SFRP4_MACMU
ID SFRP4_MACMU Reviewed; 346 AA.
AC Q7YRN1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Secreted frizzled-related protein 4;
DE Short=sFRP-4;
DE Flags: Precursor;
GN Name=SFRP4;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14724130; DOI=10.1095/biolreprod.103.018523;
RA Sun X.-Y., Li F.-X., Li J., Tan Y.-F., Piao Y.-S., Tang S., Wang Y.-L.;
RT "Determination of genes involved in the early process of embryonic
RT implantation in rhesus monkey (Macaca mulatta) by suppression subtractive
RT hybridization.";
RL Biol. Reprod. 70:1365-1373(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. SFRP4 plays a role in bone morphogenesis. May also act as a
CC regulator of adult uterine morphology and function. May also increase
CC apoptosis during ovulation possibly through modulation of FZ1/FZ4/WNT4
CC signaling. Has phosphaturic effects by specifically inhibiting sodium-
CC dependent phosphate uptake. {ECO:0000250|UniProtKB:Q9Z1N6}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6FHJ7}.
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; AY321585; AAP86211.1; -; mRNA.
DR RefSeq; NP_001028134.1; NM_001032962.1.
DR AlphaFoldDB; Q7YRN1; -.
DR SMR; Q7YRN1; -.
DR STRING; 9544.ENSMMUP00000027760; -.
DR PRIDE; Q7YRN1; -.
DR GeneID; 574393; -.
DR KEGG; mcc:574393; -.
DR CTD; 6424; -.
DR eggNOG; KOG3577; Eukaryota.
DR InParanoid; Q7YRN1; -.
DR OrthoDB; 1339129at2759; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
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:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:UniProt.
DR GO; GO:2000051; P:negative regulation of non-canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0050793; P:regulation of developmental process; IEA:UniProt.
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; IPR026560; SFRP4.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF7; PTHR11309:SF7; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..346
FT /note="Secreted frizzled-related protein 4"
FT /id="PRO_0000032551"
FT DOMAIN 19..139
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 178..307
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 294..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..85
FT /evidence="ECO:0000250"
FT DISULFID 32..78
FT /evidence="ECO:0000250"
FT DISULFID 69..108
FT /evidence="ECO:0000250"
FT DISULFID 97..136
FT /evidence="ECO:0000250"
FT DISULFID 101..125
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 39769 MW; 4A893F95D2231A47 CRC64;
MFLSILVALC LWLHLALGVR GAPCEAVRIP MCRHMPWNIT RMPNHLHHST QENAILAIEQ
YEELVDVNCS SVLRFFLCAM YAPICTLEFL HDPIKPCKSV CQRARDDCEP LMKMYNHSWP
ESLACDELPV YDRGVCISPE AIVTDLPEDV KWIDITPDMM VQERPLDVDC KRLSPDRCKC
KKVKPTLATY LSKNCSYVIH AKIKAVQRSG CNEVTTVVDV KEIFKSSSPI PRTQVPLITN
SSCQCPHILP HQDVLIMCYE WRSRMMLLEN CLVEKWRDQL SKRSIQWEER LREQRRTIQD
KKKTAGRTSR SNPPKPKGKP PAPKPASPKK NIKTRSAQKK TNPKKV
