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Q8BFU0

- RSPO2_MOUSE

UniProt

Q8BFU0 - RSPO2_MOUSE

Protein

R-spondin-2

Gene

Rspo2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Probably also acts as a ligand for frizzled and LRP receptors.1 Publication

    GO - Molecular functioni

    1. heparin binding Source: MGI

    GO - Biological processi

    1. bone mineralization Source: MGI
    2. embryonic forelimb morphogenesis Source: MGI
    3. embryonic hindlimb morphogenesis Source: MGI
    4. epithelial tube branching involved in lung morphogenesis Source: MGI
    5. lung growth Source: MGI
    6. osteoblast differentiation Source: MGI
    7. positive regulation of canonical Wnt signaling pathway Source: MGI
    8. trachea cartilage morphogenesis Source: MGI
    9. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Biological processi

    Sensory transduction, Wnt signaling pathway

    Keywords - Ligandi

    Heparin-binding

    Enzyme and pathway databases

    ReactomeiREACT_213035. regulation of FZD by ubiquitination.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    R-spondin-2
    Alternative name(s):
    Cysteine-rich and single thrombospondin domain-containing protein 2
    Short name:
    Cristin-2
    Short name:
    mCristin-2
    Roof plate-specific spondin-2
    Gene namesi
    Name:Rspo2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1922667. Rspo2.

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. cell surface Source: MGI
    2. extracellular region Source: MGI

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 243220R-spondin-2PRO_0000234440Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi40 ↔ 46PROSITE-ProRule annotation
    Disulfide bondi43 ↔ 52PROSITE-ProRule annotation
    Disulfide bondi55 ↔ 74PROSITE-ProRule annotation
    Disulfide bondi78 ↔ 93PROSITE-ProRule annotation
    Disulfide bondi96 ↔ 104PROSITE-ProRule annotation
    Disulfide bondi101 ↔ 110PROSITE-ProRule annotation
    Disulfide bondi113 ↔ 124PROSITE-ProRule annotation
    Disulfide bondi128 ↔ 141PROSITE-ProRule annotation
    Disulfide bondi145 ↔ 187PROSITE-ProRule annotation
    Disulfide bondi156 ↔ 163PROSITE-ProRule annotation
    Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi196 ↔ 203PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ8BFU0.

    PTM databases

    PhosphoSiteiQ8BFU0.

    Expressioni

    Developmental stagei

    Detected from day 9.5 in various neural and mesodermal derivatives, mainly along diencephalon. Strongly expressed in limb buds, particularly in the morphogenetically active region such as the apical ectodermal ridge (AER).1 Publication

    Gene expression databases

    BgeeiQ8BFU0.
    CleanExiMM_RSPO2.
    GenevestigatoriQ8BFU0.

    Interactioni

    Subunit structurei

    Interacts with WNT1. Binds heparin. Interacts with LGR4, LGR5 and LGR6.2 Publications

    Protein-protein interaction databases

    BioGridi232079. 2 interactions.

    Structurei

    Secondary structure

    1
    243
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi43 – 453
    Turni48 – 503
    Beta strandi51 – 555
    Beta strandi59 – 668
    Beta strandi69 – 779
    Beta strandi105 – 1084
    Beta strandi118 – 1203
    Beta strandi123 – 1275
    Turni136 – 1383

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4C99X-ray2.80B/D37-144[»]
    ProteinModelPortaliQ8BFU0.
    SMRiQ8BFU0. Positions 39-143.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati90 – 13445FUAdd
    BLAST
    Domaini144 – 20461TSP type-1PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The FU repeat is required for activation and stabilization of beta-catenin.By similarity

    Sequence similaritiesi

    Belongs to the R-spondin family.Curated
    Contains 1 FU (furin-like) repeat.Curated
    Contains 1 TSP type-1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG285562.
    GeneTreeiENSGT00390000011447.
    HOGENOMiHOG000290668.
    HOVERGENiHBG082751.
    InParanoidiQ8BFU0.
    OMAiDNGCIRC.
    OrthoDBiEOG7X9G7G.
    PhylomeDBiQ8BFU0.
    TreeFamiTF331799.

    Family and domain databases

    InterProiIPR006212. Furin_repeat.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    SMARTiSM00261. FU. 2 hits.
    SM00209. TSP1. 1 hit.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 1 hit.
    SSF82895. SSF82895. 1 hit.
    PROSITEiPS50092. TSP1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8BFU0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRFCLFSFAL IILNCMDYSQ CQGNRWRRNK RASYVSNPIC KGCLSCSKDN    50
    GCSRCQQKLF FFLRREGMRQ YGECLHSCPS GYYGHRAPDM NRCARCRIEN 100
    CDSCFSKDFC TKCKVGFYLH RGRCFDECPD GFAPLDETME CVEGCEVGHW 150
    SEWGTCSRNN RTCGFKWGLE TRTRQIVKKP AKDTIPCPTI AESRRCKMAM 200
    RHCPGGKRTP KAKEKRNKKK RRKLIERAQE QHSVFLATDR VNQ 243
    Length:243
    Mass (Da):28,276
    Last modified:March 1, 2003 - v1
    Checksum:iED76A08D61012ED7
    GO

    Sequence cautioni

    The sequence BC052844 differs from that shown. Reason: Erroneous termination at position 153. Translated as Trp.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK049891 mRNA. Translation: BAC33974.1.
    AK087485 mRNA. Translation: BAC39893.1.
    BC052844 mRNA. No translation available.
    CCDSiCCDS27451.1.
    RefSeqiNP_766403.1. NM_172815.3.
    XP_006520968.1. XM_006520905.1.
    UniGeneiMm.193274.

    Genome annotation databases

    EnsembliENSMUST00000063492; ENSMUSP00000067325; ENSMUSG00000051920.
    GeneIDi239405.
    KEGGimmu:239405.
    UCSCiuc007vpg.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK049891 mRNA. Translation: BAC33974.1 .
    AK087485 mRNA. Translation: BAC39893.1 .
    BC052844 mRNA. No translation available.
    CCDSi CCDS27451.1.
    RefSeqi NP_766403.1. NM_172815.3.
    XP_006520968.1. XM_006520905.1.
    UniGenei Mm.193274.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4C99 X-ray 2.80 B/D 37-144 [» ]
    ProteinModelPortali Q8BFU0.
    SMRi Q8BFU0. Positions 39-143.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 232079. 2 interactions.

    PTM databases

    PhosphoSitei Q8BFU0.

    Proteomic databases

    PRIDEi Q8BFU0.

    Protocols and materials databases

    DNASUi 239405.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000063492 ; ENSMUSP00000067325 ; ENSMUSG00000051920 .
    GeneIDi 239405.
    KEGGi mmu:239405.
    UCSCi uc007vpg.1. mouse.

    Organism-specific databases

    CTDi 340419.
    MGIi MGI:1922667. Rspo2.

    Phylogenomic databases

    eggNOGi NOG285562.
    GeneTreei ENSGT00390000011447.
    HOGENOMi HOG000290668.
    HOVERGENi HBG082751.
    InParanoidi Q8BFU0.
    OMAi DNGCIRC.
    OrthoDBi EOG7X9G7G.
    PhylomeDBi Q8BFU0.
    TreeFami TF331799.

    Enzyme and pathway databases

    Reactomei REACT_213035. regulation of FZD by ubiquitination.

    Miscellaneous databases

    NextBioi 384105.
    PROi Q8BFU0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BFU0.
    CleanExi MM_RSPO2.
    Genevestigatori Q8BFU0.

    Family and domain databases

    InterProi IPR006212. Furin_repeat.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view ]
    SMARTi SM00261. FU. 2 hits.
    SM00209. TSP1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 1 hit.
    SSF82895. SSF82895. 1 hit.
    PROSITEi PS50092. TSP1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: Eye and Hippocampus.
    2. "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: C57BL/6J.
      Tissue: Egg.
    3. "R-Spondin2 is a secreted activator of Wnt/beta-catenin signaling and is required for Xenopus myogenesis."
      Kazanskaya O., Glinka A., del Barco Barrantes I., Stannek P., Niehrs C., Wu W.
      Dev. Cell 7:525-534(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    4. "Mouse cristin/R-spondin family proteins are novel ligands for the Frizzled 8 and LRP6 receptors and activate beta-catenin-dependent gene expression."
      Nam J.-S., Turcotte T.J., Smith P.F., Choi S., Yoon J.K.
      J. Biol. Chem. 281:13247-13257(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, HEPARIN-BINDING, INTERACTION WITH WNT1.
    5. "R-spondins function as ligands of the orphan receptors LGR4 and LGR5 to regulate Wnt/beta-catenin signaling."
      Carmon K.S., Gong X., Lin Q., Thomas A., Liu Q.
      Proc. Natl. Acad. Sci. U.S.A. 108:11452-11457(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LGR4 AND LGR5.

    Entry informationi

    Entry nameiRSPO2_MOUSE
    AccessioniPrimary (citable) accession number: Q8BFU0
    Secondary accession number(s): Q7TPX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2006
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3