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Database: UniProt
Entry: G1R3H6_NOMLE
LinkDB: G1R3H6_NOMLE
Original site: G1R3H6_NOMLE 
ID   G1R3H6_NOMLE            Unreviewed;       325 AA.
AC   G1R3H6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Secreted frizzled-related protein 3 {ECO:0000256|ARBA:ARBA00020513};
DE   AltName: Full=Frizzled-related protein 1 {ECO:0000256|ARBA:ARBA00031515};
DE   AltName: Full=FrzB-1 {ECO:0000256|ARBA:ARBA00029575};
GN   Name=FRZB {ECO:0000313|Ensembl:ENSNLEP00000007748.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000007748.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000007748.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000007748.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Soluble frizzled-related proteins (sFRPS) function as
CC       modulators of Wnt signaling through direct interaction with Wnts. They
CC       have a role in regulating cell growth and differentiation in specific
CC       cell types. SFRP3/FRZB appears to be involved in limb skeletogenesis.
CC       Antagonist of Wnt8 signaling. Regulates chondrocyte maturation and long
CC       bone development. {ECO:0000256|ARBA:ARBA00025169}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the secreted frizzled-related protein (sFRP)
CC       family. {ECO:0000256|ARBA:ARBA00010054}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR   EMBL; ADFV01059039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003253864.1; XM_003253816.3.
DR   AlphaFoldDB; G1R3H6; -.
DR   STRING; 61853.ENSNLEP00000007748; -.
DR   Ensembl; ENSNLET00000008121.2; ENSNLEP00000007748.1; ENSNLEG00000006370.2.
DR   GeneID; 100579183; -.
DR   KEGG; nle:100579183; -.
DR   CTD; 2487; -.
DR   eggNOG; KOG3577; Eukaryota.
DR   GeneTree; ENSGT00940000160494; -.
DR   HOGENOM; CLU_058446_1_0_1; -.
DR   InParanoid; G1R3H6; -.
DR   OMA; IRYRHAW; -.
DR   OrthoDB; 2919179at2759; -.
DR   Proteomes; UP000001073; Chromosome 22a.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0017147; F:Wnt-protein binding; IEA:Ensembl.
DR   GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR   GO; GO:0060029; P:convergent extension involved in organogenesis; IEA:Ensembl.
DR   GO; GO:0002064; P:epithelial cell development; IEA:Ensembl.
DR   GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0061037; P:negative regulation of cartilage development; IEA:Ensembl.
DR   GO; GO:0010721; P:negative regulation of cell development; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0070367; P:negative regulation of hepatocyte differentiation; IEA:Ensembl.
DR   GO; GO:0014033; P:neural crest cell differentiation; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0061053; P:somite development; IEA:Ensembl.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd07441; CRD_SFRP3; 1.
DR   CDD; cd03581; NTR_Sfrp3_like; 1.
DR   Gene3D; 2.40.50.120; -; 1.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   InterPro; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR001134; Netrin_domain.
DR   InterPro; IPR018933; Netrin_module_non-TIMP.
DR   InterPro; IPR035813; NTR_Sfrp3.
DR   InterPro; IPR041759; SFRP3_CRD.
DR   InterPro; IPR008993; TIMP-like_OB-fold.
DR   PANTHER; PTHR11309; FRIZZLED; 1.
DR   PANTHER; PTHR11309:SF97; SECRETED FRIZZLED-RELATED PROTEIN 3; 1.
DR   Pfam; PF01392; Fz; 1.
DR   Pfam; PF01759; NTR; 1.
DR   SMART; SM00643; C345C; 1.
DR   SMART; SM00063; FRI; 1.
DR   SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR   SUPFAM; SSF50242; TIMP-like; 1.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS50189; NTR; 1.
PE   3: Inferred from homology;
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00090}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..325
FT                   /note="Secreted frizzled-related protein 3"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003420501"
FT   DOMAIN          30..150
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          178..298
FT                   /note="NTR"
FT                   /evidence="ECO:0000259|PROSITE:PS50189"
FT   REGION          297..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        35..96
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        43..89
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        112..136
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   325 AA;  36208 MW;  FEB4DED89852BB0D CRC64;
     MVCGSPGGML LLRAGLLALA ALCLLRVPGA RAAACEPVRI PLCKSLPWNM TKMPNHLHHS
     TQANAILAIE QFEGLLGTHC SPDLLFFLCA MYAPICTIDF QHEPIKPCKS VCERARQGCE
     PILIKYRHSW PESLACEELP VYDRGVCISP EAIVTADGAD FPMDSSNGNC RGASSERCKC
     KPIRATQKTY FRNNYNYVIR AKVKEIKTKC HDVTAVVEVK EILKSSLVNI PRDTVNLYTS
     SGCLCPPLNV NEEYIIMGYE DEERSRLLLV EGSIAEKWKD RLGKKVKRWD MKLHHLGLSK
     SDSSNSDSTQ SQKSGRNSNP RQARN
//
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