ID SFRP1_MOUSE Reviewed; 314 AA.
AC Q8C4U3; O08861; Q505A2; Q8R1J4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 24-JAN-2024, entry version 165.
DE RecName: Full=Secreted frizzled-related protein 1 {ECO:0000312|MGI:MGI:892014};
DE Short=sFRP-1 {ECO:0000312|MGI:MGI:892014};
DE Flags: Precursor;
GN Name=Sfrp1 {ECO:0000312|MGI:MGI:892014};
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Embryonic eye;
RX PubMed=9096311; DOI=10.1073/pnas.94.7.2859;
RA Rattner A., Hsieh J.-C., Smallwood P.M., Gilbert D.J., Copeland N.G.,
RA Jenkins N.A., Nathans J.;
RT "A family of secreted proteins contains homology to the cysteine-rich
RT ligand-binding domain of frizzled receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:2859-2863(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-314.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=9739103; DOI=10.1016/s0925-4773(98)00072-0;
RA Leimeister C., Bach A., Gessler M.;
RT "Developmental expression patterns of mouse sFRP genes encoding members of
RT the secreted frizzled related protein family.";
RL Mech. Dev. 75:29-42(1998).
RN [5]
RP INTERACTION WITH WNT8, AND DEVELOPMENTAL STAGE.
RX PubMed=10640709; DOI=10.1016/s0925-4773(99)00236-1;
RA Jaspard B., Couffinhal T., Dufourcq P., Moreau C., Duplaa C.;
RT "Expression pattern of mouse sFRP-1 and mWnt-8 gene during heart
RT morphogenesis.";
RL Mech. Dev. 90:263-267(2000).
RN [6]
RP FUNCTION AS AN ANGIOGENIC FACTOR.
RX PubMed=15306229; DOI=10.1016/j.cardiores.2004.05.006;
RA Ezan J., Leroux L., Barandon L., Dufourcq P., Jaspard B., Moreau C.,
RA Allieres C., Daret D., Couffinhal T., Duplaa C.;
RT "FrzA/sFRP-1, a secreted antagonist of the Wnt-Frizzled pathway, controls
RT vascular cell proliferation in vitro and in vivo.";
RL Cardiovasc. Res. 63:731-738(2004).
RN [7]
RP INTERACTION WITH MYOC.
RX PubMed=19188438; DOI=10.1128/mcb.01274-08;
RA Kwon H.S., Lee H.S., Ji Y., Rubin J.S., Tomarev S.I.;
RT "Myocilin is a modulator of Wnt signaling.";
RL Mol. Cell. Biol. 29:2139-2154(2009).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=27713059; DOI=10.1016/j.ydbio.2016.10.001;
RA Jia S., Kwon H.E., Lan Y., Zhou J., Liu H., Jiang R.;
RT "Bmp4-Msx1 signaling and Osr2 control tooth organogenesis through
RT antagonistic regulation of secreted Wnt antagonists.";
RL Dev. Biol. 420:110-119(2016).
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. SFRP1 decreases intracellular beta-catenin levels (By
CC similarity). Has antiproliferative effects on vascular cells, in vitro
CC and in vivo, and can induce, in vivo, an angiogenic response. In
CC vascular cell cycle, delays the G1 phase and entry into the S phase. In
CC kidney development, inhibits tubule formation and bud growth in
CC metanephroi (By similarity). Inhibits WNT1/WNT4-mediated TCF-dependent
CC transcription (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:15306229}.
CC -!- SUBUNIT: Interacts with WNT8, WNT1, WNT2, WNT4 and FRZD6 (By
CC similarity). Interacts with MYOC. {ECO:0000250,
CC ECO:0000269|PubMed:10640709, ECO:0000269|PubMed:19188438}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Cell membrane or
CC extracellular matrix-associated. Released by heparin-binding (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney and embryonic heart.
CC Also highly expressed in the eye, where it is principally localized to
CC the ciliary body and the lens epithelium. Weaker expression in heart,
CC lung and brain. In the brain, is expressed exclusively in the choroid
CC plexus. {ECO:0000269|PubMed:9096311}.
CC -!- DEVELOPMENTAL STAGE: In the developing kidney expressed at 13.5 dpc in
CC the periphery of the metanophros and surrounding the uretic and
CC nephrogenic tubules. At 14.5 dpc, expression decreases in the outer
CC cortical cells and becomes visible in the tubular parts of the nephron.
CC From 15.5 dpc, highly expressed in the future loops of Henle. In the
CC developing CNS, expression located to the forebrain and hindbrain. At
CC 8.0 dpc, expressed in the future forebrain and in the ventral portion
CC of the presumptive hindbrain. At 8.5 dpc, expression is maintained in
CC these tissues with a strong signal in rhombomere 4. Until 11.5 dpc,
CC expression continues in the hindbrain with additional expression at 9.5
CC dpc and 10.5 dpc, in the nasal and epibranchial placodes. In the
CC forebrain, initial expression is found in the proencephalon of the
CC forebrain, and then strong expression in the telencephalic vesicle up
CC to 15.5 dpc. Expression is then found in specific cell populations
CC throughout the brain. In the developing eye, expression, by 10.5 dpc,
CC is confined to ectodermal cells overlying the dorsal part of the optic
CC cup. In later stages, expression limited to the lens fiber cells and
CC the future pigmented retina. By 15.5 dpc, expression is confined to the
CC anterior part of the lens. During limb development, barely expressed
CC until later stages, when it is found in the distal part of the
CC separating phalanges. In other developing structures, expressed in
CC nasal placodes at 9.5 dpc, in medial nasal processes at 10.5 dpc and
CC then in the anterior portion of the invaginating olfactory epithelium.
CC At 15.5 dpc, expressed on the basal side of the nasal epithelium.
CC Expressed in the mandibular molar tooth mesenchyme at 13.5 dpc
CC (PubMed:27713059). Expressed in developing teeth, with the highest
CC levels at 15.5 dpc and 16.5 dpc in the mesenchyme and the dental
CC epithelium of the developing molars. As well, expressed in the ventral
CC body wall, in the mesenchyme derived adrenal cortex, the cochlear
CC epithelium and the branching epithelium of the salivary gland. In the
CC developing heart, weakly expressed from 8.5 dpc in the tubular heart
CC endocardium and myocardium. From 8.5 dpc to 12.5 dpc expressed in
CC cardiomyocytes. At 9.5 dpc, expression found in the common ventricular
CC and atrial chamber of the developing heart, in the aortic sac and in
CC the sinus venosus. High expression found from 11.5 dpc-12.5 dpc, in the
CC trabeculated wall of the ventricular chamber together with the wall of
CC the atrial chamber. Expression also found in the muscular part of the
CC interventricular septum. From 9.5 dpc-11.5 dpc expression in the
CC visceral yolk sac confined to the inner lining endothelial cell layer.
CC Expression in the developing heart decreases after 14.5 dpc.
CC {ECO:0000269|PubMed:10640709, ECO:0000269|PubMed:27713059,
CC ECO:0000269|PubMed:9739103}.
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; U88566; AAC53145.1; -; mRNA.
DR EMBL; BC024495; AAH24495.1; -; mRNA.
DR EMBL; BC094662; AAH94662.1; -; mRNA.
DR EMBL; AK081052; BAC38123.1; -; mRNA.
DR CCDS; CCDS22191.1; -.
DR RefSeq; NP_038862.2; NM_013834.3.
DR RefSeq; XP_011240430.1; XM_011242128.1.
DR AlphaFoldDB; Q8C4U3; -.
DR SMR; Q8C4U3; -.
DR BioGRID; 203185; 10.
DR STRING; 10090.ENSMUSP00000033952; -.
DR ChEMBL; CHEMBL1075304; -.
DR MEROPS; I93.002; -.
DR GlyCosmos; Q8C4U3; 1 site, No reported glycans.
DR GlyGen; Q8C4U3; 1 site.
DR iPTMnet; Q8C4U3; -.
DR PhosphoSitePlus; Q8C4U3; -.
DR MaxQB; Q8C4U3; -.
DR PaxDb; 10090-ENSMUSP00000033952; -.
DR PeptideAtlas; Q8C4U3; -.
DR ProteomicsDB; 255399; -.
DR Pumba; Q8C4U3; -.
DR Antibodypedia; 3767; 479 antibodies from 40 providers.
DR DNASU; 20377; -.
DR Ensembl; ENSMUST00000033952.8; ENSMUSP00000033952.8; ENSMUSG00000031548.8.
DR GeneID; 20377; -.
DR KEGG; mmu:20377; -.
DR UCSC; uc009lev.2; mouse.
DR AGR; MGI:892014; -.
DR CTD; 6422; -.
DR MGI; MGI:892014; Sfrp1.
DR VEuPathDB; HostDB:ENSMUSG00000031548; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000159875; -.
DR HOGENOM; CLU_054647_0_0_1; -.
DR InParanoid; Q8C4U3; -.
DR OMA; YKRMVLP; -.
DR OrthoDB; 4814466at2759; -.
DR PhylomeDB; Q8C4U3; -.
DR TreeFam; TF350133; -.
DR BioGRID-ORCS; 20377; 1 hit in 79 CRISPR screens.
DR ChiTaRS; Sfrp1; mouse.
DR PRO; PR:Q8C4U3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8C4U3; Protein.
DR Bgee; ENSMUSG00000031548; Expressed in epithelium of lens and 285 other cell types or tissues.
DR Genevisible; Q8C4U3; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0005109; F:frizzled binding; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0017147; F:Wnt-protein binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IGI:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IGI:MGI.
DR GO; GO:0060346; P:bone trabecula formation; IMP:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:UniProtKB.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISO:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:MGI.
DR GO; GO:0071504; P:cellular response to heparin; ISO:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEA:Ensembl.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0071305; P:cellular response to vitamin D; IEA:Ensembl.
DR GO; GO:0071481; P:cellular response to X-ray; IDA:UniProtKB.
DR GO; GO:0090246; P:convergent extension involved in somitogenesis; IGI:MGI.
DR GO; GO:0046546; P:development of primary male sexual characteristics; IGI:MGI.
DR GO; GO:0048546; P:digestive tract morphogenesis; IGI:MGI.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0009950; P:dorsal/ventral axis specification; ISO:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0008585; P:female gonad development; IGI:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:MGI.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; ISO:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; IGI:MGI.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0045578; P:negative regulation of B cell differentiation; IMP:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IGI:MGI.
DR GO; GO:0046851; P:negative regulation of bone remodeling; ISO:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:2000080; P:negative regulation of canonical Wnt signaling pathway involved in controlling type B pancreatic cell proliferation; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; ISO:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
DR GO; GO:0030279; P:negative regulation of ossification; IMP:MGI.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:MGI.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; IMP:MGI.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:2000041; P:negative regulation of planar cell polarity pathway involved in axis elongation; IGI:MGI.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IGI:MGI.
DR GO; GO:2000054; P:negative regulation of Wnt signaling pathway involved in dorsal/ventral axis specification; ISO:MGI.
DR GO; GO:0014034; P:neural crest cell fate commitment; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR GO; GO:0021915; P:neural tube development; IGI:MGI.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0030316; P:osteoclast differentiation; IMP: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:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISO:MGI.
DR GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; ISO:MGI.
DR GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISO:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:MGI.
DR GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; IMP:MGI.
DR GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; IMP:MGI.
DR GO; GO:0010564; P:regulation of cell cycle process; ISO:MGI.
DR GO; GO:0090175; P:regulation of establishment of planar polarity; IGI:MGI.
DR GO; GO:1904956; P:regulation of midbrain dopaminergic neuron differentiation; IGI:ParkinsonsUK-UCL.
DR GO; GO:0010975; P:regulation of neuron projection development; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030278; P:regulation of ossification; ISO:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0001756; P:somitogenesis; IGI:MGI.
DR GO; GO:0044345; P:stromal-epithelial cell signaling involved in prostate gland development; IEP:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
DR GO; GO:0090244; P:Wnt signaling pathway involved in somitogenesis; IGI:MGI.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IDA:MGI.
DR CDD; cd07443; CRD_SFRP1; 1.
DR CDD; cd03580; NTR_Sfrp1_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; IPR041760; SFRP1_CRD.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11309; FRIZZLED; 1.
DR PANTHER; PTHR11309:SF87; SECRETED FRIZZLED-RELATED PROTEIN 1; 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 1: Evidence at protein level;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..314
FT /note="Secreted frizzled-related protein 1"
FT /id="PRO_0000032539"
FT DOMAIN 53..169
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 186..306
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 58..121
FT /evidence="ECO:0000250"
FT DISULFID 68..114
FT /evidence="ECO:0000250"
FT DISULFID 105..140
FT /evidence="ECO:0000250"
FT DISULFID 129..166
FT /evidence="ECO:0000250"
FT DISULFID 133..157
FT /evidence="ECO:0000250"
FT DISULFID 186..256
FT /evidence="ECO:0000250"
FT DISULFID 189..258
FT /evidence="ECO:0000250"
FT DISULFID 203..306
FT /evidence="ECO:0000250"
FT CONFLICT 28
FT /note="A -> S (in Ref. 2; AAH24495)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="R -> A (in Ref. 1; AAC53145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 35413 MW; 3D98A15127DFA421 CRC64;
MGVGRSARGR GGAASGVLLA LAAALLAAGS ASEYDYVSFQ SDIGSYQSGR FYTKPPQCVD
IPVDLRLCHN VGYKKMVLPN LLEHETMAEV KQQASSWVPL LNKNCHMGTQ VFLCSLFAPV
CLDRPIYPCR WLCEAVRDSC EPVMQFFGFY WPEMLKCDKF PEGDVCIAMT PPNTTEASKP
QGTTVCPPCD NELKSEAIIE HLCASEFALR MKIKEVKKEN GDKKIVPKKK KPLKLGPIKK
KELKRLVLFL KNGADCPCHQ LDNLSHNFLI MGRKVKSQYL LTAIHKWDKK NKEFKNFMKR
MKNHECPTFQ SVFK
//
