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 22-FEB-2023, entry version 182. 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}; 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; 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 GlyCosmos; Q9UP52; 4 sites, No reported glycans. 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 ProteomicsDB; 85352; -. [Q9UP52-1] DR ProteomicsDB; 85353; -. [Q9UP52-2] DR ProteomicsDB; 85354; -. [Q9UP52-3] DR Antibodypedia; 2306; 218 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 AGR; HGNC:11762; -. 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; 2428249at2759; -. 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 1149 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:0005886; C:plasma membrane; IGI:BHF-UCL. DR GO; GO:0098794; C:postsynapse; IEA:Ensembl. 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:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IEA:Ensembl. DR GO; GO:0010039; P:response to iron ion; IMP:BHF-UCL. DR GO; GO:0033572; P:transferrin transport; IGI:BHF-UCL. DR CDD; cd09848; M28_TfR; 1. DR CDD; cd02128; PA_TfR; 1. DR Gene3D; 3.50.30.30; -; 1. DR Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR InterPro; IPR046450; PA_dom_sf. 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; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1. DR PANTHER; PTHR10404:SF33; TRANSFERRIN RECEPTOR PROTEIN 2; 1. DR Pfam; PF02225; PA; 1. DR Pfam; PF04389; Peptidase_M28; 1. DR SUPFAM; SSF52025; PA domain; 1. DR SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 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 //