ID NB5R4_MOUSE Reviewed; 528 AA. AC Q3TDX8; E9Q129; Q3TJH3; Q3U012; Q6VXY4; Q6VXY5; Q8BJV8; Q8BTI5; Q8R3H8; AC Q99LY4; Q99P29; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 3. DT 27-MAR-2024, entry version 150. DE RecName: Full=Cytochrome b5 reductase 4; DE EC=1.6.2.2; DE AltName: Full=Flavohemoprotein b5/b5R; DE Short=b5+b5R; DE AltName: Full=N-terminal cytochrome b5 and cytochrome b5 oxidoreductase domain-containing protein; DE AltName: Full=cb5/cb5R; GN Name=Cyb5r4; Synonyms=Ncb5or; 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] (ISOFORM 1), AND VARIANT RP ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS. RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye, Liver, Spinal cord, and Spleen; 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 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS. RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 35-528 (ISOFORM 1), AND VARIANT RP ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS. RX PubMed=10611283; DOI=10.1073/pnas.96.26.14742; RA Zhu H., Qiu H., Yoon H.-W., Huang S., Bunn H.F.; RT "Identification of a cytochrome b-type NAD(P)H oxidoreductase ubiquitously RT expressed in human cells."; RL Proc. Natl. Acad. Sci. U.S.A. 96:14742-14747(1999). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-528 (ISOFORMS 1 AND 2), VARIANT RP ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS, AND TISSUE SPECIFICITY. RC STRAIN=SWR/J; TISSUE=Testis; RX PubMed=14962668; DOI=10.1016/j.ygeno.2003.08.020; RA Curry B.J., Roman S.D., Wallace C.A., Scott R., Miriami E., Aitken R.J.; RT "Identification and characterization of a novel splice variant of mouse and RT rat cytochrome b5/cytochrome b5 reductase."; RL Genomics 83:425-438(2004). RN [6] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=15247412; DOI=10.1073/pnas.0404044101; RA Xie J., Zhu H., Larade K., Ladoux A., Seguritan A., Chu M., Ito S., RA Bronson R.T., Leiter E.H., Zhang C.-Y., Rosen E.D., Bunn H.F.; RT "Absence of a reductase, NCB5OR, causes insulin-deficient diabetes."; RL Proc. Natl. Acad. Sci. U.S.A. 101:10750-10755(2004). RN [7] RP TISSUE SPECIFICITY. RX PubMed=16814408; DOI=10.1016/j.bbaexp.2006.05.002; RA Larade K., Bunn H.F.; RT "Promoter characterization and transcriptional regulation of Ncb5or, a RT novel reductase necessary for pancreatic beta-cell maintenance."; RL Biochim. Biophys. Acta 1759:257-262(2006). CC -!- FUNCTION: NADH-cytochrome b5 reductase involved in endoplasmic CC reticulum stress response pathway. Plays a critical role in protecting CC pancreatic beta-cells against oxidant stress, possibly by protecting CC the cell from excess buildup of reactive oxygen species (ROS). CC {ECO:0000269|PubMed:15247412}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + CC H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA- CC COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Note=Soluble protein. CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q3TDX8-4; Sequence=Displayed; CC Name=2; Synonyms=cb5/cb5rDelta12; CC IsoId=Q3TDX8-5; Sequence=VSP_041453; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 2 is expressed in CC testis, brain, skeletal muscle and in the male germline. CC {ECO:0000269|PubMed:14962668, ECO:0000269|PubMed:16814408}. CC -!- DISRUPTION PHENOTYPE: Mice display insulin-deficient diabetes. Embryos CC and fetus develop normally. At 4 weeks of age, mice show have normal CC blood glucose levels but impaired glucose tolerance. Isolated islets CC have markedly impaired glucose- or arginine-stimulated insulin CC secretion. By 7 weeks of age, they develop severe hyperglycemia with CC markedly decreased serum insulin levels and nearly normal insulin CC tolerance. As the animals age, there is a progressive loss of beta CC cells in pancreatic islets, but there is no loss of alpha, delta, or PP CC cells. 4 week-old mice have enhanced sensitivity to the diabetogenic CC agent streptozotocin. {ECO:0000269|PubMed:15247412}. CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome CC reductase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH25438.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC41118.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAE34044.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAE42908.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK078682; BAC37357.1; -; mRNA. DR EMBL; AK090159; BAC41118.1; ALT_INIT; mRNA. DR EMBL; AK157312; BAE34044.1; ALT_INIT; mRNA. DR EMBL; AK167436; BAE39522.1; -; mRNA. DR EMBL; AK169937; BAE41470.1; -; mRNA. DR EMBL; AK172252; BAE42908.1; ALT_INIT; mRNA. DR EMBL; AC156793; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC025438; AAH25438.1; ALT_INIT; mRNA. DR EMBL; BC002170; AAH02170.1; -; mRNA. DR EMBL; AF338818; AAK08116.1; -; mRNA. DR EMBL; AY321368; AAQ83900.1; -; mRNA. DR EMBL; AY321369; AAQ83901.1; -; mRNA. DR CCDS; CCDS40716.2; -. [Q3TDX8-4] DR RefSeq; NP_077157.2; NM_024195.2. [Q3TDX8-4] DR RefSeq; XP_006511262.1; XM_006511199.1. DR AlphaFoldDB; Q3TDX8; -. DR SMR; Q3TDX8; -. DR BioGRID; 234467; 4. DR IntAct; Q3TDX8; 4. DR MINT; Q3TDX8; -. DR STRING; 10090.ENSMUSP00000126119; -. DR GlyGen; Q3TDX8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q3TDX8; -. DR PhosphoSitePlus; Q3TDX8; -. DR EPD; Q3TDX8; -. DR MaxQB; Q3TDX8; -. DR PaxDb; 10090-ENSMUSP00000126119; -. DR PeptideAtlas; Q3TDX8; -. DR ProteomicsDB; 252784; -. [Q3TDX8-4] DR ProteomicsDB; 252785; -. [Q3TDX8-5] DR Pumba; Q3TDX8; -. DR Antibodypedia; 18533; 178 antibodies from 30 providers. DR DNASU; 266690; -. DR Ensembl; ENSMUST00000168529.9; ENSMUSP00000126119.3; ENSMUSG00000032872.17. [Q3TDX8-4] DR GeneID; 266690; -. DR KEGG; mmu:266690; -. DR UCSC; uc009qyc.2; mouse. [Q3TDX8-4] DR UCSC; uc009qyf.2; mouse. [Q3TDX8-5] DR AGR; MGI:2386848; -. DR CTD; 51167; -. DR MGI; MGI:2386848; Cyb5r4. DR VEuPathDB; HostDB:ENSMUSG00000032872; -. DR eggNOG; KOG0534; Eukaryota. DR eggNOG; KOG0536; Eukaryota. DR GeneTree; ENSGT00940000155536; -. DR HOGENOM; CLU_003827_0_2_1; -. DR InParanoid; Q3TDX8; -. DR OMA; WIRLCNS; -. DR OrthoDB; 163533at2759; -. DR PhylomeDB; Q3TDX8; -. DR TreeFam; TF313874; -. DR BRENDA; 1.6.2.2; 3474. DR Reactome; R-MMU-1237044; Erythrocytes take up carbon dioxide and release oxygen. DR BioGRID-ORCS; 266690; 11 hits in 75 CRISPR screens. DR ChiTaRS; Cyb5r4; mouse. DR PRO; PR:Q3TDX8; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q3TDX8; Protein. DR Bgee; ENSMUSG00000032872; Expressed in granulocyte and 83 other cell types or tissues. DR ExpressionAtlas; Q3TDX8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IDA:MGI. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISO:MGI. DR GO; GO:0020037; F:heme binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IEA:Ensembl. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; ISO:MGI. DR GO; GO:0016653; F:oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor; ISO:MGI. DR GO; GO:0048468; P:cell development; IMP:MGI. DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISO:MGI. DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI. DR GO; GO:0042168; P:heme metabolic process; ISO:MGI. DR GO; GO:0030073; P:insulin secretion; IMP:MGI. DR GO; GO:0006739; P:NADP metabolic process; ISO:MGI. DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISO:MGI. DR GO; GO:0046677; P:response to antibiotic; IMP:MGI. DR GO; GO:0006801; P:superoxide metabolic process; ISO:MGI. DR CDD; cd06183; cyt_b5_reduct_like; 1. DR CDD; cd06490; p23_NCB5OR; 1. DR Gene3D; 2.60.40.790; -; 1. DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR InterPro; IPR001834; CBR-like. DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom. DR InterPro; IPR007052; CS_dom. DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd. DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf. DR InterPro; IPR018506; Cyt_B5_heme-BS. DR InterPro; IPR017927; FAD-bd_FR_type. DR InterPro; IPR039261; FNR_nucleotide-bd. DR InterPro; IPR008978; HSP20-like_chaperone. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR037908; p23_NCB5OR. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR19370; NADH-CYTOCHROME B5 REDUCTASE; 1. DR Pfam; PF04969; CS; 1. DR Pfam; PF00173; Cyt-b5; 1. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00406; CYTB5RDTASE. DR PRINTS; PR00363; CYTOCHROMEB5. DR SMART; SM01117; Cyt-b5; 1. DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF49764; HSP20-like chaperones; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1. DR PROSITE; PS51203; CS; 1. DR PROSITE; PS00191; CYTOCHROME_B5_1; 1. DR PROSITE; PS50255; CYTOCHROME_B5_2; 1. DR PROSITE; PS51384; FAD_FR; 1. DR Genevisible; Q3TDX8; MM. PE 2: Evidence at transcript level; KW Acetylation; Alternative splicing; Endoplasmic reticulum; FAD; KW Flavoprotein; Heme; Iron; Metal-binding; NAD; Oxidoreductase; KW Reference proteome. FT CHAIN 1..528 FT /note="Cytochrome b5 reductase 4" FT /id="PRO_0000410469" FT DOMAIN 54..130 FT /note="Cytochrome b5 heme-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279" FT DOMAIN 172..263 FT /note="CS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547" FT DOMAIN 280..392 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716" FT REGION 1..29 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..27 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 89 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279" FT BINDING 112 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279" FT BINDING 372..387 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 399..431 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q7L1T6" FT VAR_SEQ 326..376 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14962668" FT /id="VSP_041453" FT VARIANT 156 FT /note="S -> SDTLPRDVT" FT /evidence="ECO:0000269|PubMed:10611283, FT ECO:0000269|PubMed:14962668, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072" FT CONFLICT 171 FT /note="D -> G (in Ref. 1; BAE34044/BAE41470/BAE42908, 4; FT AAK08116 and 5; AAQ83900/AAQ83901)" FT /evidence="ECO:0000305" FT CONFLICT 216 FT /note="V -> I (in Ref. 3; AAH25438)" FT /evidence="ECO:0000305" FT CONFLICT 300 FT /note="F -> L (in Ref. 1; BAE34044/BAE41470/BAE42908, 3; FT AAH02170, 4; AAK08116 and 5; AAQ83900/AAQ83901)" FT /evidence="ECO:0000305" FT CONFLICT 336 FT /note="V -> L (in Ref. 1; BAE34044)" FT /evidence="ECO:0000305" FT CONFLICT 339 FT /note="S -> P (in Ref. 1; BAE41470)" FT /evidence="ECO:0000305" FT CONFLICT 356 FT /note="C -> Y (in Ref. 1; BAE34044/BAE41470/BAE42908, 3; FT AAH02170/AAH25438, 4; AAK08116 and 5; AAQ83900)" FT /evidence="ECO:0000305" FT CONFLICT 388 FT /note="D -> N (in Ref. 1; BAE34044/BAE41470/BAE42908, 3; FT AAH02170/AAH25438, 4; AAK08116 and 5; AAQ83900/AAQ83901)" FT /evidence="ECO:0000305" FT CONFLICT 393 FT /note="K -> T (in Ref. 3; AAH25438)" FT /evidence="ECO:0000305" FT CONFLICT 438 FT /note="E -> D (in Ref. 1; BAC37357)" FT /evidence="ECO:0000305" FT CONFLICT 504 FT /note="P -> Q (in Ref. 1; BAE39522)" FT /evidence="ECO:0000305" SQ SEQUENCE 528 AA; 59716 MW; 8CF34CE865980A66 CRC64; MLNVPSQAFP APGSQQRVSS QGRSKVPLKQ GRSLMDWIRL TKSGKDLTGL KGGLIEVTEE ELKKHNKKED CWICIRGFVY NVSPYMEYHP GGEDELMRAA GADGTDLFNE VHRWVNYESM LKECLVGRMA VKPAVPKDCH EGKRVLNGML PKSQMSDTLP RDVTDTLPRE DLSSPSYDWF QTESSVTIVV YTKQKNISLD SVIVDLQDDS LRAEAVIKDH SYLVHVGLSH EVQENFSVRV IENVGKIEIV LQKKESVSWQ CLGDHLEKHD SFIPKKDTGL YYRRCQLISK EDVTHDTRLF CLMLPPSTHL QVPVGQHVYL KLSVTGAEIV KPYTPVSDSL LSDFKEPVLS PNKYICFLIK IYPAGLFTPE LDRLQIGDFI SVSGPEGDFK VSKLQEVEDL FLLAAGTGFT PMVTVLNYAL SHMSSLRKVK LMFFNKTEDD IIWRCQLEKL ALREKRFDVE FVLSAPSPEW NGKQGHISRA LLSEFLQRSS ENSRAFLCIC GPTPFTDEGI RLLHDLNFSD DEIHGFTA //