FXL17_HUMAN
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 03-AUG-2022, entry version 170.
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, ECO:0000312|HGNC:HGNC:13615};
GN Synonyms=FBL17 {ECO:0000312|HGNC:HGNC:13615},
GN FBX13 {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 -!- 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_001163315.2. [Q9UF56-1]
DR PDB; 6W66; X-ray; 3.21 A; B=310-701.
DR PDB; 6WCQ; EM; 8.50 A; B=310-701.
DR PDBsum; 6W66; -.
DR PDBsum; 6WCQ; -.
DR AlphaFoldDB; Q9UF56; -.
DR SMR; Q9UF56; -.
DR BioGRID; 122315; 87.
DR IntAct; Q9UF56; 12.
DR STRING; 9606.ENSP00000437464; -.
DR iPTMnet; Q9UF56; -.
DR PhosphoSitePlus; Q9UF56; -.
DR BioMuta; FBXL17; -.
DR DMDM; 229462981; -.
DR EPD; Q9UF56; -.
DR jPOST; Q9UF56; -.
DR MassIVE; Q9UF56; -.
DR MaxQB; Q9UF56; -.
DR PaxDb; Q9UF56; -.
DR PeptideAtlas; Q9UF56; -.
DR PRIDE; Q9UF56; -.
DR ProteomicsDB; 84171; -. [Q9UF56-1]
DR ProteomicsDB; 84172; -. [Q9UF56-2]
DR ProteomicsDB; 84173; -. [Q9UF56-3]
DR Antibodypedia; 25280; 128 antibodies from 18 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 CTD; 64839; -.
DR DisGeNET; 64839; -.
DR GeneCards; FBXL17; -.
DR HGNC; HGNC:13615; FBXL17.
DR HPA; ENSG00000145743; Low tissue specificity.
DR MIM; 609083; gene.
DR neXtProt; NX_Q9UF56; -.
DR OpenTargets; ENSG00000145743; -.
DR PharmGKB; PA134920563; -.
DR VEuPathDB; HostDB:ENSG00000145743; -.
DR eggNOG; KOG1947; Eukaryota.
DR GeneTree; ENSGT00940000156973; -.
DR HOGENOM; CLU_024577_3_0_1; -.
DR InParanoid; Q9UF56; -.
DR OMA; KLGANCR; -.
DR OrthoDB; 524674at2759; -.
DR PhylomeDB; Q9UF56; -.
DR TreeFam; TF332421; -.
DR PathwayCommons; Q9UF56; -.
DR Reactome; R-HSA-9708530; Regulation of BACH1 activity.
DR SignaLink; Q9UF56; -.
DR SIGNOR; Q9UF56; -.
DR BioGRID-ORCS; 64839; 17 hits in 1086 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 199 other tissues.
DR ExpressionAtlas; Q9UF56; baseline and differential.
DR Genevisible; Q9UF56; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0043153; P:entrainment of circadian clock by photoperiod; IBA:GO_Central.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
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:0051726; P:regulation of cell cycle; IBA:GO_Central.
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 Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF13516; LRR_6; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 11.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Neurogenesis; Nucleus;
KW 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..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..267
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:6W66"
FT HELIX 326..334
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 338..342
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 350..357
FT /evidence="ECO:0007829|PDB:6W66"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 376..384
FT /evidence="ECO:0007829|PDB:6W66"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 401..410
FT /evidence="ECO:0007829|PDB:6W66"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 427..436
FT /evidence="ECO:0007829|PDB:6W66"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 456..462
FT /evidence="ECO:0007829|PDB:6W66"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 479..487
FT /evidence="ECO:0007829|PDB:6W66"
FT STRAND 494..499
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 505..512
FT /evidence="ECO:0007829|PDB:6W66"
FT STRAND 520..524
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 530..533
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 534..538
FT /evidence="ECO:0007829|PDB:6W66"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 555..564
FT /evidence="ECO:0007829|PDB:6W66"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 581..590
FT /evidence="ECO:0007829|PDB:6W66"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 606..615
FT /evidence="ECO:0007829|PDB:6W66"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 632..641
FT /evidence="ECO:0007829|PDB:6W66"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 658..667
FT /evidence="ECO:0007829|PDB:6W66"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:6W66"
FT HELIX 676..688
FT /evidence="ECO:0007829|PDB:6W66"
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
