FRIH_MOUSE
ID FRIH_MOUSE Reviewed; 182 AA.
AC P09528; Q3UI44;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Ferritin heavy chain;
DE Short=Ferritin H subunit;
DE EC=1.16.3.1;
DE Contains:
DE RecName: Full=Ferritin heavy chain, N-terminally processed;
GN Name=Fth1; Synonyms=Fth;
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.
RC STRAIN=BALB/cJ;
RX PubMed=2798146; DOI=10.1093/nar/17.19.8005;
RA Yachaou A., Renaudie F., Grandchamp B., Beaumont C.;
RT "Nucleotide sequence of the mouse ferritin H chain gene.";
RL Nucleic Acids Res. 17:8005-8005(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Macrophage;
RX PubMed=3194211; DOI=10.1093/nar/16.21.10373;
RA Miyazaki Y., Setoguchi M., Higuchi Y., Yoshida S., Akizuki S., Yamamoto S.;
RT "Nucleotide sequence of cDNA encoding the heavy subunit of mouse macrophage
RT ferritin.";
RL Nucleic Acids Res. 16:10373-10373(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3410854; DOI=10.1016/s0021-9258(18)37801-3;
RA Torti S.V., Kwak E.L., Miller S.C., Miller L.L., Ringold G.M., Myambo K.B.,
RA Young A.P., Torti F.M.;
RT "The molecular cloning and characterization of murine ferritin heavy chain,
RT a tumor necrosis factor-inducible gene.";
RL J. Biol. Chem. 263:12638-12644(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2258056; DOI=10.1016/0378-1119(90)90396-9;
RA Kwak E.L., Torti S.V., Torti F.M.;
RT "Murine ferritin heavy chain: isolation and characterization of a
RT functional gene.";
RL Gene 94:255-261(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2708374; DOI=10.1016/s0021-9258(18)83262-8;
RA Beaumont C., Dugast I., Renaudie F., Souroujon M., Grandchamp B.;
RT "Transcriptional regulation of ferritin H and L subunits in adult erythroid
RT and liver cells from the mouse. Unambiguous identification of mouse
RT ferritin subunits and in vitro formation of the ferritin shells.";
RL J. Biol. Chem. 264:7498-7504(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Heart, and Kidney;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [8]
RP PROTEIN SEQUENCE OF 11-23 AND 55-64, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=10652280; DOI=10.1074/jbc.275.5.3021;
RA Ferreira C., Bucchini D., Martin M.E., Levi S., Arosio P., Grandchamp B.,
RA Beaumont C.;
RT "Early embryonic lethality of H ferritin gene deletion in mice.";
RL J. Biol. Chem. 275:3021-3024(2000).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=11468145; DOI=10.1182/blood.v98.3.525;
RA Ferreira C., Santambrogio P., Martin M.E., Andrieu V., Feldmann G.,
RA Henin D., Beaumont C.;
RT "H ferritin knockout mice: a model of hyperferritinemia in the absence of
RT iron overload.";
RL Blood 98:525-532(2001).
RN [11]
RP FUNCTION.
RX PubMed=19154717; DOI=10.1016/j.devcel.2008.12.002;
RA Li J.Y., Paragas N., Ned R.M., Qiu A., Viltard M., Leete T., Drexler I.R.,
RA Chen X., Sanna-Cherchi S., Mohammed F., Williams D., Lin C.S.,
RA Schmidt-Ott K.M., Andrews N.C., Barasch J.;
RT "Scara5 is a ferritin receptor mediating non-transferrin iron delivery.";
RL Dev. Cell 16:35-46(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form.
CC Important for iron homeostasis. Has ferroxidase activity. Iron is taken
CC up in the ferrous form and deposited as ferric hydroxides after
CC oxidation. Also plays a role in delivery of iron to cells. Mediates
CC iron uptake in capsule cells of the developing kidney.
CC {ECO:0000269|PubMed:19154717}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC -!- SUBUNIT: Oligomer of 24 subunits. There are two types of subunits: L
CC (light) chain and H (heavy) chain. The major chain can be light or
CC heavy, depending on the species and tissue type. The functional
CC molecule forms a roughly spherical shell with a diameter of 12 nm and
CC contains a central cavity into which the insoluble mineral iron core is
CC deposited.
CC -!- INTERACTION:
CC P09528; P09528: Fth1; NbExp=3; IntAct=EBI-308950, EBI-308950;
CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc, detected at low levels in the
CC developing heart and central nervous system. At later stages of
CC development, widely expressed, predominantly in the heart and brown fat
CC tissue. {ECO:0000269|PubMed:10652280}.
CC -!- DISRUPTION PHENOTYPE: Homozygous mutant embryos die in utero between
CC 3.5 and 9.5 dpc (PubMed:10652280). Heterozygous animals are healthy and
CC fertile and do not present any apparent abnormalities. They show
CC slightly elevated tissue light chain ferritin content and 7- to 10-fold
CC more light chain ferritin in the serum than normal mice, but their
CC serum iron remains unchanged. {ECO:0000269|PubMed:10652280,
CC ECO:0000269|PubMed:11468145}.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR EMBL; X52561; CAA36795.1; -; Genomic_DNA.
DR EMBL; X12812; CAA31300.1; -; mRNA.
DR EMBL; J03941; AAA37611.1; -; mRNA.
DR EMBL; M60170; AAA37613.1; -; Genomic_DNA.
DR EMBL; M24509; AAA37612.1; -; mRNA.
DR EMBL; AK027998; BAC25694.1; -; mRNA.
DR EMBL; AK139622; BAE24084.1; -; mRNA.
DR EMBL; AK147082; BAE27662.1; -; mRNA.
DR EMBL; AK150262; BAE29419.1; -; mRNA.
DR EMBL; AK150508; BAE29621.1; -; mRNA.
DR EMBL; AK150628; BAE29718.1; -; mRNA.
DR EMBL; AK150679; BAE29759.1; -; mRNA.
DR EMBL; AK150693; BAE29772.1; -; mRNA.
DR EMBL; AK151192; BAE30189.1; -; mRNA.
DR EMBL; AK151241; BAE30233.1; -; mRNA.
DR EMBL; AK151399; BAE30367.1; -; mRNA.
DR EMBL; AK151609; BAE30548.1; -; mRNA.
DR EMBL; AK151675; BAE30600.1; -; mRNA.
DR EMBL; AK152071; BAE30924.1; -; mRNA.
DR EMBL; AK152542; BAE31297.1; -; mRNA.
DR EMBL; AK152702; BAE31431.1; -; mRNA.
DR EMBL; AK153017; BAE31651.1; -; mRNA.
DR EMBL; AK153195; BAE31795.1; -; mRNA.
DR EMBL; AK153199; BAE31799.1; -; mRNA.
DR EMBL; AK159243; BAE34925.1; -; mRNA.
DR EMBL; AK168601; BAE40468.1; -; mRNA.
DR EMBL; AK169004; BAE40803.1; -; mRNA.
DR EMBL; BC012314; AAH12314.1; -; mRNA.
DR CCDS; CCDS29567.1; -.
DR PIR; S06070; S06070.
DR RefSeq; NP_034369.1; NM_010239.2.
DR PDB; 3WNW; X-ray; 2.24 A; A/B/C/D/E/F/G/H/I/J/K/L=1-182.
DR PDB; 5OBA; X-ray; 2.85 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-177.
DR PDB; 5OBB; X-ray; 2.65 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-177.
DR PDB; 6S61; EM; 1.84 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-182.
DR PDB; 6SHT; EM; 2.73 A; A=1-182.
DR PDB; 6V21; EM; 1.75 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=5-178.
DR PDB; 7A4M; EM; 1.22 A; A=6-177.
DR PDB; 7KOD; EM; 1.66 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-182.
DR PDB; 7TB3; EM; 2.57 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=7-182.
DR PDB; 7TBH; EM; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=7-182.
DR PDBsum; 3WNW; -.
DR PDBsum; 5OBA; -.
DR PDBsum; 5OBB; -.
DR PDBsum; 6S61; -.
DR PDBsum; 6SHT; -.
DR PDBsum; 6V21; -.
DR PDBsum; 7A4M; -.
DR PDBsum; 7KOD; -.
DR PDBsum; 7TB3; -.
DR PDBsum; 7TBH; -.
DR AlphaFoldDB; P09528; -.
DR SMR; P09528; -.
DR BioGRID; 199755; 11.
DR IntAct; P09528; 5.
DR MINT; P09528; -.
DR STRING; 10090.ENSMUSP00000025563; -.
DR iPTMnet; P09528; -.
DR MetOSite; P09528; -.
DR PhosphoSitePlus; P09528; -.
DR SwissPalm; P09528; -.
DR REPRODUCTION-2DPAGE; P09528; -.
DR CPTAC; non-CPTAC-3809; -.
DR EPD; P09528; -.
DR jPOST; P09528; -.
DR MaxQB; P09528; -.
DR PaxDb; P09528; -.
DR PeptideAtlas; P09528; -.
DR PRIDE; P09528; -.
DR ProteomicsDB; 271802; -.
DR Antibodypedia; 28385; 887 antibodies from 41 providers.
DR DNASU; 14319; -.
DR Ensembl; ENSMUST00000025563; ENSMUSP00000025563; ENSMUSG00000024661.
DR Ensembl; ENSMUST00000235196; ENSMUSP00000158539; ENSMUSG00000024661.
DR GeneID; 14319; -.
DR KEGG; mmu:14319; -.
DR UCSC; uc008got.2; mouse.
DR CTD; 2495; -.
DR MGI; MGI:95588; Fth1.
DR VEuPathDB; HostDB:ENSMUSG00000024661; -.
DR eggNOG; KOG2332; Eukaryota.
DR GeneTree; ENSGT00950000182841; -.
DR HOGENOM; CLU_065681_4_0_1; -.
DR InParanoid; P09528; -.
DR OMA; YLSMGYF; -.
DR OrthoDB; 1249457at2759; -.
DR PhylomeDB; P09528; -.
DR TreeFam; TF313885; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-917937; Iron uptake and transport.
DR BioGRID-ORCS; 14319; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Fth1; mouse.
DR PRO; PR:P09528; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P09528; protein.
DR Bgee; ENSMUSG00000024661; Expressed in globus pallidus and 275 other tissues.
DR ExpressionAtlas; P09528; baseline and differential.
DR Genevisible; P09528; MM.
DR GO; GO:0044754; C:autolysosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005506; F:iron ion binding; IDA:MGI.
DR GO; GO:0006955; P:immune response; ISS:UniProtKB.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; ISO:MGI.
DR GO; GO:0006826; P:iron ion transport; IDA:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0060547; P:negative regulation of necrotic cell death; ISO:MGI.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR001519; Ferritin.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009040; Ferritin-like_diiron.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR014034; Ferritin_CS.
DR InterPro; IPR008331; Ferritin_DPS_dom.
DR PANTHER; PTHR11431; PTHR11431; 1.
DR Pfam; PF00210; Ferritin; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00540; FERRITIN_1; 1.
DR PROSITE; PS00204; FERRITIN_2; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Iron; Iron storage;
KW Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..182
FT /note="Ferritin heavy chain"
FT /id="PRO_0000424473"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02794"
FT CHAIN 2..182
FT /note="Ferritin heavy chain, N-terminally processed"
FT /id="PRO_0000201049"
FT DOMAIN 11..160
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 28
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 66
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 108
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 142
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P02794"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Ferritin heavy chain, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P02794"
FT CONFLICT 17
FT /note="A -> S (in Ref. 5; AAA37612)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="Y -> H (in Ref. 5; AAA37612)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="S -> N (in Ref. 5; AAA37612)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="A -> S (in Ref. 5; AAA37612)"
FT /evidence="ECO:0000305"
FT HELIX 15..42
FT /evidence="ECO:0007829|PDB:7A4M"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:7A4M"
FT HELIX 50..76
FT /evidence="ECO:0007829|PDB:7A4M"
FT HELIX 97..124
FT /evidence="ECO:0007829|PDB:7A4M"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:7A4M"
FT HELIX 139..159
FT /evidence="ECO:0007829|PDB:7A4M"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:7A4M"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:7A4M"
SQ SEQUENCE 182 AA; 21067 MW; 129A8887A2BC650B CRC64;
MTTASPSQVR QNYHQDAEAA INRQINLELY ASYVYLSMSC YFDRDDVALK NFAKYFLHQS
HEEREHAEKL MKLQNQRGGR IFLQDIKKPD RDDWESGLNA MECALHLEKS VNQSLLELHK
LATDKNDPHL CDFIETYYLS EQVKSIKELG DHVTNLRKMG APEAGMAEYL FDKHTLGHGD
ES
