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Protein

Secreted frizzled-related protein 3

Gene

FRZB

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Wnt signaling pathway

Protein family/group databases

MEROPSiI93.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Secreted frizzled-related protein 3
Short name:
sFRP-3
Alternative name(s):
Frizzled-related protein 1
FrzB-1
Gene namesi
Name:FRZB
Synonyms:FRZB1, SFRP3
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence AnalysisAdd
BLAST
Chaini33 – 325293Secreted frizzled-related protein 3PRO_0000032545Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 96By similarity
Disulfide bondi43 ↔ 89By similarity
Glycosylationi49 – 491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi80 ↔ 119By similarity
Disulfide bondi108 ↔ 147By similarity
Disulfide bondi112 ↔ 136By similarity
Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Interacts with MYOC.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000014572.

Structurei

3D structure databases

ProteinModelPortaliQ95117.
SMRiQ95117. Positions 33-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 150118FZPROSITE-ProRule annotationAdd
BLAST
Domaini178 – 298121NTRPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi301 – 31818Ser-richAdd
BLAST

Domaini

The FZ domain is involved in binding with Wnt ligands.

Sequence similaritiesi

Contains 1 FZ (frizzled) domain.PROSITE-ProRule annotation
Contains 1 NTR domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG304384.
GeneTreeiENSGT00760000118864.
HOGENOMiHOG000231879.
HOVERGENiHBG070536.
InParanoidiQ95117.
OMAiEEYLIMG.
OrthoDBiEOG79PJPC.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiIPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR026556. SFRP3.
IPR008993. TIMP-like_OB-fold.
[Graphical view]
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF76. PTHR11309:SF76. 1 hit.
PfamiPF01392. Fz. 1 hit.
PF01759. NTR. 1 hit.
[Graphical view]
SMARTiSM00643. C345C. 1 hit.
SM00063. FRI. 1 hit.
[Graphical view]
SUPFAMiSSF50242. SSF50242. 1 hit.
SSF63501. SSF63501. 1 hit.
PROSITEiPS50038. FZ. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q95117-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVCGSRGGML LLPAGLLALA ALCLLRVPGA RAAACEPVRI PLCKSLPWNM
60 70 80 90 100
TKMPNHLHHS TQANAILAIE QFEGLLGTHC SPDLLFFLCA MYAPICTIDF
110 120 130 140 150
QHEPIKPCKS VCERARQGCE PILIKYRHSW PESLACEELP VYDRGVCISP
160 170 180 190 200
EAIVTADGAD FPMDSSNGNC RGASSERCKC KPVRATQKTY FRNNYNYVIR
210 220 230 240 250
AKVKEIKTKC HDVTAVVEVK EILKASLVNI PRETVNLYTS SGCLCPPLNV
260 270 280 290 300
NEEYLIMGYE DEERSRLLLV EGSIAEKWKD RLGKKVKRWD MKLRHLGLNT
310 320
SDSSHSDSTQ SQKPGRNSNS RQARN
Length:325
Mass (Da):36,234
Last modified:February 1, 1997 - v1
Checksum:i39E337A9C6E98BB3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24164 mRNA. Translation: AAC48662.1.
BC112842 mRNA. Translation: AAI12843.1.
RefSeqiNP_776484.1. NM_174059.2.
XP_005202312.1. XM_005202255.2.
XP_005202313.1. XM_005202256.2.
UniGeneiBt.121.

Genome annotation databases

EnsembliENSBTAT00000014572; ENSBTAP00000014572; ENSBTAG00000010977.
GeneIDi281170.
KEGGibta:281170.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24164 mRNA. Translation: AAC48662.1.
BC112842 mRNA. Translation: AAI12843.1.
RefSeqiNP_776484.1. NM_174059.2.
XP_005202312.1. XM_005202255.2.
XP_005202313.1. XM_005202256.2.
UniGeneiBt.121.

3D structure databases

ProteinModelPortaliQ95117.
SMRiQ95117. Positions 33-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000014572.

Protein family/group databases

MEROPSiI93.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000014572; ENSBTAP00000014572; ENSBTAG00000010977.
GeneIDi281170.
KEGGibta:281170.

Organism-specific databases

CTDi2487.

Phylogenomic databases

eggNOGiNOG304384.
GeneTreeiENSGT00760000118864.
HOGENOMiHOG000231879.
HOVERGENiHBG070536.
InParanoidiQ95117.
OMAiEEYLIMG.
OrthoDBiEOG79PJPC.

Miscellaneous databases

NextBioi20805230.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiIPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR026556. SFRP3.
IPR008993. TIMP-like_OB-fold.
[Graphical view]
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF76. PTHR11309:SF76. 1 hit.
PfamiPF01392. Fz. 1 hit.
PF01759. NTR. 1 hit.
[Graphical view]
SMARTiSM00643. C345C. 1 hit.
SM00063. FRI. 1 hit.
[Graphical view]
SUPFAMiSSF50242. SSF50242. 1 hit.
SSF63501. SSF63501. 1 hit.
PROSITEiPS50038. FZ. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure and tissue distribution of FRZB, a novel protein related to Drosophila frizzled, suggest a role in skeletal morphogenesis."
    Hoang B., Moos M. Jr., Vukicevic S., Luyten F.P.
    J. Biol. Chem. 271:26131-26137(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Cartilage.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Kidney.
  3. "The cysteine-rich frizzled domain of Frzb-1 is required and sufficient for modulation of Wnt signaling."
    Lin K., Wang S., Julius M.A., Kitajewski J., Moos M. Jr., Luyten F.P.
    Proc. Natl. Acad. Sci. U.S.A. 94:11196-11200(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF THE FZ DOMAIN WITH WNT PROTEINS.

Entry informationi

Entry nameiSFRP3_BOVIN
AccessioniPrimary (citable) accession number: Q95117
Secondary accession number(s): Q2KHY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: February 1, 1997
Last modified: June 24, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.