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R-spondin-2 (Cysteine-rich and single thrombospondin domain-containing protein 2) (Cristin-2) (mCristin-2) (Roof plate-specific spondin-2)

 RSPO2_MOUSE             Reviewed;         243 AA.
Q8BFU0; Q7TPX3;
16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
23-MAY-2018, entry version 117.
RecName: Full=R-spondin-2;
AltName: Full=Cysteine-rich and single thrombospondin domain-containing protein 2;
Short=Cristin-2;
Short=mCristin-2;
AltName: Full=Roof plate-specific spondin-2;
Flags: Precursor;
Name=Rspo2;
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 [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Eye, and Hippocampus;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Egg;
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).
[3]
DEVELOPMENTAL STAGE.
PubMed=15469841; DOI=10.1016/j.devcel.2004.07.019;
Kazanskaya O., Glinka A., del Barco Barrantes I., Stannek P.,
Niehrs C., Wu W.;
"R-Spondin2 is a secreted activator of Wnt/beta-catenin signaling and
is required for Xenopus myogenesis.";
Dev. Cell 7:525-534(2004).
[4]
SUBCELLULAR LOCATION, HEPARIN-BINDING, AND INTERACTION WITH WNT1.
PubMed=16543246; DOI=10.1074/jbc.M508324200;
Nam J.-S., Turcotte T.J., Smith P.F., Choi S., Yoon J.K.;
"Mouse cristin/R-spondin family proteins are novel ligands for the
Frizzled 8 and LRP6 receptors and activate beta-catenin-dependent gene
expression.";
J. Biol. Chem. 281:13247-13257(2006).
[5]
FUNCTION, AND INTERACTION WITH LGR4 AND LGR5.
PubMed=21693646; DOI=10.1073/pnas.1106083108;
Carmon K.S., Gong X., Lin Q., Thomas A., Liu Q.;
"R-spondins function as ligands of the orphan receptors LGR4 and LGR5
to regulate Wnt/beta-catenin signaling.";
Proc. Natl. Acad. Sci. U.S.A. 108:11452-11457(2011).
-!- FUNCTION: 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. {ECO:0000269|PubMed:21693646}.
-!- SUBUNIT: Interacts with WNT1. Binds heparin. Interacts with LGR4,
LGR5 and LGR6. {ECO:0000269|PubMed:16543246,
ECO:0000269|PubMed:21693646}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16543246}.
-!- DEVELOPMENTAL STAGE: 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).
{ECO:0000269|PubMed:15469841}.
-!- DOMAIN: The FU repeat is required for activation and stabilization
of beta-catenin. {ECO:0000250}.
-!- SIMILARITY: Belongs to the R-spondin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BC052844; Type=Erroneous termination; Positions=153; Note=Translated as Trp.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK049891; BAC33974.1; -; mRNA.
EMBL; AK087485; BAC39893.1; -; mRNA.
EMBL; BC052844; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS27451.1; -.
RefSeq; NP_766403.1; NM_172815.3.
RefSeq; XP_006520968.1; XM_006520905.1.
UniGene; Mm.193274; -.
PDB; 4C99; X-ray; 2.80 A; B/D=37-144.
PDB; 4UFR; X-ray; 2.20 A; B/D=39-144.
PDB; 4UFS; X-ray; 4.80 A; B=39-144.
PDBsum; 4C99; -.
PDBsum; 4UFR; -.
PDBsum; 4UFS; -.
ProteinModelPortal; Q8BFU0; -.
SMR; Q8BFU0; -.
BioGrid; 232079; 3.
CORUM; Q8BFU0; -.
STRING; 10090.ENSMUSP00000067325; -.
iPTMnet; Q8BFU0; -.
PhosphoSitePlus; Q8BFU0; -.
PaxDb; Q8BFU0; -.
PeptideAtlas; Q8BFU0; -.
PRIDE; Q8BFU0; -.
DNASU; 239405; -.
Ensembl; ENSMUST00000063492; ENSMUSP00000067325; ENSMUSG00000051920.
Ensembl; ENSMUST00000226810; ENSMUSP00000154600; ENSMUSG00000051920.
GeneID; 239405; -.
KEGG; mmu:239405; -.
UCSC; uc007vpg.1; mouse.
CTD; 340419; -.
MGI; MGI:1922667; Rspo2.
eggNOG; ENOG410KCR4; Eukaryota.
eggNOG; ENOG410ZI6H; LUCA.
GeneTree; ENSGT00390000011447; -.
HOGENOM; HOG000290668; -.
HOVERGEN; HBG082751; -.
InParanoid; Q8BFU0; -.
OMA; DNGCIRC; -.
OrthoDB; EOG091G0FYC; -.
PhylomeDB; Q8BFU0; -.
TreeFam; TF331799; -.
Reactome; R-MMU-4641263; Regulation of FZD by ubiquitination.
PRO; PR:Q8BFU0; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000051920; -.
CleanEx; MM_RSPO2; -.
Genevisible; Q8BFU0; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005576; C:extracellular region; IDA:MGI.
GO; GO:0008201; F:heparin binding; IDA:MGI.
GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
GO; GO:0030282; P:bone mineralization; IGI:MGI.
GO; GO:0071542; P:dopaminergic neuron differentiation; IMP:MGI.
GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IMP:MGI.
GO; GO:0060437; P:lung growth; IMP:MGI.
GO; GO:0042489; P:negative regulation of odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0001649; P:osteoblast differentiation; IGI:MGI.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:MGI.
GO; GO:0060535; P:trachea cartilage morphogenesis; IGI:MGI.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
Gene3D; 2.20.100.10; -; 1.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
Pfam; PF15913; Furin-like_2; 1.
SMART; SM00261; FU; 2.
SMART; SM00209; TSP1; 1.
SUPFAM; SSF57184; SSF57184; 1.
SUPFAM; SSF82895; SSF82895; 1.
PROSITE; PS50092; TSP1; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
Heparin-binding; Reference proteome; Secreted; Sensory transduction;
Signal; Wnt signaling pathway.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 243 R-spondin-2.
/FTId=PRO_0000234440.
REPEAT 90 134 FU.
DOMAIN 144 204 TSP type-1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 40 46 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 43 52 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 55 74 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 78 93 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 96 104 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 101 110 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 113 124 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 128 141 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 145 187 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 156 163 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 196 203 {ECO:0000255|PROSITE-ProRule:PRU00210}.
STRAND 43 45 {ECO:0000244|PDB:4C99}.
STRAND 48 55 {ECO:0000244|PDB:4UFR}.
STRAND 59 65 {ECO:0000244|PDB:4UFR}.
STRAND 67 77 {ECO:0000244|PDB:4UFR}.
STRAND 82 87 {ECO:0000244|PDB:4UFR}.
STRAND 90 95 {ECO:0000244|PDB:4UFR}.
STRAND 101 106 {ECO:0000244|PDB:4UFR}.
STRAND 109 113 {ECO:0000244|PDB:4UFR}.
STRAND 118 120 {ECO:0000244|PDB:4UFR}.
STRAND 123 127 {ECO:0000244|PDB:4UFR}.
TURN 136 139 {ECO:0000244|PDB:4UFR}.
SEQUENCE 243 AA; 28276 MW; ED76A08D61012ED7 CRC64;
MRFCLFSFAL IILNCMDYSQ CQGNRWRRNK RASYVSNPIC KGCLSCSKDN GCSRCQQKLF
FFLRREGMRQ YGECLHSCPS GYYGHRAPDM NRCARCRIEN CDSCFSKDFC TKCKVGFYLH
RGRCFDECPD GFAPLDETME CVEGCEVGHW SEWGTCSRNN RTCGFKWGLE TRTRQIVKKP
AKDTIPCPTI AESRRCKMAM RHCPGGKRTP KAKEKRNKKK RRKLIERAQE QHSVFLATDR
VNQ


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