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Reviewed, UniProtKB/Swiss-Prot Q9Z1N6 (SFRP4_MOUSE)

Last modified January 19, 2010. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Secreted frizzled-related sequence protein 4
      Short name=sFRP-4
      Short name=Frizzled-related protein 4
      Short name=FRP-4
Gene names
Name: Sfrp4
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP4 may act as a regulator of adult uterine morphology and function. Increases apoptosis during ovulation possibly through modulation of FZ1/FZ4/WNT4 signaling. Has phosphaturic effects by specifically inhibiting sodium-dependent phosphate uptake By similarity.

Subcellular location

Secreted By similarity.

Tissue specificity

Expressed the ovary. Localized to granulosa cells of periovulatory follicles and corpora lutea. Weakly expressed in adult tissues including kidney, brain and lung. Ref.7

Developmental stage

Only weakly expressed in developing embryo except for developing teeth, eye and salivary gland. In the developing eye, from E12.5, expressed in the future neural retina, in both the inner and outer cell layers. In the developing teeth, strong expression detected in the developing incisor teeth at E14.5. Expression localized to the mesenchyme of the dental follicle surrounding the enamel organ only at the early cap stage. Highly expressed in the branching epithelium of the salivary gland. Ref.6

Induction

Induced in ovaries by chorionic gonadotropin (CG). Ref.7

Domain

The FZ domain is involved in binding with Wnt ligands By similarity.

Sequence similarities

Belongs to the secreted frizzled-related protein (sFRP) family.

Contains 1 FZ (frizzled) domain.

Contains 1 NTR domain.

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Ontologies

Keywords
   Biological processDifferentiation
Wnt signaling pathway
   Cellular componentSecreted
   DomainSignal
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processWnt receptor signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionWnt-protein binding

Inferred from physical interaction. Source: MGI

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 351333Secreted frizzled-related sequence protein 4
PRO_0000032552

Regions

Domain19 – 139121FZ
Domain178 – 306129NTR

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1941N-linked (GlcNAc...) Potential
Glycosylation2401N-linked (GlcNAc...) Potential
Disulfide bond24 ↔ 85 By similarity
Disulfide bond32 ↔ 78 By similarity
Disulfide bond69 ↔ 108 By similarity
Disulfide bond97 ↔ 136 By similarity
Disulfide bond101 ↔ 125 By similarity

Experimental info

Sequence conflict991S → F Ref.4

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Sequences

Sequence LengthMass (Da)Tools
Q9Z1N6-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 6CB0B625920A54FE

FASTA35140,342
        10         20         30         40         50         60 
MLRSILVALC LWLRLALGVR GAPCEAVRIP MCRHMPWNIT RMPNHLHHST QENAILAIEQ 

        70         80         90        100        110        120 
YEELVDVNCS SVLRFFLCAM YAPICTLEFL HDPIKPCKSV CQRARDDCEP LMKMYNHSWP 

       130        140        150        160        170        180 
ESLACDELPV YDRGVCISPE AIVTDLPEDV KWIDITPDMM VQERSFDADC KRLSPDRCKC 

       190        200        210        220        230        240 
KKVKPTLATY LSKNYSYVIH AKIKAVQRSG CNEVTTVVDV KEIFKSLSPI PRTQVPLITN 

       250        260        270        280        290        300 
SSCQCPHILP HQDVLIMCYE WRSRMMLLEN CLVEKWRDQL SRRSIQWEER LQEQQRTIQD 

       310        320        330        340        350 
KKQIASRTSR TSRSNPPKSK GRPPAPKPAS PKKNIKARSA PKKSNLKKSA S

« Hide

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References

« Hide 'large scale' references
[1]"Cloning and characterization of a secreted frizzled-related protein that is expressed by the retinal pigment epithelium."
Chang J.T., Esumi N., Moore K., Li Y., Zhang S., Chew C., Goodman B., Rattner A., Moody S., Stetten G., Campochiaro P.A., Zack D.J.
Hum. Mol. Genet. 8:575-583(1999) [PubMed: 10072424] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Retina.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.
[4]"A family of secreted proteins contains homology to the cysteine-rich ligand-binding domain of frizzled receptors."
Rattner A., Hsieh J.-C., Smallwood P.M., Gilbert D.J., Copeland N.G., Jenkins N.A., Nathans J.
Proc. Natl. Acad. Sci. U.S.A. 94:2859-2863(1997) [PubMed: 9096311] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-161.
Strain: C57BL/6J.
Tissue: Embryonic eye.
[5]"Transcriptional activity of the promoter region of rat frizzled-related protein gene."
Yam J.W.P., Chan K.W., Wong V.K.W., Hsiao W.L.W.
Biochem. Biophys. Res. Commun. 286:94-100(2001) [PubMed: 11485313] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-148.
Strain: 129/SvCp.
[6]"Developmental expression patterns of mouse sFRP genes encoding members of the secreted frizzled related protein family."
Leimeister C., Bach A., Gessler M.
Mech. Dev. 75:29-42(1998) [PubMed: 9739103] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[7]"Expression and localization of secreted frizzled-related protein-4 in the rodent ovary: evidence for selective up-regulation in luteinized granulosa cells."
Hsieh M., Mulders S.M., Friis R.R., Dharmarajan A., Richards J.S.
Endocrinology 144:4597-4606(2003) [PubMed: 12960062] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF117709 mRNA. Translation: AAD12306.1.
AK080766 mRNA. Translation: BAC38013.1.
BC034853 mRNA. Translation: AAH34853.1.
U88569 Genomic DNA. No translation available.
AF364906 Genomic DNA. Translation: AAL14904.1.
IPIIPI00130292.
RefSeqNP_057896.1.
UniGeneMm.42095

3D structure databases

SMRQ9Z1N6. Positions 22-144, 179-282.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9Z1N6.

PTM databases

PhosphoSiteQ9Z1N6.

Proteomic databases

PRIDEQ9Z1N6.

Genome annotation databases

EnsemblENSMUST00000002883; ENSMUSP00000002883; ENSMUSG00000021319; Mus musculus. [Genome view]
GeneID20379.
KEGGmmu:20379.
UCSCuc007ppg.1. mouse.

Organism-specific databases

CTD20379.
MGIMGI:892010. Sfrp4.

Phylogenomic databases

eggNOGroNOG14236.
HOGENOMHBG403122.
HOVERGENQ9Z1N6.
InParanoidQ9Z1N6.
OMAIKTRSAQ.
OrthoDBEOG9C8BBX.
PhylomeDBQ9Z1N6.

Gene expression databases

ArrayExpressQ9Z1N6.
BgeeQ9Z1N6.
CleanExMM_SFRP4.
GenevestigatorQ9Z1N6.
GermOnlineENSMUSG00000021319. Mus musculus.

Family and domain databases

InterProIPR020067. Frizzled-like_dom.
IPR000024. Frizzled_Cys-rich.
IPR020068. Frizzled_dom_subgr.
IPR015526. Frizzled_related.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR008993. TIMP-like_OB-fold.
[Graphical view]
Gene3DG3DSA:1.10.2000.10. Frizzled_Cys-rich. 1 hit.
PANTHERPTHR11309. Fz_related. 1 hit.
PfamPF01392. Fz. 1 hit.
PF01759. NTR. 1 hit.
[Graphical view]
SMARTSM00643. C345C. 1 hit.
SM00063. FRI. 1 hit.
[Graphical view]
PROSITEPS50038. FZ. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio298294.
SOURCESearch...

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Entry information

Entry nameSFRP4_MOUSE
AccessionPrimary (citable) accession number: Q9Z1N6
Secondary accession number(s): Q91ZX9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: May 1, 1999
Last modified: January 19, 2010
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents