FBX31_HUMAN
ID FBX31_HUMAN Reviewed; 539 AA.
AC Q5XUX0; Q5K680; Q8WYV1; Q96D73; Q9UFV4;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=F-box only protein 31;
GN Name=FBXO31; Synonyms=FBX14, FBX31; ORFNames=PP2386;
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 1).
RX PubMed=15520277; DOI=10.1101/gad.1255304;
RA Jin J., Cardozo T., Lovering R.C., Elledge S.J., Pagano M., Harper J.W.;
RT "Systematic analysis and nomenclature of mammalian F-box proteins.";
RL Genes Dev. 18:2573-2580(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Choriocarcinoma;
RA Banham A.H., Cordell J.L., Jones M., Liggins A.P., Pulford K., Mason D.Y.;
RT "A novel F-box protein is differentially expressed in hematopoietic
RT malignancies.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-539 (ISOFORM 1).
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 [7]
RP TISSUE SPECIFICITY, SUBUNIT, FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=16357137; DOI=10.1158/0008-5472.can-05-0936;
RA Kumar R., Neilsen P.M., Crawford J., McKirdy R., Lee J., Powell J.A.,
RA Saif Z., Martin J.M., Lombaerts M., Cornelisse C.J., Cleton-Jansen A.-M.,
RA Callen D.F.;
RT "FBXO31 is the chromosome 16q24.3 senescence gene, a candidate breast tumor
RT suppressor, and a component of an SCF complex.";
RL Cancer Res. 65:11304-11313(2005).
RN [8]
RP FUNCTION, IDENTIFICATION IN A SCF PROTEIN LIGASE COMPLEX, INDUCTION,
RP INTERACTION WITH CCND1, PHOSPHORYLATION AT SER-278, AND MUTAGENESIS OF
RP SER-278 AND SER-400.
RX PubMed=19412162; DOI=10.1038/nature08011;
RA Santra M.K., Wajapeyee N., Green M.R.;
RT "F-box protein FBXO31 mediates cyclin D1 degradation to induce G1 arrest
RT after DNA damage.";
RL Nature 459:722-725(2009).
RN [9]
RP INVOLVEMENT IN MRT45.
RX PubMed=24623383; DOI=10.1007/s00439-014-1438-0;
RA Mir A., Sritharan K., Mittal K., Vasli N., Araujo C., Jamil T., Rafiq M.A.,
RA Anwar Z., Mikhailov A., Rauf S., Mahmood H., Shakoor A., Ali S., So J.,
RA Naeem F., Ayub M., Vincent J.B.;
RT "Truncation of the E3 ubiquitin ligase component FBXO31 causes non-
RT syndromic autosomal recessive intellectual disability in a Pakistani
RT family.";
RL Hum. Genet. 133:975-984(2014).
CC -!- FUNCTION: Component of some SCF (SKP1-cullin-F-box) protein ligase
CC complex that plays a central role in G1 arrest following DNA damage.
CC Specifically recognizes phosphorylated cyclin-D1 (CCND1), promoting its
CC ubiquitination and degradation by the proteasome, resulting in G1
CC arrest. May act as a tumor suppressor. {ECO:0000269|PubMed:16357137,
CC ECO:0000269|PubMed:19412162}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC {ECO:0000269|PubMed:16357137, ECO:0000269|PubMed:19412162}.
CC -!- INTERACTION:
CC Q5XUX0; Q13315: ATM; NbExp=2; IntAct=EBI-6162477, EBI-495465;
CC Q5XUX0; P24385: CCND1; NbExp=4; IntAct=EBI-6162477, EBI-375001;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5XUX0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XUX0-2; Sequence=VSP_037469;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Expressed at moderate
CC levels in most tissues, except bone marrow.
CC {ECO:0000269|PubMed:16357137}.
CC -!- DEVELOPMENTAL STAGE: Expression is cell-cycle regulated, and peaks at
CC late G2 to early G1 phase (at protein level).
CC {ECO:0000269|PubMed:16357137}.
CC -!- INDUCTION: By DNA damage. Increases after UV irradiation, X-ray
CC irradiation, oxidative stress (H(2)O(2)) or addition of the
CC chemotherapeutic DNA-damaging agents etoposide, adriamycin, cisplatin
CC or fluorouracil. {ECO:0000269|PubMed:19412162}.
CC -!- PTM: Phosphorylation at Ser-278 by ATM following gamma-irradiation
CC results in its stabilization. {ECO:0000269|PubMed:19412162}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 45
CC (MRT45) [MIM:615979]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRT45
CC manifestations include mild to moderate intellectual disability and
CC dysmorphic features, including coarse facies, broad nasal bridge,
CC fleshy nares, and thick, prominent lips. {ECO:0000269|PubMed:24623383}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the FBXO31 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12748.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL55855.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB55929.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FBXO31ID44280ch16q24.html";
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DR EMBL; AY736035; AAU50679.1; -; mRNA.
DR EMBL; AF428140; AAQ04213.1; -; mRNA.
DR EMBL; AF318348; AAL55855.1; ALT_FRAME; mRNA.
DR EMBL; AC010531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012748; AAH12748.1; ALT_INIT; mRNA.
DR EMBL; AL117444; CAB55929.2; ALT_INIT; mRNA.
DR CCDS; CCDS32501.1; -. [Q5XUX0-1]
DR PIR; T17239; T17239.
DR RefSeq; NP_001269612.1; NM_001282683.1.
DR RefSeq; NP_079011.3; NM_024735.4. [Q5XUX0-1]
DR PDB; 5VZT; X-ray; 2.70 A; B/D=66-539.
DR PDB; 5VZU; X-ray; 2.70 A; B/D=66-539.
DR PDBsum; 5VZT; -.
DR PDBsum; 5VZU; -.
DR AlphaFoldDB; Q5XUX0; -.
DR SMR; Q5XUX0; -.
DR BioGRID; 122890; 38.
DR CORUM; Q5XUX0; -.
DR DIP; DIP-60449N; -.
DR IntAct; Q5XUX0; 22.
DR STRING; 9606.ENSP00000310841; -.
DR iPTMnet; Q5XUX0; -.
DR PhosphoSitePlus; Q5XUX0; -.
DR BioMuta; FBXO31; -.
DR DMDM; 146345419; -.
DR EPD; Q5XUX0; -.
DR jPOST; Q5XUX0; -.
DR MassIVE; Q5XUX0; -.
DR MaxQB; Q5XUX0; -.
DR PaxDb; Q5XUX0; -.
DR PeptideAtlas; Q5XUX0; -.
DR PRIDE; Q5XUX0; -.
DR ProteomicsDB; 65845; -. [Q5XUX0-1]
DR ProteomicsDB; 65846; -. [Q5XUX0-2]
DR Antibodypedia; 30677; 247 antibodies from 24 providers.
DR DNASU; 79791; -.
DR Ensembl; ENST00000311635.12; ENSP00000310841.4; ENSG00000103264.18. [Q5XUX0-1]
DR GeneID; 79791; -.
DR KEGG; hsa:79791; -.
DR MANE-Select; ENST00000311635.12; ENSP00000310841.4; NM_024735.5; NP_079011.3.
DR UCSC; uc002fjw.5; human. [Q5XUX0-1]
DR CTD; 79791; -.
DR DisGeNET; 79791; -.
DR GeneCards; FBXO31; -.
DR HGNC; HGNC:16510; FBXO31.
DR HPA; ENSG00000103264; Tissue enhanced (skeletal).
DR MalaCards; FBXO31; -.
DR MIM; 609102; gene.
DR MIM; 615979; phenotype.
DR neXtProt; NX_Q5XUX0; -.
DR OpenTargets; ENSG00000103264; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR PharmGKB; PA28042; -.
DR VEuPathDB; HostDB:ENSG00000103264; -.
DR eggNOG; ENOG502QR2A; Eukaryota.
DR GeneTree; ENSGT00390000001368; -.
DR HOGENOM; CLU_035961_0_0_1; -.
DR InParanoid; Q5XUX0; -.
DR OMA; HIQIVKR; -.
DR OrthoDB; 484321at2759; -.
DR PhylomeDB; Q5XUX0; -.
DR TreeFam; TF331818; -.
DR PathwayCommons; Q5XUX0; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q5XUX0; -.
DR SIGNOR; Q5XUX0; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 79791; 13 hits in 1121 CRISPR screens.
DR ChiTaRS; FBXO31; human.
DR GeneWiki; FBXO31; -.
DR GenomeRNAi; 79791; -.
DR Pharos; Q5XUX0; Tbio.
DR PRO; PR:Q5XUX0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q5XUX0; protein.
DR Bgee; ENSG00000103264; Expressed in cerebellar hemisphere and 178 other tissues.
DR ExpressionAtlas; Q5XUX0; baseline and differential.
DR Genevisible; Q5XUX0; HS.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:2001224; P:positive regulation of neuron migration; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR026941; FBXO31.
DR InterPro; IPR045048; FBXO31/39.
DR PANTHER; PTHR10706; PTHR10706; 1.
DR PANTHER; PTHR10706:SF130; PTHR10706:SF130; 1.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; DNA damage;
KW Intellectual disability; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..539
FT /note="F-box only protein 31"
FT /id="PRO_0000119921"
FT DOMAIN 64..110
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REGION 11..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TQF0"
FT MOD_RES 37
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3TQF0"
FT MOD_RES 278
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000269|PubMed:19412162"
FT VAR_SEQ 1..113
FT /note="MAVCARLCGVGPSRGCRRRQQRRGPAETAAADSEPDTDPEEERIEASAGVGG
FT GLCAGPSPPPPRCSLLELPPELLVEIFASLPGTDLPSLAQVCTKFRRILHTDTIWRRRC
FT RE -> MFLVT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_037469"
FT MUTAGEN 278
FT /note="S->A: Fails to accumulate following gamma-
FT irradiation."
FT /evidence="ECO:0000269|PubMed:19412162"
FT MUTAGEN 400
FT /note="S->A: No effect following gamma-irradiation."
FT /evidence="ECO:0000269|PubMed:19412162"
FT CONFLICT 138
FT /note="L -> V (in Ref. 1; AAU50679)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="D -> E (in Ref. 1; AAU50679)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="C -> S (in Ref. 1; AAU50679)"
FT /evidence="ECO:0000305"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5VZT"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:5VZT"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:5VZT"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:5VZT"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:5VZT"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:5VZT"
FT HELIX 121..126
FT /evidence="ECO:0007829|PDB:5VZT"
FT HELIX 131..137
FT /evidence="ECO:0007829|PDB:5VZT"
FT TURN 138..142
FT /evidence="ECO:0007829|PDB:5VZT"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:5VZT"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:5VZT"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:5VZT"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:5VZU"
FT HELIX 264..278
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:5VZT"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 323..332
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 341..352
FT /evidence="ECO:0007829|PDB:5VZT"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:5VZT"
FT HELIX 363..380
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 464..475
FT /evidence="ECO:0007829|PDB:5VZT"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 479..492
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 495..500
FT /evidence="ECO:0007829|PDB:5VZT"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:5VZT"
FT STRAND 505..511
FT /evidence="ECO:0007829|PDB:5VZT"
FT HELIX 524..536
FT /evidence="ECO:0007829|PDB:5VZT"
SQ SEQUENCE 539 AA; 60664 MW; E833D63A361E7381 CRC64;
MAVCARLCGV GPSRGCRRRQ QRRGPAETAA ADSEPDTDPE EERIEASAGV GGGLCAGPSP
PPPRCSLLEL PPELLVEIFA SLPGTDLPSL AQVCTKFRRI LHTDTIWRRR CREEYGVCEN
LRKLEITGVS CRDVYAKLLH RYRHILGLWQ PDIGPYGGLL NVVVDGLFII GWMYLPPHDP
HVDDPMRFKP LFRIHLMERK AATVECMYGH KGPHHGHIQI VKKDEFSTKC NQTDHHRMSG
GRQEEFRTWL REEWGRTLED IFHEHMQELI LMKFIYTSQY DNCLTYRRIY LPPSRPDDLI
KPGLFKGTYG SHGLEIVMLS FHGRRARGTK ITGDPNIPAG QQTVEIDLRH RIQLPDLENQ
RNFNELSRIV LEVRERVRQE QQEGGHEAGE GRGRQGPRES QPSPAQPRAE APSKGPDGTP
GEDGGEPGDA VAAAEQPAQC GQGQPFVLPV GVSSRNEDYP RTCRMCFYGT GLIAGHGFTS
PERTPGVFIL FDEDRFGFVW LELKSFSLYS RVQATFRNAD APSPQAFDEM LKNIQSLTS
