Q9EQD0 (FZD5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Frizzled-5
Short name=Fz-5
Short name=mFz5

Gene names

Name:

Fzd5

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	585 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Plays a role in yolk sac angiogenesis and in placental vascularization. Binds to Wnt2, Wnt10B, Wnt5A, but not to Wnt2B or Wnt4.
Subunit structure	Interacts with GOPC. Ref.8
Subcellular location	Cell membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Note: Localized at the plasma membrane and also found at the Golgi. Ref.8
Tissue specificity	Expressed in eye, kidney, lung, chondrocytes, epithelial cells of the small intestine and gobelet cells of the colon. Ref.7
Developmental stage	Expressed in the yolk sac, placenta, eye and lung bud at 9.5 dpc. At 10.5 dpc, also expressed in the placental blood vessel of embryonic origin.
Domain	The PDZ-binding motif mediates interaction with GOPC By similarity. The FZ domain is involved in binding with Wnt ligands By similarity.
Post-translational modification	Ubiquitinated by RNF43 and ZNRF3, leading to its degradation by the proteasome By similarity.
Sequence similarities	Belongs to the G-protein coupled receptor Fz/Smo family. Contains 1 FZ (frizzled) domain.
Sequence caution	The sequence AAG39355.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	Angiogenesis Differentiation Wnt signaling pathway
Cellular component	Cell membrane Golgi apparatus Membrane
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Spemann organizer formation Inferred from electronic annotation. Source: Compara T cell differentiation in thymus Inferred from mutant phenotype PubMed 11265645. Source: MGI Wnt receptor signaling pathway involved in dorsal/ventral axis specification Inferred from electronic annotation. Source: Compara angiogenesis Inferred from mutant phenotype Ref.1. Source: MGI anterior/posterior axis specification, embryo Inferred from electronic annotation. Source: Compara apoptotic process involved in morphogenesis Inferred from mutant phenotype PubMed 18791178. Source: MGI axonogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome brain development Inferred from Biological aspect of Ancestor. Source: RefGenome canonical Wnt receptor signaling pathway Inferred from mutant phenotype PubMed 11265645. Source: MGI cell maturation Inferred from mutant phenotype PubMed 15778706. Source: MGI cellular response to molecule of bacterial origin Inferred from electronic annotation. Source: Compara embryonic camera-type eye development Inferred from mutant phenotype PubMed 18791178. Source: MGI gonad development Inferred from Biological aspect of Ancestor. Source: RefGenome labyrinthine layer blood vessel development Inferred from mutant phenotype Ref.1. Source: MGI negative regulation of cell proliferation Inferred from mutant phenotype PubMed 18791178. Source: MGI positive regulation of JUN kinase activity Inferred from direct assay PubMed 15195140. Source: MGI positive regulation of interferon-gamma production Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara post-embryonic camera-type eye development Inferred from mutant phenotype PubMed 18791178. Source: MGI regulation of transcription from RNA polymerase II promoter Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	Golgi apparatus Inferred from direct assay Ref.8. Source: BHF-UCL Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell projection Inferred from Biological aspect of Ancestor. Source: RefGenome cell surface Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW perinuclear region of cytoplasm Inferred from direct assay Ref.8. Source: BHF-UCL plasma membrane Inferred from direct assay Ref.8. Source: BHF-UCL
Molecular_function	G-protein coupled receptor activity Inferred from electronic annotation. Source: UniProtKB-KW PDZ domain binding Inferred from Biological aspect of Ancestor. Source: RefGenome Wnt-activated receptor activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26	Potential
	Chain	27 – 585	559	Frizzled-5		PRO_0000243936
Regions
	Topological domain	27 – 238	212	Extracellular Potential
	Transmembrane	239 – 259	21	Helical; Name=1; Potential
	Topological domain	260 – 270	11	Cytoplasmic Potential
	Transmembrane	271 – 291	21	Helical; Name=2; Potential
	Topological domain	292 – 315	24	Extracellular Potential
	Transmembrane	316 – 336	21	Helical; Name=3; Potential
	Topological domain	337 – 358	22	Cytoplasmic Potential
	Transmembrane	359 – 379	21	Helical; Name=4; Potential
	Topological domain	380 – 402	23	Extracellular Potential
	Transmembrane	403 – 423	21	Helical; Name=5; Potential
	Topological domain	424 – 449	26	Cytoplasmic Potential
	Transmembrane	450 – 470	21	Helical; Name=6; Potential
	Topological domain	471 – 500	30	Extracellular Potential
	Transmembrane	501 – 521	21	Helical; Name=7; Potential
	Topological domain	522 – 585	64	Cytoplasmic Potential
	Domain	28 – 150	123	FZ
	Motif	582 – 584	3	PDZ-binding By similarity
Amino acid modifications
	Glycosylation	47	1	N-linked (GlcNAc...) Potential
	Glycosylation	151	1	N-linked (GlcNAc...) Potential
	Disulfide bond	33 ↔ 94		By similarity
	Disulfide bond	41 ↔ 87		By similarity
	Disulfide bond	78 ↔ 116		By similarity
	Disulfide bond	105 ↔ 147		By similarity
	Disulfide bond	109 ↔ 133		By similarity
Experimental info
	Sequence conflict	4	1	P → T in BAC26789. Ref.3
	Sequence conflict	123 – 124	2	YG → S in BAC53981. Ref.2
	Sequence conflict	402	1	G → S in AAG39355. Ref.1
	Sequence conflict	419	1	L → H in BAC53981. Ref.2
	Sequence conflict	444	1	E → G in BAC53981. Ref.2
	Sequence conflict	477	1	S → T in AAG39355. Ref.1
	Sequence conflict	481	1	A → P in AAG39355. Ref.1
	Sequence conflict	489	1	P → T in AAG39355. Ref.1
	Sequence conflict	521	1	I → F in BAC53981. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9EQD0 [UniParc]. Last modified October 3, 2012. Version 3. Checksum: 5FC03620AF087733	FASTA	585	64,138
	10 20 30 40 50 60 MARPDPSAPP SLLLLLLAQL VGRAAAASKA PVCQEITVPM CRGIGYNLTH MPNQFNHDTQ 70 80 90 100 110 120 DEAGLEVHQF WPLVEIHCSP DLRFFLCSMY TPICLPDYHK PLPPCRSVCE RAKAGCSPLM 130 140 150 160 170 180 RQYGFAWPER MSCDRLPVLG GDAEVLCMDY NRSEATTASP KSFPAKPTLP GPPGAPSSGG 190 200 210 220 230 240 ECPSGGPSVC TCREPFVPIL KESHPLYNKV RTGQVPNCAV PCYQPSFSPD ERTFATFWIG 250 260 270 280 290 300 LWSVLCFIST STTVATFLID MERFRYPERP IIFLSACYLC VSLGFLVRLV VGHASVACSR 310 320 330 340 350 360 EHSHIHYETT GPALCTVVFL LVYFFGMASS IWWVILSLTW FLAAGMKWGN EAIAGYAQYF 370 380 390 400 410 420 HLAAWLIPSV KSITALALSS VDGDPVAGIC YVGNQNLNSL RGFVLGPLVL YLLVGTLFLL 430 440 450 460 470 480 AGFVSLFRIR SVIKQGGTKT DKLEKLMIRI GIFTLLYTVP ASIVVACYLY EQHYRESWEA 490 500 510 520 530 540 ALTCACPGPD AGQPRAKPEY WVLMLKYFMC LVVGITSGVW IWSGKTLESW RRFTSRCCCS 550 560 570 580 SRRGHKSGGA MAAGDYAEAS AALTGRTGPP GPTAAYHKQV SLSHV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mouse Wnt receptor gene Fzd5 is essential for yolk sac and placental angiogenesis." Ishikawa T., Tamai Y., Zorn A.M., Yoshida H., Seldin M.F., Nishikawa S., Taketo M.M. Development 128:25-33(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6N. Tissue: Intestine.
[2]	"Molecular cloning and characterization of a gene encoding for rat Frizzled 5." Ito S., Imamura T., Shiota K. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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. , 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: Testis.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Johnson M.A., Greenberg N.M. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 211-300. Strain: C57BL/6. Tissue: Prostate.
[7]	"A large family of putative transmembrane receptors homologous to the product of the Drosophila tissue polarity gene frizzled." Wang Y., Macke J.P., Abella B.S., Andreasson K., Worley P., Gilbert D.J., Copeland N.G., Jenkins N.A., Nathans J. J. Biol. Chem. 271:4468-4476(1996) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"Identification of a PDZ domain containing Golgi protein, GOPC, as an interaction partner of frizzled." Yao R., Maeda T., Takada S., Noda T. Biochem. Biophys. Res. Commun. 286:771-778(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GOPC, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF272146 mRNA. Translation: AAG39355.1. Frameshift. AB052910 mRNA. Translation: BAC53981.1. AK030111 mRNA. Translation: BAC26789.1. AC101915 Genomic DNA. No translation available. CH466548 Genomic DNA. Translation: EDL00208.1. CH466548 Genomic DNA. Translation: EDL00209.1. AF005203 mRNA. Translation: AAC01953.1.
IPI	IPI00318553.
RefSeq	NP_001036124.1. NM_001042659.1. NP_073558.2. NM_022721.3.
UniGene	Mm.150813. Mm.470210.
3D structure databases
ProteinModelPortal	Q9EQD0.
SMR	Q9EQD0. Positions 33-149.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-41260N.
MINT	MINT-1783095.
STRING	10090.ENSMUSP00000067783.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	Q9EQD0.
Proteomic databases
PRIDE	Q9EQD0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000063982; ENSMUSP00000067783; ENSMUSG00000045005. ENSMUST00000116133; ENSMUSP00000111828; ENSMUSG00000045005.
GeneID	14367.
KEGG	mmu:14367.
Organism-specific databases
CTD	7855.
MGI	MGI:108571. Fzd5.
Phylogenomic databases
eggNOG	NOG257258.
GeneTree	ENSGT00660000095421.
HOGENOM	HOG000233236.
HOVERGEN	HBG006977.
InParanoid	Q9EQD0.
KO	K02375.
OMA	PVCQEIT.
OrthoDB	EOG4FFD1K.
Gene expression databases
CleanEx	MM_FZD5.
Genevestigator	Q9EQD0.
Family and domain databases
Gene3D	1.10.2000.10. 1 hit.
InterPro	IPR000539. Frizzled. IPR015526. Frizzled/SFRP. IPR020067. Frizzled_dom. IPR026547. FZD5. IPR017981. GPCR_2-like. [Graphical view]
PANTHER	PTHR11309. PTHR11309. 1 hit. PTHR11309:SF29. PTHR11309:SF29. 1 hit.
Pfam	PF01534. Frizzled. 1 hit. PF01392. Fz. 1 hit. [Graphical view]
PRINTS	PR00489. FRIZZLED.
SMART	SM00063. FRI. 1 hit. [Graphical view]
SUPFAM	SSF63501. Frizzled_Cys-rich. 1 hit.
PROSITE	PS50038. FZ. 1 hit. PS50261. G_PROTEIN_RECEP_F2_4. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	285839.
SOURCE	Search...

Entry information

Entry name

FZD5_MOUSE

Accession

Primary (citable) accession number: Q9EQD0
Secondary accession number(s): G5E8F0 , O08975, Q8BMR2, Q8CHK9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	October 3, 2012
Last modified:	May 1, 2013
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program