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

 TFR1_CANLF              Reviewed;         770 AA.
Q9GLD3;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-SEP-2018, entry version 112.
RecName: Full=Transferrin receptor protein 1;
Short=TR;
Short=TfR;
Short=TfR1;
Short=Trfr;
AltName: CD_antigen=CD71;
Name=TFRC;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11264378; DOI=10.1128/JVI.75.8.3896-3902.2001;
Parker J.S.L., Murphy W.J., Wang D., O'Brien S.J., Parrish C.R.;
"Canine and feline parvoviruses can use human or feline transferrin
receptors to bind, enter, and infect cells.";
J. Virol. 75:3896-3902(2001).
[2]
INTERACTION WITH CANINE PARVOVIRUS CAPSID PROTEINS.
PubMed=19656887; DOI=10.1128/JVI.00295-09;
Harbison C.E., Lyi S.M., Weichert W.S., Parrish C.R.;
"Early steps in cell infection by parvoviruses: host-specific
differences in cell receptor binding but similar endosomal
trafficking.";
J. Virol. 83:10504-10514(2009).
-!- 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}.
-!- DOMAIN: The YTRF endocytosis motif engages the clathrin-mediated
endocytic machinery through adapter protein-2.
-!- PTM: N- and O-glycosylated, phosphorylated and palmitoylated.
{ECO:0000250}.
-!- MISCELLANEOUS: Canine and feline parvoviruses bind human and
feline transferrin receptors and use these receptors to enter and
infect cells.
-!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
{ECO:0000305}.
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EMBL; AF297626; AAG24850.1; -; mRNA.
RefSeq; NP_001003111.1; NM_001003111.1.
UniGene; Cfa.33569; -.
ProteinModelPortal; Q9GLD3; -.
SMR; Q9GLD3; -.
STRING; 9615.ENSCAFP00000019067; -.
MEROPS; M28.972; -.
PaxDb; Q9GLD3; -.
PRIDE; Q9GLD3; -.
GeneID; 403703; -.
KEGG; cfa:403703; -.
CTD; 7037; -.
eggNOG; KOG2195; Eukaryota.
eggNOG; COG2234; LUCA.
HOGENOM; HOG000124067; -.
HOVERGEN; HBG023177; -.
InParanoid; Q9GLD3; -.
KO; K06503; -.
Proteomes; UP000002254; Unplaced.
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: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.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
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; Disulfide bond; Endocytosis;
Glycoprotein; Host-virus interaction; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Receptor; Reference proteome;
Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 770 Transferrin receptor protein 1.
/FTId=PRO_0000174129.
TOPO_DOM 1 70 Cytoplasmic. {ECO:0000255}.
TRANSMEM 71 90 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 91 770 Extracellular. {ECO:0000255}.
DOMAIN 233 323 PA.
REGION 1 70 Mediates interaction with SH3BP4.
{ECO:0000250}.
REGION 579 770 Ligand-binding. {ECO:0000250}.
MOTIF 20 23 Endocytosis signal.
MOTIF 61 64 Stop-transfer sequence.
MOTIF 656 658 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 65 65 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 70 70 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 107 107 O-linked (GalNAc...) threonine.
{ECO:0000250}.
CARBOHYD 261 261 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P02786}.
CARBOHYD 327 327 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P02786}.
CARBOHYD 384 384 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 732 732 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 737 737 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P02786}.
DISULFID 92 92 Interchain. {ECO:0000250}.
DISULFID 101 101 Interchain. {ECO:0000250}.
SEQUENCE 770 AA; 86649 MW; 871F8320A1E1345A CRC64;
MMDQARSAFS TLFGGEPLSY TRFSLARQVD GDNSHVEMKL AADEEENVDN NMRGNHASVP
KPKRCNGFIC YGTIAVVLFF LIGFMIGYLG YCKRVEPKAG CERPTGTEAL GTERTEPSET
EEYFPETPSR LFWTDLKTML SERLSNTDFT NTMRWLNENS YVPREAGSQK DESLALLIEN
RFREFQLSKS WRDEHFVEIQ VKSSNAQNTV TIVDMESDLV YLAESPEGYV AYSKATTVTG
RLVHVNFGTK KDFENLKSPV NGSLVIARAG KITFAEKVAN AQSYNALGVL IYMDQARFPI
VNARIPFFGH AHLGTGDPYT PGFPSFNHTQ FPPSQSSGLP SIPVQTISRA AAEKLFENME
GDCPSAWEID PSCRLETSSN KNVNLTVNNV LKEIRIFNVF GVIKGFEEPD RYVVIGAQRD
AWGPGAAKSS VGTALLLELA RIFSDMVLKG GFKPSRSIVF ASWSAGDFGA IGATEWLEGY
LSSLHLKAFT YINLDKAILG TSNFKVSASP LLYSLLEKTM KDVKHPITGQ SLYRDSNWIN
KVEKLSLDNA AFPFLAYSGI PAVSFCFCED TDYPYLGTTM DLYENLNQKI PQLNKMARGA
AEVAGQLIMK LTYDLELNLN YEMYNDRILS FVRDMNQFRT DIKEMGLNLQ WLYSARGDFF
RATSRLTTDY KNAERTNRFV MREINDRIMK VEHNFLSPYV SPRDSPFRHI FWGSGSHTLP
ALVEHLKLRQ KNKSAFNETL LRNQLALATW TIQGAANALS GDIWDIDNEF


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