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R-spondin-3 (Protein with TSP type-1 repeat) (hPWTSR) (Roof plate-specific spondin-3) (hRspo3) (Thrombospondin type-1 domain-containing protein 2)

 RSPO3_HUMAN             Reviewed;         272 AA.
Q9BXY4; B2RC27; Q5VTV4; Q96K87;
16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
22-NOV-2017, entry version 131.
RecName: Full=R-spondin-3;
AltName: Full=Protein with TSP type-1 repeat;
Short=hPWTSR;
AltName: Full=Roof plate-specific spondin-3;
Short=hRspo3;
AltName: Full=Thrombospondin type-1 domain-containing protein 2;
Flags: Precursor;
Name=RSPO3; Synonyms=PWTSR, THSD2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=12463421; DOI=10.1023/A:1020479301379;
Chen J.-Z., Wang S., Tang R., Yang Q.-S., Zhao E., Chao Y., Ying K.,
Xie Y., Mao Y.-M.;
"Cloning and identification of a cDNA that encodes a novel human
protein with thrombospondin type I repeat domain, hPWTSR.";
Mol. Biol. Rep. 29:287-292(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Amygdala, and Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[6]
INJECTION INTO MICE.
PubMed=16357527; DOI=10.4161/cc.5.1.2305;
Kim K.-A., Zhao J., Andarmani S., Kakitani M., Oshima T.,
Binnerts M.E., Abo A., Tomizuka K., Funk W.D.;
"R-spondin proteins: a novel link to beta-catenin activation.";
Cell Cycle 5:23-26(2006).
[7]
FUNCTION, AND INTERACTION WITH LGR4 AND LGR5.
PubMed=21909076; DOI=10.1038/embor.2011.175;
Glinka A., Dolde C., Kirsch N., Huang Y.L., Kazanskaya O.,
Ingelfinger D., Boutros M., Cruciat C.M., Niehrs C.;
"LGR4 and LGR5 are R-spondin receptors mediating Wnt/beta-catenin and
Wnt/PCP signalling.";
EMBO Rep. 12:1055-1061(2011).
[8]
FUNCTION, AND INTERACTION WITH LGR4; LGR5 AND LGR6.
PubMed=21727895; DOI=10.1038/nature10337;
de Lau W., Barker N., Low T.Y., Koo B.K., Li V.S., Teunissen H.,
Kujala P., Haegebarth A., Peters P.J., van de Wetering M.,
Stange D.E., van Es J.E., Guardavaccaro D., Schasfoort R.B., Mohri Y.,
Nishimori K., Mohammed S., Heck A.J., Clevers H.;
"Lgr5 homologues associate with Wnt receptors and mediate R-spondin
signalling.";
Nature 476:293-297(2011).
[9]
FUNCTION, AND INTERACTION WITH LGR6.
PubMed=22615920; DOI=10.1371/journal.pone.0037137;
Gong X., Carmon K.S., Lin Q., Thomas A., Yi J., Liu Q.;
"LGR6 is a high affinity receptor of R-spondins and potentially
functions as a tumor suppressor.";
PLoS ONE 7:E37137-E37137(2012).
[10]
TISSUE SPECIFICITY.
PubMed=26766444; DOI=10.1016/j.devcel.2015.12.015;
Scholz B., Korn C., Wojtarowicz J., Mogler C., Augustin I.,
Boutros M., Niehrs C., Augustin H.G.;
"Endothelial RSPO3 controls vascular stability and pruning through
non-canonical WNT/Ca(2+)/NFAT signaling.";
Dev. Cell 36:79-93(2016).
-!- FUNCTION: Activator of the canonical Wnt signaling pathway by
acting as a ligand for LGR4-6 receptors, which acts as a key
regulator of angiogenesis. 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. Acts as a ligand for frizzled FZD8 and LRP6.
May negatively regulate the TGF-beta pathway (PubMed:21727895,
PubMed:21909076, PubMed:22615920). Acts as a key regulator of
angiogenesis by controlling vascular stability and pruning: acts
by activating the non-canonical Wnt signaling pathway in
endothelial cells (By similarity). {ECO:0000250|UniProtKB:Q2TJ95,
ECO:0000269|PubMed:21727895, ECO:0000269|PubMed:21909076,
ECO:0000269|PubMed:22615920}.
-!- SUBUNIT: Interacts with the extracellular domain of FZD8 and LRP6
(By similarity). It however does not form a ternary complex with
FZD8 and LRP6 (By similarity). Interacts with WNT1 (By
similarity). Binds heparin. Interacts with LGR4, LGR5 and LGR6
(PubMed:21727895, PubMed:21909076, PubMed:22615920).
{ECO:0000250|UniProtKB:Q2TJ95, ECO:0000269|PubMed:21727895,
ECO:0000269|PubMed:21909076, ECO:0000269|PubMed:22615920}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q2TJ95}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BXY4-1; Sequence=Displayed;
Name=2;
IsoId=Q9BXY4-2; Sequence=VSP_018324;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at higher
level in placenta, small intestine, fetal thymus and lymph node
(PubMed:12463421). Highly expressed in endothelial cells
(PubMed:26766444). {ECO:0000269|PubMed:12463421,
ECO:0000269|PubMed:26766444}.
-!- DOMAIN: The FU repeats are required for activation and
stabilization of beta-catenin. {ECO:0000250|UniProtKB:Q2TJ95}.
-!- MISCELLANEOUS: Upon injection into mice, it induces rapid onset of
crypt cell proliferation involving beta-catenin stabilization. It
also displays efficacy in a model of chemotherapy-induced
intestinal mucositis (PubMed:16357527).
{ECO:0000305|PubMed:16357527}.
-!- SIMILARITY: Belongs to the R-spondin family. {ECO:0000305}.
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EMBL; AF251057; AAK34947.1; -; mRNA.
EMBL; AK027346; BAB55051.1; -; mRNA.
EMBL; AK314912; BAG37424.1; -; mRNA.
EMBL; AL590733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL031776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48115.1; -; Genomic_DNA.
EMBL; BC022367; AAH22367.1; -; mRNA.
CCDS; CCDS5135.1; -. [Q9BXY4-1]
RefSeq; NP_116173.2; NM_032784.4. [Q9BXY4-1]
UniGene; Hs.135254; -.
ProteinModelPortal; Q9BXY4; -.
SMR; Q9BXY4; -.
BioGrid; 124315; 3.
IntAct; Q9BXY4; 2.
MINT; MINT-8297608; -.
STRING; 9606.ENSP00000349131; -.
iPTMnet; Q9BXY4; -.
PhosphoSitePlus; Q9BXY4; -.
DMDM; 74752442; -.
PaxDb; Q9BXY4; -.
PeptideAtlas; Q9BXY4; -.
PRIDE; Q9BXY4; -.
DNASU; 84870; -.
Ensembl; ENST00000356698; ENSP00000349131; ENSG00000146374. [Q9BXY4-1]
Ensembl; ENST00000368317; ENSP00000357300; ENSG00000146374. [Q9BXY4-2]
GeneID; 84870; -.
KEGG; hsa:84870; -.
UCSC; uc003qar.5; human. [Q9BXY4-1]
CTD; 84870; -.
DisGeNET; 84870; -.
EuPathDB; HostDB:ENSG00000146374.13; -.
GeneCards; RSPO3; -.
HGNC; HGNC:20866; RSPO3.
HPA; HPA029957; -.
MIM; 610574; gene.
neXtProt; NX_Q9BXY4; -.
OpenTargets; ENSG00000146374; -.
PharmGKB; PA134885289; -.
eggNOG; KOG3525; Eukaryota.
eggNOG; COG1404; LUCA.
GeneTree; ENSGT00390000011447; -.
HOGENOM; HOG000290668; -.
HOVERGEN; HBG082751; -.
InParanoid; Q9BXY4; -.
OMA; MECTSIV; -.
OrthoDB; EOG091G0FYC; -.
PhylomeDB; Q9BXY4; -.
TreeFam; TF331799; -.
Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
Reactome; R-HSA-8939256; RUNX1 regulates transcription of genes involved in WNT signaling.
SIGNOR; Q9BXY4; -.
GeneWiki; RSPO3; -.
GenomeRNAi; 84870; -.
PRO; PR:Q9BXY4; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000146374; -.
CleanEx; HS_RSPO3; -.
Genevisible; Q9BXY4; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005109; F:frizzled binding; IEA:Ensembl.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0001974; P:blood vessel remodeling; ISS:UniProtKB.
GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IEA:Ensembl.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; NAS:ParkinsonsUK-UCL.
GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; TAS:ParkinsonsUK-UCL.
GO; GO:0030111; P:regulation of Wnt signaling pathway; TAS:Reactome.
GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Heparin-binding; Reference proteome; Repeat; Secreted;
Sensory transduction; Signal; Wnt signaling pathway.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 272 R-spondin-3.
/FTId=PRO_0000234443.
REPEAT 35 86 FU 1.
REPEAT 92 135 FU 2.
DOMAIN 147 207 TSP type-1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
CARBOHYD 36 36 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 48 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 45 54 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 57 76 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 80 95 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 98 105 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 102 111 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 114 125 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 129 142 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 148 190 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 159 166 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 199 206 {ECO:0000255|PROSITE-ProRule:PRU00210}.
VAR_SEQ 266 272 VSVSTVH -> GIEVTLAEGLTSVSQRTQPTPCRRRYL
(in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_018324.
CONFLICT 41 41 C -> R (in Ref. 2; BAB55051).
{ECO:0000305}.
CONFLICT 170 170 R -> I (in Ref. 2; BAB55051).
{ECO:0000305}.
SEQUENCE 272 AA; 30929 MW; CACAEC6B7E781189 CRC64;
MHLRLISWLF IILNFMEYIG SQNASRGRRQ RRMHPNVSQG CQGGCATCSD YNGCLSCKPR
LFFALERIGM KQIGVCLSSC PSGYYGTRYP DINKCTKCKA DCDTCFNKNF CTKCKSGFYL
HLGKCLDNCP EGLEANNHTM ECVSIVHCEV SEWNPWSPCT KKGKTCGFKR GTETRVREII
QHPSAKGNLC PPTNETRKCT VQRKKCQKGE RGKKGRERKR KKPNKGESKE AIPDSKSLES
SKEIPEQREN KQQQKKRKVQ DKQKSVSVST VH


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