ID   FBXL5_MOUSE             Reviewed;         690 AA.
AC   Q8C2S5; Q14CG1; Q3TAK6; Q3TWC9; Q3UC66; Q80XI5; Q8BGF5; Q8BNL3; Q8C3Q8;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2003, sequence version 2.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=F-box/LRR-repeat protein 5;
DE   AltName: Full=F-box and leucine-rich repeat protein 5;
GN   Name=Fbxl5;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Lung, Spleen, Testis, 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Eye;
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   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21907140; DOI=10.1016/j.cmet.2011.07.011;
RA   Moroishi T., Nishiyama M., Takeda Y., Iwai K., Nakayama K.I.;
RT   "The FBXL5-IRP2 axis is integral to control of iron metabolism in vivo.";
RL   Cell Metab. 14:339-351(2011).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=23135277; DOI=10.1074/jbc.m112.426171;
RA   Ruiz J.C., Walker S.D., Anderson S.A., Eisenstein R.S., Bruick R.K.;
RT   "F-box and leucine-rich repeat protein 5 (FBXL5) is required for
RT   maintenance of cellular and systemic iron homeostasis.";
RL   J. Biol. Chem. 288:552-560(2013).
CC   -!- FUNCTION: Component of some SCF (SKP1-cullin-F-box) protein ligase
CC       complex that plays a central role in iron homeostasis by promoting the
CC       ubiquitination and subsequent degradation of IREB2/IRP2
CC       (PubMed:21907140, PubMed:23135277). The C-terminal domain of FBXL5
CC       contains a redox-sensitive [2Fe-2S] cluster that, upon oxidation,
CC       promotes binding to IRP2 to effect its oxygen-dependent degradation.
CC       Under iron deficiency conditions, the N-terminal hemerythrin-like (Hr)
CC       region, which contains a diiron metal center, cannot bind iron and
CC       undergoes conformational changes that destabilize the FBXL5 protein and
CC       cause its ubiquitination and degradation. When intracellular iron
CC       levels start rising, the Hr region is stabilized. Additional increases
CC       in iron levels facilitate the assembly and incorporation of a redox
CC       active [2Fe-2S] cluster in the C-terminal domain. Only when oxygen
CC       level is high enough to maintain the cluster in its oxidized state can
CC       FBXL5 recruit IRP2 as a substrate for polyubiquination and degradation.
CC       Promotes ubiquitination and subsequent degradation of the dynactin
CC       complex component DCTN1. Within the nucleus, promotes the
CC       ubiquitination of SNAI1; preventing its interaction with DNA and
CC       promoting its degradation. Negatively regulates DNA damage response by
CC       mediating the ubiquitin-proteasome degradation of the DNA repair
CC       protein NABP2 (By similarity). {ECO:0000250|UniProtKB:Q9UKA1,
CC       ECO:0000269|PubMed:21907140, ECO:0000269|PubMed:23135277}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000250|UniProtKB:Q9UKA1};
CC   -!- ACTIVITY REGULATION: An iron-sulfur cluster promotes IRP2
CC       polyubiquitination and degradation in response to both iron and oxygen
CC       concentrations. {ECO:0000250|UniProtKB:Q9UKA1}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC       Interacts with ACO1/IRP1, IREB2/IRP2; the interaction depends on the
CC       [2Fe-2S] cluster. Interacts with DCTN1/p150-glued.
CC       {ECO:0000250|UniProtKB:Q9UKA1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:Q9UKA1}. Nucleus {ECO:0000250|UniProtKB:Q9UKA1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8C2S5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C2S5-2; Sequence=VSP_008418;
CC       Name=3;
CC         IsoId=Q8C2S5-3; Sequence=VSP_008419, VSP_008420;
CC       Name=4;
CC         IsoId=Q8C2S5-4; Sequence=VSP_038530;
CC       Name=5;
CC         IsoId=Q8C2S5-5; Sequence=VSP_038529, VSP_008419, VSP_008420;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in early
CC       embryogenesis with expression decreasing as the embryo progresses
CC       through development (E11 and E15). {ECO:0000269|PubMed:23135277}.
CC   -!- DOMAIN: The hemerythrin-like region acts as an oxygen and iron sensor
CC       by binding oxygen through a diiron metal-center. In absence of oxygen
CC       and iron, the protein is ubiquitinated and degraded (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Polybiquitinated upon iron and oxygen depletion, leading to its
CC       degradation by the proteasome. Ubiquitination is regulated by the
CC       hemerythrin-like region that acts as an oxygen and iron sensor.
CC       Undergoes constitutive ubiquitin-dependent degradation at the steady
CC       state by HERC2. {ECO:0000250|UniProtKB:Q9UKA1}.
CC   -!- DISRUPTION PHENOTYPE: FBXL5-deletion mice die during early
CC       embryogenesis (PubMed:23135277, PubMed:21907140). FBXL5-null embryos
CC       accumulate excess ferrous iron and are exposed to damaging levels of
CC       oxidative stress (PubMed:21907140). Simultaneous inactivation of both
CC       the FBXL5 and IRP2 genes is sufficient to rescue embryonic lethality
CC       (PubMed:21907140). {ECO:0000269|PubMed:21907140,
CC       ECO:0000269|PubMed:23135277}.
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DR   EMBL; AK029957; BAC26698.1; -; mRNA.
DR   EMBL; AK041497; BAC30964.1; -; mRNA.
DR   EMBL; AK082931; BAC38698.1; -; mRNA.
DR   EMBL; AK085100; BAC39366.1; -; mRNA.
DR   EMBL; AK088067; BAC40126.1; -; mRNA.
DR   EMBL; AK150664; BAE29748.1; -; mRNA.
DR   EMBL; AK159744; BAE35337.1; -; mRNA.
DR   EMBL; AK171783; BAE42662.1; -; mRNA.
DR   EMBL; BC047214; AAH47214.1; -; mRNA.
DR   EMBL; BC113798; AAI13799.1; -; mRNA.
DR   CCDS; CCDS19263.1; -. [Q8C2S5-3]
DR   CCDS; CCDS51489.1; -. [Q8C2S5-1]
DR   RefSeq; NP_001153435.1; NM_001159963.1. [Q8C2S5-1]
DR   RefSeq; NP_848844.1; NM_178729.4. [Q8C2S5-3]
DR   AlphaFoldDB; Q8C2S5; -.
DR   SMR; Q8C2S5; -.
DR   BioGRID; 232476; 3.
DR   STRING; 10090.ENSMUSP00000045792; -.
DR   PhosphoSitePlus; Q8C2S5; -.
DR   PaxDb; 10090-ENSMUSP00000045792; -.
DR   Antibodypedia; 9778; 243 antibodies from 28 providers.
DR   Ensembl; ENSMUST00000047857.16; ENSMUSP00000045792.10; ENSMUSG00000039753.17. [Q8C2S5-1]
DR   Ensembl; ENSMUST00000087465.11; ENSMUSP00000084733.5; ENSMUSG00000039753.17. [Q8C2S5-3]
DR   Ensembl; ENSMUST00000114047.10; ENSMUSP00000109681.4; ENSMUSG00000039753.17. [Q8C2S5-2]
DR   Ensembl; ENSMUST00000121736.6; ENSMUSP00000112444.2; ENSMUSG00000039753.17. [Q8C2S5-5]
DR   Ensembl; ENSMUST00000196483.5; ENSMUSP00000143703.2; ENSMUSG00000039753.17. [Q8C2S5-4]
DR   GeneID; 242960; -.
DR   KEGG; mmu:242960; -.
DR   UCSC; uc008xhu.2; mouse. [Q8C2S5-1]
DR   UCSC; uc008xhv.2; mouse. [Q8C2S5-4]
DR   UCSC; uc008xhw.2; mouse. [Q8C2S5-3]
DR   UCSC; uc008xhx.2; mouse. [Q8C2S5-5]
DR   AGR; MGI:2152883; -.
DR   CTD; 26234; -.
DR   MGI; MGI:2152883; Fbxl5.
DR   VEuPathDB; HostDB:ENSMUSG00000039753; -.
DR   eggNOG; ENOG502QS5I; Eukaryota.
DR   GeneTree; ENSGT00390000006172; -.
DR   HOGENOM; CLU_017503_0_0_1; -.
DR   InParanoid; Q8C2S5; -.
DR   OMA; GEMFCGH; -.
DR   OrthoDB; 2913997at2759; -.
DR   PhylomeDB; Q8C2S5; -.
DR   TreeFam; TF331105; -.
DR   Reactome; R-MMU-8951664; Neddylation.
DR   Reactome; R-MMU-917937; Iron uptake and transport.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 242960; 8 hits in 77 CRISPR screens.
DR   ChiTaRS; Fbxl5; mouse.
DR   PRO; PR:Q8C2S5; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q8C2S5; Protein.
DR   Bgee; ENSMUSG00000039753; Expressed in spermatocyte and 235 other cell types or tissues.
DR   ExpressionAtlas; Q8C2S5; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; IMP:MGI.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:MGI.
DR   GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   CDD; cd22118; F-box_FBXL5; 1.
DR   CDD; cd12109; Hr_FBXL5; 1.
DR   Gene3D; 1.20.1280.50; -; 1.
DR   Gene3D; 1.20.120.520; nmb1532 protein domain like; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR012312; Hemerythrin-like.
DR   InterPro; IPR045808; Hr_FBXL5.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR13318:SF19; F-BOX_LRR-REPEAT PROTEIN 5; 1.
DR   PANTHER; PTHR13318; UNCHARACTERIZED; 1.
DR   Pfam; PF12937; F-box-like; 1.
DR   Pfam; PF01814; Hemerythrin; 1.
DR   Pfam; PF13516; LRR_6; 2.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00367; LRR_CC; 4.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS50181; FBOX; 1.
DR   Genevisible; Q8C2S5; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Iron; Iron-sulfur; Leucine-rich repeat;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..690
FT                   /note="F-box/LRR-repeat protein 5"
FT                   /id="PRO_0000119846"
FT   DOMAIN          202..248
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REPEAT          340..364
FT                   /note="LRR 1"
FT   REPEAT          365..392
FT                   /note="LRR 2"
FT   REPEAT          393..418
FT                   /note="LRR 3"
FT   REPEAT          478..507
FT                   /note="LRR 4"
FT   REPEAT          575..606
FT                   /note="LRR 5"
FT   REPEAT          607..634
FT                   /note="LRR 6"
FT   REPEAT          635..660
FT                   /note="LRR 7"
FT   REGION          1..159
FT                   /note="Hemerythrin-like"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKA1"
FT   BINDING         15
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKA1"
FT   BINDING         57
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKA1"
FT   BINDING         58
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKA1"
FT   BINDING         61
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKA1"
FT   BINDING         61
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKA1"
FT   BINDING         80
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKA1"
FT   BINDING         126
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKA1"
FT   BINDING         130
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKA1"
FT   BINDING         130
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKA1"
FT   BINDING         661
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKA1"
FT   BINDING         675
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKA1"
FT   BINDING         685
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKA1"
FT   BINDING         686
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKA1"
FT   VAR_SEQ         1..28
FT                   /note="MAPFPDEVDVFTAPHWRMKQLVGRYCDK -> MRNNQELKYEIKWKHLDCSV
FT                   VE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_008418"
FT   VAR_SEQ         29..71
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_038529"
FT   VAR_SEQ         298
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_038530"
FT   VAR_SEQ         617..623
FT                   /note="ALTLGGG -> WVISPSC (in isoform 3 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_008419"
FT   VAR_SEQ         624..690
FT                   /note="Missing (in isoform 3 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_008420"
FT   CONFLICT        105
FT                   /note="Q -> R (in Ref. 1; BAC38698)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="M -> K (in Ref. 1; BAC40126)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   690 AA;  77894 MW;  9558476AFB3ECCA0 CRC64;
     MAPFPDEVDV FTAPHWRMKQ LVGRYCDKLS KTNFSNNNDF RALLQSLYAT FKEFKMHEQI
     ENEYIIGLLQ QRSQTIYNVH SDNKLSEMLS LFEKGLKNVK NEYEQLNYAK QLKERLEAFT
     RDFLPHMKEE EEVFQPMLME YFTYEELKDI KKKVIAQHCS QKDTAELLRG LSLWNQAEER
     QKVLKYSVDE KADTEAEVSE HSTGITHLPP EVMLSIFSYL NPQELCRCSQ VSTKWSQLAK
     TGSLWKHLYP VHWARGDWYS GPATELDTEP DEEWVRNRKD ESRAFQEWDE DADIDESEES
     AEESVAISIA QMEKRVLHGL IHNVLPYVGT SVKTLVLAYS SAVSSKMVRQ ILELCPNLEH
     LDLTQTDISD SAFDSWSWLG CCQSLRHLDL SGCEKITDMA LEKISRALGV LTSHQSGFLK
     SAGKAASTPW TSKDITMPST TQYACLHNLT DKGIGEEIDN EHSWTEPVSS ESLTSPYVWM
     LDAEDLADIE DAVEWRHRNV ESLCVMETAS NFGCSSSGCY SKDIVGLRTS VCWQQHCASP
     AFAYCGHSFC CTGTALRTMT TLPATSAMCR KALRTTLPRG KDLIYFGSEK SDQETGRVLL
     FLSLSGCYQI TDHGLRALTL GGGLPYLEHL NLSGCLTVTG AGLQDLVSAC PSLNDEYFYY
     CDNINGPHAD TASGCQNLQC GFRACCRSGE
//