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0TFR1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTFRC
DescriptionTransferrin receptor protein 1 (tfr1) (tr) (tfr) (trfr) (cd71 antigen) (t9) (p90).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005768 endosome (TAS)
0005576 extracellular region (IDA)
0005887 integral to plasma membrane (TAS)
0016020 membrane (NAS)
0004998 transferrin receptor activity (NAS)
0006879 iron ion homeostasis (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This entry represents the dimerisation domain found in the transferrin receptor.s well as in a number of other proteins including glutamate carboxypeptidase II and N-acetylated-alpha-linked acidic dipeptidase like protein. The transferrin receptor (TfR) assists iron uptake into vertebrate cells through a cycle of endo- and exocytosis of the iron transport protein transferrin (Tf). TfR binds iron-loaded (diferric) Tf at the cell surface and carries it to the endosome.here the iron dissociates from Tf. The apo-Tf remains bound to TfR until it reaches the cell surface.here apo-Tf is replaced by diferric Tf from the serum to begin the cycle again. Human TfR is a homodimeric type II transmembrane protein. The crystal structure of a TfR monomer reveals a 3-domain structure: a protease-like domain that closely resembles carboxy- and amino-peptidases; an apical domain consisting of a beta-sandwich; and a helical dimerisation domain. The dimerisation domain consists of a 4-helical bundle that makes contact with each of the three domains in the dimer partner .
  IPR007365:Transferrin receptor-like dimerisation region
The PA (Protease associated) domain is found as an insert domain in diverse proteases.hich include the MEROPS peptidase families A22B.28.nd S8A . The PA domain is also found in a plant vacuolar sorting receptor and members of the RZF family..g. .
  IPR003137:Protease-associated PA
Ribosomes are the particles that catalyze mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain.ituated in the P site as peptidyl-tRNA.s then transferred to aminoacyl-tRNA and the new peptidyl-tRNA.xtended by one residue.s translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites . About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits. Many of ribosomal proteins.articularly those of the large subunit.re composed of a globular.urfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilize its structure. Most of the proteins interact with multiple RNA elements.ften from different domains. In the large subunit.bout 1/3 of the 23S rRNA nucleotides are at least in van der Waals contact with protein.nd L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7.hich initiate assembly of the 16S rRNA.re located at junctions of five and four RNA helices.espectively. In this way proteins serve to organize and stabilize the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based.roteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome.any ribosomal proteins have some function outside the ribosome .Ribosomal S2 proteins have been shown to belong to a family that includes 40S ribosomal subunit 40kDa proteins.utative laminin-binding proteins.AB-1 protein and 29.3kDa protein from Haloarcula marismortui . The laminin-receptor proteins are thus predicted to be the eukaryotic homologue of the eubacterial S2 risosomal proteins .
  IPR001865:Ribosomal protein S2
IPR007365:TFR_dimer 
Evalue:-48.6020584106445 
Location:619-752IPR003137:PA 
Evalue:-12.6777811050415 
Location:223-313IPR001865:Ribosomal_S2 
Evalue:0 
Location:0-0
SequencesProtein: TFR1_HUMAN (760 aa)
mRNA: NM_003234
Local Annotation
Synapse Ontology
endosome of the presynaptic compartment. A cellular structure that is involved in the transport of proteins in the neuron after the proteins are endocytosed from the outside to the inside of the cell.
sdb:0088 endosome  (Evidence:keywords)
endocytosis may be initiated or blocked by all kinds of signal.
sdb:0257 regulation of endocytosis  (Evidence:keywords)
KO assignmentK06503
  Level 3 annotation:
    transferrin receptor
  Level 2 annotation:
    CD molecules
    Hematopoietic cell lineage
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 903 residues, 197260746-197263452Exon2: 49 residues, 197264685-197264826Exon3: 76 residues, 197266347-197266569Exon4: 29 residues, 197269551-197269633Exon5: 21 residues, 197269841-197269900Exon6: 24 residues, 197271447-197271515Exon7: 23 residues, 197273849-197273913Exon8: 30 residues, 197274121-197274207Exon9: 42 residues, 197275576-197275696Exon10: 54 residues, 197276710-197276868Exon11: 48 residues, 197278785-197278925Exon12: 35 residues, 197279299-197279398Exon13: 40 residues, 197280722-197280836Exon14: 36 residues, 197282663-197282766Exon15: 52 residues, 197283270-197283420Exon16: 67 residues, 197285197-197285393Exon17: 69 residues, 197286426-197286628Exon18: 21 residues, 197288331-197288390Exon19: 82 residues, 197293098-197293338Exon20: 2 residues, -Jump to TFR1_HUMAN  
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Loci Cluster (Details)Loci: 4655 197074632-197120277 ~-46K 27086(TNK2)(-)Loci: 4656 197260746-197293338 ~-33K 27090(TFRC)(-)Loci: 4654 196776866-196792278 ~-15K 27071(APOD)(-)Link out to UCSC