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TFR2_RAT
ID   TFR2_RAT                Reviewed;         798 AA.
AC   B2GUY2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Transferrin receptor protein 2;
DE            Short=TfR2;
GN   Name=Tfr2; Synonyms=Trfr2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Mediates cellular uptake of transferrin-bound iron in a non-
CC       iron dependent manner. May be involved in iron metabolism, hepatocyte
CC       function and erythrocyte differentiation (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CH473973; EDM13257.1; -; Genomic_DNA.
DR   EMBL; CH473973; EDM13258.1; -; Genomic_DNA.
DR   EMBL; CH473973; EDM13259.1; -; Genomic_DNA.
DR   EMBL; BC166451; AAI66451.1; -; mRNA.
DR   RefSeq; NP_001099386.1; NM_001105916.1.
DR   RefSeq; XP_006249179.1; XM_006249117.2.
DR   RefSeq; XP_006249180.1; XM_006249118.1.
DR   RefSeq; XP_008767347.1; XM_008769125.2.
DR   RefSeq; XP_008767348.1; XM_008769126.1.
DR   AlphaFoldDB; B2GUY2; -.
DR   SMR; B2GUY2; -.
DR   IntAct; B2GUY2; 1.
DR   STRING; 10116.ENSRNOP00000001905; -.
DR   MEROPS; M28.973; -.
DR   GlyGen; B2GUY2; 3 sites.
DR   PaxDb; B2GUY2; -.
DR   PeptideAtlas; B2GUY2; -.
DR   PRIDE; B2GUY2; -.
DR   Ensembl; ENSRNOT00000001905; ENSRNOP00000001905; ENSRNOG00000001407.
DR   GeneID; 288562; -.
DR   KEGG; rno:288562; -.
DR   UCSC; RGD:1310152; rat.
DR   CTD; 7036; -.
DR   RGD; 1310152; Tfr2.
DR   eggNOG; KOG2195; Eukaryota.
DR   GeneTree; ENSGT01030000234598; -.
DR   HOGENOM; CLU_005688_5_0_1; -.
DR   InParanoid; B2GUY2; -.
DR   OMA; FSQGPHK; -.
DR   OrthoDB; 804230at2759; -.
DR   PhylomeDB; B2GUY2; -.
DR   TreeFam; TF312981; -.
DR   Reactome; R-RNO-917977; Transferrin endocytosis and recycling.
DR   PRO; PR:B2GUY2; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Proteomes; UP000234681; Chromosome 12.
DR   Bgee; ENSRNOG00000001407; Expressed in liver and 8 other tissues.
DR   Genevisible; B2GUY2; RN.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR   GO; GO:1990712; C:HFE-transferrin receptor complex; ISO:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR   GO; GO:0039706; F:co-receptor binding; ISO:RGD.
DR   GO; GO:0004998; F:transferrin receptor activity; ISO:RGD.
DR   GO; GO:0006953; P:acute-phase response; IEP:RGD.
DR   GO; GO:0071281; P:cellular response to iron ion; ISO:RGD.
DR   GO; GO:0140298; P:endocytic iron import into cell; ISO:RGD.
DR   GO; GO:0055072; P:iron ion homeostasis; ISO:RGD.
DR   GO; GO:0045807; P:positive regulation of endocytosis; ISO:RGD.
DR   GO; GO:0090277; P:positive regulation of peptide hormone secretion; ISO:RGD.
DR   GO; GO:1903319; P:positive regulation of protein maturation; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; ISO:RGD.
DR   GO; GO:0010039; P:response to iron ion; ISO:RGD.
DR   GO; GO:0033572; P:transferrin transport; ISO:RGD.
DR   CDD; cd02128; PA_TfR; 1.
DR   Gene3D; 1.20.930.40; -; 1.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   InterPro; IPR039373; Peptidase_M28B.
DR   InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR   InterPro; IPR037324; TfR1/2_PA.
DR   PANTHER; PTHR10404; PTHR10404; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF47672; SSF47672; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..798
FT                   /note="Transferrin receptor protein 2"
FT                   /id="PRO_0000348233"
FT   TOPO_DOM        1..81
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..798
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          25..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           23..26
FT                   /note="Endocytosis signal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        535
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        106
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
FT   DISULFID        109
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   798 AA;  88328 MW;  2EFF8F3D965D85B0 CRC64;
     MEQRWGLLRK VQQWSPRPSQ TIYRRVEGPQ LENLEEEDRE EGEELPAQFC PMELKGPERL
     GSCPGRSIPI PWAAAGRKAA PYLVLTTLLI FTGAFLLGYV AFRGSCQACG DSVLVVGEDV
     NSEDSSRGTL YWSDLQDMFL RFLGEGRMED TIRLTSLRER VAGSARMATL VQDILDKLSR
     QKLDHVWTDT HYVGLQFPDP AHPNTLHWVG ADGSVQEQLP LEDPEVYCPY SATGNATGKL
     VYAHYGRRED LQDLKAKDVE LAGSLLLVRA GITSFAQKVA IAQDFGAHGV LIYPDPADFS
     QDPHKPGLSS DRAVYGHVHL GTGDPYTPGF PSFNQTQFPP VESSGLPNIP AQPISADVAD
     RLLRKLTGPV APQEWKGRLS DSPYRLGPGP GLRLVVNNHR TSTPISNIFA CIEGFAEPDH
     YVVIGAQRDA WGPGAAKSAV GTAILLELVR TFSSMVSSGF RPRRSLLFIS WDGGDFGSVG
     ATEWLEGYLS VLHLKAVVYV SLDNSVLGDG KFHAKTSPLL VSLIENILKQ VDSPNHSGQT
     LYDQVAFTHP SWDAEVIQPL PMDSSAYSFT AFAGVPAVEF SFMEDDRVYP FLHTKEDTYE
     NLHKMLRGRL PAVVLAVAQL AGQLLIRLSH DHLLPLDFGR YGDVVLRHIG NLNEFSGDLK
     ARGLTLQWVY SARGDYIRAA EKLRKEIYSS EQSDERLMRM YNVRIMRVEF YFLSQYVSPA
     DSPFRHIFLG QGDHTLGALV EHLRMLRSDG SGAASSGLSP GLGFQESRFR RQLALLTWTL
     QGAANALSGD VWNIDNNF
 
 
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