SFRP3_PONAB
ID SFRP3_PONAB Reviewed; 325 AA.
AC Q5RF67;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Secreted frizzled-related protein 3;
DE Short=sFRP-3;
DE AltName: Full=Frizzled-related protein 1;
DE AltName: Full=FrzB-1;
DE Flags: Precursor;
GN Name=FRZB; Synonyms=SFRP3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MYOC. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the secreted frizzled-related protein (sFRP)
CC family. {ECO:0000305}.
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DR EMBL; CR857294; CAH89590.1; -; mRNA.
DR RefSeq; NP_001124703.1; NM_001131231.1.
DR AlphaFoldDB; Q5RF67; -.
DR SMR; Q5RF67; -.
DR STRING; 9601.ENSPPYP00000014518; -.
DR Ensembl; ENSPPYT00000015107; ENSPPYP00000014518; ENSPPYG00000012995.
DR GeneID; 100171551; -.
DR KEGG; pon:100171551; -.
DR CTD; 2487; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000160494; -.
DR HOGENOM; CLU_058446_1_0_1; -.
DR InParanoid; Q5RF67; -.
DR OMA; CNELPLY; -.
DR OrthoDB; 1339129at2759; -.
DR Proteomes; UP000001595; Chromosome 2B.
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; 1.10.2000.10; -; 1.
DR Gene3D; 2.40.50.120; -; 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; IPR026556; SFRP3.
DR InterPro; IPR041759; SFRP3_CRD.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF97; PTHR11309:SF97; 1.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF01759; NTR; 1.
DR SMART; SM00643; C345C; 1.
DR SMART; SM00063; FRI; 1.
DR SUPFAM; SSF50242; SSF50242; 1.
DR SUPFAM; SSF63501; SSF63501; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50189; NTR; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..325
FT /note="Secreted frizzled-related protein 3"
FT /id="PRO_0000032548"
FT DOMAIN 33..150
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 178..298
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
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 CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..96
FT /evidence="ECO:0000250"
FT DISULFID 43..89
FT /evidence="ECO:0000250"
FT DISULFID 80..119
FT /evidence="ECO:0000250"
FT DISULFID 108..147
FT /evidence="ECO:0000250"
FT DISULFID 112..136
FT /evidence="ECO:0000250"
SQ SEQUENCE 325 AA; 36254 MW; 8337C51BBA9A4B07 CRC64;
MVCGSPGGML LLRAGLLALA ALCLLRVPGA RAAACEPVRI PLCKSLPWNM TKMPNHLHHS
TQANAILAIE QFEGLLGTHC SPDLLFFLCA MYAPICTIDF QHEPIKPCKS VCERARQGCE
PILIKYRHSW PENLACEELP VYDRGVCISP EAIVTADGAD FPMDSSNGNC RGASSERCKC
KPIRATQKTY FRNNYNYVIR AKVKEIKTKC HDVTAVVEVK EILKSSLVNI PRDTVNLYTS
SGCLCPPLNV NEEYIIMGYE DEERSRLLLV EGSIAEKWKD RLGKKVKRWD MKLRHLGLSK
SDSSNSDSTQ SQKSGRNSNP RQARN
