SFRP5_MOUSE
ID SFRP5_MOUSE Reviewed; 314 AA.
AC Q9WU66; Q8K269;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Secreted frizzled-related protein 5;
DE Short=sFRP-5;
DE Flags: Precursor;
GN Name=Sfrp5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Retina;
RX PubMed=10072424; DOI=10.1093/hmg/8.4.575;
RA Chang J.T., Esumi N., Moore K., Li Y., Zhang S., Chew C., Goodman B.,
RA Rattner A., Moody S., Stetten G., Campochiaro P.A., Zack D.J.;
RT "Cloning and characterization of a secreted frizzled-related protein that
RT is expressed by the retinal pigment epithelium.";
RL Hum. Mol. Genet. 8:575-583(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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. SFRP5 may be involved in determining the polarity of
CC photoreceptor, and perhaps, other cells in the retina.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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; AF117759; AAD25053.1; -; mRNA.
DR EMBL; BC032921; AAH32921.1; -; mRNA.
DR CCDS; CCDS29826.1; -.
DR RefSeq; NP_061250.2; NM_018780.3.
DR AlphaFoldDB; Q9WU66; -.
DR SMR; Q9WU66; -.
DR BioGRID; 207687; 2.
DR STRING; 10090.ENSMUSP00000018966; -.
DR iPTMnet; Q9WU66; -.
DR PhosphoSitePlus; Q9WU66; -.
DR PaxDb; Q9WU66; -.
DR PRIDE; Q9WU66; -.
DR ProteomicsDB; 256630; -.
DR DNASU; 54612; -.
DR GeneID; 54612; -.
DR KEGG; mmu:54612; -.
DR UCSC; uc008hnl.2; mouse.
DR CTD; 6425; -.
DR MGI; MGI:1860298; Sfrp5.
DR eggNOG; KOG3577; Eukaryota.
DR InParanoid; Q9WU66; -.
DR OrthoDB; 1306779at2759; -.
DR PhylomeDB; Q9WU66; -.
DR TreeFam; TF350133; -.
DR BioGRID-ORCS; 54612; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Sfrp5; mouse.
DR PRO; PR:Q9WU66; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9WU66; protein.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0060028; P:convergent extension involved in axis elongation; IGI:MGI.
DR GO; GO:0048546; P:digestive tract morphogenesis; IGI:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; IGI:MGI.
DR GO; GO:2000041; P:negative regulation of planar cell polarity pathway involved in axis elongation; IGI:MGI.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:MGI.
DR GO; GO:2000057; P:negative regulation of Wnt signaling pathway involved in digestive tract morphogenesis; ISO:MGI.
DR GO; GO:0003402; P:planar cell polarity pathway involved in axis elongation; IGI:MGI.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IGI:MGI.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IGI:MGI.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IEA:InterPro.
DR GO; GO:0090175; P:regulation of establishment of planar polarity; IGI:MGI.
DR CDD; cd07444; CRD_SFRP5; 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; IPR034860; SFRP-5.
DR InterPro; IPR041761; SFRP5_CRD.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF46; PTHR11309:SF46; 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; Reference proteome;
KW Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..314
FT /note="Secreted frizzled-related protein 5"
FT /id="PRO_0000032556"
FT DOMAIN 45..162
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 178..300
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 50..113
FT /evidence="ECO:0000250"
FT DISULFID 60..106
FT /evidence="ECO:0000250"
FT DISULFID 97..132
FT /evidence="ECO:0000250"
FT DISULFID 121..159
FT /evidence="ECO:0000250"
FT DISULFID 125..149
FT /evidence="ECO:0000250"
FT DISULFID 178..250
FT /evidence="ECO:0000250"
FT DISULFID 181..252
FT /evidence="ECO:0000250"
FT DISULFID 195..300
FT /evidence="ECO:0000250"
FT CONFLICT 128
FT /note="A -> V (in Ref. 2; AAH32921)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 35382 MW; 296847F56D1CAFDD CRC64;
MWVAWSARTA ALALLLGALH GAPTRGQEYD YYGWQAEPLH GRSYSKPPQC LDIPADLPLC
HTVGYKRMRL PNLLEHESLA EVKQQASSWL PLLAKRCHSD TQVFLCSLFA PVCLDRPIYP
CRSLCEAARA GCAPLMEAYG FPWPEMLHCH KFPLDNDLCI AVQFGHLPAT APPVTKICAQ
CEMEHSADGL MEQMCSSDFV VKMRIKEIKI DNGDRKLIGA QKKKKLLKAG PLKRKDTKKL
VLHMKNGASC PCPQLDNLTG SFLVMGRKVE GQLLLTAVYR WDKKNKEMKF AVKFMFSYPC
SLYYPFFYGA AEPH
