FBX9_HUMAN
ID FBX9_HUMAN Reviewed; 447 AA.
AC Q9UK97; A6NFW3; B3KMM6; O75986; Q59EH8; Q6PKH7; Q9NT57; Q9Y593;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=F-box only protein 9;
DE AltName: Full=Cross-immune reaction antigen 1;
DE AltName: Full=Renal carcinoma antigen NY-REN-57;
GN Name=FBXO9; Synonyms=FBX9, VCIA1;
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=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 [MRNA] (ISOFORM 2).
RC TISSUE=Endothelial cell;
RA Deng H.-X., Wei Y.-Q., Zhao X., Yang J.-L., Yang H.-S., Tian L., Wang R.;
RT "Identification of angiogenesis related genes by xenogeneic antibody
RT screening.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Skin;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 121-447.
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 [9]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A SCF PROTEIN LIGASE
RP COMPLEX, AND INTERACTION WITH TTI1 AND TELO2.
RX PubMed=23263282; DOI=10.1038/ncb2651;
RA Fernandez-Saiz V., Targosz B.S., Lemeer S., Eichner R., Langer C.,
RA Bullinger L., Reiter C., Slotta-Huspenina J., Schroeder S., Knorn A.M.,
RA Kurutz J., Peschel C., Pagano M., Kuster B., Bassermann F.;
RT "SCF(Fbxo9) and CK2 direct the cellular response to growth factor
RT withdrawal via Tel2/Tti1 degradation and promote survival in multiple
RT myeloma.";
RL Nat. Cell Biol. 15:72-81(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2
CC in a CK2-dependent manner, thereby directly regulating mTOR signaling.
CC SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they
CC are phosphorylated by CK2 following growth factor deprivation, leading
CC to their degradation. In contrast, the SCF(FBXO9) does not mediate
CC ubiquitination of TTI1 and TELO2 when they are part of the mTORC2
CC complex. As a consequence, mTORC1 is inactivated to restrain cell
CC growth and protein translation, while mTORC2 is activated due to the
CC relief of feedback inhibition by mTORC1. {ECO:0000269|PubMed:23263282}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase
CC complex SCF(FBXO9) composed of CUL1, SKP1, RBX1 and FBXO9. Interacts
CC with TTI1 and TELO2; when TTI1 and TELO2 are phosphorylated by CK2.
CC {ECO:0000269|PubMed:23263282}.
CC -!- INTERACTION:
CC Q9UK97; P63208: SKP1; NbExp=2; IntAct=EBI-2869927, EBI-307486;
CC Q9UK97; Q9Y4R8: TELO2; NbExp=5; IntAct=EBI-2869927, EBI-1043674;
CC Q9UK97; O43156: TTI1; NbExp=5; IntAct=EBI-2869927, EBI-1055680;
CC Q9UK97-2; P63208: SKP1; NbExp=3; IntAct=EBI-11023199, EBI-307486;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23263282}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UK97-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UK97-2; Sequence=VSP_012979;
CC Name=3;
CC IsoId=Q9UK97-3; Sequence=VSP_012980;
CC -!- MISCELLANEOUS: Overexpressed in multiple myeloma leading to
CC constitutive activation of the PI(3)K/mTORC2/Akt pathway to promote
CC survival. {ECO:0000305|PubMed:23263282}.
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DR EMBL; AF176704; AAF03704.1; -; mRNA.
DR EMBL; AY858798; AAW51115.1; -; mRNA.
DR EMBL; AL137520; CAB70786.2; -; mRNA.
DR EMBL; AK021559; BAG51038.1; -; mRNA.
DR EMBL; AB209833; BAD93070.1; -; mRNA.
DR EMBL; AL031178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000650; AAH00650.2; -; mRNA.
DR EMBL; AF174597; AAF04518.1; -; mRNA.
DR CCDS; CCDS55022.1; -. [Q9UK97-2]
DR CCDS; CCDS55023.1; -. [Q9UK97-1]
DR CCDS; CCDS55024.1; -. [Q9UK97-3]
DR PIR; T46366; T46366.
DR RefSeq; NP_036479.1; NM_012347.4. [Q9UK97-1]
DR RefSeq; NP_258441.1; NM_033480.2. [Q9UK97-2]
DR RefSeq; NP_258442.2; NM_033481.3. [Q9UK97-3]
DR RefSeq; XP_005249052.1; XM_005248995.4. [Q9UK97-3]
DR RefSeq; XP_005249053.1; XM_005248996.4. [Q9UK97-3]
DR AlphaFoldDB; Q9UK97; -.
DR SMR; Q9UK97; -.
DR BioGRID; 117652; 13.
DR DIP; DIP-60458N; -.
DR IntAct; Q9UK97; 16.
DR STRING; 9606.ENSP00000244426; -.
DR iPTMnet; Q9UK97; -.
DR MetOSite; Q9UK97; -.
DR PhosphoSitePlus; Q9UK97; -.
DR BioMuta; FBXO9; -.
DR DMDM; 13124238; -.
DR EPD; Q9UK97; -.
DR jPOST; Q9UK97; -.
DR MassIVE; Q9UK97; -.
DR MaxQB; Q9UK97; -.
DR PaxDb; Q9UK97; -.
DR PeptideAtlas; Q9UK97; -.
DR PRIDE; Q9UK97; -.
DR ProteomicsDB; 84742; -. [Q9UK97-1]
DR ProteomicsDB; 84743; -. [Q9UK97-2]
DR ProteomicsDB; 84744; -. [Q9UK97-3]
DR Antibodypedia; 30968; 178 antibodies from 26 providers.
DR DNASU; 26268; -.
DR Ensembl; ENST00000244426.10; ENSP00000244426.6; ENSG00000112146.17. [Q9UK97-1]
DR Ensembl; ENST00000323557.12; ENSP00000326968.7; ENSG00000112146.17. [Q9UK97-2]
DR Ensembl; ENST00000370939.7; ENSP00000359977.3; ENSG00000112146.17. [Q9UK97-3]
DR GeneID; 26268; -.
DR KEGG; hsa:26268; -.
DR MANE-Select; ENST00000323557.12; ENSP00000326968.7; NM_033480.3; NP_258441.1. [Q9UK97-2]
DR UCSC; uc063pbc.1; human. [Q9UK97-1]
DR CTD; 26268; -.
DR DisGeNET; 26268; -.
DR GeneCards; FBXO9; -.
DR HGNC; HGNC:13588; FBXO9.
DR HPA; ENSG00000112146; Low tissue specificity.
DR MIM; 609091; gene.
DR neXtProt; NX_Q9UK97; -.
DR OpenTargets; ENSG00000112146; -.
DR PharmGKB; PA28049; -.
DR VEuPathDB; HostDB:ENSG00000112146; -.
DR eggNOG; KOG2997; Eukaryota.
DR GeneTree; ENSGT00390000014256; -.
DR HOGENOM; CLU_041758_0_0_1; -.
DR InParanoid; Q9UK97; -.
DR OMA; DEFRENW; -.
DR OrthoDB; 1407789at2759; -.
DR PhylomeDB; Q9UK97; -.
DR TreeFam; TF324797; -.
DR PathwayCommons; Q9UK97; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9UK97; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 26268; 23 hits in 1121 CRISPR screens.
DR ChiTaRS; FBXO9; human.
DR GeneWiki; FBXO9; -.
DR GenomeRNAi; 26268; -.
DR Pharos; Q9UK97; Tbio.
DR PRO; PR:Q9UK97; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9UK97; protein.
DR Bgee; ENSG00000112146; Expressed in endothelial cell and 210 other tissues.
DR ExpressionAtlas; Q9UK97; baseline and differential.
DR Genevisible; Q9UK97; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; NAS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; NAS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0032006; P:regulation of TOR signaling; IMP:UniProtKB.
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; IPR045118; FBXO9/FBXO48.
DR InterPro; IPR045464; Hrt3/FBXO9_C.
DR InterPro; IPR036181; MIT_dom_sf.
DR PANTHER; PTHR12874; PTHR12874; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF19270; FBO_C; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome;
KW TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..447
FT /note="F-box only protein 9"
FT /id="PRO_0000119886"
FT REPEAT 94..127
FT /note="TPR"
FT DOMAIN 185..236
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REGION 9..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..44
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012980"
FT VAR_SEQ 1..11
FT /note="MPDIIWVFPPQ -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.5"
FT /id="VSP_012979"
SQ SEQUENCE 447 AA; 52329 MW; 2A88163DAB898D69 CRC64;
MPDIIWVFPP QAEAEEDCHS DTVRADDDEE NESPAETDLQ AQLQMFRAQW MFELAPGVSS
SNLENRPCRA ARGSLQKTSA DTKGKQEQAK EEKARELFLK AVEEEQNGAL YEAIKFYRRA
MQLVPDIEFK ITYTRSPDGD GVGNSYIEDN DDDSKMADLL SYFQQQLTFQ ESVLKLCQPE
LESSQIHISV LPMEVLMYIF RWVVSSDLDL RSLEQLSLVC RGFYICARDP EIWRLACLKV
WGRSCIKLVP YTSWREMFLE RPRVRFDGVY ISKTTYIRQG EQSLDGFYRA WHQVEYYRYI
RFFPDGHVMM LTTPEEPQSI VPRLRTRNTR TDAILLGHYR LSQDTDNQTK VFAVITKKKE
EKPLDYKYRY FRRVPVQEAD QSFHVGLQLC SSGHQRFNKL IWIHHSCHIT YKSTGETAVS
AFEIDKMYTP LFFARVRSYT AFSERPL
