LipidDB ID

LipidDB-9606-00511

Entry Name

UniProt Accession

P02786; D3DXB0; Q1HE24; Q59G55; Q9UCN0; Q9UCU5; Q9UDF9; Q9UK21;

Theoretical PI

6.18

Molecular Weight

84871.38

Genbank Protein ID

CAA25527.1; AAA61153.1; AAF04564.1; BAD92491.1; ABF47088.1; EAW53670.1; EAW53673.1; AAH01188.1;

Genbank Nucleotide ID

X01060; M11507; AF187320; AB209254; DQ496099; CH471191; CH471191; BC001188;

Protein Name

Transferrin receptor protein 1, serum form

Protein Synonyms/Alias

TR; TfR; TfR1; Trfr; T9; p90; CD71; sTfR;

Gene Name

TFRC

Gene Synonyms/Alias

Created Date

21-JUL-1986

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Reference

[1] Jing SQ, Trowbridge IS. Identification of the intermolecular disulfide bondsof the human transferrin receptor and its lipid-attachment site. EMBO J. 1987Feb;6(2):327-31.[PMID:3582362]

Functional Description

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). A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site.

Sequence Annotation

Topological domain: 1 67 Cytoplasmic.
Transmembrane: 68 88 Helical; Signal-anchor for type IImembrane protein.
Topological domain: 89 760 Extracellular.
Domain: 223 313 PA.
Region: 1 67 Mediates interaction with SH3BP4.
Region: 569 760 Ligand-binding.
Motif: 20 23 Endocytosis signal.
Motif: 58 61 Stop-transfer sequence.
Motif: 646 648 Cell attachment site; required forbinding to transferrin.
Functional site: 100 101 Cleavage; by trypsin; to produce solubleform.
Modified residue: 20 20 Phosphotyrosine.
Modified residue: 21 21 Phosphothreonine.
Modified residue: 24 24 Phosphoserine.

Protein Length

760 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0072562; C:blood microparticle; IDA:UniProt
GO:0009986; C:cell surface; IDA:UniProt
GO:0005905; C:coated pit; IDA:UniProtKB
GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI
GO:0005768; C:endosome; IDA:MGI
GO:0009897; C:external side of plasma membrane; IEA:Ensembl
GO:0005576; C:extracellular region; IDA:UniProtKB
GO:0005615; C:extracellular space; IDA:UniProt
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005887; C:integral component of plasma membrane; TAS:ProtInc
GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA
GO:0016020; C:membrane; NAS:UniProtKB
GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0055037; C:recycling endosome; IDA:MGI
GO:0031982; C:vesicle; IDA:UniProtKB
GO:0003725; F:double-stranded RNA binding; IDA:MGI
GO:0042802; F:identical protein binding; IPI:IntAct
GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB
GO:0004998; F:transferrin receptor activity; NAS:UniProtKB
GO:0006879; P:cellular iron ion homeostasis; NAS:UniProtKB
GO:0097286; P:iron ion import; IDA:UniProt
GO:0030316; P:osteoclast differentiation; IEA:Ensembl
GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl
GO:0033572; P:transferrin transport; TAS:Reactome
GO:0055085; P:transmembrane transport; TAS:Reactome
GO:0016032; P:viral process; IEA:UniProtKB-KW

Interpro

InterPro; IPR007484; Peptidase_M28
InterPro; IPR003137; Protease-assoc_domain
InterPro; IPR029513; TfR
InterPro; IPR007365; TFR-like_dimer_dom

Pfam

Pfam; PF02225; PA;
Pfam; PF04389; Peptidase_M28;
Pfam; PF04253; TFR_dimer;

SMART

PROSITE

PRINTS