FBXW8_HUMAN
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 03-AUG-2022, entry version 176.
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};
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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 AlphaFoldDB; Q8N3Y1; -.
DR SMR; Q8N3Y1; -.
DR BioGRID; 117645; 145.
DR CORUM; Q8N3Y1; -.
DR DIP; DIP-37970N; -.
DR IntAct; Q8N3Y1; 34.
DR MINT; Q8N3Y1; -.
DR STRING; 9606.ENSP00000310686; -.
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; Q8N3Y1; -.
DR PeptideAtlas; Q8N3Y1; -.
DR PRIDE; Q8N3Y1; -.
DR ProteomicsDB; 71847; -. [Q8N3Y1-1]
DR ProteomicsDB; 71848; -. [Q8N3Y1-2]
DR Antibodypedia; 31322; 146 antibodies from 20 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 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; 1046098at2759; -.
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 UniPathway; UPA00143; -.
DR BioGRID-ORCS; 26259; 8 hits in 1114 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 106 other tissues.
DR ExpressionAtlas; Q8N3Y1; baseline and differential.
DR Genevisible; Q8N3Y1; HS.
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: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:1901485; P:positive regulation of transcription factor catabolic process; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0060712; P:spongiotrophoblast layer development; IEA:Ensembl.
DR Gene3D; 2.130.10.10; -; 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_repeat.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50998; SSF50998; 1.
DR SUPFAM; SSF81383; SSF81383; 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.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Golgi apparatus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation pathway;
KW 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"
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
