ID   FBX6_HUMAN              Reviewed;         293 AA.
AC   Q9NRD1; B1AK42; B2RC88; Q9UKT3;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   10-JUN-2026, entry version 192.
DE   RecName: Full=F-box only protein 6;
DE   AltName: Full=F-box protein that recognizes sugar chains 2;
DE   AltName: Full=F-box/G-domain protein 2;
GN   Name=FBXO6; Synonyms=FBG2, FBS2, FBX6;
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].
RX   PubMed=10531035; DOI=10.1016/s0960-9822(00)80020-2;
RA   Cenciarelli C., Chiaur D.S., Guardavaccaro D., Parks W., Vidal M.,
RA   Pagano M.;
RT   "Identification of a family of human F-box proteins.";
RL   Curr. Biol. 9:1177-1179(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10945468; DOI=10.1006/geno.2000.6211;
RA   Ilyin G.P., Rialland M., Pigeon C., Guguen-Guillouzo C.;
RT   "cDNA cloning and expression analysis of new members of the mammalian F-box
RT   protein family.";
RL   Genomics 67:40-47(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   FUNCTION, SUGAR-BINDING, INTERACTION WITH CUL1, AND MUTAGENESIS OF
RP   241-TYR-TRP-242.
RX   PubMed=18203720; DOI=10.1074/jbc.m709508200;
RA   Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L.;
RT   "Diversity in tissue expression, substrate binding, and SCF complex
RT   formation for a lectin family of ubiquitin ligases.";
RL   J. Biol. Chem. 283:12717-12729(2008).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A SCF PROTEIN LIGASE
RP   COMPLEX, AND INTERACTION WITH CHEK1.
RX   PubMed=19716789; DOI=10.1016/j.molcel.2009.06.030;
RA   Zhang Y.-W., Brognard J., Coughlin C., You Z., Dolled-Filhart M.,
RA   Aslanian A., Manning G., Abraham R.T., Hunter T.;
RT   "The F box protein Fbx6 regulates Chk1 stability and cellular sensitivity
RT   to replication stress.";
RL   Mol. Cell 35:442-453(2009).
RN   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-284, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Substrate-recognition component of some SCF (SKP1-CUL1-F-box
CC       protein)-type E3 ubiquitin ligase complexes. Involved in endoplasmic
CC       reticulum-associated degradation pathway (ERAD) for misfolded lumenal
CC       proteins by recognizing and binding sugar chains on unfolded
CC       glycoproteins that are retrotranslocated into the cytosol and promoting
CC       their ubiquitination and subsequent degradation. Able to recognize and
CC       bind denatured glycoproteins, which are modified with not only high-
CC       mannose but also complex-type oligosaccharides. Also recognizes
CC       sulfated glycans. Also involved in DNA damage response by specifically
CC       recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting
CC       its ubiquitination and degradation. Ubiquitination of CHEK1 is required
CC       to ensure that activated CHEK1 does not accumulate as cells progress
CC       through S phase, or when replication forks encounter transient
CC       impediments during normal DNA replication.
CC       {ECO:0000269|PubMed:18203720, ECO:0000269|PubMed:19716789}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with VCP (By similarity). Part of a SCF (SKP1-
CC       cullin-F-box) protein ligase complex. Interacts with CHEK1 and CUL1.
CC       {ECO:0000250, ECO:0000269|PubMed:18203720,
CC       ECO:0000269|PubMed:19716789}.
CC   -!- INTERACTION:
CC       Q9NRD1; Q13616: CUL1; NbExp=6; IntAct=EBI-3938499, EBI-359390;
CC       Q9NRD1; Q08380: LGALS3BP; NbExp=2; IntAct=EBI-3938499, EBI-354956;
CC       Q9NRD1; P63208: SKP1; NbExp=10; IntAct=EBI-3938499, EBI-307486;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19716789}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF04470.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=hFBG2;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_other_821";
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DR   EMBL; AF129536; AAF04470.1; ALT_INIT; mRNA.
DR   EMBL; AF233223; AAF67153.1; -; mRNA.
DR   EMBL; AK314989; BAG37485.1; -; mRNA.
DR   EMBL; AL031731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471130; EAW71696.1; -; Genomic_DNA.
DR   EMBL; BC020880; AAH20880.1; -; mRNA.
DR   CCDS; CCDS133.1; -.
DR   RefSeq; NP_060908.1; NM_018438.6.
DR   RefSeq; XP_005263505.1; XM_005263448.6.
DR   RefSeq; XP_005263506.1; XM_005263449.6.
DR   RefSeq; XP_005263508.1; XM_005263451.6.
DR   RefSeq; XP_011539534.1; XM_011541232.4.
DR   RefSeq; XP_054191929.1; XM_054335954.1.
DR   RefSeq; XP_054191930.1; XM_054335955.1.
DR   RefSeq; XP_054191931.1; XM_054335956.1.
DR   RefSeq; XP_054191932.1; XM_054335957.1.
DR   AlphaFoldDB; Q9NRD1; -.
DR   SMR; Q9NRD1; -.
DR   BioGRID; 117654; 736.
DR   ComplexPortal; CPX-7905; SCF E3 ubiquitin ligase complex, FBXO6 variant.
DR   CORUM; Q9NRD1; -.
DR   FunCoup; Q9NRD1; 671.
DR   IntAct; Q9NRD1; 158.
DR   MINT; Q9NRD1; -.
DR   STRING; 9606.ENSP00000365944; -.
DR   iPTMnet; Q9NRD1; -.
DR   PhosphoSitePlus; Q9NRD1; -.
DR   BioMuta; FBXO6; -.
DR   DMDM; 24636846; -.
DR   jPOST; Q9NRD1; -.
DR   MassIVE; Q9NRD1; -.
DR   PaxDb; 9606-ENSP00000365944; -.
DR   PeptideAtlas; Q9NRD1; -.
DR   ProteomicsDB; 82338; -.
DR   Pumba; Q9NRD1; -.
DR   Antibodypedia; 28155; 241 antibodies from 28 providers.
DR   DNASU; 26270; -.
DR   Ensembl; ENST00000376753.9; ENSP00000365944.4; ENSG00000116663.12.
DR   Ensembl; ENST00000907480.1; ENSP00000577539.1; ENSG00000116663.12.
DR   Ensembl; ENST00000907481.1; ENSP00000577540.1; ENSG00000116663.12.
DR   Ensembl; ENST00000907482.1; ENSP00000577541.1; ENSG00000116663.12.
DR   Ensembl; ENST00000907483.1; ENSP00000577542.1; ENSG00000116663.12.
DR   Ensembl; ENST00000907484.1; ENSP00000577543.1; ENSG00000116663.12.
DR   Ensembl; ENST00000961666.1; ENSP00000631725.1; ENSG00000116663.12.
DR   Ensembl; ENST00000961667.1; ENSP00000631726.1; ENSG00000116663.12.
DR   GeneID; 26270; -.
DR   KEGG; hsa:26270; -.
DR   MANE-Select; ENST00000376753.9; ENSP00000365944.4; NM_018438.6; NP_060908.1.
DR   UCSC; uc001aso.4; human.
DR   AGR; HGNC:13585; -.
DR   ClinPGx; PA28046; -.
DR   CTD; 26270; -.
DR   DisGeNET; 26270; -.
DR   GeneCards; FBXO6; -.
DR   HGNC; HGNC:13585; FBXO6.
DR   HPA; ENSG00000116663; Low tissue specificity.
DR   MIM; 605647; gene.
DR   OpenTargets; ENSG00000116663; -.
DR   VEuPathDB; HostDB:ENSG00000116663; -.
DR   eggNOG; ENOG502RZA6; Eukaryota.
DR   GeneTree; ENSGT00940000159980; -.
DR   HOGENOM; CLU_068548_0_0_1; -.
DR   InParanoid; Q9NRD1; -.
DR   OMA; HIFFQHG; -.
DR   OrthoDB; 1107553at2759; -.
DR   PAN-GO; Q9NRD1; 7 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9NRD1; -.
DR   PathwayCommons; Q9NRD1; -.
DR   Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q9NRD1; -.
DR   SIGNOR; Q9NRD1; -.
DR   UniPathway; UPA00143; -.
DR   Agora; ENSG00000116663; -.
DR   BioGRID-ORCS; 26270; 10 hits in 1213 CRISPR screens.
DR   ChiTaRS; FBXO6; human.
DR   GeneWiki; FBXO6; -.
DR   GenomeRNAi; 26270; -.
DR   Pharos; Q9NRD1; Tbio.
DR   PRO; PR:Q9NRD1; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9NRD1; protein.
DR   Bgee; ENSG00000116663; Expressed in granulocyte and 141 other cell types or tissues.
DR   ExpressionAtlas; Q9NRD1; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IBA:GO_Central.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; TAS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; TAS:UniProtKB.
DR   GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
DR   GO; GO:0006516; P:glycoprotein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   CDD; cd22168; F-box_FBXO6-like; 1.
DR   FunFam; 2.60.120.260:FF:000012; F-box only protein 2; 1.
DR   FunFam; 1.20.1280.50:FF:000002; F-box only protein 44; 1.
DR   Gene3D; 1.20.1280.50; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR007397; F-box-assoc_dom.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR039752; F-box_only.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   PANTHER; PTHR12125:SF12; F-BOX ONLY PROTEIN 6; 1.
DR   PANTHER; PTHR12125; F-BOX ONLY PROTEIN 6-LIKE PROTEIN; 1.
DR   Pfam; PF12937; F-box-like; 1.
DR   Pfam; PF04300; FBA; 1.
DR   SMART; SM01198; FBA; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS51114; FBA; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA damage; DNA repair; Phosphoprotein;
KW   Proteomics identification; Reference proteome; Ubl conjugation pathway;
KW   Unfolded protein response.
FT   CHAIN           1..293
FT                   /note="F-box only protein 6"
FT                   /id="PRO_0000119882"
FT   DOMAIN          10..57
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   DOMAIN          78..259
FT                   /note="FBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00482"
FT   REGION          261..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         60
FT                   /note="R -> Q (in dbSNP:rs3125818)"
FT                   /id="VAR_049039"
FT   VARIANT         201
FT                   /note="P -> T (in dbSNP:rs2294639)"
FT                   /id="VAR_022158"
FT   MUTAGEN         241..242
FT                   /note="YW->AA: Abolishes interaction with glycosylated
FT                   concanavalin-A in vitro."
FT                   /evidence="ECO:0000269|PubMed:18203720"
FT   CONFLICT        18
FT                   /note="E -> D (in Ref. 1; AAF04470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="M -> L (in Ref. 1; AAF04470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61
FT                   /note="E -> K (in Ref. 1; AAF04470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        96
FT                   /note="E -> N (in Ref. 1; AAF04470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        114
FT                   /note="E -> D (in Ref. 1; AAF04470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="D -> E (in Ref. 1; AAF04470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="Y -> S (in Ref. 1; AAF04470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        139
FT                   /note="M -> L (in Ref. 1; AAF04470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143..144
FT                   /note="SQ -> WE (in Ref. 1; AAF04470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149..152
FT                   /note="VAEG -> LADR (in Ref. 1; AAF04470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="R -> G (in Ref. 1; AAF04470)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   293 AA;  33933 MW;  EA4235CD9CCD80FF CRC64;
     MDAPHSKAAL DSINELPENI LLELFTHVPA RQLLLNCRLV CSLWRDLIDL MTLWKRKCLR
     EGFITKDWDQ PVADWKIFYF LRSLHRNLLR NPCAEEDMFA WQIDFNGGDR WKVESLPGAH
     GTDFPDPKVK KYFVTSYEMC LKSQLVDLVA EGYWEELLDT FRPDIVVKDW FAARADCGCT
     YQLKVQLASA DYFVLASFEP PPVTIQQWNN ATWTEVSYTF SDYPRGVRYI LFQHGGRDTQ
     YWAGWYGPRV TNSSIVVSPK MTRNQASSEA QPGQKHGQEE AAQSPYRAVV QIF
//