ID A0A2I2UIM1_FELCA Unreviewed; 769 AA.
AC A0A2I2UIM1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Transferrin receptor protein 1 {ECO:0000256|ARBA:ARBA00016899, ECO:0000256|RuleBase:RU367157};
GN Name=TFRC {ECO:0000313|Ensembl:ENSFCAP00000032379.2,
GN ECO:0000313|VGNC:VGNC:66127};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000032379.2, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000032379.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000032379.2,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000032379.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000032379.2,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000032379.2}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000032379.2};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR EMBL; AANG04001815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_019694790.1; XM_019839231.1.
DR RefSeq; XP_019694791.1; XM_019839232.1.
DR RefSeq; XP_019694792.1; XM_019839233.1.
DR RefSeq; XP_019694793.1; XM_019839234.1.
DR AlphaFoldDB; A0A2I2UIM1; -.
DR Ensembl; ENSFCAT00000044148.3; ENSFCAP00000032379.2; ENSFCAG00000003694.6.
DR GeneID; 493880; -.
DR CTD; 7037; -.
DR VGNC; VGNC:66127; TFRC.
DR GeneTree; ENSGT01030000234598; -.
DR OMA; YQDSNWI; -.
DR OrthoDB; 2428249at2759; -.
DR Proteomes; UP000011712; Chromosome C2.
DR Bgee; ENSFCAG00000003694; Expressed in brain and 10 other cell types or tissues.
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:UP000011712};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|RuleBase:RU367157};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367157}.
FT TRANSMEM 68..91
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367157"
FT DOMAIN 237..320
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 397..587
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 646..758
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
SQ SEQUENCE 769 AA; 86238 MW; 31915957989BD757 CRC64;
MMDQARSAFS TLFGGEPLSY TRFSLARQVD GDNSHVEMKL AADEEENVDN NMRDNGASVT
KPKRFNGFIC YGTIAIILFF LIGFMIGYLG YCKRVEAKSE CERPAGTESL EVEGTEPSET
EEYFPEAPSH LFWSDLKTML SEKLSNTEFT STIRQLNENS YFPREAGSQK DESLAFFIEN
RFRELQLSKA WHDEHFVKVQ VKGSASNSVT IVGTNSGMVY LVESPEGYVA YSKAATVTGR
LVHANFGTKK DFENLNSPVN GSLVIVRAGK ITFAEKVANA ESFNAIGVLI YMDQAKFPIT
NAEIPFFGHA HLGTGDPYTP GFPSFNHTQF PPSQSSGLPN IPVQTISRAT AEKLFGNMEG
DCPSAWETDS SCRLETSRNW NVKLSVNNVL KEIRIFNVFG VIKGFEEPDH YVVVGAQRDA
WGPGAAKSSV GTALLLELAR ILSDMVLKGG FKPSRSIVFA SWTAGDFGAV GATEWLEGYL
SSLHLKAFTY INLDKAVLGT SNFKVSASPL LYSLIEKVMK DVKHPVTGQS LYRDSNWINK
VEKFSLDNAA FPFLAYSGIP AVSFCFCEDT DYPYLGTTMD VYEKLIQKVP QLNKMARAAA
EVAGQLIMKL TYDLELNLNY EMYNDKILSF VRDVSRFRAD IKEMGLNLQW LYSARGDFFR
ATSRLTTDYR NAERTNRFIM RDINDRIMRV EYHFLSPYVS PRESPFRHIF WGTGSHTLSA
LLEHLKLRQE NISAFNETLF RNQLALTTWT IQGAANALSG DIWDIDNEL
//
