FBW1B_MOUSE
ID FBW1B_MOUSE Reviewed; 542 AA.
AC Q5SRY7; Q3TGM9; Q3TLZ8; Q8BY90; Q8K022; Q923H0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=F-box/WD repeat-containing protein 11;
DE AltName: Full=F-box and WD repeats protein beta-TrCP2;
DE AltName: Full=F-box/WD repeat-containing protein 1B;
DE AltName: Full=Homologous to Slimb protein;
DE Short=HOS;
GN Name=Fbxw11; Synonyms=Btrcp2, Fbw1b, Fbxw1b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH SKP1
RP AND NFKBIA.
RC STRAIN=FVB/N;
RX PubMed=11896578; DOI=10.1038/sj.onc.1205311;
RA Bhatia N., Herter J.R., Slaga T.J., Fuchs S.Y., Spiegelman V.S.;
RT "Mouse homologue of HOS (mHOS) is overexpressed in skin tumors and
RT implicated in constitutive activation of NF-kappaB.";
RL Oncogene 21:1501-1509(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC STRAIN=C57BL/6J;
RC TISSUE=Kidney, Mammary gland, Osteoclast, Sympathetic ganglion, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; 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 [5]
RP INDUCTION.
RX PubMed=11850814; DOI=10.1038/sj.onc.1205132;
RA Spiegelman V.S., Tang W., Katoh M., Slaga T.J., Fuchs S.Y.;
RT "Inhibition of HOS expression and activities by Wnt pathway.";
RL Oncogene 21:856-860(2002).
RN [6]
RP INTERACTION WITH PER3.
RX PubMed=15917222; DOI=10.1074/jbc.m502862200;
RA Shirogane T., Jin J., Ang X.L., Harper J.W.;
RT "SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-
RT dependent degradation of the mammalian period-1 (Per1) protein.";
RL J. Biol. Chem. 280:26863-26872(2005).
RN [7]
RP FUNCTION IN CIRCADIAN RHYTHMS, INTERACTION WITH PER2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18782782; DOI=10.1093/jb/mvn112;
RA Ohsaki K., Oishi K., Kozono Y., Nakayama K., Nakayama K.I., Ishida N.;
RT "The role of {beta}-TrCP1 and {beta}-TrCP2 in circadian rhythm generation
RT by mediating degradation of clock protein PER2.";
RL J. Biochem. 144:609-618(2008).
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 target
CC proteins. Probably recognizes and binds to phosphorylated target
CC proteins. SCF(FBXW11) mediates the ubiquitination of phosphorylated
CC CTNNB1 and participates in Wnt signaling regulation. SCF(FBXW11)
CC mediates the ubiquitination of phosphorylated NFKBIA, which degradation
CC frees the associated NFKB1 to translocate into the nucleus and to
CC activate transcription. SCF(FBXW11) mediates the ubiquitination of
CC IFNAR1. SCF(FBXW11) mediates the ubiquitination of CEP68; this is
CC required for centriole separation during mitosis (By similarity).
CC Involved in the oxidative stress-induced a ubiquitin-mediated decrease
CC in RCAN1. Mediates the degradation of CDC25A induced by ionizing
CC radiation in cells progressing through S phase and thus may function in
CC the intra-S-phase checkpoint. Has an essential role in the control of
CC the clock-dependent transcription via degradation of phosphorylated
CC PER1 and phosphorylated PER2. SCF(FBXW11) mediates the ubiquitination
CC of CYTH1, and probably CYTH2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UKB1, ECO:0000269|PubMed:11896578,
CC ECO:0000269|PubMed:18782782}.
CC -!- SUBUNIT: Self-associates. Component of the SCF(FBXW11) complex formed
CC of CUL1, SKP1, RBX1 and a FBXW11 dimer. Interacts with BTRC, BST2,
CC PER1, RCAN1 and USP47. Interacts with phosphorylated ubiquitination
CC substrates CTNNB1, NFKBIA, IFNAR1, PER1 and PER2; the interaction
CC requires the phosphorylation of the two serine residues in the
CC substrates' destruction motif D-S-G-X(2,3,4)-S. Interacts with TRIM21.
CC Interacts with PER3. Interacts with phosphorylated ubiquitination
CC substrate CEP68 (By similarity). Interacts with INAVA (By similarity).
CC Interacts with REST (By similarity). {ECO:0000250|UniProtKB:Q9UKB1,
CC ECO:0000269|PubMed:11896578, ECO:0000269|PubMed:15917222,
CC ECO:0000269|PubMed:18782782}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18782782}. Nucleus
CC {ECO:0000269|PubMed:18782782}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5SRY7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SRY7-2; Sequence=VSP_039581;
CC Name=3;
CC IsoId=Q5SRY7-3; Sequence=VSP_039580;
CC Name=4;
CC IsoId=Q5SRY7-4; Sequence=VSP_039579;
CC -!- INDUCTION: Expression is negatively regulated by Wnt/beta-catenin
CC pathway. {ECO:0000269|PubMed:11850814}.
CC -!- DOMAIN: The N-terminal D domain mediates homodimerization.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK72095.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY038079; AAK72095.1; ALT_FRAME; mRNA.
DR EMBL; AK041532; BAC30975.1; -; mRNA.
DR EMBL; AK149139; BAE28749.1; -; mRNA.
DR EMBL; AK152181; BAE31012.1; -; mRNA.
DR EMBL; AK160086; BAE35617.1; -; mRNA.
DR EMBL; AK166226; BAE38644.1; -; mRNA.
DR EMBL; AK168667; BAE40519.1; -; mRNA.
DR EMBL; AL669844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL669951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034261; AAH34261.1; -; mRNA.
DR CCDS; CCDS36125.1; -. [Q5SRY7-2]
DR CCDS; CCDS70157.1; -. [Q5SRY7-1]
DR CCDS; CCDS70158.1; -. [Q5SRY7-3]
DR RefSeq; NP_001258276.1; NM_001271347.1. [Q5SRY7-1]
DR RefSeq; NP_001258277.1; NM_001271348.1. [Q5SRY7-3]
DR RefSeq; NP_001258278.1; NM_001271349.1. [Q5SRY7-4]
DR RefSeq; NP_598776.1; NM_134015.3. [Q5SRY7-2]
DR AlphaFoldDB; Q5SRY7; -.
DR SMR; Q5SRY7; -.
DR BioGRID; 222123; 36.
DR DIP; DIP-59921N; -.
DR IntAct; Q5SRY7; 22.
DR MINT; Q5SRY7; -.
DR STRING; 10090.ENSMUSP00000075721; -.
DR iPTMnet; Q5SRY7; -.
DR PhosphoSitePlus; Q5SRY7; -.
DR SwissPalm; Q5SRY7; -.
DR EPD; Q5SRY7; -.
DR MaxQB; Q5SRY7; -.
DR PaxDb; Q5SRY7; -.
DR PeptideAtlas; Q5SRY7; -.
DR PRIDE; Q5SRY7; -.
DR ProteomicsDB; 270960; -. [Q5SRY7-1]
DR ProteomicsDB; 270961; -. [Q5SRY7-2]
DR ProteomicsDB; 270962; -. [Q5SRY7-3]
DR ProteomicsDB; 270963; -. [Q5SRY7-4]
DR Antibodypedia; 28871; 250 antibodies from 29 providers.
DR DNASU; 103583; -.
DR Ensembl; ENSMUST00000076383; ENSMUSP00000075721; ENSMUSG00000020271. [Q5SRY7-2]
DR Ensembl; ENSMUST00000093205; ENSMUSP00000090893; ENSMUSG00000020271. [Q5SRY7-1]
DR Ensembl; ENSMUST00000109366; ENSMUSP00000104991; ENSMUSG00000020271. [Q5SRY7-3]
DR GeneID; 103583; -.
DR KEGG; mmu:103583; -.
DR UCSC; uc007ijx.2; mouse. [Q5SRY7-2]
DR UCSC; uc007ijy.2; mouse. [Q5SRY7-3]
DR UCSC; uc007ijz.2; mouse. [Q5SRY7-1]
DR UCSC; uc007ika.2; mouse. [Q5SRY7-4]
DR CTD; 23291; -.
DR MGI; MGI:2144023; Fbxw11.
DR VEuPathDB; HostDB:ENSMUSG00000020271; -.
DR eggNOG; KOG0281; Eukaryota.
DR GeneTree; ENSGT00940000155898; -.
DR HOGENOM; CLU_000288_103_6_1; -.
DR InParanoid; Q5SRY7; -.
DR OMA; IRRINDN; -.
DR OrthoDB; 666965at2759; -.
DR TreeFam; TF105679; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 103583; 26 hits in 76 CRISPR screens.
DR ChiTaRS; Fbxw11; mouse.
DR PRO; PR:Q5SRY7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SRY7; protein.
DR Bgee; ENSMUSG00000020271; Expressed in endocardial cushion and 251 other tissues.
DR ExpressionAtlas; Q5SRY7; baseline and differential.
DR Genevisible; Q5SRY7; MM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0048854; P:brain morphogenesis; IBA:GO_Central.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR GO; GO:0007281; P:germ cell development; IBA:GO_Central.
DR GO; GO:0031023; P:microtubule organizing center organization; IBA:GO_Central.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0042753; P:positive regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0008090; P:retrograde axonal transport; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR021977; Beta-TrCP_D.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12125; Beta-TrCP_D; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM01028; Beta-TrCP_D; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 5.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Cell cycle; Cytoplasm; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation pathway; WD repeat;
KW Wnt signaling pathway.
FT CHAIN 1..542
FT /note="F-box/WD repeat-containing protein 11"
FT /id="PRO_0000396126"
FT DOMAIN 121..167
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 238..275
FT /note="WD 1"
FT REPEAT 278..315
FT /note="WD 2"
FT REPEAT 318..355
FT /note="WD 3"
FT REPEAT 361..398
FT /note="WD 4"
FT REPEAT 401..440
FT /note="WD 5"
FT REPEAT 442..478
FT /note="WD 6"
FT REPEAT 490..527
FT /note="WD 7"
FT REGION 67..116
FT /note="Homodimerization domain D"
FT /evidence="ECO:0000250"
FT VAR_SEQ 16..49
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039579"
FT VAR_SEQ 16..48
FT /note="CSVPRSLWLGCANLVESMCALSCLQSMPSVRCL -> NTSVMEDQNEDESPK
FT KSALW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039580"
FT VAR_SEQ 49
FT /note="Q -> QNTSVMEDQNEDESPKKSALWQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11896578,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039581"
FT CONFLICT 219
FT /note="I -> V (in Ref. 2; BAE38644)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="S -> F (in Ref. 1; AAK72095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 62063 MW; D95A78A6977B828A CRC64;
MEPDSVIEDK TIELMCSVPR SLWLGCANLV ESMCALSCLQ SMPSVRCLQI SNGTSSVIVS
RKRPSEGNYQ KEKDLCIKYF DQWSESDQVE FVEHLISRMC HYQHGHINSY LKPMLQRDFI
TALPEQGLDH IAENILSYLD ARSLCAAELV CKEWQRVISE GMLWKKLIER MVRTDPLWKG
LSERRGWDQY LFKNRPTDGP PNSFYRSLYP KIIQDIETIE SNWRCGRHNL QRIQCRSENS
KGVYCLQYDD DKIISGLRDN SIKIWDKSSL ECLKVLTGHT GSVLCLQYDE RVIVTGSSDS
TVRVWDVNTG EVLNTLIHHN EAVLHLRFSN GLMVTCSKDR SIAVWDMASA TDITLRRVLV
GHRAAVNVVD FDDKYIVSAS GDRTIKVWST STCEFVRTLN GHKRGIACLQ YRDRLVVSGS
SDNTIRLWDI ECGACLRVLE GHEELVRCIR FDNKRIVSGA YDGKIKVWDL QAALDPRAPA
STLCLRTLVE HSGRVFRLQF DEFQIISSSH DDTILIWDFL NVPPSAQNET RSPSRTYTYI
SR
