ID   FXL17_HUMAN             Reviewed;         701 AA.
AC   Q9UF56; A1A4E3;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 3.
DT   10-JUN-2026, entry version 188.
DE   RecName: Full=F-box/LRR-repeat protein 17 {ECO:0000303|PubMed:24035498};
DE   AltName: Full=F-box and leucine-rich repeat protein 17 {ECO:0000305};
DE   AltName: Full=F-box only protein 13 {ECO:0000250|UniProtKB:Q9QZN1};
GN   Name=FBXL17 {ECO:0000303|PubMed:24035498,
GN   ECO:0000312|HGNC:HGNC:13615};
GN   Synonyms=FBL17 {ECO:0000312|HGNC:HGNC:13615}, FBX13
GN   {ECO:0000250|UniProtKB:Q9QZN1}, FBXO13 {ECO:0000312|HGNC:HGNC:13615};
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] (ISOFORM 2).
RC   TISSUE=Cerebellum;
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 MRNA] (ISOFORM 3).
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [6]
RP   FUNCTION, IDENTIFICATION IN THE SCF(FBXL17) COMPLEX, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=24035498; DOI=10.1016/j.molcel.2013.08.018;
RA   Tan M.K., Lim H.J., Bennett E.J., Shi Y., Harper J.W.;
RT   "Parallel SCF adaptor capture proteomics reveals a role for SCFFBXL17 in
RT   NRF2 activation via BACH1 repressor turnover.";
RL   Mol. Cell 52:9-24(2013).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SUFU.
RX   PubMed=27234298; DOI=10.15252/embj.201593374;
RA   Raducu M., Fung E., Serres S., Infante P., Barberis A., Fischer R.,
RA   Bristow C., Thezenas M.L., Finta C., Christianson J.C., Buffa F.M.,
RA   Kessler B.M., Sibson N.R., Di Marcotullio L., Toftgaard R.,
RA   D'Angiolella V.;
RT   "SCF (Fbxl17) ubiquitylation of Sufu regulates Hedgehog signaling and
RT   medulloblastoma development.";
RL   EMBO J. 35:1400-1416(2016).
RN   [8]
RP   FUNCTION, VARIANT ARG-627, AND CHARACTERIZATION OF VARIANT ARG-627.
RX   PubMed=30190310; DOI=10.1126/science.aap8236;
RA   Mena E.L., Kjolby R.A.S., Saxton R.A., Werner A., Lew B.G., Boyle J.M.,
RA   Harland R., Rape M.;
RT   "Dimerization quality control ensures neuronal development and survival.";
RL   Science 362:eaap8236-eaap8236(2018).
CC   -!- FUNCTION: Substrate-recognition component of the SCF(FBXL17) E3
CC       ubiquitin ligase complex, a key component of a quality control pathway
CC       required to ensure functional dimerization of BTB domain-containing
CC       proteins (dimerization quality control, DQC) (PubMed:30190310). FBXL17
CC       specifically recognizes and binds a conserved degron of non-consecutive
CC       residues present at the interface of BTB dimers of aberrant
CC       composition: aberrant BTB dimer are then ubiquitinated by the
CC       SCF(FBXL17) complex and degraded by the proteasome (PubMed:30190310).
CC       The ability of the SCF(FBXL17) complex to eliminate compromised BTB
CC       dimers is required for the differentiation and survival of neural crest
CC       and neuronal cells (By similarity). The SCF(FBXL17) complex mediates
CC       ubiquitination and degradation of BACH1 (PubMed:24035498,
CC       PubMed:30190310). The SCF(FBXL17) complex is also involved in the
CC       regulation of the hedgehog/smoothened (Hh) signaling pathway by
CC       mediating the ubiquitination and degradation of SUFU, allowing the
CC       release of GLI1 from SUFU for proper Hh signal transduction
CC       (PubMed:27234298). The SCF(FBXL17) complex mediates ubiquitination and
CC       degradation of PRMT1 (By similarity). {ECO:0000250|UniProtKB:B1H1X1,
CC       ECO:0000250|UniProtKB:Q9QZN1, ECO:0000269|PubMed:24035498,
CC       ECO:0000269|PubMed:27234298, ECO:0000269|PubMed:30190310}.
CC   -!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase
CC       complex SCF(FBXL17) composed of CUL1, SKP1, RBX1 and FBXL17
CC       (PubMed:24035498). Interacts with BTB domain-containing proteins such
CC       as KLHL12, BCL6 and BACH1; specifically recognizes and binds a
CC       conserved degron of non-consecutive residues present at the interface
CC       of BTB dimers of aberrant composition (PubMed:30190310). Interacts with
CC       SUFU (PubMed:27234298). Interacts with PRMT1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9QZN1, ECO:0000269|PubMed:24035498,
CC       ECO:0000269|PubMed:27234298, ECO:0000269|PubMed:30190310}.
CC   -!- INTERACTION:
CC       Q9UF56; Q8NFY9: KBTBD8; NbExp=3; IntAct=EBI-8835653, EBI-21328977;
CC       Q9UF56; Q53G59: KLHL12; NbExp=11; IntAct=EBI-8835653, EBI-740929;
CC       Q9UF56; P63208: SKP1; NbExp=17; IntAct=EBI-8835653, EBI-307486;
CC       Q9UF56; Q9UBP0: SPAST; NbExp=3; IntAct=EBI-8835653, EBI-1222832;
CC       Q9UF56; Q9UBP0-1: SPAST; NbExp=4; IntAct=EBI-8835653, EBI-36485974;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24035498}. Nucleus
CC       {ECO:0000269|PubMed:24035498, ECO:0000269|PubMed:27234298}.
CC       Note=Present in the cytoplasm and nucleus; more abundant in the
CC       cytoplasm. {ECO:0000269|PubMed:24035498}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9UF56-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UF56-3; Sequence=VSP_037034;
CC       Name=3;
CC         IsoId=Q9UF56-2; Sequence=VSP_037034, VSP_009476;
CC   -!- SIMILARITY: Belongs to the FBXL17 family. {ECO:0000305}.
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DR   EMBL; AK126722; BAC86658.1; -; mRNA.
DR   EMBL; AL133602; CAB63737.2; -; mRNA.
DR   EMBL; AC008462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC011419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471086; EAW49061.1; -; Genomic_DNA.
DR   EMBL; BC126144; AAI26145.1; -; mRNA.
DR   EMBL; BC126146; AAI26147.1; -; mRNA.
DR   CCDS; CCDS54886.1; -. [Q9UF56-1]
DR   PIR; T43444; T43444.
DR   RefSeq; NP_001156787.2; NM_001163315.3. [Q9UF56-1]
DR   PDB; 6W66; X-ray; 3.21 A; B=310-701.
DR   PDB; 6WCQ; EM; 8.50 A; B=310-701.
DR   PDB; 8UAH; EM; 3.30 A; B=310-701.
DR   PDB; 8UBT; EM; 3.10 A; C=310-701.
DR   PDB; 8UBU; EM; 4.60 A; D/K=310-701.
DR   PDB; 8UBV; EM; 4.10 A; B/H=310-701.
DR   PDBsum; 6W66; -.
DR   PDBsum; 6WCQ; -.
DR   PDBsum; 8UAH; -.
DR   PDBsum; 8UBT; -.
DR   PDBsum; 8UBU; -.
DR   PDBsum; 8UBV; -.
DR   AlphaFoldDB; Q9UF56; -.
DR   EMDB; EMD-21617; -.
DR   EMDB; EMD-42064; -.
DR   EMDB; EMD-42102; -.
DR   EMDB; EMD-42105; -.
DR   EMDB; EMD-42106; -.
DR   SMR; Q9UF56; -.
DR   BioGRID; 122315; 89.
DR   ComplexPortal; CPX-2773; SCF E3 ubiquitin ligase complex, FBXL17 variant.
DR   FunCoup; Q9UF56; 1517.
DR   IntAct; Q9UF56; 49.
DR   NDEx; IQUERY-CP-FBXL17; 2 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000437464; -.
DR   GlyGen; Q9UF56; 3 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UF56; -.
DR   PhosphoSitePlus; Q9UF56; -.
DR   SwissPalm; Q9UF56; -.
DR   BioMuta; FBXL17; -.
DR   DMDM; 229462981; -.
DR   jPOST; Q9UF56; -.
DR   MassIVE; Q9UF56; -.
DR   PaxDb; 9606-ENSP00000437464; -.
DR   PeptideAtlas; Q9UF56; -.
DR   ProteomicsDB; 84171; -. [Q9UF56-1]
DR   ProteomicsDB; 84172; -. [Q9UF56-2]
DR   ProteomicsDB; 84173; -. [Q9UF56-3]
DR   Pumba; Q9UF56; -.
DR   Antibodypedia; 25280; 121 antibodies from 17 providers.
DR   DNASU; 64839; -.
DR   Ensembl; ENST00000542267.7; ENSP00000437464.2; ENSG00000145743.18. [Q9UF56-1]
DR   GeneID; 64839; -.
DR   KEGG; hsa:64839; -.
DR   MANE-Select; ENST00000542267.7; ENSP00000437464.2; NM_001163315.3; NP_001156787.2.
DR   UCSC; uc003kon.5; human. [Q9UF56-1]
DR   AGR; HGNC:13615; -.
DR   ClinPGx; PA134920563; -.
DR   CTD; 64839; -.
DR   DisGeNET; 64839; -.
DR   GeneCards; FBXL17; -.
DR   HGNC; HGNC:13615; FBXL17.
DR   HPA; ENSG00000145743; Low tissue specificity.
DR   MIM; 609083; gene.
DR   OpenTargets; ENSG00000145743; -.
DR   VEuPathDB; HostDB:ENSG00000145743; -.
DR   eggNOG; KOG1947; Eukaryota.
DR   GeneTree; ENSGT00940000156973; -.
DR   HOGENOM; CLU_024577_3_0_1; -.
DR   InParanoid; Q9UF56; -.
DR   OMA; MGWIPSM; -.
DR   OrthoDB; 550575at2759; -.
DR   PAN-GO; Q9UF56; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9UF56; -.
DR   PathwayCommons; Q9UF56; -.
DR   Reactome; R-HSA-9708530; Regulation of BACH1 activity.
DR   SignaLink; Q9UF56; -.
DR   SIGNOR; Q9UF56; -.
DR   Agora; ENSG00000145743; -.
DR   BioGRID-ORCS; 64839; 21 hits in 1166 CRISPR screens.
DR   ChiTaRS; FBXL17; human.
DR   GenomeRNAi; 64839; -.
DR   Pharos; Q9UF56; Tbio.
DR   PRO; PR:Q9UF56; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9UF56; protein.
DR   Bgee; ENSG00000145743; Expressed in left ventricle myocardium and 201 other cell types or tissues.
DR   ExpressionAtlas; Q9UF56; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR   GO; GO:0014033; P:neural crest cell differentiation; ISS:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IDA:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:UniProtKB.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   CDD; cd22092; F-box_FBXO13; 1.
DR   FunFam; 3.80.10.10:FF:000161; F-box/LRR-repeat protein 17 isoform X1; 1.
DR   FunFam; 3.80.10.10:FF:000358; F-box/LRR-repeat protein 17 isoform X1; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR050648; F-box_LRR-repeat.
DR   InterPro; IPR057207; FBXL15_LRR.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR13382:SF72; F-BOX AND LEUCINE-RICH REPEAT PROTEIN 17; 1.
DR   PANTHER; PTHR13382; MITOCHONDRIAL ATP SYNTHASE COUPLING FACTOR B; 1.
DR   Pfam; PF12937; F-box-like; 1.
DR   Pfam; PF13516; LRR_6; 1.
DR   Pfam; PF25372; LRR_FBXL15; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00367; LRR_CC; 11.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Neurogenesis; Nucleus;
KW   Proteomics identification; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..701
FT                   /note="F-box/LRR-repeat protein 17"
FT                   /id="PRO_0000119865"
FT   DOMAIN          318..365
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..11
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..237
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..264
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..398
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT                   /id="VSP_037034"
FT   VAR_SEQ         657..701
FT                   /note="NEVTVEQLVQQYPHITFSTVLQDCKRTLERAYQMGWTPNMSAASS -> RVD
FT                   YQVVCFLHISIVNSLMSYPLSFSISTPVYYILYIHFICIYAIIAMHCLPAFVN (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_009476"
FT   VARIANT         627
FT                   /note="C -> R (impaired ability to bind substrate
FT                   proteins)"
FT                   /evidence="ECO:0000269|PubMed:30190310"
FT                   /id="VAR_081000"
FT   HELIX           321..323
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   HELIX           326..333
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   HELIX           338..342
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   HELIX           345..347
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   HELIX           350..356
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   TURN            359..361
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   STRAND          364..366
FT                   /evidence="ECO:0007829|PDB:6W66"
FT   TURN            371..373
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   HELIX           378..384
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   STRAND          389..392
FT                   /evidence="ECO:0007829|PDB:6W66"
FT   HELIX           401..403
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   TURN            404..406
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   HELIX           407..410
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   STRAND          416..418
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   HELIX           427..436
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   STRAND          442..444
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   HELIX           453..462
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   STRAND          468..470
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   HELIX           479..487
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   STRAND          494..497
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   HELIX           505..511
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   STRAND          520..523
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   HELIX           530..533
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   TURN            534..538
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   STRAND          544..546
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   HELIX           556..562
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   STRAND          570..572
FT                   /evidence="ECO:0007829|PDB:6W66"
FT   HELIX           581..590
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   STRAND          596..598
FT                   /evidence="ECO:0007829|PDB:6W66"
FT   HELIX           608..615
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   STRAND          621..623
FT                   /evidence="ECO:0007829|PDB:6W66"
FT   TURN            632..634
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   HELIX           635..641
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   STRAND          646..648
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   HELIX           660..667
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   STRAND          672..674
FT                   /evidence="ECO:0007829|PDB:6W66"
FT   TURN            676..681
FT                   /evidence="ECO:0007829|PDB:8UBT"
FT   HELIX           682..687
FT                   /evidence="ECO:0007829|PDB:8UBT"
SQ   SEQUENCE   701 AA;  75695 MW;  87B7792A9357C94C CRC64;
     MGHLLSKEPR NRPSQKRPRC CSWCRRRRPL LRLPRRTPAK VPPQPAAPRS RDCFFRGPCM
     LCFIVHSPGA PAPAGPEEEP PLSPPPRDGA YAAASSSQHL ARRYAALAAE DCAAAARRFL
     LSSAAAAAAA AASASSPASC CKELGLAAAA AWEQQGRSLF LASLGPVRFL GPPAAVQLFR
     GPTPSPAELP TPPEMVCKRK GAGVPACTPC KQPRCGGGGC GGGGGGGGGG GPAGGGASPP
     RPPDAGCCQA PEQPPQPLCP PPSSPTSEGA PTEAGGDAVR AGGTAPLSAQ QQHECGDADC
     RESPENPCDC HREPPPETPD INQLPPSILL KIFSNLSLDE RCLSASLVCK YWRDLCLDFQ
     FWKQLDLSSR QQVTDELLEK IASRSQNIIE INISDCRSMS DNGVCVLAFK CPGLLRYTAY
     RCKQLSDTSI IAVASHCPLL QKVHVGNQDK LTDEGLKQLG SKCRELKDIH FGQCYKISDE
     GMIVIAKGCL KLQRIYMQEN KLVTDQSVKA FAEHCPELQY VGFMGCSVTS KGVIHLTKLR
     NLSSLDLRHI TELDNETVME IVKRCKNLSS LNLCLNWIIN DRCVEVIAKE GQNLKELYLV
     SCKITDYALI AIGRYSMTIE TVDVGWCKEI TDQGATLIAQ SSKSLRYLGL MRCDKVNEVT
     VEQLVQQYPH ITFSTVLQDC KRTLERAYQM GWTPNMSAAS S
//