ID   RSPO1_DANRE             Reviewed;         261 AA.
AC   Q6DHR0;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=R-spondin-1;
DE   AltName: Full=Roof plate-specific spondin-1;
DE   Flags: Precursor;
GN   Name=rspo1; ORFNames=zgc:92153;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Activator of the canonical Wnt signaling pathway by acting as
CC       a ligand for lgr4-6 receptors. Upon binding to lgr4-6 (lgr4, lgr5 or
CC       lgr6), lgr4-6 associate with phosphorylated lrp6 and frizzled receptors
CC       that are activated by extracellular Wnt receptors, triggering the
CC       canonical Wnt signaling pathway to increase expression of target genes.
CC       Acts both in the canonical Wnt/beta-catenin-dependent pathway and in
CC       non-canonical Wnt signaling pathway (By similarity).
CC       {ECO:0000250|UniProtKB:Q2MKA7}.
CC   -!- SUBUNIT: Binds heparin. {ECO:0000250|UniProtKB:Q9Z132}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9Z132}.
CC   -!- DOMAIN: The FU repeats are required for activation and stabilization of
CC       beta-catenin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the R-spondin family. {ECO:0000305}.
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DR   EMBL; BC075907; AAH75907.1; -; mRNA.
DR   RefSeq; NP_001002352.1; NM_001002352.1.
DR   AlphaFoldDB; Q6DHR0; -.
DR   SMR; Q6DHR0; -.
DR   STRING; 7955.ENSDARP00000058458; -.
DR   PaxDb; Q6DHR0; -.
DR   Ensembl; ENSDART00000160671; ENSDARP00000135809; ENSDARG00000104340.
DR   Ensembl; ENSDART00000181769; ENSDARP00000149963; ENSDARG00000104340.
DR   Ensembl; ENSDART00000182147; ENSDARP00000154153; ENSDARG00000111655.
DR   Ensembl; ENSDART00000188395; ENSDARP00000151422; ENSDARG00000104340.
DR   GeneID; 436625; -.
DR   KEGG; dre:436625; -.
DR   CTD; 284654; -.
DR   ZFIN; ZDB-GENE-040718-44; rspo1.
DR   eggNOG; KOG3525; Eukaryota.
DR   GeneTree; ENSGT00940000158871; -.
DR   HOGENOM; CLU_064219_0_1_1; -.
DR   InParanoid; Q6DHR0; -.
DR   OMA; CREGLYL; -.
DR   OrthoDB; 1441603at2759; -.
DR   PhylomeDB; Q6DHR0; -.
DR   TreeFam; TF331799; -.
DR   Reactome; R-DRE-4641263; Regulation of FZD by ubiquitination.
DR   PRO; PR:Q6DHR0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 16.
DR   Bgee; ENSDARG00000104340; Expressed in pharyngeal gill and 16 other tissues.
DR   ExpressionAtlas; Q6DHR0; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:ZFIN.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:ZFIN.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; IMP:ZFIN.
DR   GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:ZFIN.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IGI:ZFIN.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd00064; FU; 1.
DR   Gene3D; 2.20.100.10; -; 1.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR042991; RSPO1.
DR   InterPro; IPR043601; Rspo_Fu-CRD_dom.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR46987:SF5; PTHR46987:SF5; 1.
DR   Pfam; PF15913; Furin-like_2; 1.
DR   SMART; SM00261; FU; 2.
DR   SMART; SM00209; TSP1; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   SUPFAM; SSF82895; SSF82895; 1.
DR   PROSITE; PS50092; TSP1; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Heparin-binding; Reference proteome; Repeat;
KW   Secreted; Sensory transduction; Signal; Wnt signaling pathway.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..261
FT                   /note="R-spondin-1"
FT                   /id="PRO_0000234438"
FT   REPEAT          34..86
FT                   /note="FU 1"
FT   REPEAT          92..136
FT                   /note="FU 2"
FT   DOMAIN          145..213
FT                   /note="TSP type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   REGION          168..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        41..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        45..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        57..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        80..95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        98..106
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        103..112
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        115..126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        130..142
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        146..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        157..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        204..212
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ   SEQUENCE   261 AA;  29050 MW;  B2B01315A5C6D980 CRC64;
     MHLGLLALAL VFFSSMGHAD NLKASKARRQ RRISTEVPPS CSNGCEHCSE YNGCLKCRPR
     LFILLERNDI RQIGICLAAC PVGYYGIRNR DMNKCTQCKI ENCEACFSRN FCTKCKEGLY
     SHRGRCFSSC PEGFTVNGTM ECVVQCDLSE WSPWGPCMKK NKTCGFKKGN QTRTREPLQV
     PSPATSTGAA PASGCVPEIQ TQRCTVQKKI PCKGENKKNQ QNRGENSKNR GRDSKERGGN
     KKRKNTNRST TVPTITTSMV T