ID   HFE_PANTR               Reviewed;         348 AA.
AC   P60018;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   21-NOV-2003, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Hereditary hemochromatosis protein homolog;
DE   Flags: Precursor;
GN   Name=HFE; Synonyms=Patr-H;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12196404; DOI=10.1093/genetics/161.4.1609;
RA   Toomajian C., Kreitman M.;
RT   "Sequence variation and haplotype structure at the Human HFE Locus.";
RL   Genetics 161:1609-1623(2002).
CC   -!- FUNCTION: Binds to transferrin receptor (TFR) and reduces its affinity
CC       for iron-loaded transferrin. {ECO:0000250|UniProtKB:Q30201}.
CC   -!- SUBUNIT: Binds TFR through the extracellular domain in a pH-dependent
CC       manner. {ECO:0000250|UniProtKB:Q30201}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q30201};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q30201}.
CC   -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
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DR   EMBL; AF447807; AAN09793.1; -; Genomic_DNA.
DR   RefSeq; NP_001009101.1; NM_001009101.1.
DR   AlphaFoldDB; P60018; -.
DR   SMR; P60018; -.
DR   STRING; 9598.ENSPTRP00000056517; -.
DR   PaxDb; P60018; -.
DR   GeneID; 462489; -.
DR   KEGG; ptr:462489; -.
DR   CTD; 3077; -.
DR   eggNOG; KOG1745; Eukaryota.
DR   InParanoid; P60018; -.
DR   OrthoDB; 912212at2759; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:1990712; C:HFE-transferrin receptor complex; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:1990459; F:transferrin receptor binding; IEA:InterPro.
DR   GO; GO:0098711; P:iron ion import across plasma membrane; IEA:InterPro.
DR   GO; GO:0002626; P:negative regulation of T cell antigen processing and presentation; IEA:InterPro.
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   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Iron;
KW   Iron transport; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..348
FT                   /note="Hereditary hemochromatosis protein homolog"
FT                   /id="PRO_0000018893"
FT   TOPO_DOM        23..306
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q30201"
FT   TRANSMEM        307..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        331..348
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q30201"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        225..282
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
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