ID A0A091PUW4_HALAL Unreviewed; 777 AA.
AC A0A091PUW4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Transferrin receptor protein 1 {ECO:0000256|RuleBase:RU367157};
GN ORFNames=N329_07836 {ECO:0000313|EMBL:KFQ00495.1};
OS Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC Accipitrinae; Haliaeetus.
OX NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ00495.1, ECO:0000313|Proteomes:UP000054379};
RN [1] {ECO:0000313|EMBL:KFQ00495.1, ECO:0000313|Proteomes:UP000054379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ00495.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cellular uptake of iron occurs via receptor-mediated
CC endocytosis of ligand-occupied transferrin receptor into specialized
CC endosomes. Endosomal acidification leads to iron release. The
CC apotransferrin-receptor complex is then recycled to the cell surface
CC with a return to neutral pH and the concomitant loss of affinity of
CC apotransferrin for its receptor. Transferrin receptor is necessary for
CC development of erythrocytes and the nervous system. Acts as a lipid
CC sensor that regulates mitochondrial fusion by regulating activation of
CC the JNK pathway. {ECO:0000256|RuleBase:RU367157}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|RuleBase:RU367157}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367157};
CC Single-pass type II membrane protein {ECO:0000256|RuleBase:RU367157}.
CC Melanosome {ECO:0000256|RuleBase:RU367157}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- PTM: Stearoylated. {ECO:0000256|RuleBase:RU367157}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634, ECO:0000256|RuleBase:RU367157}.
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DR EMBL; KK648641; KFQ00495.1; -; Genomic_DNA.
DR RefSeq; XP_009912690.1; XM_009914388.1.
DR AlphaFoldDB; A0A091PUW4; -.
DR GeneID; 104314743; -.
DR KEGG; hald:104314743; -.
DR CTD; 7037; -.
DR OrthoDB; 2428249at2759; -.
DR Proteomes; UP000054379; Unassembled WGS sequence.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004998; F:transferrin receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:UniProtKB-UniRule.
DR GO; GO:0031623; P:receptor internalization; IEA:UniProtKB-UniRule.
DR GO; GO:0033572; P:transferrin transport; IEA:UniProtKB-UniRule.
DR CDD; cd09848; M28_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; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR PANTHER; PTHR10404:SF26; TRANSFERRIN RECEPTOR PROTEIN 1; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU367157};
KW Endocytosis {ECO:0000256|RuleBase:RU367157};
KW Glycoprotein {ECO:0000256|RuleBase:RU367157};
KW Lipoprotein {ECO:0000256|RuleBase:RU367157};
KW Membrane {ECO:0000256|RuleBase:RU367157};
KW Palmitate {ECO:0000256|RuleBase:RU367157};
KW Receptor {ECO:0000256|RuleBase:RU367157, ECO:0000313|EMBL:KFQ00495.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054379};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|RuleBase:RU367157};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367157}.
FT TRANSMEM 70..91
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367157"
FT DOMAIN 402..595
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 657..766
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
SQ SEQUENCE 777 AA; 86319 MW; B4878F37981E8A5B CRC64;
MDHARAAISN LFGGEPMSYT RFSIARQMDG DNSHVEMKLA ADDEEGGEIG RPEHLHANMP
PPWRRGKNRC FLVIAAVLLL LIGFLIGYLS YGGRMQKASR CLDGSGKCEM TPTTSYLVDD
DEAEEEEVPG PPVLYWPELR TILSNKLSAR RLEDNLRQRA SKDSFEAGQS EDESVASYIH
DQFTSFLLDE VWNDEHYIKL QVKGSSNNKV SILENGEEEE LESPDAYVAY SKSGSVVGKP
VHVNYGLKAD FQKLQKQGVS LNETIIIFRA GKITLAEKVA NAEEAGAVGA LMYLDPSDYK
MTDALAPFGH AHLGTGDPFT PGFPSFNHTQ FPPVESSGLP RIAVQTISSK AVGKLFRRMD
GENCFLEWNS GVLGCKVMLS STSNLAVKLS VNNIMVDRKI LNIFGAIKGF EEPDRYVVIG
AQRDSWGPGA AKAGVGTAIL LELAHVISDM VKHDGYKPRR SIIFASWSAG EYGAVGATEW
LEGYSATLHA KAFTYINLDA AVLGFNNMKI SASPLLYTLL ERTMKGVKDP AKDSGSLYDR
VGSDWVKTVV PLGLDNAAFP FLAYSGIPVV SFGFCNKEEE YSFLGTTEDT VENLKKIDKL
YALMRAAAEV AGQIALRLTH DHELFLDFER YGEELLAFQE KFLPYYRDVK ALGLTLNWLF
FARGDFQRAT DALRRDIANS DKENRVVRRA LNDRIMKVEY DFLSPYLSPK DTPFRHIFFG
KGSHTLQSLL ENLQLLRTSR DSVNVNMLKE QLALVTWTIK GAANALVGDI WDTDNEF
//
