NB5R4_MOUSE
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 03-AUG-2022, entry version 141.
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};
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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 iPTMnet; Q3TDX8; -.
DR PhosphoSitePlus; Q3TDX8; -.
DR EPD; Q3TDX8; -.
DR MaxQB; Q3TDX8; -.
DR PaxDb; Q3TDX8; -.
DR PeptideAtlas; Q3TDX8; -.
DR PRIDE; Q3TDX8; -.
DR ProteomicsDB; 252784; -. [Q3TDX8-4]
DR ProteomicsDB; 252785; -. [Q3TDX8-5]
DR Antibodypedia; 18533; 157 antibodies from 30 providers.
DR DNASU; 266690; -.
DR Ensembl; ENSMUST00000168529; ENSMUSP00000126119; ENSMUSG00000032872. [Q3TDX8-4]
DR GeneID; 266690; -.
DR KEGG; mmu:266690; -.
DR UCSC; uc009qyc.2; mouse. [Q3TDX8-4]
DR UCSC; uc009qyf.2; mouse. [Q3TDX8-5]
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; DFNHDSF; -.
DR OrthoDB; 1311668at2759; -.
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 70 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 80 other tissues.
DR ExpressionAtlas; Q3TDX8; baseline and differential.
DR Genevisible; Q3TDX8; MM.
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; cd06490; p23_NCB5OR; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 3.10.120.10; -; 1.
DR Gene3D; 3.40.50.80; -; 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; PTHR19370; 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; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR SUPFAM; SSF63380; SSF63380; 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.
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
