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Q9JKX3

- TFR2_MOUSE

UniProt

Q9JKX3 - TFR2_MOUSE

Protein

Transferrin receptor protein 2

Gene

Tfr2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (11 Feb 2002)
      Previous versions | rss
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    Functioni

    Mediates cellular uptake of transferrin-bound iron in a non-iron dependent manner. May be involved in iron metabolism, hepatocyte function and erythrocyte differentiation.

    GO - Molecular functioni

    1. peptidase activity Source: InterPro
    2. transferrin receptor activity Source: MGI

    GO - Biological processi

    1. cellular iron ion homeostasis Source: MGI
    2. receptor-mediated endocytosis Source: GOC

    Keywords - Molecular functioni

    Receptor

    Protein family/group databases

    MEROPSiM28.973.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transferrin receptor protein 2
    Short name:
    TfR2
    Gene namesi
    Name:Tfr2
    Synonyms:Trfr2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1354956. Tfr2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. integral component of membrane Source: MGI
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 798798Transferrin receptor protein 2PRO_0000174137Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi106 – 106InterchainSequence Analysis
    Disulfide bondi109 – 109InterchainSequence Analysis
    Glycosylationi235 – 2351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi535 – 5351N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ9JKX3.
    PaxDbiQ9JKX3.
    PRIDEiQ9JKX3.

    PTM databases

    PhosphoSiteiQ9JKX3.

    Expressioni

    Tissue specificityi

    Predominantly expressed in liver. Also expressed in kidney, spleen, brain, lung, heart and muscle with very low expression in kidney, muscle and heart.

    Developmental stagei

    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.

    Inductioni

    Down-regulated during erythrocyte differentiation. Expression unchanged by cellular iron status.

    Gene expression databases

    BgeeiQ9JKX3.
    CleanExiMM_TRFR2.
    GenevestigatoriQ9JKX3.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9JKX3. 2 interactions.
    MINTiMINT-1857634.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JKX3.
    SMRiQ9JKX3. Positions 130-798.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 8181CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini103 – 798696ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei82 – 10221Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi23 – 264Endocytosis signalSequence Analysis

    Sequence similaritiesi

    Belongs to the peptidase M28 family. M28B subfamily.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG74799.
    GeneTreeiENSGT00550000074421.
    HOGENOMiHOG000124067.
    HOVERGENiHBG023177.
    InParanoidiQ9JKX3.
    OMAiLFISWDG.
    OrthoDBiEOG780RKW.
    PhylomeDBiQ9JKX3.
    TreeFamiTF312981.

    Family and domain databases

    Gene3Di1.20.930.40. 1 hit.
    InterProiIPR007484. Peptidase_M28.
    IPR003137. Protease-assoc_domain.
    IPR007365. TFR-like_dimer_dom.
    [Graphical view]
    PfamiPF02225. PA. 1 hit.
    PF04389. Peptidase_M28. 1 hit.
    PF04253. TFR_dimer. 1 hit.
    [Graphical view]
    SUPFAMiSSF47672. SSF47672. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9JKX3-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEQRWGLLRR VQQWSPRPSQ TIYRRVEGPQ LEHLEEEDRE EGAELPAQFC    50
    PMELKGPEHL GSCPGRSIPI PWAAAGRKAA PYLVLITLLI FTGAFLLGYV 100
    AFRGSCQACG DSVLVVDEDV NPEDSGRTTL YWSDLQAMFL RFLGEGRMED 150
    TIRLTSLRER VAGSARMATL VQDILDKLSR QKLDHVWTDT HYVGLQFPDP 200
    AHANTLHWVD ADGSVQEQLP LEDPEVYCPY SATGNATGKL VYAHYGRSED 250
    LQDLKAKGVE LAGSLLLVRV GITSFAQKVA VAQDFGAQGV LIYPDPSDFS 300
    QDPHKPGLSS HQAVYGHVHL GTGDPYTPGF PSFNQTQFPP VESSGLPSIP 350
    AQPISADIAD QLLRKLTGPV APQEWKGHLS GSPYRLGPGP DLRLVVNNHR 400
    VSTPISNIFA CIEGFAEPDH YVVIGAQRDA WGPGAAKSAV GTAILLELVR 450
    TFSSMVSNGF RPRRSLLFIS WDGGDFGSVG ATEWLEGYLS VLHLKAVVYV 500
    SLDNSVLGDG KFHAKTSPLL VSLIENILKQ VDSPNHSGQT LYEQVALTHP 550
    SWDAEVIQPL PMDSSAYSFT AFAGVPAVEF SFMEDDRVYP FLHTKEDTYE 600
    NLHKMLRGRL PAVVQAVAQL AGQLLIRLSH DHLLPLDFGR YGDVVLRHIG 650
    NLNEFSGDLK ERGLTLQWVY SARGDYIRAA EKLRKEIYSS ERNDERLMRM 700
    YNVRIMRVEF YFLSQYVSPA DSPFRHIFLG QGDHTLGALV DHLRMLRADG 750
    SGAASSRLTA GLGFQESRFR RQLALLTWTL QGAANALSGD VWNIDNNF 798
    Length:798
    Mass (Da):88,402
    Last modified:February 11, 2002 - v2
    Checksum:iFA6161FE3FFF2AA4
    GO
    Isoform 2 (identifier: Q9JKX3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         237-237: T → TVRFPGWGAHHVLIG
         238-798: Missing.

    Note: Lacks most of the extracellular domain. No experimental confirmation available.

    Show »
    Length:251
    Mass (Da):28,167
    Checksum:i2A991D52876D5C18
    GO
    Isoform 3 (identifier: Q9JKX3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         12-93: Missing.

    Show »
    Length:716
    Mass (Da):79,255
    Checksum:iCFDA8CA8F8723197
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251R → P in AAL05977. (PubMed:11535534)Curated
    Sequence conflicti42 – 421G → V in AAL05977. (PubMed:11535534)Curated
    Sequence conflicti42 – 421G → V in AAK28830. (PubMed:11239002)Curated
    Sequence conflicti103 – 1031R → P in AAL05977. (PubMed:11535534)Curated
    Sequence conflicti151 – 1511T → N in AAH13654. (PubMed:15489334)Curated
    Sequence conflicti248 – 2481S → L in AAL05976. (PubMed:11535534)Curated
    Sequence conflicti287 – 2871A → V in AAL05976. (PubMed:11535534)Curated
    Sequence conflicti595 – 5951K → E in AAF37272. (PubMed:10681454)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei12 – 9382Missing in isoform 3. 1 PublicationVSP_005356Add
    BLAST
    Alternative sequencei237 – 2371T → TVRFPGWGAHHVLIG in isoform 2. 1 PublicationVSP_005357
    Alternative sequencei238 – 798561Missing in isoform 2. 1 PublicationVSP_005358Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF222895 mRNA. Translation: AAF37272.1.
    AF207741 mRNA. Translation: AAL05976.1.
    AF207742 Genomic DNA. Translation: AAL05977.1.
    AK004965 mRNA. Translation: BAB23705.1.
    AK004848 mRNA. Translation: BAB23614.1.
    BC013654 mRNA. Translation: AAH13654.1.
    AF312033 Genomic DNA. Translation: AAK28830.1.
    CCDSiCCDS39333.1. [Q9JKX3-1]
    RefSeqiNP_001276436.1. NM_001289507.1.
    NP_001276438.1. NM_001289509.1. [Q9JKX3-1]
    NP_001276440.1. NM_001289511.1. [Q9JKX3-1]
    NP_056614.3. NM_015799.4. [Q9JKX3-1]
    XP_006504656.1. XM_006504593.1. [Q9JKX3-1]
    XP_006504657.1. XM_006504594.1. [Q9JKX3-1]
    UniGeneiMm.21757.

    Genome annotation databases

    EnsembliENSMUST00000031729; ENSMUSP00000031729; ENSMUSG00000029716. [Q9JKX3-1]
    GeneIDi50765.
    KEGGimmu:50765.
    UCSCiuc009acv.1. mouse. [Q9JKX3-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF222895 mRNA. Translation: AAF37272.1 .
    AF207741 mRNA. Translation: AAL05976.1 .
    AF207742 Genomic DNA. Translation: AAL05977.1 .
    AK004965 mRNA. Translation: BAB23705.1 .
    AK004848 mRNA. Translation: BAB23614.1 .
    BC013654 mRNA. Translation: AAH13654.1 .
    AF312033 Genomic DNA. Translation: AAK28830.1 .
    CCDSi CCDS39333.1. [Q9JKX3-1 ]
    RefSeqi NP_001276436.1. NM_001289507.1.
    NP_001276438.1. NM_001289509.1. [Q9JKX3-1 ]
    NP_001276440.1. NM_001289511.1. [Q9JKX3-1 ]
    NP_056614.3. NM_015799.4. [Q9JKX3-1 ]
    XP_006504656.1. XM_006504593.1. [Q9JKX3-1 ]
    XP_006504657.1. XM_006504594.1. [Q9JKX3-1 ]
    UniGenei Mm.21757.

    3D structure databases

    ProteinModelPortali Q9JKX3.
    SMRi Q9JKX3. Positions 130-798.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9JKX3. 2 interactions.
    MINTi MINT-1857634.

    Protein family/group databases

    MEROPSi M28.973.

    PTM databases

    PhosphoSitei Q9JKX3.

    Proteomic databases

    MaxQBi Q9JKX3.
    PaxDbi Q9JKX3.
    PRIDEi Q9JKX3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031729 ; ENSMUSP00000031729 ; ENSMUSG00000029716 . [Q9JKX3-1 ]
    GeneIDi 50765.
    KEGGi mmu:50765.
    UCSCi uc009acv.1. mouse. [Q9JKX3-1 ]

    Organism-specific databases

    CTDi 7036.
    MGIi MGI:1354956. Tfr2.

    Phylogenomic databases

    eggNOGi NOG74799.
    GeneTreei ENSGT00550000074421.
    HOGENOMi HOG000124067.
    HOVERGENi HBG023177.
    InParanoidi Q9JKX3.
    OMAi LFISWDG.
    OrthoDBi EOG780RKW.
    PhylomeDBi Q9JKX3.
    TreeFami TF312981.

    Miscellaneous databases

    NextBioi 307667.
    PROi Q9JKX3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9JKX3.
    CleanExi MM_TRFR2.
    Genevestigatori Q9JKX3.

    Family and domain databases

    Gene3Di 1.20.930.40. 1 hit.
    InterProi IPR007484. Peptidase_M28.
    IPR003137. Protease-assoc_domain.
    IPR007365. TFR-like_dimer_dom.
    [Graphical view ]
    Pfami PF02225. PA. 1 hit.
    PF04389. Peptidase_M28. 1 hit.
    PF04253. TFR_dimer. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47672. SSF47672. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Transferrin receptor 2: continued expression in mouse liver in the face of iron overload and in hereditary hemochromatosis."
      Fleming R.E., Migas M.C., Holden C.C., Waheed A., Britton R.S., Tomatsu S., Bacon B.R., Sly W.S.
      Proc. Natl. Acad. Sci. U.S.A. 97:2214-2219(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Embryo.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Erythroleukemia.
    3. "The transcriptional landscape of the mammalian genome."
      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.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Liver.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver.
    5. "Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5."
      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.
      Nucleic Acids Res. 29:1352-1365(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-278.
      Strain: 129/Sv.

    Entry informationi

    Entry nameiTFR2_MOUSE
    AccessioniPrimary (citable) accession number: Q9JKX3
    Secondary accession number(s): Q920I6, Q99MQ9, Q9CPT2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 11, 2002
    Last sequence update: February 11, 2002
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3