HFE_HUMAN
ID HFE_HUMAN Reviewed; 348 AA.
AC Q30201; B2CKL0; O75929; O75930; O75931; Q17RT0; Q96KU5; Q96KU6; Q96KU7;
AC Q96KU8; Q9HC64; Q9HC68; Q9HC70; Q9HC83;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Hereditary hemochromatosis protein;
DE AltName: Full=HLA-H;
DE Flags: Precursor;
GN Name=HFE; Synonyms=HLAH;
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] (ISOFORM 1), VARIANT HFE1 TYR-282, AND VARIANT
RP ASP-63.
RX PubMed=8696333; DOI=10.1038/ng0896-399;
RA Feder J.N., Gnirke A., Thomas W., Tsuchihashi Z., Ruddy D.A., Basava A.,
RA Dormishian F., Domingo R. Jr., Ellis M.C. Jr., Fullan A., Hinton L.M.,
RA Jones N.L., Kimmel B.E., Kronmal G.S., Lauer P., Lee V.K., Loeb D.B.,
RA Mapa F.A., McClelland E., Meyer N.C., Mintier G.A., Moeller N., Moore T.,
RA Morikang E., Prass C.E., Quintana L., Starnes S.M., Schatzman R.C.,
RA Brunke K.J., Drayna D.T., Risch N.J., Bacon B.R., Wolff R.K.;
RT "A novel MHC class I-like gene is mutated in patients with hereditary
RT haemochromatosis.";
RL Nat. Genet. 13:399-409(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=9149941; DOI=10.1101/gr.7.5.441;
RA Ruddy D.A., Kronmal G.S., Lee V.K., Mintier G.A., Quintana L.,
RA Domingo R. Jr., Meyer N.C., Irrinki A., McClelland E.E., Fullan A.,
RA Mapa F.A., Moore T., Thomas W., Loeb D.B., Harmon C., Tsuchihashi Z.,
RA Wolff R.K., Schatzman R.C., Feder J.N.;
RT "A 1.1-Mb transcript map of the hereditary hemochromatosis locus.";
RL Genome Res. 7:441-456(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=9548560;
RX DOI=10.1002/(sici)1097-4644(19980501)69:2<117::aid-jcb3>3.0.co;2-v;
RA Albig W., Drabent B., Burmester N., Bode C., Doenecke D.;
RT "The haemochromatosis candidate gene HFE (HLA-H) of man and mouse is
RT located in syntenic regions within the histone gene.";
RL J. Cell. Biochem. 69:117-126(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA Gasparini P.;
RT "Hereditary hemochromatosis genomic structure and organization of HLA-H
RT gene.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
RX PubMed=10079302; DOI=10.1007/s002510050505;
RA Rhodes D.A., Trowsdale J.;
RT "Alternate splice variants of the hemochromatosis gene Hfe.";
RL Immunogenetics 49:357-359(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 7; 8; 9 AND 10).
RX PubMed=11001625; DOI=10.1006/bcmd.2000.0291;
RA Thenie A., Orhant M., Gicquel I., Fergelot P., Le Gall J.-Y., David V.,
RA Mosser J.;
RT "The HFE gene undergoes alternate splicing processes.";
RL Blood Cells Mol. Dis. 26:155-162(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 5; 6; 7 AND 11).
RX PubMed=11358357; DOI=10.1006/bcmd.2000.0346;
RA Sanchez M., Bruguera M., Rodos J., Oliva R.;
RT "Complete characterization of the 3' region of the human and mouse
RT hereditary hemochromatosis HFE gene and detection of novel splicing
RT forms.";
RL Blood Cells Mol. Dis. 27:35-43(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-53; ASP-63; GLN-224 AND
RP TYR-282.
RG NIEHS SNPs program;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9465039; DOI=10.1073/pnas.95.4.1472;
RA Feder J.N., Penny D.M., Irrinki A., Lee V.K., Lebron J.A., Watson N.,
RA Tsuchihashi Z., Sigal E., Bjorkman P.J., Schatzman R.C.;
RT "The hemochromatosis gene product complexes with the transferrin receptor
RT and lowers its affinity for ligand binding.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:1472-1477(1998).
RN [12]
RP INVOLVEMENT IN TFQTL2.
RX PubMed=19084217; DOI=10.1016/j.ajhg.2008.11.011;
RA Benyamin B., McRae A.F., Zhu G., Gordon S., Henders A.K., Palotie A.,
RA Peltonen L., Martin N.G., Montgomery G.W., Whitfield J.B., Visscher P.M.;
RT "Variants in TF and HFE explain approximately 40% of genetic variation in
RT serum-transferrin levels.";
RL Am. J. Hum. Genet. 84:60-65(2009).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 23-297 IN COMPLEX WITH TFR.
RX PubMed=9546397; DOI=10.1016/s0092-8674(00)81151-4;
RA Lebron J.A., Bennett M.J., Vaughn D.E., Chirino A.J., Snow P.M.,
RA Mintier G.A., Feder J.N., Bjorkman P.J.;
RT "Crystal structure of the hemochromatosis protein HFE and characterization
RT of its interaction with transferrin receptor.";
RL Cell 93:111-123(1998).
RN [14]
RP 3D-STRUCTURE MODELING OF 26-293 IN COMPLEX WITH B2MG.
RX PubMed=11018711; DOI=10.1016/s0167-4838(00)00126-6;
RA Dupradeau F., Altenberg-Greulich B., Warin R., Fuentes V., Monti J.,
RA Rochette J.;
RT "A 3-dimensional model building by homology of the HFE protein: molecular
RT consequences and application to antibody development.";
RL Biochim. Biophys. Acta 1481:213-221(2000).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-297 IN COMPLEX WITH TFR.
RX PubMed=10638746; DOI=10.1038/47417;
RA Bennett M.J., Lebron J.A., Bjorkman P.J.;
RT "Crystal structure of the hereditary haemochromatosis protein HFE complexed
RT with transferrin receptor.";
RL Nature 403:46-53(2000).
RN [16]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [17]
RP VARIANT HFE1 TYR-282, AND VARIANT ASP-63.
RX PubMed=9106528;
RA Carella M., D'Ambrosio L., Totaro A., Grifa A., Valentino M.A., Piperno A.,
RA Girelli D., Roetto A., Franco B., Gasparini P., Camaschella C.;
RT "Mutation analysis of the HLA-H gene in Italian hemochromatosis patients.";
RL Am. J. Hum. Genet. 60:828-832(1997).
RN [18]
RP VARIANT HFE1 TYR-282, AND ASSOCIATION WITH PORPHYRIA CUTANEA TARDA.
RX PubMed=9024376; DOI=10.1016/s0140-6736(96)09436-6;
RA Roberts A.G., Whatley S.D., Morgan R.R., Worwood M., Elder G.H.;
RT "Increased frequency of the haemochromatosis Cys282Tyr mutation in sporadic
RT porphyria cutanea tarda.";
RL Lancet 349:321-323(1997).
RN [19]
RP VARIANT ASP-63.
RX PubMed=9425935; DOI=10.1002/hep.510270128;
RA Sampietro M., Piperno A., Lupica L., Arosio C., Vergani A., Corbetta N.,
RA Malosio I., Mattioli M., Fracanzani A.L., Cappellini M.D., Fiorelli G.,
RA Fargion S.;
RT "High prevalence of the His63Asp HFE mutation in Italian patients with
RT porphyria cutanea tarda.";
RL Hepatology 27:181-184(1998).
RN [20]
RP VARIANT HFE1 TYR-282, AND VARIANT ASP-63.
RX PubMed=9620340; DOI=10.1002/hep.510270627;
RA Bonkovsky H.L., Poh-Fitzpatrick M., Pimstone N., Obando J.,
RA Di Bisceglie A., Tattrie C., Tortorelli K., LeClair P., Mercurio M.G.,
RA Lambrecht R.W.;
RT "Porphyria cutanea tarda, hepatitis C, and HFE gene mutations in North
RT America.";
RL Hepatology 27:1661-1669(1998).
RN [21]
RP VARIANTS HFE1 CYS-65 AND TYR-282, AND VARIANT ASP-63.
RX PubMed=10194428;
RA Mura C., Raguenes O., Ferec C.;
RT "HFE mutations analysis in 711 hemochromatosis probands: evidence for S65C
RT implication in mild form of hemochromatosis.";
RL Blood 93:2502-2505(1999).
RN [22]
RP VARIANTS HFE1 CYS-65; ARG-93 AND THR-105.
RX PubMed=10575540; DOI=10.1006/bcmd.1999.0240;
RA Barton J.C., Sawada-Hirai R., Rothenberg B.E., Acton R.T.;
RT "Two novel missense mutations of the HFE gene (I105T and G93R) and
RT identification of the S65C mutation in Alabama hemochromatosis probands.";
RL Blood Cells Mol. Dis. 25:147-155(1999).
RN [23]
RP VARIANTS HFE1 HIS-127 AND MET-330, AND VARIANTS MET-53; MET-59 AND ASP-63.
RX PubMed=10401000; DOI=10.1093/hmg/8.8.1517;
RA de Villiers J.N.P., Hillermann R., Loubser L., Kotze M.J.;
RT "Spectrum of mutations in the HFE gene implicated in haemochromatosis and
RT porphyria.";
RL Hum. Mol. Genet. 8:1517-1522(1999).
RN [24]
RP VARIANT HFE1 TYR-282, AND VARIANT ASP-63.
RX PubMed=10094552;
RX DOI=10.1002/(sici)1098-1004(1999)13:2<154::aid-humu8>3.0.co;2-e;
RA Merryweather-Clarke A.T., Simonsen H., Shearman J.D., Pointon J.J.,
RA Norgaard-Pedersen B., Robson K.J.H.;
RT "A retrospective anonymous pilot study in screening newborns for HFE
RT mutations in Scandinavian populations.";
RL Hum. Mutat. 13:154-159(1999).
RN [25]
RP VARIANT HFE1 CYS-65.
RA Fagan E., Payne S.J.;
RT "A novel missense mutation S65C in the HFE gene with a possible role in
RT hereditary haemochromatosis.";
RL Hum. Mutat. 13:507-508(1999).
RN [26]
RP VARIANT LYS-277.
RX PubMed=10612845;
RX DOI=10.1002/(sici)1098-1004(200001)15:1<120::aid-humu32>3.0.co;2-b;
RA Bradbury R., Fagan E., Payne S.J.;
RT "Two novel polymorphisms (E277K and V212V) in the haemochromatosis gene
RT HFE.";
RL Hum. Mutat. 15:120-120(2000).
RN [27]
RP VARIANTS ASP-63 AND TYR-282.
RX PubMed=11069625; DOI=10.1046/j.1523-1747.2000.00148.x;
RA Brady J.J., Jackson H.A., Roberts A.G., Morgan R.R., Whatley S.D.,
RA Rowlands G.L., Darby C., Shudell E., Watson R., Paiker J., Worwood M.W.,
RA Elder G.H.;
RT "Co-inheritance of mutations in the uroporphyrinogen decarboxylase and
RT hemochromatosis genes accelerates the onset of porphyria cutanea tarda.";
RL J. Invest. Dermatol. 115:868-874(2000).
RN [28]
RP VARIANT HFE1 TYR-282, VARIANT ASP-63, AND ASSOCIATION WITH DIABETIC
RP NEPHROPATHY SUSCEPTIBILITY.
RX PubMed=11423500; DOI=10.2337/diacare.24.7.1187;
RA Moczulski D.K., Grzeszczak W., Gawlik B.;
RT "Role of hemochromatosis C282Y and H63D mutations in HFE gene in
RT development of type 2 diabetes and diabetic nephropathy.";
RL Diabetes Care 24:1187-1191(2001).
RN [29]
RP VARIANT HFE1 VAL-176.
RX PubMed=11446670; DOI=10.2169/internalmedicine.40.479;
RA Imanishi H., Liu W., Cheng J., Ikeda N., Amuro Y., Hada T.;
RT "Idiopathic hemochromatosis with the mutation of Ala176Val heterozygous for
RT HFE gene.";
RL Intern. Med. 40:479-483(2001).
RN [30]
RP VARIANTS HFE1 CYS-65; TYR-282 AND ALA-295.
RX PubMed=12542741; DOI=10.1034/j.1399-0039.2002.600603.x;
RA Jones D.C., Young N.T., Pigott C., Fuggle S.V., Barnardo M.C.N.M.,
RA Marshall S.E., Bunce M.;
RT "Comprehensive hereditary hemochromatosis genotyping.";
RL Tissue Antigens 60:481-488(2002).
RN [31]
RP VARIANT HFE1 PRO-283, AND CHARACTERIZATION OF VARIANT HFE1 PRO-283.
RX PubMed=12737937; DOI=10.1016/s1079-9796(03)00036-6;
RA Le Gac G., Dupradeau F.-Y., Mura C., Jacolot S., Scotet V., Esnault G.,
RA Mercier A.-Y., Rochette J., Ferec C.;
RT "Phenotypic expression of the C282Y/Q283P compound heterozygosity in HFE
RT and molecular modeling of the Q283P mutation effect.";
RL Blood Cells Mol. Dis. 30:231-237(2003).
RN [32]
RP VARIANTS HFE1 CYS-65; CYS-66; GLY-224 AND TYR-282.
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).
RN [33]
RP VARIANT HFE1 SER-6.
RX PubMed=12584229; DOI=10.1136/gut.52.3.433;
RA Wigg A.J., Harley H., Casey G.;
RT "Heterozygous recipient and donor HFE mutations associated with a
RT hereditary haemochromatosis phenotype after liver transplantation.";
RL Gut 52:433-435(2003).
RN [34]
RP VARIANT HFE1 ALA-295.
RX PubMed=15046077;
RA Bento M.C., Ribeiro M.L., Relvas L.;
RT "Gene symbol: HFE. Disease: haemochromatosis.";
RL Hum. Genet. 114:405-405(2004).
RN [35]
RP CHARACTERIZATION OF VARIANT HFE1 PRO-283.
RX PubMed=15965644; DOI=10.1007/s00439-005-1307-y;
RA Ka C., Le Gac G., Dupradeau F.-Y., Rochette J., Ferec C.;
RT "The Q283P amino-acid change in HFE leads to structural and functional
RT consequences similar to those described for the mutated 282Y HFE protein.";
RL Hum. Genet. 117:467-475(2005).
RN [36]
RP VARIANTS HFE1 ASP-43 AND TYR-282, AND VARIANT ASP-63.
RX PubMed=18157833; DOI=10.1002/humu.9517;
RA Dupradeau F.-Y., Pissard S., Coulhon M.-P., Cadet E., Foulon K.,
RA Fourcade C., Goossens M., Case D.A., Rochette J.;
RT "An unusual case of hemochromatosis due to a new compound heterozygosity in
RT HFE (p.[Gly43Asp;His63Asp]+[Cys282Tyr]): structural implications with
RT respect to binding with transferrin receptor 1.";
RL Hum. Mutat. 29:206-206(2008).
CC -!- FUNCTION: Binds to transferrin receptor (TFR) and reduces its affinity
CC for iron-loaded transferrin. {ECO:0000269|PubMed:9465039}.
CC -!- SUBUNIT: Binds TFR through the extracellular domain in a pH-dependent
CC manner. {ECO:0000269|PubMed:10638746, ECO:0000269|PubMed:9546397}.
CC -!- INTERACTION:
CC Q30201; P61769: B2M; NbExp=4; IntAct=EBI-1028850, EBI-714718;
CC Q30201; P02786: TFRC; NbExp=3; IntAct=EBI-1028850, EBI-355727;
CC Q30201-1; P02786: TFRC; NbExp=3; IntAct=EBI-15489346, EBI-355727;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9465039};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:8696333}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q30201-1; Sequence=Displayed;
CC Name=2; Synonyms=delE2;
CC IsoId=Q30201-2; Sequence=VSP_003218;
CC Name=3; Synonyms=del14E4;
CC IsoId=Q30201-3; Sequence=VSP_003225;
CC Name=4; Synonyms=delE214E4;
CC IsoId=Q30201-4; Sequence=VSP_003218, VSP_003225;
CC Name=5;
CC IsoId=Q30201-5; Sequence=VSP_003219;
CC Name=6;
CC IsoId=Q30201-6; Sequence=VSP_047336, VSP_003220;
CC Name=7; Synonyms=delE3;
CC IsoId=Q30201-7; Sequence=VSP_003221;
CC Name=8; Synonyms=1043-2283del,intron6ins;
CC IsoId=Q30201-8; Sequence=VSP_003226, VSP_003227;
CC Name=9; Synonyms=delE3-7;
CC IsoId=Q30201-9; Sequence=VSP_003223, VSP_003224;
CC Name=10; Synonyms=562-878del;
CC IsoId=Q30201-10; Sequence=VSP_003222;
CC Name=11;
CC IsoId=Q30201-11; Sequence=VSP_043477, VSP_043478;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested except brain.
CC -!- POLYMORPHISM: Genetic variations in HFE define the transferrin serum
CC level quantitative trait locus 2 (TFQTL2) [MIM:614193]. Iron is
CC essential for biochemical functions such as oxygen transport and
CC oxidative phosphorylation. Excessive iron can cause iron-overload-
CC related liver diseases, whereas iron deficiency can lead to anemia.
CC Iron status can be assessed by measuring the levels of serum iron,
CC serum transferrin, transferrin saturation with iron, and serum
CC ferritin.
CC -!- DISEASE: Hemochromatosis 1 (HFE1) [MIM:235200]: 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:10094552, ECO:0000269|PubMed:10194428,
CC ECO:0000269|PubMed:10401000, ECO:0000269|PubMed:10575540,
CC ECO:0000269|PubMed:11423500, ECO:0000269|PubMed:11446670,
CC ECO:0000269|PubMed:12542741, ECO:0000269|PubMed:12584229,
CC ECO:0000269|PubMed:12737937, ECO:0000269|PubMed:14633868,
CC ECO:0000269|PubMed:15046077, ECO:0000269|PubMed:15965644,
CC ECO:0000269|PubMed:18157833, ECO:0000269|PubMed:8696333,
CC ECO:0000269|PubMed:9024376, ECO:0000269|PubMed:9106528,
CC ECO:0000269|PubMed:9620340, ECO:0000269|Ref.25}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Variegate porphyria (VP) [MIM:176200]: A form of porphyria.
CC Porphyrias are inherited defects in the biosynthesis of heme, resulting
CC in the accumulation and increased excretion of porphyrins or porphyrin
CC precursors. They are classified as erythropoietic or hepatic, depending
CC on whether the enzyme deficiency occurs in red blood cells or in the
CC liver. Variegate porphyria is the most common form of porphyria in
CC South Africa. It is characterized by skin hyperpigmentation and
CC hypertrichosis, abdominal pain, tachycardia, hypertension and
CC neuromuscular disturbances. High fecal levels of protoporphyrin and
CC coproporphyrin, increased urine uroporphyrins and iron overload are
CC typical markers of the disease. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC Iron overload due to HFE variants is a precipitating or exacerbating
CC factor in variegate porphyria.
CC -!- DISEASE: Microvascular complications of diabetes 7 (MVCD7)
CC [MIM:612635]: Pathological conditions that develop in numerous tissues
CC and organs as a consequence of diabetes mellitus. They include diabetic
CC retinopathy, diabetic nephropathy leading to end-stage renal disease,
CC and diabetic neuropathy. Diabetic retinopathy remains the major cause
CC of new-onset blindness among diabetic adults. It is characterized by
CC vascular permeability and increased tissue ischemia and angiogenesis.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 1]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay.
CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/HFEID44099ch6p22.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hfe/";
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DR EMBL; U60319; AAC51823.1; -; mRNA.
DR EMBL; U91328; AAB82083.1; -; Genomic_DNA.
DR EMBL; Z92910; CAB07442.1; -; Genomic_DNA.
DR EMBL; Y09801; CAA70934.1; -; Genomic_DNA.
DR EMBL; Y09800; CAA70934.1; JOINED; Genomic_DNA.
DR EMBL; Y09803; CAA70934.1; JOINED; Genomic_DNA.
DR EMBL; Y09799; CAA70934.1; JOINED; Genomic_DNA.
DR EMBL; AF079407; AAC62646.1; -; mRNA.
DR EMBL; AF079408; AAC62647.1; -; mRNA.
DR EMBL; AF079409; AAC62648.1; -; mRNA.
DR EMBL; AF115264; AAG29571.1; -; mRNA.
DR EMBL; AF115265; AAG29572.1; -; mRNA.
DR EMBL; AF144240; AAG29575.1; -; mRNA.
DR EMBL; AF144242; AAG29577.1; -; mRNA.
DR EMBL; AF149804; AAG29342.1; -; mRNA.
DR EMBL; AJ249335; CAC67792.1; -; mRNA.
DR EMBL; AJ249336; CAC67793.1; -; mRNA.
DR EMBL; AJ249337; CAC67794.1; -; mRNA.
DR EMBL; AJ249338; CAC67795.1; -; mRNA.
DR EMBL; AJ250635; CAC80805.1; -; mRNA.
DR EMBL; EU523119; ACB21042.1; -; Genomic_DNA.
DR EMBL; CH471087; EAW55524.1; -; Genomic_DNA.
DR EMBL; CH471087; EAW55526.1; -; Genomic_DNA.
DR EMBL; BC117201; AAI17202.1; -; mRNA.
DR EMBL; BC117203; AAI17204.1; -; mRNA.
DR CCDS; CCDS4578.1; -. [Q30201-1]
DR CCDS; CCDS4579.1; -. [Q30201-7]
DR CCDS; CCDS4580.1; -. [Q30201-2]
DR CCDS; CCDS4581.1; -. [Q30201-6]
DR CCDS; CCDS4582.1; -. [Q30201-11]
DR CCDS; CCDS47386.1; -. [Q30201-10]
DR CCDS; CCDS47387.1; -. [Q30201-5]
DR CCDS; CCDS54974.1; -. [Q30201-3]
DR CCDS; CCDS54975.1; -. [Q30201-4]
DR RefSeq; NP_000401.1; NM_000410.3. [Q30201-1]
DR RefSeq; NP_001287678.1; NM_001300749.1.
DR RefSeq; NP_620572.1; NM_139003.2. [Q30201-10]
DR RefSeq; NP_620573.1; NM_139004.2. [Q30201-7]
DR RefSeq; NP_620575.1; NM_139006.2. [Q30201-3]
DR RefSeq; NP_620576.1; NM_139007.2. [Q30201-2]
DR RefSeq; NP_620577.1; NM_139008.2. [Q30201-4]
DR RefSeq; NP_620578.1; NM_139009.2. [Q30201-5]
DR RefSeq; NP_620579.1; NM_139010.2. [Q30201-6]
DR RefSeq; NP_620580.1; NM_139011.2. [Q30201-11]
DR PDB; 1A6Z; X-ray; 2.60 A; A/C=23-297.
DR PDB; 1DE4; X-ray; 2.80 A; A/D/G=23-297.
DR PDBsum; 1A6Z; -.
DR PDBsum; 1DE4; -.
DR AlphaFoldDB; Q30201; -.
DR SMR; Q30201; -.
DR BioGRID; 109325; 172.
DR DIP; DIP-2737N; -.
DR IntAct; Q30201; 10.
DR MINT; Q30201; -.
DR STRING; 9606.ENSP00000417404; -.
DR GlyGen; Q30201; 3 sites.
DR iPTMnet; Q30201; -.
DR PhosphoSitePlus; Q30201; -.
DR BioMuta; HFE; -.
DR DMDM; 2497915; -.
DR EPD; Q30201; -.
DR jPOST; Q30201; -.
DR MassIVE; Q30201; -.
DR MaxQB; Q30201; -.
DR PaxDb; Q30201; -.
DR PeptideAtlas; Q30201; -.
DR PRIDE; Q30201; -.
DR ProteomicsDB; 61558; -. [Q30201-1]
DR ProteomicsDB; 61559; -. [Q30201-10]
DR ProteomicsDB; 61560; -. [Q30201-11]
DR ProteomicsDB; 61561; -. [Q30201-2]
DR ProteomicsDB; 61562; -. [Q30201-3]
DR ProteomicsDB; 61563; -. [Q30201-4]
DR ProteomicsDB; 61564; -. [Q30201-5]
DR ProteomicsDB; 61565; -. [Q30201-6]
DR ProteomicsDB; 61566; -. [Q30201-7]
DR ProteomicsDB; 61567; -. [Q30201-8]
DR ProteomicsDB; 61568; -. [Q30201-9]
DR TopDownProteomics; Q30201-1; -. [Q30201-1]
DR Antibodypedia; 2221; 347 antibodies from 32 providers.
DR DNASU; 3077; -.
DR Ensembl; ENST00000317896.11; ENSP00000313776.7; ENSG00000010704.19. [Q30201-7]
DR Ensembl; ENST00000336625.12; ENSP00000337819.8; ENSG00000010704.19. [Q30201-10]
DR Ensembl; ENST00000349999.8; ENSP00000259699.6; ENSG00000010704.19. [Q30201-2]
DR Ensembl; ENST00000352392.8; ENSP00000315936.4; ENSG00000010704.19. [Q30201-11]
DR Ensembl; ENST00000353147.9; ENSP00000312342.5; ENSG00000010704.19. [Q30201-6]
DR Ensembl; ENST00000357618.10; ENSP00000417404.1; ENSG00000010704.19. [Q30201-1]
DR Ensembl; ENST00000397022.7; ENSP00000380217.3; ENSG00000010704.19. [Q30201-5]
DR Ensembl; ENST00000461397.5; ENSP00000420802.1; ENSG00000010704.19. [Q30201-3]
DR Ensembl; ENST00000488199.5; ENSP00000420559.1; ENSG00000010704.19. [Q30201-4]
DR GeneID; 3077; -.
DR KEGG; hsa:3077; -.
DR MANE-Select; ENST00000357618.10; ENSP00000417404.1; NM_000410.4; NP_000401.1.
DR UCSC; uc003nfx.2; human. [Q30201-1]
DR CTD; 3077; -.
DR DisGeNET; 3077; -.
DR GeneCards; HFE; -.
DR GeneReviews; HFE; -.
DR HGNC; HGNC:4886; HFE.
DR HPA; ENSG00000010704; Low tissue specificity.
DR MalaCards; HFE; -.
DR MIM; 176200; phenotype.
DR MIM; 235200; phenotype.
DR MIM; 612635; phenotype.
DR MIM; 613609; gene.
DR MIM; 614193; phenotype.
DR neXtProt; NX_Q30201; -.
DR OpenTargets; ENSG00000010704; -.
DR Orphanet; 586; Cystic fibrosis.
DR Orphanet; 443062; Familial porphyria cutanea tarda.
DR Orphanet; 139498; NON RARE IN EUROPE: Hemochromatosis type 1.
DR Orphanet; 443057; Sporadic porphyria cutanea tarda.
DR Orphanet; 465508; Symptomatic form of hemochromatosis type 1.
DR PharmGKB; PA29263; -.
DR VEuPathDB; HostDB:ENSG00000010704; -.
DR eggNOG; KOG1745; Eukaryota.
DR GeneTree; ENSGT01040000240396; -.
DR HOGENOM; CLU_047501_10_1_1; -.
DR InParanoid; Q30201; -.
DR OMA; KGWEHMF; -.
DR OrthoDB; 912212at2759; -.
DR PhylomeDB; Q30201; -.
DR TreeFam; TF336617; -.
DR PathwayCommons; Q30201; -.
DR Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
DR SignaLink; Q30201; -.
DR BioGRID-ORCS; 3077; 14 hits in 1071 CRISPR screens.
DR EvolutionaryTrace; Q30201; -.
DR GeneWiki; HFE_(gene); -.
DR GenomeRNAi; 3077; -.
DR Pharos; Q30201; Tbio.
DR PRO; PR:Q30201; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q30201; protein.
DR Bgee; ENSG00000010704; Expressed in stromal cell of endometrium and 181 other tissues.
DR ExpressionAtlas; Q30201; baseline and differential.
DR Genevisible; Q30201; HS.
DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR GO; GO:0045178; C:basal part of cell; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:1990712; C:HFE-transferrin receptor complex; IDA:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0030881; F:beta-2-microglobulin binding; IPI:BHF-UCL.
DR GO; GO:0039706; F:co-receptor binding; IPI:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:1990459; F:transferrin receptor binding; IPI:BHF-UCL.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IDA:UniProtKB.
DR GO; GO:0071281; P:cellular response to iron ion; IGI:BHF-UCL.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:Ensembl.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:BHF-UCL.
DR GO; GO:0098711; P:iron ion import across plasma membrane; IEA:InterPro.
DR GO; GO:0060586; P:multicellular organismal iron ion homeostasis; IEA:Ensembl.
DR GO; GO:1904283; P:negative regulation of antigen processing and presentation of endogenous peptide antigen via MHC class I; IGI:BHF-UCL.
DR GO; GO:2001186; P:negative regulation of CD8-positive, alpha-beta T cell activation; IGI:BHF-UCL.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IC:BHF-UCL.
DR GO; GO:1900121; P:negative regulation of receptor binding; IDA:BHF-UCL.
DR GO; GO:2000272; P:negative regulation of signaling receptor activity; IDA:BHF-UCL.
DR GO; GO:0002626; P:negative regulation of T cell antigen processing and presentation; IEA:InterPro.
DR GO; GO:0002725; P:negative regulation of T cell cytokine production; IGI:BHF-UCL.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
DR GO; GO:1904434; P:positive regulation of ferrous iron binding; IGI:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0090277; P:positive regulation of peptide hormone secretion; IMP:BHF-UCL.
DR GO; GO:0032092; P:positive regulation of protein binding; IGI:BHF-UCL.
DR GO; GO:1900122; P:positive regulation of receptor binding; IGI:BHF-UCL.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IGI:BHF-UCL.
DR GO; GO:2000273; P:positive regulation of signaling receptor activity; IGI:BHF-UCL.
DR GO; GO:1904437; P:positive regulation of transferrin receptor binding; IGI:BHF-UCL.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR GO; GO:0034756; P:regulation of iron ion transport; IGI:BHF-UCL.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; IMP:BHF-UCL.
DR GO; GO:0010039; P:response to iron ion; IMP:BHF-UCL.
DR GO; GO:1990641; P:response to iron ion starvation; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 1.
DR InterPro; IPR031092; HFE.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR011161; MHC_I-like_Ag-recog.
DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR001039; MHC_I_a_a1/a2.
DR PANTHER; PTHR16675:SF172; PTHR16675:SF172; 1.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 1.
DR PRINTS; PR01638; MHCCLASSI.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Disulfide bond; Glycoprotein; Ion transport; Iron; Iron transport;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..22
FT CHAIN 23..348
FT /note="Hereditary hemochromatosis protein"
FT /id="PRO_0000018892"
FT TOPO_DOM 23..306
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9465039"
FT TRANSMEM 307..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9465039"
FT DOMAIN 207..298
FT /note="Ig-like C1-type"
FT REGION 23..114
FT /note="Alpha-1"
FT REGION 115..205
FT /note="Alpha-2"
FT REGION 206..297
FT /note="Alpha-3"
FT REGION 298..306
FT /note="Connecting peptide"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 124..187
FT DISULFID 225..282
FT VAR_SEQ 26..114
FT /note="RSHSLHYLFMGASEQDLGLSLFEALGYVDDQLFVFYDHESRRVEPRTPWVSS
FT RISSQMWLQLSQSLKGWDHMFTVDFWTIMENHNHSKE -> Q (in isoform 2
FT and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10079302,
FT ECO:0000303|PubMed:11358357"
FT /id="VSP_003218"
FT VAR_SEQ 26..49
FT /note="RSHSLHYLFMGASEQDLGLSLFEA -> P (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11358357"
FT /id="VSP_003219"
FT VAR_SEQ 26
FT /note="R -> Q (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:11358357"
FT /id="VSP_043477"
FT VAR_SEQ 26
FT /note="R -> L (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:11358357"
FT /id="VSP_047336"
FT VAR_SEQ 27..298
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:11358357"
FT /id="VSP_043478"
FT VAR_SEQ 27..206
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:11358357"
FT /id="VSP_003220"
FT VAR_SEQ 114..219
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:11001625"
FT /id="VSP_003222"
FT VAR_SEQ 114..205
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:11001625,
FT ECO:0000303|PubMed:11358357"
FT /id="VSP_003221"
FT VAR_SEQ 144..161
FT /note="DHLEFCPDTLDWRAAEPR -> VLQDTIYSSEVSSLGIKF (in isoform
FT 9)"
FT /evidence="ECO:0000303|PubMed:11001625"
FT /id="VSP_003223"
FT VAR_SEQ 162..348
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:11001625"
FT /id="VSP_003224"
FT VAR_SEQ 207..220
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10079302"
FT /id="VSP_003225"
FT VAR_SEQ 275..276
FT /note="GE -> KY (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:11001625"
FT /id="VSP_003226"
FT VAR_SEQ 277..348
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:11001625"
FT /id="VSP_003227"
FT VARIANT 6
FT /note="R -> S (in HFE1; unknown pathological significance;
FT dbSNP:rs149342416)"
FT /evidence="ECO:0000269|PubMed:12584229"
FT /id="VAR_042506"
FT VARIANT 43
FT /note="G -> D (in HFE1; associated with D-63 in one
FT patient)"
FT /evidence="ECO:0000269|PubMed:18157833"
FT /id="VAR_042507"
FT VARIANT 53
FT /note="V -> M (in dbSNP:rs28934889)"
FT /evidence="ECO:0000269|PubMed:10401000, ECO:0000269|Ref.8"
FT /id="VAR_008111"
FT VARIANT 59
FT /note="V -> M (in dbSNP:rs111033557)"
FT /evidence="ECO:0000269|PubMed:10401000"
FT /id="VAR_008112"
FT VARIANT 63
FT /note="H -> D (associated with hemochromatosis and
FT variegate porphyria; increased frequency among patients
FT with diabetic nephropathy; dbSNP:rs1799945)"
FT /evidence="ECO:0000269|PubMed:10094552,
FT ECO:0000269|PubMed:10194428, ECO:0000269|PubMed:10401000,
FT ECO:0000269|PubMed:11069625, ECO:0000269|PubMed:11423500,
FT ECO:0000269|PubMed:18157833, ECO:0000269|PubMed:8696333,
FT ECO:0000269|PubMed:9106528, ECO:0000269|PubMed:9425935,
FT ECO:0000269|PubMed:9620340, ECO:0000269|Ref.8"
FT /id="VAR_004396"
FT VARIANT 65
FT /note="S -> C (in HFE1; mild form; dbSNP:rs1800730)"
FT /evidence="ECO:0000269|PubMed:10194428,
FT ECO:0000269|PubMed:10575540, ECO:0000269|PubMed:12542741,
FT ECO:0000269|PubMed:14633868, ECO:0000269|Ref.25"
FT /id="VAR_004397"
FT VARIANT 66
FT /note="R -> C (in HFE1; dbSNP:rs747739169)"
FT /evidence="ECO:0000269|PubMed:14633868"
FT /id="VAR_042508"
FT VARIANT 93
FT /note="G -> R (in HFE1; dbSNP:rs28934597)"
FT /evidence="ECO:0000269|PubMed:10575540"
FT /id="VAR_008729"
FT VARIANT 105
FT /note="I -> T (in HFE1; dbSNP:rs28934596)"
FT /evidence="ECO:0000269|PubMed:10575540"
FT /id="VAR_008730"
FT VARIANT 127
FT /note="Q -> H (in HFE1; dbSNP:rs28934595)"
FT /evidence="ECO:0000269|PubMed:10401000"
FT /id="VAR_008113"
FT VARIANT 176
FT /note="A -> V (in HFE1; uncertain pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:11446670"
FT /id="VAR_042509"
FT VARIANT 217
FT /note="T -> I (in dbSNP:rs4986950)"
FT /id="VAR_020270"
FT VARIANT 224
FT /note="R -> G (in HFE1)"
FT /evidence="ECO:0000269|PubMed:14633868"
FT /id="VAR_042510"
FT VARIANT 224
FT /note="R -> Q (in dbSNP:rs62625346)"
FT /evidence="ECO:0000269|Ref.8"
FT /id="VAR_062279"
FT VARIANT 277
FT /note="E -> K (in dbSNP:rs140080192)"
FT /evidence="ECO:0000269|PubMed:10612845"
FT /id="VAR_008731"
FT VARIANT 282
FT /note="C -> Y (in HFE1; associated with susceptibility to
FT porphyria cutanea tarda; associated with increased serum
FT transferrin levels; higher frequency in patients with type
FT 2 diabetes than in controls; dbSNP:rs1800562)"
FT /evidence="ECO:0000269|PubMed:10094552,
FT ECO:0000269|PubMed:10194428, ECO:0000269|PubMed:11069625,
FT ECO:0000269|PubMed:11423500, ECO:0000269|PubMed:12542741,
FT ECO:0000269|PubMed:14633868, ECO:0000269|PubMed:18157833,
FT ECO:0000269|PubMed:8696333, ECO:0000269|PubMed:9024376,
FT ECO:0000269|PubMed:9106528, ECO:0000269|PubMed:9620340,
FT ECO:0000269|Ref.8"
FT /id="VAR_004398"
FT VARIANT 283
FT /note="Q -> P (in HFE1; destabilizing effect on the
FT tertiary structure of the protein; prevents the normal
FT interaction between HFE and B2M and between HFE and TFRC;
FT decreases the capacity of HFE to reduce transferrin-
FT mediated iron uptake; dbSNP:rs111033563)"
FT /evidence="ECO:0000269|PubMed:12737937,
FT ECO:0000269|PubMed:15965644"
FT /id="VAR_037304"
FT VARIANT 295
FT /note="V -> A (in HFE1; dbSNP:rs143175221)"
FT /evidence="ECO:0000269|PubMed:12542741,
FT ECO:0000269|PubMed:15046077"
FT /id="VAR_042511"
FT VARIANT 330
FT /note="R -> M (in HFE1; dbSNP:rs111033558)"
FT /evidence="ECO:0000269|PubMed:10401000"
FT /id="VAR_008114"
FT CONFLICT 230
FT /note="Y -> H (in Ref. 7; AAG29342)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="A -> T (in Ref. 7; AAG29575)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="V -> A (in Ref. 7; AAG29577)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="G -> E (in Ref. 7; AAG29342)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="S -> R (in Ref. 7; AAG29342)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="M -> V (in Ref. 7; AAG29577)"
FT /evidence="ECO:0000305"
FT STRAND 28..38
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1A6Z"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1DE4"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:1A6Z"
FT HELIX 83..107
FT /evidence="ECO:0007829|PDB:1A6Z"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:1A6Z"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:1A6Z"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1A6Z"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:1A6Z"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:1A6Z"
FT HELIX 186..198
FT /evidence="ECO:0007829|PDB:1A6Z"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 221..233
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:1A6Z"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 264..272
FT /evidence="ECO:0007829|PDB:1A6Z"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:1A6Z"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:1A6Z"
SQ SEQUENCE 348 AA; 40108 MW; 432EB9A314A55BEA CRC64;
MGPRARPALL LLMLLQTAVL QGRLLRSHSL HYLFMGASEQ DLGLSLFEAL GYVDDQLFVF
YDHESRRVEP RTPWVSSRIS SQMWLQLSQS LKGWDHMFTV DFWTIMENHN HSKESHTLQV
ILGCEMQEDN STEGYWKYGY DGQDHLEFCP DTLDWRAAEP RAWPTKLEWE RHKIRARQNR
AYLERDCPAQ LQQLLELGRG VLDQQVPPLV KVTHHVTSSV TTLRCRALNY YPQNITMKWL
KDKQPMDAKE FEPKDVLPNG DGTYQGWITL AVPPGEEQRY TCQVEHPGLD QPLIVIWEPS
PSGTLVIGVI SGIAVFVVIL FIGILFIILR KRQGSRGAMG HYVLAERE
