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R-spondin-4 (Roof plate-specific spondin-4) (hRspo4)

 RSPO4_HUMAN             Reviewed;         234 AA.
Q2I0M5; A2A2I6; Q9UGB2;
16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 2.
22-NOV-2017, entry version 110.
RecName: Full=R-spondin-4;
AltName: Full=Roof plate-specific spondin-4;
Short=hRspo4;
Flags: Precursor;
Name=RSPO4; Synonyms=C20orf182;
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 2), AND 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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Glial tumor;
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=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[5]
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).
[6]
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).
[7]
VARIANTS NDNC4 ARG-65; PHE-95; ARG-107 AND TYR-118.
PubMed=17041604; DOI=10.1038/ng1883;
Blaydon D.C., Ishii Y., O'Toole E.A., Unsworth H.C., Teh M.-T.,
Rueschendorf F., Sinclair C., Hopsu-Havu V.K., Tidman N., Moss C.,
Watson R., de Berker D., Wajid M., Christiano A.M., Kelsell D.P.;
"The gene encoding R-spondin 4 (RSPO4), a secreted protein implicated
in Wnt signaling, is mutated in inherited anonychia.";
Nat. Genet. 38:1245-1247(2006).
-!- 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. {ECO:0000269|PubMed:21727895,
ECO:0000269|PubMed:21909076}.
-!- SUBUNIT: Binds heparin (By similarity). Interacts with LGR4, LGR5
and LGR6. {ECO:0000250, ECO:0000269|PubMed:21727895,
ECO:0000269|PubMed:21909076}.
-!- INTERACTION:
Q9Y3S2:ZNF330; NbExp=4; IntAct=EBI-12821217, EBI-373456;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q2I0M5-1; Sequence=Displayed;
Name=2;
IsoId=Q2I0M5-2; Sequence=VSP_018325;
-!- DOMAIN: The FU repeat is required for activation and stabilization
of beta-catenin. {ECO:0000250}.
-!- PTM: Tyr-112 may be phosphorylated; however as this position is
probably extracellular, the vivo relevance is not proven.
-!- DISEASE: Nail disorder, non-syndromic congenital, 4 (NDNC4)
[MIM:206800]: A nail disorder characterized by congenital
anonychia or its milder phenotypic variant hyponychia.
Anonychia/hyponychia is the absence or severe hypoplasia of all
fingernails and toenails without significant bone anomalies.
{ECO:0000269|PubMed:17041604}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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; DQ355152; ABC75877.1; -; mRNA.
EMBL; AK122609; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AL050325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS42845.1; -. [Q2I0M5-2]
CCDS; CCDS42846.1; -. [Q2I0M5-1]
RefSeq; NP_001025042.2; NM_001029871.3. [Q2I0M5-1]
RefSeq; NP_001035096.1; NM_001040007.2. [Q2I0M5-2]
UniGene; Hs.444980; -.
ProteinModelPortal; Q2I0M5; -.
SMR; Q2I0M5; -.
BioGrid; 131268; 1.
IntAct; Q2I0M5; 14.
STRING; 9606.ENSP00000217260; -.
iPTMnet; Q2I0M5; -.
PhosphoSitePlus; Q2I0M5; -.
BioMuta; RSPO4; -.
DMDM; 97189858; -.
PaxDb; Q2I0M5; -.
PRIDE; Q2I0M5; -.
DNASU; 343637; -.
Ensembl; ENST00000217260; ENSP00000217260; ENSG00000101282. [Q2I0M5-1]
Ensembl; ENST00000400634; ENSP00000383475; ENSG00000101282. [Q2I0M5-2]
GeneID; 343637; -.
KEGG; hsa:343637; -.
UCSC; uc002wej.4; human. [Q2I0M5-1]
CTD; 343637; -.
DisGeNET; 343637; -.
EuPathDB; HostDB:ENSG00000101282.8; -.
GeneCards; RSPO4; -.
HGNC; HGNC:16175; RSPO4.
HPA; HPA048887; -.
MalaCards; RSPO4; -.
MIM; 206800; phenotype.
MIM; 610573; gene.
neXtProt; NX_Q2I0M5; -.
OpenTargets; ENSG00000101282; -.
Orphanet; 79143; Congenital anonychia.
PharmGKB; PA25726; -.
eggNOG; KOG3525; Eukaryota.
eggNOG; COG1404; LUCA.
GeneTree; ENSGT00390000011447; -.
HOGENOM; HOG000290668; -.
HOVERGEN; HBG082751; -.
InParanoid; Q2I0M5; -.
OMA; RPCPGER; -.
OrthoDB; EOG091G0FYC; -.
PhylomeDB; Q2I0M5; -.
TreeFam; TF331799; -.
Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
GenomeRNAi; 343637; -.
PRO; PR:Q2I0M5; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101282; -.
CleanEx; HS_RSPO4; -.
Genevisible; Q2I0M5; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0035878; P:nail development; IMP:MGI.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; NAS:ParkinsonsUK-UCL.
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.
Pfam; PF15913; Furin-like_2; 1.
SMART; SM00261; FU; 2.
SMART; SM00209; TSP1; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS50092; TSP1; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disease mutation;
Disulfide bond; Glycoprotein; Heparin-binding; Phosphoprotein;
Polymorphism; Reference proteome; Secreted; Sensory transduction;
Signal; Wnt signaling pathway.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 234 R-spondin-4.
/FTId=PRO_0000234446.
REPEAT 85 128 FU.
DOMAIN 138 197 TSP type-1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
CARBOHYD 34 34 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 35 41 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 38 47 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 50 69 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 73 88 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 91 98 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 95 104 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 107 118 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 122 135 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 139 181 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 150 157 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 190 196 {ECO:0000255|PROSITE-ProRule:PRU00210}.
VAR_SEQ 137 198 Missing (in isoform 2).
{ECO:0000303|PubMed:16357527}.
/FTId=VSP_018325.
VARIANT 65 65 Q -> R (in NDNC4; dbSNP:rs74315420).
{ECO:0000269|PubMed:17041604}.
/FTId=VAR_030399.
VARIANT 95 95 C -> F (in NDNC4; dbSNP:rs780506366).
{ECO:0000269|PubMed:17041604}.
/FTId=VAR_030400.
VARIANT 106 106 R -> Q (in dbSNP:rs6140807).
/FTId=VAR_052665.
VARIANT 107 107 C -> R (in NDNC4; dbSNP:rs74315421).
{ECO:0000269|PubMed:17041604}.
/FTId=VAR_030401.
VARIANT 118 118 C -> Y (in NDNC4; dbSNP:rs74315422).
{ECO:0000269|PubMed:17041604}.
/FTId=VAR_030402.
SEQUENCE 234 AA; 26171 MW; 853E4494533B73F7 CRC64;
MRAPLCLLLL VAHAVDMLAL NRRKKQVGTG LGGNCTGCII CSEENGCSTC QQRLFLFIRR
EGIRQYGKCL HDCPPGYFGI RGQEVNRCKK CGATCESCFS QDFCIRCKRQ FYLYKGKCLP
TCPPGTLAHQ NTRECQGECE LGPWGGWSPC THNGKTCGSA WGLESRVREA GRAGHEEAAT
CQVLSESRKC PIQRPCPGER SPGQKKGRKD RRPRKDRKLD RRLDVRPRQP GLQP


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