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

 TFR1_CRIGR              Reviewed;         757 AA.
Q07891;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 99.
RecName: Full=Transferrin receptor protein 1;
Short=TR;
Short=TfR;
Short=TfR1;
Short=Trfr;
AltName: CD_antigen=CD71;
Name=TFRC;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=8408022;
Collawn J.F., Lai A., Domingo D.L., Fitch M., Hatton S.,
Trowbridge I.S.;
"YTRF is the conserved internalization signal of the transferrin
receptor, and a second YTRF signal at position 31-34 enhances
endocytosis.";
J. Biol. Chem. 268:21686-21692(1993).
[2]
PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE.
PubMed=2327986; DOI=10.1042/bj2670031;
Alvarez E., Girones N., Davis R.J.;
"A point mutation in the cytoplasmic domain of the transferrin
receptor inhibits endocytosis.";
Biochem. J. 267:31-35(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}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P02786}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:P02786}. Melanosome
{ECO:0000250|UniProtKB:P02786}.
-!- 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; L19142; AAA03576.1; -; mRNA.
PIR; A48592; A48592.
RefSeq; NP_001233748.1; NM_001246819.1.
ProteinModelPortal; Q07891; -.
SMR; Q07891; -.
MEROPS; M28.972; -.
PRIDE; Q07891; -.
GeneID; 100689395; -.
KEGG; cge:100689395; -.
CTD; 7037; -.
HOVERGEN; HBG023177; -.
KO; K06503; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0055037; C:recycling endosome; IDA:MGI.
GO; GO:0004998; F:transferrin receptor activity; ISS:UniProtKB.
GO; GO:0033570; F:transferrin transmembrane transporter activity; IEA:InterPro.
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:0033572; P:transferrin transport; ISS:UniProtKB.
CDD; cd02128; PA_TfR; 1.
Gene3D; 1.20.930.40; -; 1.
InterPro; IPR003137; PA_domain.
InterPro; IPR007484; Peptidase_M28.
InterPro; IPR039373; Peptidase_M28B.
InterPro; IPR029513; TfR.
InterPro; IPR007365; TFR-like_dimer_dom.
InterPro; IPR036757; TFR-like_dimer_dom_sf.
InterPro; IPR037324; TfR1/2_PA.
PANTHER; PTHR10404; PTHR10404; 1.
PANTHER; PTHR10404:SF26; PTHR10404:SF26; 1.
Pfam; PF02225; PA; 1.
Pfam; PF04389; Peptidase_M28; 1.
Pfam; PF04253; TFR_dimer; 1.
SUPFAM; SSF47672; SSF47672; 1.
2: Evidence at transcript level;
Cell membrane; Disulfide bond; Endocytosis; Glycoprotein; Lipoprotein;
Membrane; Palmitate; Phosphoprotein; Receptor; Signal-anchor;
Transmembrane; Transmembrane helix.
CHAIN 1 757 Transferrin receptor protein 1.
/FTId=PRO_0000174130.
TOPO_DOM 1 67 Cytoplasmic. {ECO:0000255}.
TRANSMEM 68 88 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 89 757 Extracellular. {ECO:0000255}.
DOMAIN 220 310 PA.
REGION 1 67 Mediates interaction with SH3BP4.
{ECO:0000250}.
REGION 566 757 Ligand-binding. {ECO:0000250}.
MOTIF 20 23 Endocytosis signal.
MOTIF 58 61 Stop-transfer sequence.
MOTIF 643 645 Cell attachment site. {ECO:0000255}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:P02786}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000250|UniProtKB:Q62351}.
MOD_RES 20 20 Phosphotyrosine.
{ECO:0000250|UniProtKB:P02786}.
MOD_RES 21 21 Phosphothreonine.
{ECO:0000250|UniProtKB:P02786}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000250|UniProtKB:P02786}.
LIPID 67 67 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 103 103 O-linked (GalNAc...) threonine.
{ECO:0000250}.
CARBOHYD 248 248 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P02786}.
CARBOHYD 314 314 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P02786}.
CARBOHYD 719 719 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 724 724 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P02786}.
DISULFID 89 89 Interchain. {ECO:0000250}.
DISULFID 97 97 Interchain. {ECO:0000250}.
CONFLICT 20 20 Y -> T (in Ref. 2). {ECO:0000305}.
SEQUENCE 757 AA; 85081 MW; A6E6D1B8BB57C2EE CRC64;
MMDQARSAIS NLFGGEPLSY TRFSLARQVD GDNSHVEMKL AVDEEENTDN NMKASVRKHR
RLNGRLCFGT IAVVIFFLIG FMIGYLGYCK RTEQKDCVRL AETETGNSEI IQEENIPQSS
RLYWADLKKL LSEKLDAIEF TDTIKQLSQT SREAGSQKDE NLAYYIENQF RDFKLSKVWR
DEHYVKIQVK GSAAQNAVTI INVNGDSDLV ENPGGYVAYS KATTVSGKLI HANFGTKKDF
EDLKYPVNGS LVIVRAGKIT FAEKVANAQS FNAIGVLIYM DQTKFPVVEA ELSLFGHAHL
GTGDPYTPGF PSFNHTQFPP SQSSGLPSIP VQTISRKAAE KLFQNMETNC PPSWNTDSLC
KLESSQGINV NLSVNNVLKE TRILNIFGVI KGFEEPDRYI VVGAQRDAWG PGAAKSSVGT
GLLLKLAQAF SDMVSRGGFK PSRSIIFASW SAGDFGAVGA TEWLEGYLSS LHLKAFTYIN
LDKVVLGTRN FKVSASPLLY TLIEKTMQDV RHPIDGKPLY RDSNWISKVE DLSLDNAAFP
FLAYSGIPAV SFWFCENEDY PYLDTNLDTY EKLIQKVPQL NKMVRAAAEV AGQFIIKLTH
DIELNLDYDM YNNKILSFVK ELNQFRADIK AMGLSLQWLY SARGDFFRAT SRLTTDFHNA
EKTNRFVVRE INNRIMKVEY HFLSPYVSPR ESPFRHIFWG SGSHTLTALV ENLKLRQKNS
SAFNETLFRN QLALATWTIQ GVANALSGDI WDIDNEF


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