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Protein

Transferrin receptor protein 1

Gene

Tfrc

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. double-stranded RNA binding Source: MGI
  2. identical protein binding Source: MGI
  3. iron ion transmembrane transporter activity Source: MGI
  4. poly(A) RNA binding Source: MGI
  5. transferrin receptor activity Source: MGI

GO - Biological processi

  1. cellular iron ion homeostasis Source: MGI
  2. cellular response to drug Source: MGI
  3. iron ion import Source: MGI
  4. iron ion transmembrane transport Source: GOC
  5. osteoclast differentiation Source: DFLAT
  6. positive regulation of bone resorption Source: DFLAT
  7. transferrin transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Enzyme and pathway databases

ReactomeiREACT_290403. Transferrin endocytosis and recycling.
REACT_342454. Golgi Associated Vesicle Biogenesis.

Protein family/group databases

MEROPSiM28.972.

Names & Taxonomyi

Protein namesi
Recommended name:
Transferrin receptor protein 1
Short name:
TR
Short name:
TfR
Short name:
TfR1
Short name:
Trfr
Alternative name(s):
CD_antigen: CD71
Gene namesi
Name:Tfrc
Synonyms:Trfr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:98822. Tfrc.

Subcellular locationi

  1. Cell membrane By similarity; Single-pass type II membrane protein By similarity
  2. Melanosome By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6767CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei68 – 8821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini89 – 763675ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. blood microparticle Source: MGI
  2. cell surface Source: MGI
  3. coated pit Source: MGI
  4. cytoplasmic membrane-bounded vesicle Source: MGI
  5. endosome Source: MGI
  6. external side of plasma membrane Source: MGI
  7. extracellular region Source: MGI
  8. extracellular space Source: MGI
  9. extracellular vesicular exosome Source: MGI
  10. integral component of membrane Source: UniProtKB-KW
  11. intracellular membrane-bounded organelle Source: MGI
  12. melanosome Source: UniProtKB-SubCell
  13. membrane Source: ParkinsonsUK-UCL
  14. perinuclear region of cytoplasm Source: MGI
  15. plasma membrane Source: MGI
  16. recycling endosome Source: MGI
  17. vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 763763Transferrin receptor protein 1PRO_0000174133Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Phosphotyrosine2 Publications
Modified residuei21 – 211PhosphothreonineBy similarity
Modified residuei24 – 241PhosphoserineBy similarity
Lipidationi67 – 671S-palmitoyl cysteineBy similarity
Disulfide bondi89 – 89InterchainBy similarity
Disulfide bondi98 – 98InterchainBy similarity
Glycosylationi104 – 1041O-linked (GalNAc...)By similarity
Glycosylationi253 – 2531N-linked (GlcNAc...)By similarity
Glycosylationi319 – 3191N-linked (GlcNAc...)By similarity
Glycosylationi725 – 7251N-linked (GlcNAc...)1 Publication
Glycosylationi730 – 7301N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N- and O-glycosylated, phosphorylated and palmitoylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ62351.
PaxDbiQ62351.
PRIDEiQ62351.

PTM databases

PhosphoSiteiQ62351.

Expressioni

Gene expression databases

BgeeiQ62351.
CleanExiMM_TFRC.
ExpressionAtlasiQ62351. baseline and differential.
GenevestigatoriQ62351.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Binds one transferrin molecule per subunit. Interacts with SH3BP4 (By similarity).By similarity

Protein-protein interaction databases

BioGridi204314. 2 interactions.
IntActiQ62351. 3 interactions.
MINTiMINT-1858479.

Structurei

3D structure databases

ProteinModelPortaliQ62351.
SMRiQ62351. Positions 123-762.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini225 – 31591PAAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6767Mediates interaction with SH3BP4By similarityAdd
BLAST
Regioni572 – 763192Ligand-bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi20 – 234Endocytosis signal
Motifi58 – 614Stop-transfer sequence
Motifi649 – 6513Cell attachment siteSequence Analysis

Sequence similaritiesi

Belongs to the peptidase M28 family. M28B subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG74799.
GeneTreeiENSGT00550000074421.
HOGENOMiHOG000124067.
HOVERGENiHBG023177.
InParanoidiQ62351.
KOiK06503.
OMAiDNSHVEM.
OrthoDBiEOG780RKW.
PhylomeDBiQ62351.
TreeFamiTF312981.

Family and domain databases

Gene3Di1.20.930.40. 1 hit.
InterProiIPR007484. Peptidase_M28.
IPR003137. Protease-assoc_domain.
IPR029513. TfR.
IPR007365. TFR-like_dimer_dom.
[Graphical view]
PANTHERiPTHR10404:SF26. PTHR10404:SF26. 1 hit.
PfamiPF02225. PA. 1 hit.
PF04389. Peptidase_M28. 1 hit.
PF04253. TFR_dimer. 1 hit.
[Graphical view]
SUPFAMiSSF47672. SSF47672. 1 hit.

Sequencei

Sequence statusi: Complete.

Q62351-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMDQARSAFS NLFGGEPLSY TRFSLARQVD GDNSHVEMKL AADEEENADN
60 70 80 90 100
NMKASVRKPK RFNGRLCFAA IALVIFFLIG FMSGYLGYCK RVEQKEECVK
110 120 130 140 150
LAETEETDKS ETMETEDVPT SSRLYWADLK TLLSEKLNSI EFADTIKQLS
160 170 180 190 200
QNTYTPREAG SQKDESLAYY IENQFHEFKF SKVWRDEHYV KIQVKSSIGQ
210 220 230 240 250
NMVTIVQSNG NLDPVESPEG YVAFSKPTEV SGKLVHANFG TKKDFEELSY
260 270 280 290 300
SVNGSLVIVR AGEITFAEKV ANAQSFNAIG VLIYMDKNKF PVVEADLALF
310 320 330 340 350
GHAHLGTGDP YTPGFPSFNH TQFPPSQSSG LPNIPVQTIS RAAAEKLFGK
360 370 380 390 400
MEGSCPARWN IDSSCKLELS QNQNVKLIVK NVLKERRILN IFGVIKGYEE
410 420 430 440 450
PDRYVVVGAQ RDALGAGVAA KSSVGTGLLL KLAQVFSDMI SKDGFRPSRS
460 470 480 490 500
IIFASWTAGD FGAVGATEWL EGYLSSLHLK AFTYINLDKV VLGTSNFKVS
510 520 530 540 550
ASPLLYTLMG KIMQDVKHPV DGKSLYRDSN WISKVEKLSF DNAAYPFLAY
560 570 580 590 600
SGIPAVSFCF CEDADYPYLG TRLDTYEALT QKVPQLNQMV RTAAEVAGQL
610 620 630 640 650
IIKLTHDVEL NLDYEMYNSK LLSFMKDLNQ FKTDIRDMGL SLQWLYSARG
660 670 680 690 700
DYFRATSRLT TDFHNAEKTN RFVMREINDR IMKVEYHFLS PYVSPRESPF
710 720 730 740 750
RHIFWGSGSH TLSALVENLK LRQKNITAFN ETLFRNQLAL ATWTIQGVAN
760
ALSGDIWNID NEF
Length:763
Mass (Da):85,731
Last modified:November 1, 1996 - v1
Checksum:i832A148CC26CE489
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 262LA → AL in AAA37616 (PubMed:2984291).Curated
Sequence conflicti743 – 7431W → H AA sequence (PubMed:6092468).Curated
Sequence conflicti757 – 7571W → I AA sequence (PubMed:6092468).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57349 mRNA. Translation: CAA40624.1.
BC054522 mRNA. Translation: AAH54522.1.
M29618 mRNA. Translation: AAA37616.1.
CCDSiCCDS28123.1.
PIRiS29548.
RefSeqiNP_035768.1. NM_011638.4.
XP_006522062.1. XM_006521999.2.
UniGeneiMm.28683.

Genome annotation databases

EnsembliENSMUST00000023486; ENSMUSP00000023486; ENSMUSG00000022797.
GeneIDi22042.
KEGGimmu:22042.
UCSCiuc007yza.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57349 mRNA. Translation: CAA40624.1.
BC054522 mRNA. Translation: AAH54522.1.
M29618 mRNA. Translation: AAA37616.1.
CCDSiCCDS28123.1.
PIRiS29548.
RefSeqiNP_035768.1. NM_011638.4.
XP_006522062.1. XM_006521999.2.
UniGeneiMm.28683.

3D structure databases

ProteinModelPortaliQ62351.
SMRiQ62351. Positions 123-762.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204314. 2 interactions.
IntActiQ62351. 3 interactions.
MINTiMINT-1858479.

Protein family/group databases

MEROPSiM28.972.

PTM databases

PhosphoSiteiQ62351.

Proteomic databases

MaxQBiQ62351.
PaxDbiQ62351.
PRIDEiQ62351.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023486; ENSMUSP00000023486; ENSMUSG00000022797.
GeneIDi22042.
KEGGimmu:22042.
UCSCiuc007yza.2. mouse.

Organism-specific databases

CTDi7037.
MGIiMGI:98822. Tfrc.

Phylogenomic databases

eggNOGiNOG74799.
GeneTreeiENSGT00550000074421.
HOGENOMiHOG000124067.
HOVERGENiHBG023177.
InParanoidiQ62351.
KOiK06503.
OMAiDNSHVEM.
OrthoDBiEOG780RKW.
PhylomeDBiQ62351.
TreeFamiTF312981.

Enzyme and pathway databases

ReactomeiREACT_290403. Transferrin endocytosis and recycling.
REACT_342454. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSiTfrc. mouse.
NextBioi301828.
PROiQ62351.
SOURCEiSearch...

Gene expression databases

BgeeiQ62351.
CleanExiMM_TFRC.
ExpressionAtlasiQ62351. baseline and differential.
GenevestigatoriQ62351.

Family and domain databases

Gene3Di1.20.930.40. 1 hit.
InterProiIPR007484. Peptidase_M28.
IPR003137. Protease-assoc_domain.
IPR029513. TfR.
IPR007365. TFR-like_dimer_dom.
[Graphical view]
PANTHERiPTHR10404:SF26. PTHR10404:SF26. 1 hit.
PfamiPF02225. PA. 1 hit.
PF04389. Peptidase_M28. 1 hit.
PF04253. TFR_dimer. 1 hit.
[Graphical view]
SUPFAMiSSF47672. SSF47672. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Trowbridge I.S., Domingo D.L., Thomas M.L., Chain A.
    Submitted (JAN-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X DBA/2.
    Tissue: Hematopoietic.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  3. "cDNA cloning of the murine transferrin receptor: sequence of trans-membrane and adjacent regions."
    Stearne P.A., Pietersz G.A., Goding J.W.
    J. Immunol. 134:3474-3479(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-301.
    Tissue: Myeloma.
  4. "The receptor for transferrin on murine myeloma cells: one-step purification based on its physiology, and partial amino acid sequence."
    van Driel I.R., Stearne P.A., Grego B., Simpson R.J., Goding J.W.
    J. Immunol. 133:3220-3224(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 7-19; 158-179; 196-208; 450-467 AND 736-759.
    Tissue: Myeloma.
  5. "Transferrin receptor is necessary for development of erythrocytes and the nervous system."
    Levy J.E., Jin O., Fujiwara Y., Kuo F., Andrews N.C.
    Nat. Genet. 21:396-399(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  8. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-725 AND ASN-730.

Entry informationi

Entry nameiTFR1_MOUSE
AccessioniPrimary (citable) accession number: Q62351
Secondary accession number(s): Q61560
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: November 1, 1996
Last modified: April 1, 2015
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.