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P97401 (SFRP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Secreted frizzled-related protein 3

Short name=sFRP-3
Alternative name(s):
Frezzled
Fritz
Frizzled-related protein 1
FrzB-1
Gene names
Name:Frzb
Synonyms:Fiz, Fre, Frzb1, Sfrp3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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. SFRP3/FRZB appears to be involved in limb skeletogenesis. Antagonist of Wnt8 signaling. Regulates chondrocyte maturation and long bone development By similarity. Ref.2

Subunit structure

Interacts with MYOC. Ref.6

Subcellular location

Secreted Probable.

Tissue specificity

Expressed in kidney, brain, testis. Weak expression in spleen and heart. Ref.2 Ref.3

Developmental stage

In early gastrulation, expressed in all three germ layers. In later embryogenesis, expressed in a range of tissues including the central and peripheral nervous systems and the nephogenic mesenchyme.

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.

Ontologies

Keywords
   Biological processDifferentiation
Wnt signaling pathway
   Cellular componentSecreted
   DomainSignal
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

brain development

Inferred from Biological aspect of Ancestor. Source: RefGenome

cochlea morphogenesis

Inferred from genetic interaction PubMed 17433286. Source: MGI

convergent extension involved in organogenesis

Inferred from genetic interaction PubMed 17433286. Source: MGI

gonad development

Inferred from Biological aspect of Ancestor. Source: RefGenome

inner ear morphogenesis

Inferred from direct assay PubMed 18991062. Source: MGI

mammary gland involution

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of Wnt signaling pathway

Inferred from direct assay Ref.2. Source: UniProtKB

negative regulation of canonical Wnt signaling pathway

Inferred from genetic interaction PubMed 19961844. Source: MGI

negative regulation of cartilage development

Inferred from genetic interaction PubMed 18991062. Source: MGI

negative regulation of cell development

Inferred from direct assay PubMed 19562671. Source: MGI

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of hepatocyte differentiation

Inferred from direct assay PubMed 19562671. Source: MGI

neural crest cell differentiation

Inferred from expression pattern PubMed 10654605. Source: BHF-UCL

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of fat cell differentiation

Inferred from sequence orthology PubMed 12055200. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

somite development

Inferred from expression pattern PubMed 10654605. Source: BHF-UCL

vasculature development

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular region

Non-traceable author statement Ref.2. Source: UniProtKB

extracellular space

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionPDZ domain binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Wnt-activated receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Wnt-protein binding

Inferred from direct assay Ref.2. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 323291Secreted frizzled-related protein 3
PRO_0000032547

Regions

Domain33 – 150118FZ
Domain178 – 298121NTR
Compositional bias301 – 31818Ser/Thr-rich

Amino acid modifications

Glycosylation491N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 96 Ref.7
Disulfide bond43 ↔ 89 Ref.7
Disulfide bond80 ↔ 119 Ref.7
Disulfide bond108 ↔ 147 Ref.7
Disulfide bond112 ↔ 136 Ref.7

Experimental info

Sequence conflict3211A → V in AAH16884. Ref.5

Secondary structure

........................ 323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P97401 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 3F1456F8CFC97740

FASTA32336,011
        10         20         30         40         50         60 
MVCCGPGRML LGWAGLLVLA ALCLLQVPGA QAAACEPVRI PLCKSLPWNM TKMPNHLHHS 

        70         80         90        100        110        120 
TQANAILAME QFEGLLGTHC SPDLLFFLCA MYAPICTIDF QHEPIKPCKS VCERARQGCE 

       130        140        150        160        170        180 
PILIKYRHSW PESLACDELP VYDRGVCISP EAIVTADGAD FPMDSSTGHC RGASSERCKC 

       190        200        210        220        230        240 
KPVRATQKTY FRNNYNYVIR AKVKEVKMKC HDVTAVVEVK EILKASLVNI PRDTVNLYTT 

       250        260        270        280        290        300 
SGCLCPPLTV NEEYVIMGYE DEERSRLLLV EGSIAEKWKD RLGKKVKRWD MKLRHLGLGK 

       310        320 
TDASDSTQNQ KSGRNSNPRP ARS 

« Hide

References

« Hide 'large scale' references
[1]"Frzb-1 is a secreted antagonist of Wnt signaling expressed in the Spemann organizer."
Leyns L., Bouwmeester T., Kim S.-H., Piccolo S., de Robertis E.M.
Cell 88:747-756(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Fritz: a secreted frizzled-related protein that inhibits Wnt activity."
Mayr T., Deutsch U., Kuehl M., Drexler H.C.A., Lottspeich F., Deutzmann R., Wedlich D., Risau W.
Mech. Dev. 63:109-125(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Embryo.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Tongue.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[6]"Myocilin is a modulator of Wnt signaling."
Kwon H.S., Lee H.S., Ji Y., Rubin J.S., Tomarev S.I.
Mol. Cell. Biol. 29:2139-2154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYOC.
[7]"Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains."
Dann C.E., Hsieh J.-C., Rattner A., Sharma D., Nathans J., Leahy D.J.
Nature 412:86-90(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 33-157, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U68058 mRNA. Translation: AAC53135.1.
U91905 mRNA. Translation: AAB51300.1.
U88568 mRNA. Translation: AAC53147.1.
AK019093 mRNA. Translation: BAB31542.1.
AK029941 mRNA. Translation: BAC26690.1.
BC016884 mRNA. Translation: AAH16884.1.
CCDSCCDS16176.1.
RefSeqNP_035486.1. NM_011356.4.
UniGeneMm.427436.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IJXX-ray1.90A/B/C/D/E/F33-157[»]
ProteinModelPortalP97401.
SMRP97401. Positions 33-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203186. 2 interactions.

PTM databases

PhosphoSiteP97401.

Proteomic databases

PRIDEP97401.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028389; ENSMUSP00000028389; ENSMUSG00000027004.
GeneID20378.
KEGGmmu:20378.
UCSCuc008khl.1. mouse.

Organism-specific databases

CTD2487.
MGIMGI:892032. Frzb.

Phylogenomic databases

eggNOGNOG304384.
GeneTreeENSGT00750000117492.
HOGENOMHOG000231879.
HOVERGENHBG070536.
InParanoidP97401.
OMAEEYLIMG.
OrthoDBEOG79PJPC.
PhylomeDBP97401.

Gene expression databases

BgeeP97401.
CleanExMM_FRZB.
GenevestigatorP97401.

Family and domain databases

Gene3D1.10.2000.10. 1 hit.
InterProIPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR026556. SFRP3.
IPR008993. TIMP-like_OB-fold.
[Graphical view]
PANTHERPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF76. PTHR11309:SF76. 1 hit.
PfamPF01392. Fz. 1 hit.
PF01759. NTR. 1 hit.
[Graphical view]
SMARTSM00643. C345C. 1 hit.
SM00063. FRI. 1 hit.
[Graphical view]
SUPFAMSSF50242. SSF50242. 1 hit.
SSF63501. SSF63501. 1 hit.
PROSITEPS50038. FZ. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFRZB. mouse.
EvolutionaryTraceP97401.
NextBio298290.
PROP97401.
SOURCESearch...

Entry information

Entry nameSFRP3_MOUSE
AccessionPrimary (citable) accession number: P97401
Secondary accession number(s): O09075, O09093, Q91W58
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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