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Q9Z0L0

- TPBG_MOUSE

UniProt

Q9Z0L0 - TPBG_MOUSE

Protein

Trophoblast glycoprotein

Gene

Tpbg

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    May function as an inhibitor of Wnt/beta-catenin signaling by indirectly interacting with LRP6 and blocking Wnt3a-dependent LRP6 internalization.By similarity

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trophoblast glycoprotein
    Alternative name(s):
    5T4 oncofetal trophoblast glycoprotein
    Short name:
    5T4 oncotrophoblast glycoprotein
    Wnt-activated inhibitory factor 1
    Short name:
    WAIF1
    Gene namesi
    Name:Tpbg
    Synonyms:5t4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1341264. Tpbg.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 426395Trophoblast glycoproteinPRO_0000019593Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi62 ↔ 68By similarity
    Disulfide bondi66 ↔ 77By similarity
    Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi281 – 2811N-linked (GlcNAc...)1 Publication
    Disulfide bondi304 ↔ 329By similarity
    Disulfide bondi306 ↔ 350By similarity

    Post-translational modificationi

    Highly glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9Z0L0.
    PRIDEiQ9Z0L0.

    PTM databases

    PhosphoSiteiQ9Z0L0.

    Expressioni

    Tissue specificityi

    Highly expressed in embryo and placenta. In adult, expressed only in brain and ovary. Not detected in kidney small intestine, heart, spleen, testis, liver, lung, thymus and stomach.1 Publication

    Gene expression databases

    ArrayExpressiQ9Z0L0.
    BgeeiQ9Z0L0.
    CleanExiMM_TPBG.
    GenevestigatoriQ9Z0L0.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z0L0.
    SMRiQ9Z0L0. Positions 59-350.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 361330ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini383 – 42644CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei362 – 38221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 9139LRRNTAdd
    BLAST
    Repeati92 – 11322LRR 1Add
    BLAST
    Repeati116 – 13924LRR 2Add
    BLAST
    Repeati141 – 16323LRR 3Add
    BLAST
    Repeati172 – 21039LRR 4Add
    BLAST
    Repeati215 – 23824LRR 5Add
    BLAST
    Repeati239 – 26123LRR 6Add
    BLAST
    Repeati262 – 28120LRR 7Add
    BLAST
    Domaini289 – 35264LRRCTAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi32 – 5322Ser-richAdd
    BLAST

    Domaini

    The C-terminus of LRR N-terminal cap (LRRNT) and LRR 1 are essential for the inhibition of the Wnt signaling pathway.By similarity

    Sequence similaritiesi

    Contains 7 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRCT domain.Curated
    Contains 1 LRRNT domain.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG301461.
    GeneTreeiENSGT00620000088023.
    HOGENOMiHOG000013090.
    HOVERGENiHBG053843.
    InParanoidiQ3UPI2.
    OMAiSFRNLTH.
    OrthoDBiEOG7QNVM8.
    TreeFamiTF351115.

    Family and domain databases

    InterProiIPR000483. Cys-rich_flank_reg_C.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    [Graphical view]
    PfamiPF13855. LRR_8. 2 hits.
    PF01462. LRRNT. 1 hit.
    [Graphical view]
    SMARTiSM00369. LRR_TYP. 3 hits.
    SM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view]
    PROSITEiPS51450. LRR. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9Z0L0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGAGSRGPS AGDGRLRLAR LALVLLGWVS ASAPSSSVPS SSTSPAAFLA    50
    SGSAQPPPAE RCPAACECSE AARTVKCVNR NLLEVPADLP PYVRNLFLTG 100
    NQMTVLPAGA FARQPPLADL EALNLSGNHL KEVCAGAFEH LPGLRRLDLS 150
    HNPLTNLSAF AFAGSNASVS APSPLEELIL NHIVPPEDQR QNGSFEGMVA 200
    FEGMVAAALR SGLALRGLTR LELASNHFLF LPRDLLAQLP SLRYLDLRNN 250
    SLVSLTYASF RNLTHLESLH LEDNALKVLH NSTLAEWHGL AHVKVFLDNN 300
    PWVCDCYMAD MVAWLKETEV VPDKARLTCA FPEKMRNRGL LDLNSSDLDC 350
    DAVLPQSLQT SYVFLGIVLA LIGAIFLLVL YLNRKGIKKW MHNIRDACRD 400
    HMEGYHYRYE INADPRLTNL SSNSDV 426
    Length:426
    Mass (Da):46,451
    Last modified:July 27, 2011 - v3
    Checksum:iA03A76377F68D2A4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti47 – 471A → D in CAA09931. (PubMed:10366710)Curated
    Sequence conflicti161 – 1611A → V in CAA09931. (PubMed:10366710)Curated
    Sequence conflicti220 – 2201R → C in AAH58198. (PubMed:15489334)Curated
    Sequence conflicti288 – 2881H → Q in CAA09931. (PubMed:10366710)Curated
    Sequence conflicti288 – 2881H → Q in AAH58198. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ012160 Genomic DNA. Translation: CAA09931.1.
    AK051162 mRNA. Translation: BAC34540.1.
    AK143519 mRNA. Translation: BAE25413.1.
    BC058198 mRNA. Translation: AAH58198.1.
    CCDSiCCDS23380.1.
    RefSeqiNP_001158264.1. NM_001164792.1.
    NP_035757.2. NM_011627.4.
    UniGeneiMm.20864.
    Mm.484180.

    Genome annotation databases

    EnsembliENSMUST00000006559; ENSMUSP00000006559; ENSMUSG00000035274.
    ENSMUST00000098500; ENSMUSP00000096101; ENSMUSG00000035274.
    GeneIDi21983.
    KEGGimmu:21983.
    UCSCiuc009qwz.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ012160 Genomic DNA. Translation: CAA09931.1 .
    AK051162 mRNA. Translation: BAC34540.1 .
    AK143519 mRNA. Translation: BAE25413.1 .
    BC058198 mRNA. Translation: AAH58198.1 .
    CCDSi CCDS23380.1.
    RefSeqi NP_001158264.1. NM_001164792.1.
    NP_035757.2. NM_011627.4.
    UniGenei Mm.20864.
    Mm.484180.

    3D structure databases

    ProteinModelPortali Q9Z0L0.
    SMRi Q9Z0L0. Positions 59-350.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9Z0L0.

    Proteomic databases

    PaxDbi Q9Z0L0.
    PRIDEi Q9Z0L0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000006559 ; ENSMUSP00000006559 ; ENSMUSG00000035274 .
    ENSMUST00000098500 ; ENSMUSP00000096101 ; ENSMUSG00000035274 .
    GeneIDi 21983.
    KEGGi mmu:21983.
    UCSCi uc009qwz.2. mouse.

    Organism-specific databases

    CTDi 7162.
    MGIi MGI:1341264. Tpbg.

    Phylogenomic databases

    eggNOGi NOG301461.
    GeneTreei ENSGT00620000088023.
    HOGENOMi HOG000013090.
    HOVERGENi HBG053843.
    InParanoidi Q3UPI2.
    OMAi SFRNLTH.
    OrthoDBi EOG7QNVM8.
    TreeFami TF351115.

    Miscellaneous databases

    NextBioi 301700.
    PROi Q9Z0L0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z0L0.
    Bgeei Q9Z0L0.
    CleanExi MM_TPBG.
    Genevestigatori Q9Z0L0.

    Family and domain databases

    InterProi IPR000483. Cys-rich_flank_reg_C.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    [Graphical view ]
    Pfami PF13855. LRR_8. 2 hits.
    PF01462. LRRNT. 1 hit.
    [Graphical view ]
    SMARTi SM00369. LRR_TYP. 3 hits.
    SM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Organisation of the mouse and human 5T4 oncofetal leucine-rich glycoprotein gene and expression in foetal and adult murine tissues."
      King K.W., Sheppard F.C., Westwater C., Stern P.L., Myers K.A.
      Biochim. Biophys. Acta 1445:257-270(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
      Strain: 129/Sv.
    2. "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].
      Strain: C57BL/6J.
      Tissue: Spinal ganglion.
    3. "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].
      Strain: FVB/N.
      Tissue: Mammary gland.
    4. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-281.

    Entry informationi

    Entry nameiTPBG_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z0L0
    Secondary accession number(s): Q3UPI2, Q6PE98, Q8BQA4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 107 of the entry and version 3 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3