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Protein

Frizzled-10-A

Gene

fzd10-a

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Activated by Wnt8. Could have an antagonizing activity in the morphogenesis during development.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein, G-protein coupled receptor, Receptor, Transducer
Biological processWnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Frizzled-10-A
Short name:
Fz-10A
Short name:
Xfz10-A
Gene namesi
Name:fzd10-a
Synonyms:fz10a
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-865370. fzd10.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini27 – 230ExtracellularSequence analysisAdd BLAST204
Transmembranei231 – 251Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini252 – 267CytoplasmicSequence analysisAdd BLAST16
Transmembranei268 – 288Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini289 – 315ExtracellularSequence analysisAdd BLAST27
Transmembranei316 – 336Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini337 – 356CytoplasmicSequence analysisAdd BLAST20
Transmembranei357 – 377Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini378 – 401ExtracellularSequence analysisAdd BLAST24
Transmembranei402 – 422Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini423 – 448CytoplasmicSequence analysisAdd BLAST26
Transmembranei449 – 469Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini470 – 507ExtracellularSequence analysisAdd BLAST38
Transmembranei508 – 528Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini529 – 586CytoplasmicSequence analysisAdd BLAST58

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000001300827 – 586Frizzled-10-AAdd BLAST560

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi40 ↔ 101PROSITE-ProRule annotation
Disulfide bondi48 ↔ 94PROSITE-ProRule annotation
Glycosylationi54N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi85 ↔ 123PROSITE-ProRule annotation
Disulfide bondi112 ↔ 153PROSITE-ProRule annotation
Disulfide bondi116 ↔ 140PROSITE-ProRule annotation
Glycosylationi159N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed in liver, lung, brain, testis, stomach, kidney, eye, skeletal muscle and skin.

Developmental stagei

Expressed from blastula stage, peak expression at late gastrula stage. Expression localizes in neural fold at neurula stage; in the dorsal region of midbrain, hindbrain and spinal cord at tadpole stage.

Structurei

3D structure databases

ProteinModelPortaliQ9DEB5.
SMRiQ9DEB5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 156FZPROSITE-ProRule annotationAdd BLAST122

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi531 – 536Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family membersBy similarity6
Motifi584 – 586PDZ-binding3

Domaini

Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway.By similarity
The FZ domain is involved in binding with Wnt ligands.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG006977.
KOiK02842.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiView protein in InterPro
IPR015526. Frizzled/SFRP.
IPR000539. Frizzled/Smoothened_TM.
IPR020067. Frizzled_dom.
IPR036790. Frizzled_dom_sf.
IPR026549. FZD10.
IPR017981. GPCR_2-like.
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF86. PTHR11309:SF86. 1 hit.
PfamiView protein in Pfam
PF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
PRINTSiPR00489. FRIZZLED.
SMARTiView protein in SMART
SM00063. FRI. 1 hit.
SM01330. Frizzled. 1 hit.
SUPFAMiSSF63501. SSF63501. 1 hit.
PROSITEiView protein in PROSITE
PS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9DEB5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVSGVTGLL RGTALLLVLA AALCSAISSI NPDRSGDGRC QAIEIPMCKD
60 70 80 90 100
IGYNMTRMPN LMGHENQKEA AIQLHEFAPL VEYGCHSHLK FFLCSLYAPM
110 120 130 140 150
CTEQVSTPIP ACRVMCEQAR LKCSPIMEQF NFKWPDSLDC SKLPNKNDPN
160 170 180 190 200
YLCMEAPNNG TDETPRGSSM LPPIFRPQRP SSGHEIYPKD PTSRSSCENS
210 220 230 240 250
GKFHHVEKSA SCAPLCSSSV DVYWSKDDKK FAFIWIAIWS ILCFFSSAFT
260 270 280 290 300
VLTFLVDPLR FKYPERPIIF LSMCYCVYSV GYIIRLFAGA DSIACDRDSG
310 320 330 340 350
QLYVIQEGLE STGCTIVFLI LYYFGMASSL WWVILTLTWF LAAGKKWGHE
360 370 380 390 400
AIEANSSYFH LAAWAIPAVK TIMILVMRRV AGDELTGVCY VGSMDVNALT
410 420 430 440 450
GFVLIPLACY LIIGTSFILS GFVALFHIRR VMKTGGENTD KLEKLMVRIG
460 470 480 490 500
VFSVLYTVPA TCVIACYFYE RLNMDFWKIL ATQDKCKMDS QTKTLDCTMT
510 520 530 540 550
SSIPAVEIFM VKIFMLLVVG ITSGMWIWTS KTVQSWQNVF SKRLKKRNRS
560 570 580
KPASVITSAG IYKKPQHPPK VHHGKYESAL QSPTCV
Length:586
Mass (Da):65,579
Last modified:March 1, 2001 - v1
Checksum:iA71B5BEF5BDCCEA5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB046534 mRNA. Translation: BAB19017.1.
RefSeqiNP_001080925.1. NM_001087456.1.
UniGeneiXl.57146.

Genome annotation databases

GeneIDi387604.
KEGGixla:387604.

Similar proteinsi

Entry informationi

Entry nameiFZ10A_XENLA
AccessioniPrimary (citable) accession number: Q9DEB5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: March 1, 2001
Last modified: October 25, 2017
This is version 93 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. SIMILARITY comments
    Index of protein domains and families