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Transferrin receptor protein 1 (TR) (TfR) (TfR1) (Trfr) (CD antigen CD71) (Fragment)

 TFR1_RAT                Reviewed;         622 AA.
Q99376;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 127.
RecName: Full=Transferrin receptor protein 1;
Short=TR;
Short=TfR;
Short=TfR1;
Short=Trfr;
AltName: CD_antigen=CD71;
Flags: Fragment;
Name=Tfrc; Synonyms=Trfr;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=2126342; DOI=10.1210/mend-4-4-531;
Roberts K.P., Griswold M.D.;
"Characterization of rat transferrin receptor cDNA: the regulation of
transferrin receptor mRNA in testes and in Sertoli cells in culture.";
Mol. Endocrinol. 4:531-542(1990).
-!- FUNCTION: Cellular uptake of iron occurs via receptor-mediated
endocytosis of ligand-occupied transferrin receptor into
specialized endosomes. Endosomal acidification leads to iron
release. The apotransferrin-receptor complex is then recycled to
the cell surface with a return to neutral pH and the concomitant
loss of affinity of apotransferrin for its receptor. Transferrin
receptor is necessary for development of erythrocytes and the
nervous system (By similarity). Positively regulates T and B cell
proliferation through iron uptake (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P02786}.
-!- SUBUNIT: Homodimer; disulfide-linked. Binds one transferrin
molecule per subunit. Interacts with SH3BP4 (By similarity).
Interacts with STEAP3; facilitates TFRC endocytosis in erythroid
precursor cells (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P02786}.
-!- INTERACTION:
Q9BRI3:SLC30A2 (xeno); NbExp=3; IntAct=EBI-2112551, EBI-8644112;
O14863:SLC30A4 (xeno); NbExp=5; IntAct=EBI-2112551, EBI-13918058;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P02786}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:P02786}. Melanosome
{ECO:0000250|UniProtKB:P02786}.
-!- TISSUE SPECIFICITY: In testis, expressed in Sertoli cells,
peritubular myoid cells and in germinal cells. Highest levels in
Sertoli cells.
-!- PTM: N- and O-glycosylated, phosphorylated and palmitoylated.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
{ECO:0000305}.
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EMBL; M58040; AAA42273.1; -; mRNA.
PIR; A34549; A34549.
UniGene; Rn.98672; -.
ProteinModelPortal; Q99376; -.
SMR; Q99376; -.
IntAct; Q99376; 6.
MINT; Q99376; -.
STRING; 10116.ENSRNOP00000002407; -.
PhosphoSitePlus; Q99376; -.
PaxDb; Q99376; -.
PeptideAtlas; Q99376; -.
PRIDE; Q99376; -.
UCSC; RGD:70488; rat.
RGD; 70488; Tfrc.
eggNOG; KOG2195; Eukaryota.
eggNOG; COG2234; LUCA.
HOGENOM; HOG000124067; -.
HOVERGEN; HBG023177; -.
InParanoid; Q99376; -.
PhylomeDB; Q99376; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:CAFA.
GO; GO:0055038; C:recycling endosome membrane; IDA:RGD.
GO; GO:0004998; F:transferrin receptor activity; IDA:RGD.
GO; GO:0033570; F:transferrin transmembrane transporter activity; IEA:InterPro.
GO; GO:0006953; P:acute-phase response; IEP:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
GO; GO:0030890; P:positive regulation of B cell proliferation; ISS:UniProtKB.
GO; GO:0045830; P:positive regulation of isotype switching; ISS:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
GO; GO:0046688; P:response to copper ion; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
GO; GO:0010039; P:response to iron ion; IEP:RGD.
GO; GO:0010042; P:response to manganese ion; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
CDD; cd02128; PA_TfR; 1.
Gene3D; 1.20.930.40; -; 1.
InterPro; IPR003137; PA_domain.
InterPro; IPR007484; Peptidase_M28.
InterPro; IPR029513; TfR.
InterPro; IPR007365; TFR-like_dimer_dom.
InterPro; IPR036757; TFR-like_dimer_dom_sf.
InterPro; IPR037324; TfR1/2_PA.
PANTHER; PTHR10404:SF26; PTHR10404:SF26; 1.
Pfam; PF02225; PA; 1.
Pfam; PF04389; Peptidase_M28; 1.
Pfam; PF04253; TFR_dimer; 1.
SUPFAM; SSF47672; SSF47672; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Endocytosis;
Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
Receptor; Reference proteome; Signal-anchor; Transmembrane.
CHAIN <1 622 Transferrin receptor protein 1.
/FTId=PRO_0000174134.
DOMAIN 85 175 PA.
REGION 431 622 Ligand-binding. {ECO:0000250}.
MOTIF 508 510 Cell attachment site. {ECO:0000255}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P02786}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P02786}.
CARBOHYD 584 584 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 589 589 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P02786}.
NON_TER 1 1
SEQUENCE 622 AA; 70153 MW; 831E4FC16DE55703 CRC64;
IEFTDIIKQL SQNTYTPREA GSQKDENLAY YIENLFHDFK FSKVWRDEHY VKIQVKNSVS
QNLVTINSGS NIDPVEAPEG YVAFSKAGEV TGKLVHANFG TKKDFEELNY SVNGSLVIVR
AGKITFAEKV ANAQSFNAIG VLIYMDRNTF PVVEADLQFF GHAHLGTGDP YTPGFPSFNH
TQFPPSQSSG LPSIPVQTIS RAPAEKLFKN MEGNCPPSWN IDSSCKLELS QNQNVKLTVN
NVLKETRILN IFGVIKGYEE PDRYIVVGAQ RDAWGPGVAK SSVGTGLLLK LAQVFSDMIS
KDGFRPSRSI IFASWTAGDY GAVGPTEWLE GYLSSLHLKA FTYINLDKVV LGTSNFKVSA
SPLLYTLMGK IMQDVKHPID GKYLYRNSNW ISKIEELSLD NAAFPFLAYS GIPAVSFCFC
EDEDYPYLGT KLDTYEILIQ KVPQLNQMVR TAAEVAGQFI IKLTHDIELT LDYEMYNSKL
LSFMKDLNQF KADIKDMGLS LQWLYSARGD YFRATSRLTT DFHNAEKTNR FVMREINDRI
MKVEYHFLSP YVSPRESPFR HIFWGSGSHT LSALVENLRL RQKNITAFNE TLFRNQLALA
TWTIQGVANA LSGDIWNIDN EF


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