ID A0A226MPJ0_CALSU Unreviewed; 835 AA.
AC A0A226MPJ0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Transferrin receptor protein 1 {ECO:0000256|ARBA:ARBA00016899, ECO:0000256|RuleBase:RU367157};
GN ORFNames=ASZ78_000931 {ECO:0000313|EMBL:OXB57197.1};
OS Callipepla squamata (Scaled quail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC Callipepla.
OX NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB57197.1, ECO:0000313|Proteomes:UP000198323};
RN [1] {ECO:0000313|EMBL:OXB57197.1, ECO:0000313|Proteomes:UP000198323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texas {ECO:0000313|EMBL:OXB57197.1,
RC ECO:0000313|Proteomes:UP000198323};
RC TISSUE=Leg muscle {ECO:0000313|EMBL:OXB57197.1};
RA Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA Decker J.E., Seabury C.M.;
RT "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cellular uptake of iron occurs via receptor-mediated
CC endocytosis of ligand-occupied transferrin receptor into specialized
CC endosomes. Endosomal acidification leads to iron release. The
CC apotransferrin-receptor complex is then recycled to the cell surface
CC with a return to neutral pH and the concomitant loss of affinity of
CC apotransferrin for its receptor. Transferrin receptor is necessary for
CC development of erythrocytes and the nervous system. Acts as a lipid
CC sensor that regulates mitochondrial fusion by regulating activation of
CC the JNK pathway. {ECO:0000256|RuleBase:RU367157}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|RuleBase:RU367157}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367157};
CC Single-pass type II membrane protein {ECO:0000256|RuleBase:RU367157}.
CC Melanosome {ECO:0000256|RuleBase:RU367157}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- PTM: Stearoylated. {ECO:0000256|RuleBase:RU367157}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634, ECO:0000256|RuleBase:RU367157}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXB57197.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MCFN01000566; OXB57197.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226MPJ0; -.
DR STRING; 9009.A0A226MPJ0; -.
DR Proteomes; UP000198323; Unassembled WGS sequence.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004998; F:transferrin receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:UniProtKB-UniRule.
DR GO; GO:0031623; P:receptor internalization; IEA:UniProtKB-UniRule.
DR GO; GO:0033572; P:transferrin transport; IEA:UniProtKB-UniRule.
DR CDD; cd09848; M28_TfR; 1.
DR CDD; cd02128; PA_TfR; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR InterPro; IPR037324; TfR1/2_PA.
DR PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR PANTHER; PTHR10404:SF26; TRANSFERRIN RECEPTOR PROTEIN 1; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU367157};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583, ECO:0000256|RuleBase:RU367157};
KW Glycoprotein {ECO:0000256|RuleBase:RU367157};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|RuleBase:RU367157};
KW Membrane {ECO:0000256|RuleBase:RU367157};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|RuleBase:RU367157};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU367157};
KW Reference proteome {ECO:0000313|Proteomes:UP000198323};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|RuleBase:RU367157};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367157}.
FT TRANSMEM 127..149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367157"
FT DOMAIN 295..354
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 460..654
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 713..824
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
SQ SEQUENCE 835 AA; 92212 MW; C32DF7860F4C0EAD CRC64;
MIGAASAGAG ICAAARRAEG AAEARERRAG GRGTARVDLL YFTFLGLRSS WWVLVRKAMD
HARAALSNLF SGEPMSYTRF SIARQTDGDN SHVEMKLSAD DEEGGDVERP EHLHASMAQP
QRNVKKLCFL VTAAVLLLLI GFLIGYLSYR GRMQLAARCQ DGSGRCEMTP TASYLLDGDE
TEEEEIQGPS VLYWPDLKNM LSDKLSAKRL GDNLRQRAGV DSFEAGEAED TRMATYIHDQ
FNSFLLDKVW NDEHYIKLQV RGSTKNKVSV LMGGSQETLE TPDAYVAYSE SGSVSGKPVY
VNYGLKEDFE KIQKSVPSLN GTIVIVRSGK ITLAEKVANA KEAGAAGVLM YIDPLNYRVT
DTLVPFGHAH LGTGDPYTPG FPSFNHTQFP PVESSGLPHI AVQTISSNAA ARLFSKMDGD
SCFENWKGGI LPCKVTTKQE SEIMVKLDVN NSMKDRKILN IFGAIQGFEE PDRYVVIGAQ
RDSWGPGVAK AGTGTAILLE LARVISDMVK NGGYKPRRSI IFASWSAGDY GAVGATEWLE
GYSAMLHAKA FTYISLDAAV LGGTHVRISA SPLLYTLLER VMKGVKDPAT GSGKLYDRVG
SDWVKAVFPL GLDNAAFPFL AYSGIPVVSF GFYNKDEEYL FLDTKYDTLE NLRKIENLDA
LLHAAAEVAG QIALRLTHDH ELFLDFGRYS EELLAYQEKF LPYVKDVQEL GLTLDWLFFA
RGDFQRAADA LRRDITNSDR ENKVIRRALN DRIMKVEYDF LSPYLSPKDV PFRHIFFGKG
THTLQGLVEH LQQLKTSKSS VDLNLLKEQL ALATWTIKGA ANALGGDIWD TDNEF
//
