SFRP3_CHICK
ID SFRP3_CHICK Reviewed; 315 AA.
AC Q9IA95; Q4U3E3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=10656762; DOI=10.1006/dbio.1999.9586;
RA Ladher R.K., Church V.L., Allen S., Robson L., Abdelfattah A., Brown N.A.,
RA Hattersley G., Rosen V., Luyten F.P., Dale L., Francis-West P.H.;
RT "Cloning and expression of the Wnt antagonists Sfrp-2 and Frzb during chick
RT development.";
RL Dev. Biol. 218:183-198(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16425220; DOI=10.1002/dvdy.20681;
RA Galli L.M., Barnes T., Cheng T., Acosta L., Anglade A., Willert K.,
RA Nusse R., Burrus L.W.;
RT "Differential inhibition of Wnt-3a by Sfrp-1, Sfrp-2, and Sfrp-3.";
RL Dev. Dyn. 235:681-690(2006).
RN [3]
RP DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=12413904; DOI=10.1006/dbio.2002.0802;
RA Enomoto-Iwamoto M., Kitagaki J., Koyama E., Tamamura Y., Wu C.,
RA Kanatani N., Koike T., Okada H., Komori T., Yoneda T., Church V.L.,
RA Francis-West P.H., Kurisu K., Nohno T., Pacifici M., Iwamoto M.;
RT "The Wnt antagonist Frzb-1 regulates chondrocyte maturation and long bone
RT development during limb skeletogenesis.";
RL Dev. Biol. 251:142-156(2002).
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:0000269|PubMed:12413904}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: At stage 7 of embryonic development, expressed in
CC the neural plate with lower expression in the midline. At stage 9,
CC expression restricted to the dorsal neural tube and cranial neural
CC crest. At stage 12, expressed in the lateral plate mesoderm. In the
CC developing trunk, expressed, from stages 9-12, in the ventral migrating
CC neural crest with some expression at stage 12 in the dorsal streams
CC From stage 15, expressed in the endocardial cells of the outflow tract
CC of the developing heart. From stage 18, expression found in the
CC epibranchial placodes, in endocardial and mesenchymal cells of the
CC developing atrioventricular canal and of the outflow tract cushions.
CC Expression in these regions of the developing heart continue until
CC stage 26. During limb development, low expression found, by stage 18,
CC in the developing limb buds, By stage 20, highly expressed in the
CC ventral mesenchyme of both fore- and hind-limb buds. By stage 24,
CC expression localized to the central core of the developing limb bud,
CC which contains the chondrogenic precursors. Also expressed in the
CC surrounding nonchondrogenic mesenchyme. Later expression confined to
CC the perichondrium and to the epiphyses of the early developing skeletal
CC elements. {ECO:0000269|PubMed:10656762, ECO:0000269|PubMed:12413904}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF218057; AAF27643.1; -; mRNA.
DR EMBL; DQ017062; AAY42147.1; -; mRNA.
DR RefSeq; NP_990103.1; NM_204772.2.
DR AlphaFoldDB; Q9IA95; -.
DR SMR; Q9IA95; -.
DR STRING; 9031.ENSGALP00000004354; -.
DR GeneID; 395545; -.
DR KEGG; gga:395545; -.
DR CTD; 2487; -.
DR VEuPathDB; HostDB:geneid_395545; -.
DR eggNOG; KOG3577; Eukaryota.
DR InParanoid; Q9IA95; -.
DR OrthoDB; 1339129at2759; -.
DR PhylomeDB; Q9IA95; -.
DR PRO; PR:Q9IA95; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0017147; F:Wnt-protein binding; ISS:AgBase.
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:0030178; P:negative regulation of Wnt signaling pathway; ISS:AgBase.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..315
FT /note="Secreted frizzled-related protein 3"
FT /id="PRO_0000032549"
FT DOMAIN 22..142
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 170..290
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 284..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..88
FT /evidence="ECO:0000250"
FT DISULFID 35..81
FT /evidence="ECO:0000250"
FT DISULFID 72..111
FT /evidence="ECO:0000250"
FT DISULFID 100..139
FT /evidence="ECO:0000250"
FT DISULFID 104..128
FT /evidence="ECO:0000250"
SQ SEQUENCE 315 AA; 35004 MW; 6EBC58DB5335505D CRC64;
MWRGLPALAL AALLLLGRAP AGRAAACEPV RIPLCKPLPW NMTKMPNHLH HSTQANAVLA
MEQFEGLLGT NCSPDLLFFL CAMYAPICTI DFQHEPIKPC KSVCERARAG CEPVLIRYRH
AWPESLACDE LPLYDRGVCI SPEAIVTAEG ADFPMDSNNG NCRGTGIERC KCKPIKATQK
TYLRNNYNYV IRAKVKEVKT KCHDVTAVVE VKEILKSSLV NIPKDTVNLY TNSGCLCPPL
SANEEYIIMG YEDEERSRLL LVEGSIAEKW KDRLGKKVKR WDQKLRHLGK GKGEPGQSDS
ALKTGKPGNA RQTRS
