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3S9M

Complex between transferrin receptor 1 and transferrin with iron in the N-Lobe, cryocooled 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004998molecular_functiontransferrin receptor activity
A0033572biological_processtransferrin transport
B0004998molecular_functiontransferrin receptor activity
B0033572biological_processtransferrin transport
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005768cellular_componentendosome
C0005769cellular_componentearly endosome
C0005770cellular_componentlate endosome
C0005788cellular_componentendoplasmic reticulum lumen
C0005886cellular_componentplasma membrane
C0005905cellular_componentclathrin-coated pit
C0006811biological_processmonoatomic ion transport
C0006826biological_processiron ion transport
C0006879biological_processintracellular iron ion homeostasis
C0007166biological_processcell surface receptor signaling pathway
C0008198molecular_functionferrous iron binding
C0008199molecular_functionferric iron binding
C0009617biological_processresponse to bacterium
C0009925cellular_componentbasal plasma membrane
C0009986cellular_componentcell surface
C0010008cellular_componentendosome membrane
C0016020cellular_componentmembrane
C0016324cellular_componentapical plasma membrane
C0019731biological_processantibacterial humoral response
C0019899molecular_functionenzyme binding
C0030139cellular_componentendocytic vesicle
C0030316biological_processosteoclast differentiation
C0030669cellular_componentclathrin-coated endocytic vesicle membrane
C0031410cellular_componentcytoplasmic vesicle
C0031647biological_processregulation of protein stability
C0031982cellular_componentvesicle
C0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
C0034774cellular_componentsecretory granule lumen
C0034986molecular_functioniron chaperone activity
C0044325molecular_functiontransmembrane transporter binding
C0045178cellular_componentbasal part of cell
C0046872molecular_functionmetal ion binding
C0048260biological_processpositive regulation of receptor-mediated endocytosis
C0048471cellular_componentperinuclear region of cytoplasm
C0055037cellular_componentrecycling endosome
C0060586biological_processmulticellular organismal-level iron ion homeostasis
C0070062cellular_componentextracellular exosome
C0071281biological_processcellular response to iron ion
C0072562cellular_componentblood microparticle
C1903988biological_processiron ion export across plasma membrane
C1990459molecular_functiontransferrin receptor binding
C1990712cellular_componentHFE-transferrin receptor complex
D0005506molecular_functioniron ion binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005768cellular_componentendosome
D0005769cellular_componentearly endosome
D0005770cellular_componentlate endosome
D0005788cellular_componentendoplasmic reticulum lumen
D0005886cellular_componentplasma membrane
D0005905cellular_componentclathrin-coated pit
D0006811biological_processmonoatomic ion transport
D0006826biological_processiron ion transport
D0006879biological_processintracellular iron ion homeostasis
D0007166biological_processcell surface receptor signaling pathway
D0008198molecular_functionferrous iron binding
D0008199molecular_functionferric iron binding
D0009617biological_processresponse to bacterium
D0009925cellular_componentbasal plasma membrane
D0009986cellular_componentcell surface
D0010008cellular_componentendosome membrane
D0016020cellular_componentmembrane
D0016324cellular_componentapical plasma membrane
D0019731biological_processantibacterial humoral response
D0019899molecular_functionenzyme binding
D0030139cellular_componentendocytic vesicle
D0030316biological_processosteoclast differentiation
D0030669cellular_componentclathrin-coated endocytic vesicle membrane
D0031410cellular_componentcytoplasmic vesicle
D0031647biological_processregulation of protein stability
D0031982cellular_componentvesicle
D0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
D0034774cellular_componentsecretory granule lumen
D0034986molecular_functioniron chaperone activity
D0044325molecular_functiontransmembrane transporter binding
D0045178cellular_componentbasal part of cell
D0046872molecular_functionmetal ion binding
D0048260biological_processpositive regulation of receptor-mediated endocytosis
D0048471cellular_componentperinuclear region of cytoplasm
D0055037cellular_componentrecycling endosome
D0060586biological_processmulticellular organismal-level iron ion homeostasis
D0070062cellular_componentextracellular exosome
D0071281biological_processcellular response to iron ion
D0072562cellular_componentblood microparticle
D1903988biological_processiron ion export across plasma membrane
D1990459molecular_functiontransferrin receptor binding
D1990712cellular_componentHFE-transferrin receptor complex
Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD
ChainResidueDetails
CTYR95-ASP104

site_idPS00206
Number of Residues17
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF
ChainResidueDetails
CTYR188-PHE204

site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV
ChainResidueDetails
CGLN222-VAL252
CASP558-VAL588

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues180
DetailsDomain: {"description":"PA"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsMotif: {"description":"Cell attachment site; required for binding to transferrin"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10531064","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10531064","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000173","evidences":[{"source":"PubMed","id":"10531064","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7780197","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues322
DetailsDomain: {"description":"Transferrin-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V83","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343719","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31636418","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V83","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VE1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6SOY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6SOZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Dimethylated arginine","evidences":[{"source":"UniProtKB","id":"P12346","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GalNAc...) serine","featureId":"CAR_000073"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000074","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15536627","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31636418","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6SOY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6SOZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000075","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15536627","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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