TFR2_HUMAN
ID TFR2_HUMAN Reviewed; 801 AA.
AC Q9UP52; A6NGM7; O75422; Q1HE13; Q9HA99; Q9NX67;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Transferrin receptor protein 2;
DE Short=TfR2;
GN Name=TFR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RC TISSUE=Erythroleukemia, and Myeloid leukemia cell;
RX PubMed=10409623; DOI=10.1074/jbc.274.30.20826;
RA Kawabata H., Yang R., Hirama T., Vuong P.T., Kawano S., Gombart A.F.,
RA Koeffler H.P.;
RT "Molecular cloning of transferrin receptor 2: a new member of the
RT transferrin receptor-like family.";
RL J. Biol. Chem. 274:20826-20832(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM GAMMA).
RX PubMed=9799793; DOI=10.1101/gr.8.10.1060;
RA Gloeckner G., Scherer S., Schattevoy R., Boright A.P., Weber J.,
RA Tsui L.-C., Rosenthal A.;
RT "Large-scale sequencing of two regions in human chromosome 7q22: analysis
RT of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17
RT genes.";
RL Genome Res. 8:1060-1073(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-158 AND 370-801.
RC TISSUE=Carcinoma, and Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP DISEASE.
RX PubMed=10802645; DOI=10.1038/75534;
RA Camaschella C., Roetto A., Cali A., De Gobbi M., Garozzo G., Carella M.,
RA Majorano N., Totaro A., Gasparini P.;
RT "The gene TFR2 is mutated in a new type of haemochromatosis mapping to
RT 7q22.";
RL Nat. Genet. 25:14-15(2000).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-339 AND ASN-754.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP VARIANT HFE3 LYS-172.
RX PubMed=11313241; DOI=10.1182/blood.v97.9.2555;
RA Roetto A., Totaro A., Piperno A., Piga A., Longo F., Garozzo G., Cali A.,
RA De Gobbi M., Gasparini P., Camaschella C.;
RT "New mutations inactivating transferrin 2 in hemochromatosis type 3.";
RL Blood 97:2555-2560(2001).
RN [11]
RP VARIANT HFE3 PRO-690.
RX PubMed=12130528; DOI=10.1182/blood-2002-01-0133;
RA Mattman A., Huntsman D., Lockitch G., Langlois S., Buskard N., Ralston D.,
RA Butterfield Y., Rodrigues P., Jones S., Porto G., Marra M., De Sousa M.,
RA Vatcher G.;
RT "Transferrin receptor 2 (TfR2) and HFE mutational analysis in non-C282Y
RT iron overload: identification of a novel TfR2 mutation.";
RL Blood 100:1075-1077(2002).
RN [12]
RP VARIANT GLN-455.
RX PubMed=12150153; DOI=10.1182/blood-2002-04-1077;
RA Hofmann W.-K., Tong X.-J., Ajioka R.S., Kushner J.P., Koeffler H.P.;
RT "Mutation analysis of transferrin-receptor 2 in patients with atypical
RT hemochromatosis.";
RL Blood 100:1099-1100(2002).
RN [13]
RP VARIANT HFE3 ILE-22.
RX PubMed=14633868; DOI=10.1373/clinchem.2003.023440;
RA Biasiotto G., Belloli S., Ruggeri G., Zanella I., Gerardi G., Corrado M.,
RA Gobbi E., Albertini A., Arosio P.;
RT "Identification of new mutations of the HFE, hepcidin, and transferrin
RT receptor 2 genes by denaturing HPLC analysis of individuals with
RT biochemical indications of iron overload.";
RL Clin. Chem. 49:1981-1988(2003).
CC -!- FUNCTION: Mediates cellular uptake of transferrin-bound iron in a non-
CC iron dependent manner. May be involved in iron metabolism, hepatocyte
CC function and erythrocyte differentiation.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC Q9UP52; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-3934135, EBI-2804156;
CC Q9UP52; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-3934135, EBI-8652744;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein.
CC -!- SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm {ECO:0000305}.
CC Note=Lacks the transmembrane domain. Probably intracellular.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Alpha;
CC IsoId=Q9UP52-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q9UP52-2; Sequence=VSP_005354;
CC Name=Gamma;
CC IsoId=Q9UP52-3; Sequence=VSP_005355;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in liver. While the alpha
CC form is also expressed in spleen, lung, muscle, prostate and peripheral
CC blood mononuclear cells, the beta form is expressed in all tissues
CC tested, albeit weakly.
CC -!- DISEASE: Hemochromatosis 3 (HFE3) [MIM:604250]: A disorder of iron
CC metabolism characterized by iron overload. Excess iron is deposited in
CC a variety of organs leading to their failure, and resulting in serious
CC illnesses including cirrhosis, hepatomas, diabetes, cardiomyopathy,
CC arthritis, and hypogonadotropic hypogonadism. Severe effects of the
CC disease usually do not appear until after decades of progressive iron
CC loading. {ECO:0000269|PubMed:11313241, ECO:0000269|PubMed:12130528,
CC ECO:0000269|PubMed:14633868}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: The variant Lys-172 found in hereditary hemochromatosis
CC type III affects the putative initiation codon of the beta isoform thus
CC preventing its translation.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91153.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF067864; AAD45561.1; -; mRNA.
DR EMBL; AF053356; AAC78796.1; -; Genomic_DNA.
DR EMBL; DQ496110; ABF47099.1; -; Genomic_DNA.
DR EMBL; AC099394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC142630; AAI42631.1; -; mRNA.
DR EMBL; AK022002; BAB13951.1; -; mRNA.
DR EMBL; AK000421; BAA91153.1; ALT_INIT; mRNA.
DR CCDS; CCDS34707.1; -. [Q9UP52-1]
DR RefSeq; NP_001193784.1; NM_001206855.1. [Q9UP52-2]
DR RefSeq; NP_003218.2; NM_003227.3. [Q9UP52-1]
DR RefSeq; XP_005250610.1; XM_005250553.4.
DR RefSeq; XP_016868062.1; XM_017012573.1.
DR AlphaFoldDB; Q9UP52; -.
DR SMR; Q9UP52; -.
DR BioGRID; 112894; 41.
DR IntAct; Q9UP52; 4.
DR STRING; 9606.ENSP00000420525; -.
DR ChEMBL; CHEMBL3988361; -.
DR DrugBank; DB15617; Ferric derisomaltose.
DR DrugBank; DB13257; Ferrous sulfate anhydrous.
DR MEROPS; M28.973; -.
DR TCDB; 9.B.229.1.2; the transferrin receptor, cd71, (tfr) family.
DR GlyGen; Q9UP52; 4 sites.
DR iPTMnet; Q9UP52; -.
DR PhosphoSitePlus; Q9UP52; -.
DR BioMuta; TFR2; -.
DR DMDM; 20140912; -.
DR jPOST; Q9UP52; -.
DR MassIVE; Q9UP52; -.
DR MaxQB; Q9UP52; -.
DR PaxDb; Q9UP52; -.
DR PeptideAtlas; Q9UP52; -.
DR PRIDE; Q9UP52; -.
DR ProteomicsDB; 85352; -. [Q9UP52-1]
DR ProteomicsDB; 85353; -. [Q9UP52-2]
DR ProteomicsDB; 85354; -. [Q9UP52-3]
DR Antibodypedia; 2306; 215 antibodies from 28 providers.
DR DNASU; 7036; -.
DR Ensembl; ENST00000223051.8; ENSP00000223051.3; ENSG00000106327.13. [Q9UP52-1]
DR Ensembl; ENST00000462107.1; ENSP00000420525.1; ENSG00000106327.13. [Q9UP52-1]
DR GeneID; 7036; -.
DR KEGG; hsa:7036; -.
DR MANE-Select; ENST00000223051.8; ENSP00000223051.3; NM_003227.4; NP_003218.2.
DR UCSC; uc003uvv.2; human. [Q9UP52-1]
DR CTD; 7036; -.
DR DisGeNET; 7036; -.
DR GeneCards; TFR2; -.
DR GeneReviews; TFR2; -.
DR HGNC; HGNC:11762; TFR2.
DR HPA; ENSG00000106327; Tissue enriched (liver).
DR MalaCards; TFR2; -.
DR MIM; 604250; phenotype.
DR MIM; 604720; gene.
DR neXtProt; NX_Q9UP52; -.
DR OpenTargets; ENSG00000106327; -.
DR Orphanet; 225123; Hemochromatosis type 3.
DR PharmGKB; PA36477; -.
DR VEuPathDB; HostDB:ENSG00000106327; -.
DR eggNOG; KOG2195; Eukaryota.
DR GeneTree; ENSGT01030000234598; -.
DR HOGENOM; CLU_005688_5_0_1; -.
DR InParanoid; Q9UP52; -.
DR OMA; FSQGPHK; -.
DR OrthoDB; 804230at2759; -.
DR PhylomeDB; Q9UP52; -.
DR TreeFam; TF312981; -.
DR PathwayCommons; Q9UP52; -.
DR Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
DR SignaLink; Q9UP52; -.
DR BioGRID-ORCS; 7036; 13 hits in 1073 CRISPR screens.
DR GeneWiki; TFR2; -.
DR GenomeRNAi; 7036; -.
DR Pharos; Q9UP52; Tbio.
DR PRO; PR:Q9UP52; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UP52; protein.
DR Bgee; ENSG00000106327; Expressed in right lobe of liver and 165 other tissues.
DR ExpressionAtlas; Q9UP52; baseline and differential.
DR Genevisible; Q9UP52; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IGI:BHF-UCL.
DR GO; GO:1990712; C:HFE-transferrin receptor complex; IDA:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IGI:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0039706; F:co-receptor binding; IPI:BHF-UCL.
DR GO; GO:0004998; F:transferrin receptor activity; IDA:BHF-UCL.
DR GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:UniProtKB.
DR GO; GO:0071281; P:cellular response to iron ion; IGI:BHF-UCL.
DR GO; GO:0140298; P:endocytic iron import into cell; IGI:BHF-UCL.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:BHF-UCL.
DR GO; GO:0006826; P:iron ion transport; NAS:UniProtKB.
DR GO; GO:0045807; P:positive regulation of endocytosis; IGI:BHF-UCL.
DR GO; GO:0090277; P:positive regulation of peptide hormone secretion; IMP:BHF-UCL.
DR GO; GO:1903319; P:positive regulation of protein maturation; IGI:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:BHF-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IGI:BHF-UCL.
DR GO; GO:0010039; P:response to iron ion; IMP:BHF-UCL.
DR GO; GO:0033572; P:transferrin transport; IGI:BHF-UCL.
DR CDD; cd02128; PA_TfR; 1.
DR Gene3D; 1.20.930.40; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR InterPro; IPR037324; TfR1/2_PA.
DR PANTHER; PTHR10404; PTHR10404; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Disease variant;
KW Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..801
FT /note="Transferrin receptor protein 2"
FT /id="PRO_0000174136"
FT TOPO_DOM 1..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..801
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 16..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 23..26
FT /note="Endocytosis signal"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 108
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT DISULFID 111
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..171
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:10409623"
FT /id="VSP_005354"
FT VAR_SEQ 343..369
FT /note="Missing (in isoform Gamma)"
FT /evidence="ECO:0000305"
FT /id="VSP_005355"
FT VARIANT 22
FT /note="V -> I (in HFE3; dbSNP:rs80338876)"
FT /evidence="ECO:0000269|PubMed:14633868"
FT /id="VAR_042515"
FT VARIANT 172
FT /note="M -> K (in HFE3; dbSNP:rs80338879)"
FT /evidence="ECO:0000269|PubMed:11313241"
FT /id="VAR_012738"
FT VARIANT 230
FT /note="D -> E (in dbSNP:rs41303465)"
FT /id="VAR_034122"
FT VARIANT 238
FT /note="I -> M (in dbSNP:rs34242818)"
FT /id="VAR_034123"
FT VARIANT 455
FT /note="R -> Q (hereditary hemochromatosis modifier;
FT dbSNP:rs41303501)"
FT /evidence="ECO:0000269|PubMed:12150153"
FT /id="VAR_042516"
FT VARIANT 690
FT /note="Q -> P (in HFE3; dbSNP:rs80338889)"
FT /evidence="ECO:0000269|PubMed:12130528"
FT /id="VAR_042517"
FT VARIANT 752
FT /note="R -> H (in dbSNP:rs41295942)"
FT /id="VAR_034124"
FT CONFLICT 712
FT /note="R -> RIPLSAQV (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 801 AA; 88755 MW; D3D3082BA835413A CRC64;
MERLWGLFQR AQQLSPRSSQ TVYQRVEGPR KGHLEEEEED GEEGAETLAH FCPMELRGPE
PLGSRPRQPN LIPWAAAGRR AAPYLVLTAL LIFTGAFLLG YVAFRGSCQA CGDSVLVVSE
DVNYEPDLDF HQGRLYWSDL QAMFLQFLGE GRLEDTIRQT SLRERVAGSA GMAALTQDIR
AALSRQKLDH VWTDTHYVGL QFPDPAHPNT LHWVDEAGKV GEQLPLEDPD VYCPYSAIGN
VTGELVYAHY GRPEDLQDLR ARGVDPVGRL LLVRVGVISF AQKVTNAQDF GAQGVLIYPE
PADFSQDPPK PSLSSQQAVY GHVHLGTGDP YTPGFPSFNQ TQFPPVASSG LPSIPAQPIS
ADIASRLLRK LKGPVAPQEW QGSLLGSPYH LGPGPRLRLV VNNHRTSTPI NNIFGCIEGR
SEPDHYVVIG AQRDAWGPGA AKSAVGTAIL LELVRTFSSM VSNGFRPRRS LLFISWDGGD
FGSVGSTEWL EGYLSVLHLK AVVYVSLDNA VLGDDKFHAK TSPLLTSLIE SVLKQVDSPN
HSGQTLYEQV VFTNPSWDAE VIRPLPMDSS AYSFTAFVGV PAVEFSFMED DQAYPFLHTK
EDTYENLHKV LQGRLPAVAQ AVAQLAGQLL IRLSHDRLLP LDFGRYGDVV LRHIGNLNEF
SGDLKARGLT LQWVYSARGD YIRAAEKLRQ EIYSSEERDE RLTRMYNVRI MRVEFYFLSQ
YVSPADSPFR HIFMGRGDHT LGALLDHLRL LRSNSSGTPG ATSSTGFQES RFRRQLALLT
WTLQGAANAL SGDVWNIDNN F
