; AAF03129.1; ALT_SEQ; mRNA. DR EMBL; AC026368; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC083806; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC127164; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC037296; AAH37296.1; -; mRNA. DR CCDS; CCDS44988.1; -. [Q8N3Y1-2] DR CCDS; CCDS9182.1; -. [Q8N3Y1-1] DR RefSeq; NP_036306.1; NM_012174.1. [Q8N3Y1-2] DR RefSeq; NP_699179.2; NM_153348.2. [Q8N3Y1-1] DR PDB; 7Z8B; EM; 2.80 A; F=1-598. DR PDBsum; 7Z8B; -. DR AlphaFoldDB; Q8N3Y1; -. DR EMDB; EMD-14547; -. DR SMR; Q8N3Y1; -. DR BioGRID; 117645; 154. DR ComplexPortal; CPX-7784; SCF E3 ubiquitin ligase complex, FBXW8-CUL7 variant. DR CORUM; Q8N3Y1; -. DR DIP; DIP-37970N; -. DR IntAct; Q8N3Y1; 36. DR MINT; Q8N3Y1; -. DR STRING; 9606.ENSP00000498999; -. DR GlyGen; Q8N3Y1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8N3Y1; -. DR PhosphoSitePlus; Q8N3Y1; -. DR BioMuta; FBXW8; -. DR DMDM; 296434513; -. DR EPD; Q8N3Y1; -. DR jPOST; Q8N3Y1; -. DR MassIVE; Q8N3Y1; -. DR MaxQB; Q8N3Y1; -. DR PaxDb; 9606-ENSP00000310686; -. DR PeptideAtlas; Q8N3Y1; -. DR ProteomicsDB; 71847; -. [Q8N3Y1-1] DR ProteomicsDB; 71848; -. [Q8N3Y1-2] DR Pumba; Q8N3Y1; -. DR Antibodypedia; 31322; 162 antibodies from 21 providers. DR DNASU; 26259; -. DR Ensembl; ENST00000455858.2; ENSP00000389144.2; ENSG00000174989.13. [Q8N3Y1-2] DR Ensembl; ENST00000652555.1; ENSP00000498999.1; ENSG00000174989.13. [Q8N3Y1-1] DR GeneID; 26259; -. DR KEGG; hsa:26259; -. DR MANE-Select; ENST00000652555.1; ENSP00000498999.1; NM_153348.3; NP_699179.2. DR UCSC; uc001twf.2; human. [Q8N3Y1-1] DR AGR; HGNC:13597; -. DR CTD; 26259; -. DR DisGeNET; 26259; -. DR GeneCards; FBXW8; -. DR HGNC; HGNC:13597; FBXW8. DR HPA; ENSG00000174989; Low tissue specificity. DR MIM; 609073; gene. DR neXtProt; NX_Q8N3Y1; -. DR OpenTargets; ENSG00000174989; -. DR PharmGKB; PA28039; -. DR VEuPathDB; HostDB:ENSG00000174989; -. DR eggNOG; KOG0274; Eukaryota. DR GeneTree; ENSGT00390000017221; -. DR HOGENOM; CLU_024087_1_0_1; -. DR InParanoid; Q8N3Y1; -. DR OMA; VFQECRA; -. DR OrthoDB; 5391593at2759; -. DR PhylomeDB; Q8N3Y1; -. DR TreeFam; TF332593; -. DR PathwayCommons; Q8N3Y1; -. DR Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q8N3Y1; -. DR SIGNOR; Q8N3Y1; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 26259; 9 hits in 1193 CRISPR screens. DR ChiTaRS; FBXW8; human. DR GeneWiki; FBXW8; -. DR GenomeRNAi; 26259; -. DR Pharos; Q8N3Y1; Tbio. DR PRO; PR:Q8N3Y1; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q8N3Y1; Protein. DR Bgee; ENSG00000174989; Expressed in stromal cell of endometrium and 108 other cell types or tissues. DR ExpressionAtlas; Q8N3Y1; baseline and differential. DR GO; GO:0005814; C:centriole; IBA:GO_Central. DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central. DR GO; GO:0031467; C:Cul7-RING ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IEA:Ensembl. DR GO; GO:0008283; P:cell population proliferation; IDA:UniProtKB. DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central. DR GO; GO:0007030; P:Golgi organization; IGI:UniProtKB. DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl. DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IDA:UniProtKB. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0060712; P:spongiotrophoblast layer development; IEA:Ensembl. DR CDD; cd22134; F-box_FBXW8; 1. DR Gene3D; 1.20.1280.50; -; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR036047; F-box-like_dom_sf. DR InterPro; IPR001810; F-box_dom. DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR19855:SF16; F-BOX DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR19855; WD40 REPEAT PROTEIN 12, 37; 1. DR Pfam; PF12937; F-box-like; 1. DR SMART; SM00256; FBOX; 1. DR SMART; SM00320; WD40; 5. DR SUPFAM; SSF81383; F-box domain; 1. DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1. DR PROSITE; PS50181; FBOX; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. DR Genevisible; Q8N3Y1; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Golgi apparatus; Phosphoprotein; Reference proteome; Repeat; KW Ubl conjugation pathway; WD repeat. FT CHAIN 1..598 FT /note="F-box/WD repeat-containing protein 8" FT /id="PRO_0000050997" FT DOMAIN 113..159 FT /note="F-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080" FT REPEAT 197..245 FT /note="WD 1" FT REPEAT 254..294 FT /note="WD 2" FT REPEAT 297..336 FT /note="WD 3" FT REPEAT 430..470 FT /note="WD 4" FT REPEAT 473..510 FT /note="WD 5" FT REGION 17..93 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 17..42 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 83 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BIA4" FT MOD_RES 85 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BIA4" FT VAR_SEQ 41..106 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10531037" FT /id="VSP_008501" FT VARIANT 192 FT /note="R -> Q (in dbSNP:rs4076700)" FT /evidence="ECO:0000269|PubMed:10531037, FT ECO:0000269|PubMed:15489334" FT /id="VAR_060326" FT VARIANT 211 FT /note="T -> A (in dbSNP:rs36021180)" FT /id="VAR_057597" FT VARIANT 536 FT /note="T -> M (in dbSNP:rs3741466)" FT /id="VAR_057598" FT VARIANT 563 FT /note="V -> M (in dbSNP:rs56350562)" FT /id="VAR_062096" FT CONFLICT 46 FT /note="G -> S (in Ref. 3; AAH37296)" FT /evidence="ECO:0000305" FT CONFLICT 58 FT /note="R -> G (in Ref. 3; AAH37296)" FT /evidence="ECO:0000305" FT CONFLICT 380 FT /note="L -> I (in Ref. 3; AAH37296)" FT /evidence="ECO:0000305" FT CONFLICT 510 FT /note="E -> K (in Ref. 1; AAF03129)" FT /evidence="ECO:0000305" FT HELIX 122..129 FT /evidence="ECO:0007829|PDB:7Z8B" FT HELIX 133..136 FT /evidence="ECO:0007829|PDB:7Z8B" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:7Z8B" FT HELIX 144..150 FT /evidence="ECO:0007829|PDB:7Z8B" FT HELIX 153..163 FT /evidence="ECO:0007829|PDB:7Z8B" FT TURN 171..173 FT /evidence="ECO:0007829|PDB:7Z8B" FT HELIX 177..196 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 200..204 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 213..227 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 232..236 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 239..241 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 262..267 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 269..276 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 279..285 FT /evidence="ECO:0007829|PDB:7Z8B" FT TURN 286..288 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 293..297 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 304..307 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 309..312 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 314..317 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 319..326 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 334..340 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 355..357 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 359..364 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 367..372 FT /evidence="ECO:0007829|PDB:7Z8B" FT TURN 373..376 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 377..382 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 384..386 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 388..393 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 395..402 FT /evidence="ECO:0007829|PDB:7Z8B" FT TURN 406..409 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 413..418 FT /evidence="ECO:0007829|PDB:7Z8B" FT TURN 419..421 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 424..428 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 435..439 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 441..443 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 447..452 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 455..461 FT /evidence="ECO:0007829|PDB:7Z8B" FT TURN 462..464 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 467..472 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 478..483 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 488..492 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 495..501 FT /evidence="ECO:0007829|PDB:7Z8B" FT TURN 502..505 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 506..512 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 517..523 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 526..531 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 555..561 FT /evidence="ECO:0007829|PDB:7Z8B" FT HELIX 563..565 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 567..569 FT /evidence="ECO:0007829|PDB:7Z8B" FT STRAND 571..575 FT /evidence="ECO:0007829|PDB:7Z8B" FT HELIX 580..592 FT /evidence="ECO:0007829|PDB:7Z8B" SQ SEQUENCE 598 AA; 67394 MW; 03B3C283BA46DB6B CRC64; MDDYSLDEFR RRWQEELAQA QAPKKRRRPE AAERRARRPE VGSGRGEQAS GDPALAQRLL EGAGRPPAAR ATRAEGQDVA SRSRSPLARE GAGGGEQLVD QLIRDLNEMN DVPFFDIQLP YELAINIFQY LDRKELGRCA QVSKTWKVIA EDEVLWYRLC QQEGHLPDSS ISDYSCWKLI FQECRAKEHM LRTNWKNRKG AVSELEHVPD TVLCDVHSHD GVVIAGYTSG DVRVWDTRTW DYVAPFLESE DEEDEPGMQP NVSFVRINSS LAVAAYEDGF LNIWDLRTGK YPVHRFEHDA RIQALALSQD DATVATASAF DVVMLSPNEE GYWQIAAEFE VPKLVQYLEI VPETRRYPVA VAAAGDLMYL LKAEDSARTL LYAHGPPVTC LDVSANQVAF GVQGLGWVYE GSKILVYSLE AGRRLLKLGN VLRDFTCVNL SDSPPNLMVS GNMDGRVRIH DLRSGNIALS LSAHQLRVSA VQMDDWKIVS GGEEGLVSVW DYRMNQKLWE VYSGHPVQHI SFSSHSLITA NVPYQTVMRN ADLDSFTTHR RHRGLIRAYE FAVDQLAFQS PLPVCRSSCD AMATHYYDLA LAFPYNHV //