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Q5T4F7 (SFRP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 5

Short name=sFRP-5
Alternative name(s):
Frizzled-related protein 1b
Short name=FRP-1b
Secreted apoptosis-related protein 3
Short name=SARP-3
Gene names
Name:SFRP5
Synonyms:FRP1B, SARP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. SFRP5 may be involved in determining the polarity of photoreceptor, and perhaps, other cells in the retina.

Subcellular location

Secreted By similarity.

Tissue specificity

Highly expressed in the retinal pigment epithelium (RPE) and pancreas. Weak expression in heart, liver and muscle. Ref.1 Ref.2 Ref.3

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
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionDevelopmental protein
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanatomical structure morphogenesis

Traceable author statement Ref.3. Source: ProtInc

apoptotic process

Traceable author statement Ref.1. Source: ProtInc

brain development

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

convergent extension involved in axis elongation

Inferred from electronic annotation. Source: Ensembl

digestive tract morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryo development

Inferred from Biological aspect of Ancestor. Source: RefGenome

establishment or maintenance of cell polarity

Traceable author statement Ref.3. Source: ProtInc

gonad development

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of Wnt signaling pathway involved in digestive tract morphogenesis

Inferred from mutant phenotype PubMed 18981481. Source: BHF-UCL

negative regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 19957335. Source: BHF-UCL

negative regulation of catenin import into nucleus

Inferred from mutant phenotype PubMed 19957335. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 19957335. Source: BHF-UCL

negative regulation of planar cell polarity pathway involved in axis elongation

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 19957335. Source: BHF-UCL

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype PubMed 19957335. Source: BHF-UCL

planar cell polarity pathway involved in neural tube closure

Inferred from electronic annotation. Source: Ensembl

post-anal tail morphogenesis

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.3. Source: ProtInc

vasculature development

Inferred from Biological aspect of Ancestor. Source: RefGenome

visual perception

Traceable author statement Ref.3. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular space

Traceable author statement Ref.3. Source: ProtInc

plasma membrane

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 Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 317288Secreted frizzled-related protein 5
PRO_0000032555

Regions

Domain48 – 165118FZ
Domain181 – 303123NTR

Amino acid modifications

Disulfide bond53 ↔ 116 By similarity
Disulfide bond63 ↔ 109 By similarity
Disulfide bond100 ↔ 135 By similarity
Disulfide bond124 ↔ 162 By similarity
Disulfide bond128 ↔ 152 By similarity
Disulfide bond181 ↔ 253 By similarity
Disulfide bond184 ↔ 255 By similarity
Disulfide bond198 ↔ 303 By similarity

Natural variations

Natural variant71G → A. Ref.1 Ref.2 Ref.3 Ref.6
Corresponds to variant rs11815012 [ dbSNP | Ensembl ].
VAR_021412

Experimental info

Sequence conflict331D → H Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q5T4F7 [UniParc].

Last modified June 26, 2007. Version 3.
Checksum: 4BF060F1161751F9

FASTA31735,563
        10         20         30         40         50         60 
MRAAAAGGGV RTAALALLLG ALHWAPARCE EYDYYGWQAE PLHGRSYSKP PQCLDIPADL 

        70         80         90        100        110        120 
PLCHTVGYKR MRLPNLLEHE SLAEVKQQAS SWLPLLAKRC HSDTQVFLCS LFAPVCLDRP 

       130        140        150        160        170        180 
IYPCRSLCEA VRAGCAPLME AYGFPWPEML HCHKFPLDND LCIAVQFGHL PATAPPVTKI 

       190        200        210        220        230        240 
CAQCEMEHSA DGLMEQMCSS DFVVKMRIKE IKIENGDRKL IGAQKKKKLL KPGPLKRKDT 

       250        260        270        280        290        300 
KRLVLHMKNG AGCPCPQLDS LAGSFLVMGR KVDGQLLLMA VYRWDKKNKE MKFAVKFMFS 

       310 
YPCSLYYPFF YGAAEPH 

« Hide

References

« Hide 'large scale' references
[1]"SARPs: a family of secreted apoptosis-related proteins."
Melkonyan H.S., Chang W.C., Shapiro J.P., Mahadevappa M., Fitzpatrick P.A., Kiefer M.C., Tomei L.D., Umansky S.R.
Proc. Natl. Acad. Sci. U.S.A. 94:13636-13641(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-7, TISSUE SPECIFICITY.
Tissue: Pancreas.
[2]"Tissue restricted expression of two human Frzbs in preadipocytes and pancreas."
Hu E., Zhu Y., Fredrickson T., Barnes M., Kelsell D., Beeley L., Brooks D.
Biochem. Biophys. Res. Commun. 247:287-293(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-7, TISSUE SPECIFICITY.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT ALA-7, TISSUE SPECIFICITY.
Tissue: Retina.
[4]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Fetal brain.
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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], VARIANT ALA-7.
Tissue: PNS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF017988 mRNA. Translation: AAB70794.1.
AF117758 mRNA. Translation: AAD25052.1.
CR596705 mRNA. No translation available.
AL358938 Genomic DNA. Translation: CAI14274.1.
BC050435 mRNA. Translation: AAH50435.2.
PIRJE0175.
RefSeqNP_003006.2. NM_003015.3.
UniGeneHs.279565.

3D structure databases

ProteinModelPortalQ5T4F7.
SMRQ5T4F7. Positions 60-156.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000266066.

Protein family/group databases

MEROPSI93.001.

PTM databases

PhosphoSiteQ5T4F7.

Polymorphism databases

DMDM150421670.

Proteomic databases

PaxDbQ5T4F7.
PRIDEQ5T4F7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266066; ENSP00000266066; ENSG00000120057.
GeneID6425.
KEGGhsa:6425.
UCSCuc001kor.4. human.

Organism-specific databases

CTD6425.
GeneCardsGC10M099516.
H-InvDBHIX0035310.
HGNCHGNC:10779. SFRP5.
HPAHPA019840.
MIM604158. gene.
neXtProtNX_Q5T4F7.
PharmGKBPA35695.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG240950.
HOGENOMHOG000231058.
HOVERGENHBG052928.
InParanoidQ5T4F7.
KOK02222.
OMALMEAYGF.
OrthoDBEOG789CBZ.
PhylomeDBQ5T4F7.
TreeFamTF350133.

Gene expression databases

BgeeQ5T4F7.
CleanExHS_SFRP5.
GenevestigatorQ5T4F7.

Family and domain databases

Gene3D1.10.2000.10. 1 hit.
InterProIPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR026559. SFRP1/5.
IPR008993. TIMP-like_OB-fold.
[Graphical view]
PANTHERPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF46. PTHR11309:SF46. 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

GeneWikiSFRP5.
GenomeRNAi6425.
NextBio24951.
PROQ5T4F7.
SOURCESearch...

Entry information

Entry nameSFRP5_HUMAN
AccessionPrimary (citable) accession number: Q5T4F7
Secondary accession number(s): O14780, Q86TH7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM