ID A0A2I0LU15_COLLI Unreviewed; 776 AA.
AC A0A2I0LU15;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Transferrin receptor protein 1 {ECO:0000256|RuleBase:RU367157};
GN Name=TFRC {ECO:0000313|EMBL:PKK20932.1};
GN ORFNames=A306_00012854 {ECO:0000313|EMBL:PKK20932.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK20932.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK20932.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK20932.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK20932.1}.
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DR EMBL; AKCR02000095; PKK20932.1; -; Genomic_DNA.
DR RefSeq; XP_005513284.1; XM_005513227.1.
DR AlphaFoldDB; A0A2I0LU15; -.
DR Proteomes; UP000053872; 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 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; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
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: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:PKK20932.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872};
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 401..595
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 654..765
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 30..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 86114 MW; 19350D2D9B149F4A CRC64;
MDHARAVISN LFSGEPMSYT RFSIARQTEG DNSHVEMKLS ADDEDGGEPG RPEHLHAIMS
PPPRSGRNRC FLVIAAVLLL LIGFLIGYLS YRGRMQKAGR CLDGSGKCEV TPTASYLADD
DETEEEEVPG PPVLYWPDLR DLLSDKLSVE RLEVNLRQRA NKYSFEAGDT EDQSTANYIH
DQFTRFLLDE VWNDEHYIKL QVKGSNNKVS VVEDGKEEEL ESPDAYVAYS KTGSVVGKPV
YVNYGLKADF QRVQKLDVSL NETIIIFRAG KITLAEKVAN AKEVGAVGAL MYLDPSDYRN
TDALVPFGHA HLGTGDPFTP GFPSFNHTQF PPVESSGLPR IAVQTVSSQA VDRLFSKMGG
KECPLEWKGG VMGCKVMPES TTNVTVKLTV NNVMADRKIL NIFGAIKGLE EPDRYVVIGA
QRDSWGPGAA KAGVGTAILL ELARVISDMV KKDGYKPRRS IIFASWSAGE YGAVGATEWL
EGYSATLHTK AFTYINLDAA VLGSKHMKIS ASPLLYTLLE RTMKGVKDPG KGTGNLYDRV
GTDWVKTVVP LGLDNAAFPF LAFSGIPVVS FGFYNKDEEY AFLGTTQDTV ANLKTTGNLY
GLMRAAAEVA GQIALRLTHD HELFLDFERY AEELLAFQEK FFPYGQDVKT LGLTLKWLYF
ARGDFQRATN ALRRDIANSD RENRIVRRAL NDRIMKVEYD FLSPYLSPKD VPFRHIFFGK
GSHTLQSLLE NLEQLRANKE SVDVNMLKEQ LALATWTIKG AANALVGDIW DTDNEF
//