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Transferrin receptor protein 2 (TfR2)

 TFR2_MOUSE              Reviewed;         798 AA.
Q9JKX3; Q920I6; Q99MQ9; Q9CPT2;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
11-FEB-2002, sequence version 2.
23-MAY-2018, entry version 139.
RecName: Full=Transferrin receptor protein 2;
Short=TfR2;
Name=Tfr2; Synonyms=Trfr2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Embryo;
PubMed=10681454; DOI=10.1073/pnas.040548097;
Fleming R.E., Migas M.C., Holden C.C., Waheed A., Britton R.S.,
Tomatsu S., Bacon B.R., Sly W.S.;
"Transferrin receptor 2: continued expression in mouse liver in the
face of iron overload and in hereditary hemochromatosis.";
Proc. Natl. Acad. Sci. U.S.A. 97:2214-2219(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Erythroleukemia;
PubMed=11535534; DOI=10.1182/blood.V98.6.1949;
Kawabata H., Germain R.S., Ikezoe T., Tong X., Green E.M.,
Gombart A.F., Koeffler H.P.;
"Regulation of expression of murine transferrin receptor 2.";
Blood 98:1949-1954(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-278.
STRAIN=129/Sv;
PubMed=11239002; DOI=10.1093/nar/29.6.1352;
Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C.,
Miller W., Koop B.F.;
"Comparative analysis of the gene-dense ACHE/TFR2 region on human
chromosome 7q22 with the orthologous region on mouse chromosome 5.";
Nucleic Acids Res. 29:1352-1365(2001).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Mediates cellular uptake of transferrin-bound iron in a
non-iron dependent manner. May be involved in iron metabolism,
hepatocyte function and erythrocyte differentiation.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
protein.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9JKX3-1; Sequence=Displayed;
Name=2;
IsoId=Q9JKX3-2; Sequence=VSP_005357, VSP_005358;
Note=Lacks most of the extracellular domain. No experimental
confirmation available.;
Name=3;
IsoId=Q9JKX3-3; Sequence=VSP_005356;
-!- TISSUE SPECIFICITY: Predominantly expressed in liver. Also
expressed in kidney, spleen, brain, lung, heart and muscle with
very low expression in kidney, muscle and heart.
-!- DEVELOPMENTAL STAGE: First expressed between embryo days 8 and 11.
In the liver, expression increases during development from embryo
day 13 to adulthood while, in the spleen, levels remain constant
throughout development.
-!- INDUCTION: Down-regulated during erythrocyte differentiation.
Expression unchanged by cellular iron status.
-!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF222895; AAF37272.1; -; mRNA.
EMBL; AF207741; AAL05976.1; -; mRNA.
EMBL; AF207742; AAL05977.1; -; Genomic_DNA.
EMBL; AK004965; BAB23705.1; -; mRNA.
EMBL; AK004848; BAB23614.1; -; mRNA.
EMBL; BC013654; AAH13654.1; -; mRNA.
EMBL; AF312033; AAK28830.1; -; Genomic_DNA.
CCDS; CCDS39333.1; -. [Q9JKX3-1]
RefSeq; NP_001276436.1; NM_001289507.1.
RefSeq; NP_001276438.1; NM_001289509.1. [Q9JKX3-1]
RefSeq; NP_001276440.1; NM_001289511.1. [Q9JKX3-1]
RefSeq; NP_056614.3; NM_015799.4. [Q9JKX3-1]
RefSeq; XP_006504656.1; XM_006504593.3. [Q9JKX3-1]
RefSeq; XP_006504657.1; XM_006504594.3. [Q9JKX3-1]
RefSeq; XP_011239249.1; XM_011240947.2.
UniGene; Mm.21757; -.
ProteinModelPortal; Q9JKX3; -.
SMR; Q9JKX3; -.
IntAct; Q9JKX3; 2.
MINT; Q9JKX3; -.
STRING; 10090.ENSMUSP00000031729; -.
MEROPS; M28.973; -.
iPTMnet; Q9JKX3; -.
PhosphoSitePlus; Q9JKX3; -.
PaxDb; Q9JKX3; -.
PeptideAtlas; Q9JKX3; -.
PRIDE; Q9JKX3; -.
Ensembl; ENSMUST00000031729; ENSMUSP00000031729; ENSMUSG00000029716. [Q9JKX3-1]
Ensembl; ENSMUST00000196471; ENSMUSP00000142814; ENSMUSG00000029716. [Q9JKX3-1]
Ensembl; ENSMUST00000198783; ENSMUSP00000142502; ENSMUSG00000029716. [Q9JKX3-1]
Ensembl; ENSMUST00000198866; ENSMUSP00000142720; ENSMUSG00000029716. [Q9JKX3-1]
Ensembl; ENSMUST00000199054; ENSMUSP00000142478; ENSMUSG00000029716. [Q9JKX3-1]
GeneID; 50765; -.
KEGG; mmu:50765; -.
UCSC; uc009acv.2; mouse. [Q9JKX3-1]
CTD; 7036; -.
MGI; MGI:1354956; Tfr2.
eggNOG; KOG2195; Eukaryota.
eggNOG; COG2234; LUCA.
GeneTree; ENSGT00550000074421; -.
HOGENOM; HOG000124067; -.
HOVERGEN; HBG023177; -.
InParanoid; Q9JKX3; -.
OMA; LFISWDG; -.
OrthoDB; EOG091G02ZM; -.
PhylomeDB; Q9JKX3; -.
TreeFam; TF312981; -.
Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
ChiTaRS; Tfr2; mouse.
PRO; PR:Q9JKX3; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029716; -.
CleanEx; MM_TRFR2; -.
ExpressionAtlas; Q9JKX3; baseline and differential.
Genevisible; Q9JKX3; MM.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
GO; GO:1990712; C:HFE-transferrin receptor complex; IDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; ISA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0039706; F:co-receptor binding; ISO:MGI.
GO; GO:0004998; F:transferrin receptor activity; ISO:MGI.
GO; GO:0033570; F:transferrin transmembrane transporter activity; IEA:InterPro.
GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:MGI.
GO; GO:0071281; P:cellular response to iron ion; ISO:MGI.
GO; GO:0033216; P:ferric iron import; ISO:MGI.
GO; GO:0055072; P:iron ion homeostasis; IMP:MGI.
GO; GO:0097286; P:iron ion import; ISO:MGI.
GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
GO; GO:0090277; P:positive regulation of peptide hormone secretion; ISO:MGI.
GO; GO:1903319; P:positive regulation of protein maturation; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
GO; GO:0010039; P:response to iron ion; ISO:MGI.
GO; GO:0033572; P:transferrin transport; ISO:MGI.
CDD; cd02128; PA_TfR; 1.
Gene3D; 1.20.930.40; -; 1.
InterPro; IPR003137; PA_domain.
InterPro; IPR007484; Peptidase_M28.
InterPro; IPR036757; TFR-like_dimer_dom_sf.
InterPro; IPR037324; TfR1/2_PA.
Pfam; PF02225; PA; 1.
Pfam; PF04389; Peptidase_M28; 1.
SUPFAM; SSF47672; SSF47672; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 798 Transferrin receptor protein 2.
/FTId=PRO_0000174137.
TOPO_DOM 1 81 Cytoplasmic. {ECO:0000255}.
TRANSMEM 82 102 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 103 798 Extracellular. {ECO:0000255}.
MOTIF 23 26 Endocytosis signal. {ECO:0000255}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 334 334 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 535 535 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 106 106 Interchain. {ECO:0000255}.
DISULFID 109 109 Interchain. {ECO:0000255}.
VAR_SEQ 12 93 Missing (in isoform 3).
{ECO:0000303|PubMed:11535534}.
/FTId=VSP_005356.
VAR_SEQ 237 237 T -> TVRFPGWGAHHVLIG (in isoform 2).
{ECO:0000303|PubMed:11535534}.
/FTId=VSP_005357.
VAR_SEQ 238 798 Missing (in isoform 2).
{ECO:0000303|PubMed:11535534}.
/FTId=VSP_005358.
CONFLICT 25 25 R -> P (in Ref. 2; AAL05977).
{ECO:0000305}.
CONFLICT 42 42 G -> V (in Ref. 2; AAL05977 and 5;
AAK28830). {ECO:0000305}.
CONFLICT 103 103 R -> P (in Ref. 2; AAL05977).
{ECO:0000305}.
CONFLICT 151 151 T -> N (in Ref. 4; AAH13654).
{ECO:0000305}.
CONFLICT 248 248 S -> L (in Ref. 2; AAL05976).
{ECO:0000305}.
CONFLICT 287 287 A -> V (in Ref. 2; AAL05976).
{ECO:0000305}.
CONFLICT 595 595 K -> E (in Ref. 1; AAF37272).
{ECO:0000305}.
SEQUENCE 798 AA; 88402 MW; FA6161FE3FFF2AA4 CRC64;
MEQRWGLLRR VQQWSPRPSQ TIYRRVEGPQ LEHLEEEDRE EGAELPAQFC PMELKGPEHL
GSCPGRSIPI PWAAAGRKAA PYLVLITLLI FTGAFLLGYV AFRGSCQACG DSVLVVDEDV
NPEDSGRTTL YWSDLQAMFL RFLGEGRMED TIRLTSLRER VAGSARMATL VQDILDKLSR
QKLDHVWTDT HYVGLQFPDP AHANTLHWVD ADGSVQEQLP LEDPEVYCPY SATGNATGKL
VYAHYGRSED LQDLKAKGVE LAGSLLLVRV GITSFAQKVA VAQDFGAQGV LIYPDPSDFS
QDPHKPGLSS HQAVYGHVHL GTGDPYTPGF PSFNQTQFPP VESSGLPSIP AQPISADIAD
QLLRKLTGPV APQEWKGHLS GSPYRLGPGP DLRLVVNNHR VSTPISNIFA CIEGFAEPDH
YVVIGAQRDA WGPGAAKSAV GTAILLELVR TFSSMVSNGF RPRRSLLFIS WDGGDFGSVG
ATEWLEGYLS VLHLKAVVYV SLDNSVLGDG KFHAKTSPLL VSLIENILKQ VDSPNHSGQT
LYEQVALTHP SWDAEVIQPL PMDSSAYSFT AFAGVPAVEF SFMEDDRVYP FLHTKEDTYE
NLHKMLRGRL PAVVQAVAQL AGQLLIRLSH DHLLPLDFGR YGDVVLRHIG NLNEFSGDLK
ERGLTLQWVY SARGDYIRAA EKLRKEIYSS ERNDERLMRM YNVRIMRVEF YFLSQYVSPA
DSPFRHIFLG QGDHTLGALV DHLRMLRADG SGAASSRLTA GLGFQESRFR RQLALLTWTL
QGAANALSGD VWNIDNNF


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