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Entry version 74 (18 Sep 2019)
Sequence version 1 (14 Dec 2011)
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Protein

Frizzled-2

Gene

cfz-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Receptor for Wnt proteins (PubMed:19855022, PubMed:20711352). Most 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 (Probable). Required for the migration and axon formation and guidance of different neuronal cell types including canal-associated neurons (CAN), hermaphrodite-specific neurons (HSN), anterior lateral microtubule neurons (ALM), and the right Q neuroblast (QR) and its descendants (PubMed:16109397). Directs ALM migration through frizzled protein mom-5 and Wnt ligands cwn-1, cwn-2 and egl-20 (PubMed:16109397). May act redundantly with mom-5 to direct CAN migration (PubMed:16109397). Plays a role in the organization of head ganglion cells (PubMed:16109397). Probably by acting as a receptor for Wnt ligand cwn-2, plays a role in the positioning of the nerve ring and may in addition positively regulate the neurite outgrowth of RME GABAergic motor neurons along the anterior-posterior axis of the body (PubMed:19855022, PubMed:20711352).Curated3 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-4086398 Ca2+ pathway
R-CEL-4608870 Asymmetric localization of PCP proteins
R-CEL-4641262 Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-CEL-5140745 WNT5A-dependent internalization of FZD2, FZD5 and ROR2

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Frizzled-2Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:cfz-2Imported
ORF Names:F27E11.3Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCaenorhabditis elegansImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri6239 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001940 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome V

Organism-specific databases

WormBase

More...
WormBasei
F27E11.3 ; CE39149 ; WBGene00000478 ; cfz-2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini18 – 236ExtracellularCuratedAdd BLAST219
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei237 – 257Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini258 – 268CytoplasmicCuratedAdd BLAST11
Transmembranei269 – 289Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini290 – 312ExtracellularCuratedAdd BLAST23
Transmembranei313 – 333Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini334 – 354CytoplasmicCuratedAdd BLAST21
Transmembranei355 – 375Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini376 – 398ExtracellularCuratedAdd BLAST23
Transmembranei399 – 419Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini420 – 449CytoplasmicCuratedAdd BLAST30
Transmembranei450 – 470Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini471 – 497ExtracellularCuratedAdd BLAST27
Transmembranei498 – 518Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini519 – 578CytoplasmicCuratedAdd BLAST60

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Displaced anterior nerve ring and neuronal cell migration defects including irregular localization of canal-associated neurons (CAN), hermaphrodite-specific neurons (HSN), anterior lateral microtubule neurons (ALM), and the right (but not the left) Q neuroblast (QR) and its descendants (PubMed:16109397, PubMed:9851916). Axon growth and guidance defects whereby some HSN, male CP neurons and CAN extend ectopic axons or branches, and furthermore some HSN irregularly route towards the ventral midline of the body (PubMed:16109397). Disorganized cells of the anterior ganglion which are normally compacted together when they form the head ganglion in wild-type animals (PubMed:16109397). Double knockout with mom-5 or cwn-2 results in enhanced CAN migration defects (PubMed:16109397). Double knockout with Wnt ligands cwn-1, cwn-2, egl-20 or frizzled protein mom-5 rescues the ALM migration defects in the single cfz-2 knockout (PubMed:16109397). Triple knockout with cwn-1 and cwn-2 results in enhanced neuronal cell migratory defects (PubMed:16109397).2 Publications

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 17Sequence analysisAdd BLAST17
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_500766123818 – 578Frizzled-2CuratedAdd BLAST561

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi25 ↔ 86PROSITE-ProRule annotation
Disulfide bondi33 ↔ 79PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi39N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi70 ↔ 108PROSITE-ProRule annotation
Disulfide bondi97 ↔ 141PROSITE-ProRule annotation
Disulfide bondi101 ↔ 125PROSITE-ProRule annotation
Glycosylationi213N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
G5ECQ2

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
G5ECQ2

PeptideAtlas

More...
PeptideAtlasi
G5ECQ2

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in two pairs of head neurons and throughout the pharynx.1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

First expressed at the 100-cell stage of embryogenesis. During embryonic elongation, expressed in anterior, posterior and midbody cells of the embryo and in cellular projections. At hatching, expression is restricted to a few cells in the head and a pair of cells in the tail.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00000478 Expressed in 4 organ(s), highest expression level in pharyngeal muscle cell (C elegans)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

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IntActi
G5ECQ2, 11 interactors

STRING: functional protein association networks

More...
STRINGi
6239.F27E11.3a

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
G5ECQ2

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini20 – 144FZPROSITE-ProRule annotationAdd BLAST125

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi522 – 527Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family membersBy similarity6
Motifi556 – 558PDZ-bindingSequence analysis3

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3577 Eukaryota
ENOG410XRC8 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000166857

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000233236

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
G5ECQ2

KEGG Orthology (KO)

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KOi
K02375

Identification of Orthologs from Complete Genome Data

More...
OMAi
VEIHCSP

Database of Orthologous Groups

More...
OrthoDBi
509772at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
G5ECQ2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.2000.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR015526 Frizzled/SFRP
IPR000539 Frizzled/Smoothened_TM
IPR020067 Frizzled_dom
IPR036790 Frizzled_dom_sf
IPR017981 GPCR_2-like

The PANTHER Classification System

More...
PANTHERi
PTHR11309 PTHR11309, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01534 Frizzled, 1 hit
PF01392 Fz, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00489 FRIZZLED

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00063 FRI, 1 hit
SM01330 Frizzled, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF63501 SSF63501, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50038 FZ, 1 hit
PS50261 G_PROTEIN_RECEP_F2_4, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

G5ECQ2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLLRISVLFL LLGSCGALFG KRQKCEQITI PLCKGIGYNM TSFPNSYGHE
60 70 80 90 100
KQEEAGLEVH QFYPLVEVGC FQHLKFFLCT MYTPICQENY DKPILPCMEL
110 120 130 140 150
CVEARSKCSP IMAKYGFRWP ETLSCEALPK MSDQMSTGNI CAAPPDTPKK
160 170 180 190 200
QHKGHHHKNQ NQNQNQNHNY SPDGPEVGIS KIDNEVIAGP SECQCTCNQP
210 220 230 240 250
FQFVASEKSK VGNVTNCAYS CHSPALAESH SLVSNWMAFW SITCCVLASF
260 270 280 290 300
TFLTFLIETD RFQYPERPIF MLAFCQLMVA VGFMIRYFVG HEEIACDSMR
310 320 330 340 350
IKGADDNSGS LCFVVFLLTY FFGMAASVWW VILSLTWVLS AASKWSPEAI
360 370 380 390 400
SSFSFHFHVV GWCLPAIQTV LVIVFNAIDG DPITGICYVG NTDLQFQRIF
410 420 430 440 450
VLFPLLVYFI VGVLFLVIGF CNLWSIRNEV QKQHPSLESA HKITQLMSKI
460 470 480 490 500
GIFSLLYTIP SLLIICVLFY EQNHRSLWEQ SQLCSCSPKQ TIGDSSLIIS
510 520 530 540 550
LIKTCCMCIL GWTSGFWVCS TKTLSSWKNA ICCLGSSRSL PKYQPADILY
560 570
AKSDMSSSQF YNTSLRHNHL YGGIPDKL
Length:578
Mass (Da):65,025
Last modified:December 14, 2011 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3B2A3666A8DB3596
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA84678 differs from that shown. Reason: Erroneous gene model prediction.1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
DQ178242 mRNA Translation: ABA18181.1
BX284605 Genomic DNA Translation: CCD62501.1
AB026113 Genomic DNA Translation: BAA84678.1 Sequence problems.

Protein sequence database of the Protein Information Resource

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PIRi
T37325

NCBI Reference Sequences

More...
RefSeqi
NP_503965.2, NM_071564.5

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
F27E11.3.1; F27E11.3.1; WBGene00000478

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
178768

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cel:CELE_F27E11.3

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ178242 mRNA Translation: ABA18181.1
BX284605 Genomic DNA Translation: CCD62501.1
AB026113 Genomic DNA Translation: BAA84678.1 Sequence problems.
PIRiT37325
RefSeqiNP_503965.2, NM_071564.5

3D structure databases

SMRiG5ECQ2
ModBaseiSearch...

Protein-protein interaction databases

IntActiG5ECQ2, 11 interactors
STRINGi6239.F27E11.3a

Protein family/group databases

Information system for G protein-coupled receptors (GPCRs)

More...
GPCRDBi
Search...

Proteomic databases

EPDiG5ECQ2
PaxDbiG5ECQ2
PeptideAtlasiG5ECQ2

Genome annotation databases

EnsemblMetazoaiF27E11.3.1; F27E11.3.1; WBGene00000478
GeneIDi178768
KEGGicel:CELE_F27E11.3

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
178768
WormBaseiF27E11.3 ; CE39149 ; WBGene00000478 ; cfz-2

Phylogenomic databases

eggNOGiKOG3577 Eukaryota
ENOG410XRC8 LUCA
GeneTreeiENSGT00940000166857
HOGENOMiHOG000233236
InParanoidiG5ECQ2
KOiK02375
OMAiVEIHCSP
OrthoDBi509772at2759
PhylomeDBiG5ECQ2

Enzyme and pathway databases

ReactomeiR-CEL-4086398 Ca2+ pathway
R-CEL-4608870 Asymmetric localization of PCP proteins
R-CEL-4641262 Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-CEL-5140745 WNT5A-dependent internalization of FZD2, FZD5 and ROR2

Miscellaneous databases

Protein Ontology

More...
PROi
PR:G5ECQ2

Gene expression databases

BgeeiWBGene00000478 Expressed in 4 organ(s), highest expression level in pharyngeal muscle cell (C elegans)

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
IPR017981 GPCR_2-like
PANTHERiPTHR11309 PTHR11309, 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFRIZ2_CAEEL
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: G5ECQ2
Secondary accession number(s): Q9U8U6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 2, 2016
Last sequence update: December 14, 2011
Last modified: September 18, 2019
This is version 74 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
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