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

 TFR1_MOUSE              Reviewed;         763 AA.
Q62351; Q61560;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
05-DEC-2018, entry version 164.
RecName: Full=Transferrin receptor protein 1;
Short=TR;
Short=TfR;
Short=TfR1;
Short=Trfr;
AltName: CD_antigen=CD71;
Name=Tfrc; Synonyms=Trfr;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6 X DBA/2; TISSUE=Hematopoietic;
Trowbridge I.S., Domingo D.L., Thomas M.L., Chain A.;
Submitted (JAN-1991) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 25-301.
TISSUE=Myeloma;
PubMed=2984291;
Stearne P.A., Pietersz G.A., Goding J.W.;
"cDNA cloning of the murine transferrin receptor: sequence of trans-
membrane and adjacent regions.";
J. Immunol. 134:3474-3479(1985).
[4]
PROTEIN SEQUENCE OF 7-19; 158-179; 196-208; 450-467 AND 736-759.
TISSUE=Myeloma;
PubMed=6092468;
van Driel I.R., Stearne P.A., Grego B., Simpson R.J., Goding J.W.;
"The receptor for transferrin on murine myeloma cells: one-step
purification based on its physiology, and partial amino acid
sequence.";
J. Immunol. 133:3220-3224(1984).
[5]
FUNCTION.
PubMed=10192390; DOI=10.1038/7727;
Levy J.E., Jin O., Fujiwara Y., Kuo F., Andrews N.C.;
"Transferrin receptor is necessary for development of erythrocytes and
the nervous system.";
Nat. Genet. 21:396-399(1999).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-725 AND ASN-730.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
MUTAGENESIS OF TYR-20, AND FUNCTION.
PubMed=26642240; DOI=10.1038/ng.3465;
Jabara H.H., Boyden S.E., Chou J., Ramesh N., Massaad M.J., Benson H.,
Bainter W., Fraulino D., Rahimov F., Sieff C., Liu Z.J.,
Alshemmari S.H., Al-Ramadi B.K., Al-Dhekri H., Arnaout R.,
Abu-Shukair M., Vatsayan A., Silver E., Ahuja S., Davies E.G.,
Sola-Visner M., Ohsumi T.K., Andrews N.C., Notarangelo L.D.,
Fleming M.D., Al-Herz W., Kunkel L.M., Geha R.S.;
"A missense mutation in TFRC, encoding transferrin receptor 1, causes
combined immunodeficiency.";
Nat. Genet. 48:74-78(2016).
-!- 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). Upon stimulation, positively
regulates T and B cell proliferation through iron uptake
(PubMed:26642240). {ECO:0000250, ECO:0000269|PubMed:10192390,
ECO:0000269|PubMed:26642240}.
-!- 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; X57349; CAA40624.1; -; mRNA.
EMBL; BC054522; AAH54522.1; -; mRNA.
EMBL; M29618; AAA37616.1; -; mRNA.
CCDS; CCDS28123.1; -.
PIR; S29548; S29548.
RefSeq; NP_035768.1; NM_011638.4.
RefSeq; XP_006522062.1; XM_006521999.3.
UniGene; Mm.28683; -.
ProteinModelPortal; Q62351; -.
SMR; Q62351; -.
BioGrid; 204314; 6.
IntAct; Q62351; 12.
MINT; Q62351; -.
STRING; 10090.ENSMUSP00000023486; -.
MEROPS; M28.972; -.
iPTMnet; Q62351; -.
PhosphoSitePlus; Q62351; -.
SwissPalm; Q62351; -.
EPD; Q62351; -.
MaxQB; Q62351; -.
PaxDb; Q62351; -.
PRIDE; Q62351; -.
Ensembl; ENSMUST00000023486; ENSMUSP00000023486; ENSMUSG00000022797.
GeneID; 22042; -.
KEGG; mmu:22042; -.
UCSC; uc007yza.2; mouse.
CTD; 7037; -.
MGI; MGI:98822; Tfrc.
eggNOG; KOG2195; Eukaryota.
eggNOG; COG2234; LUCA.
GeneTree; ENSGT00940000153978; -.
HOGENOM; HOG000124067; -.
HOVERGEN; HBG023177; -.
InParanoid; Q62351; -.
KO; K06503; -.
OMA; IMKVEYH; -.
OrthoDB; EOG091G02ZM; -.
PhylomeDB; Q62351; -.
TreeFam; TF312981; -.
Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
ChiTaRS; Tfrc; mouse.
PRO; PR:Q62351; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022797; Expressed in 297 organ(s), highest expression level in placenta labyrinth.
CleanEx; MM_TFRC; -.
ExpressionAtlas; Q62351; baseline and differential.
Genevisible; Q62351; MM.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005905; C:clathrin-coated pit; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
GO; GO:0005769; C:early endosome; IDA:MGI.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0010008; C:endosome membrane; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; IDA:MGI.
GO; GO:0005576; C:extracellular region; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:1990712; C:HFE-transferrin receptor complex; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IMP:ParkinsonsUK-UCL.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0055037; C:recycling endosome; IDA:MGI.
GO; GO:0055038; C:recycling endosome membrane; ISO:MGI.
GO; GO:0051087; F:chaperone binding; ISO:MGI.
GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0005381; F:iron ion transmembrane transporter activity; TAS:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO: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; IMP:MGI.
GO; GO:0035690; P:cellular response to drug; ISO:MGI.
GO; GO:0031668; P:cellular response to extracellular stimulus; TAS:BHF-UCL.
GO; GO:0071281; P:cellular response to iron ion; TAS:BHF-UCL.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0097286; P:iron ion import; ISO:MGI.
GO; GO:0030316; P:osteoclast differentiation; IMP:DFLAT.
GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:UniProtKB.
GO; GO:0045780; P:positive regulation of bone resorption; IDA:DFLAT.
GO; GO:0045830; P:positive regulation of isotype switching; ISS:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA: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.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing;
Disulfide bond; Endocytosis; Glycoprotein; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Receptor; Reference proteome;
Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 763 Transferrin receptor protein 1.
/FTId=PRO_0000174133.
TOPO_DOM 1 67 Cytoplasmic. {ECO:0000255}.
TRANSMEM 68 88 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 89 763 Extracellular. {ECO:0000255}.
DOMAIN 225 315 PA.
REGION 1 67 Mediates interaction with SH3BP4.
{ECO:0000250}.
REGION 572 763 Ligand-binding. {ECO:0000250}.
MOTIF 20 23 Endocytosis signal.
MOTIF 58 61 Stop-transfer sequence.
MOTIF 649 651 Cell attachment site. {ECO:0000255}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:P02786}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 20 20 Phosphotyrosine.
{ECO:0000244|PubMed:17947660,
ECO:0000244|PubMed:19131326}.
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 104 104 O-linked (GalNAc...) threonine.
{ECO:0000250}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P02786}.
CARBOHYD 319 319 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P02786}.
CARBOHYD 725 725 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 730 730 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
DISULFID 89 89 Interchain. {ECO:0000250}.
DISULFID 98 98 Interchain. {ECO:0000250}.
MUTAGEN 20 20 Y->H: Negatively regulates of T and B
cell proliferation upon activation.
Significantly increases cell surface
expression on T and B cells. Impairs
internalization.
{ECO:0000269|PubMed:26642240}.
CONFLICT 25 26 LA -> AL (in Ref. 3; AAA37616).
{ECO:0000305}.
CONFLICT 743 743 W -> H (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 757 757 W -> I (in Ref. 4; AA sequence).
{ECO:0000305}.
SEQUENCE 763 AA; 85731 MW; 832A148CC26CE489 CRC64;
MMDQARSAFS NLFGGEPLSY TRFSLARQVD GDNSHVEMKL AADEEENADN NMKASVRKPK
RFNGRLCFAA IALVIFFLIG FMSGYLGYCK RVEQKEECVK LAETEETDKS ETMETEDVPT
SSRLYWADLK TLLSEKLNSI EFADTIKQLS QNTYTPREAG SQKDESLAYY IENQFHEFKF
SKVWRDEHYV KIQVKSSIGQ NMVTIVQSNG NLDPVESPEG YVAFSKPTEV SGKLVHANFG
TKKDFEELSY SVNGSLVIVR AGEITFAEKV ANAQSFNAIG VLIYMDKNKF PVVEADLALF
GHAHLGTGDP YTPGFPSFNH TQFPPSQSSG LPNIPVQTIS RAAAEKLFGK MEGSCPARWN
IDSSCKLELS QNQNVKLIVK NVLKERRILN IFGVIKGYEE PDRYVVVGAQ RDALGAGVAA
KSSVGTGLLL KLAQVFSDMI SKDGFRPSRS IIFASWTAGD FGAVGATEWL EGYLSSLHLK
AFTYINLDKV VLGTSNFKVS ASPLLYTLMG KIMQDVKHPV DGKSLYRDSN WISKVEKLSF
DNAAYPFLAY SGIPAVSFCF CEDADYPYLG TRLDTYEALT QKVPQLNQMV RTAAEVAGQL
IIKLTHDVEL NLDYEMYNSK LLSFMKDLNQ FKTDIRDMGL SLQWLYSARG DYFRATSRLT
TDFHNAEKTN RFVMREINDR IMKVEYHFLS PYVSPRESPF RHIFWGSGSH TLSALVENLK
LRQKNITAFN ETLFRNQLAL ATWTIQGVAN ALSGDIWNID NEF


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