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0CELR3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCELSR3
DescriptionCadherin egf lag seven-pass g-type receptor 3 precursor (flamingo homolog 1) (hfmi1) (multiple epidermal growth factor-like domains 2) (epidermal growth factor-like 1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016021 integral to membrane (TAS)
0004930 G-protein coupled receptor activity (TAS)
0005198 structural molecule activity (NAS)
0007186 G-protein coupled receptor protein signalin... (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains assigned to SynO:
Laminins are large heterotrimeric glycoproteins involved in basement membrane function . The laminin globular (G) domain can be found in one to several copies in various laminin family members.ncluding a large number of extracellular proteins. The C-terminus of the laminin alpha chain contains a tandem repeat of five laminin G domains.hich are critical for heparin-binding and cell attachment activity . Laminin alpha4 is distributed in a variety of tissues including peripheral nerves.orsal root ganglion.keletal muscle and capillaries; in the neuromuscular junction.t is required for synaptic specialisation . The structure of the laminin-G domain has been predicted to resemble that of pentraxin .Laminin G domains can vary in their function.nd a variety of binding functions have been ascribed to different LamG modules. For example.he laminin alpha1 and alpha2 chains each have five C-teminal laminin G domains.here only domains LG4 and LG5 contain binding sites for heparin.ulphatides and the cell surface receptor dystroglycan . Laminin G-containing proteins appear to have a wide variety of roles in cell adhesion.ignalling.igration.ssembly and differentiation. Proteins with laminin-G domains include:Laminin.Merosin.Agrin.Neurexins.Vitamin K dependent protein S.Sex steroid binding protein SBP/SHBG.Drosophila proteins Slit.rumbs.at.several proteoglycan precursors.
  IPR001791:Laminin G
InterPro domains unassigned to SynO:
G-protein-coupled receptors.PCRs.onstitute a vast protein family that encompasses a wide range of functions (including various autocrine.aracrine and endocrine processes). They show considerable diversity at the sequence level.n the basis of which they can be separated into distinct groups. We use the term clan to describe the GPCRs.s they embrace a group of families for which there are indications of evolutionary relationship.ut between which there is no statistically significant similarity in sequence . The currently known clan members include the rhodopsin-like GPCRs.he secretin-like GPCRs.he cAMP receptors.he fungal mating pheromone receptors.nd the metabotropic glutamate receptor family. There is a specialized database for GPCRs: http://www.gpcr.org/7tm/. The secretin-like GPCRs include secretin .alcitonin .arathyroid hormone/parathyroid hormone-related peptides and vasoactive intestinal peptide .ll of which activate adenylyl cyclase and the phosphatidyl-inositol-calcium pathway. The amino acid sequences of the receptors contain high proportions of hydrophobic residues grouped into 7 domains.n a manner reminiscent of the rhodopsins and other receptors believed to interact with G-proteins. However.hile a similar 3D framework has been proposed to account for this.here is no significant sequence identity between these families: the secretin-like receptors thus bear their own unique 7TM signature.
  IPR000832:GPCR, family 2, secretin-like
Laminins are large heterotrimeric glycoproteins involved in basement membrane function . The laminin globular (G) domain can be found in one to several copies in various laminin family members.ncluding a large number of extracellular proteins. The C-terminus of the laminin alpha chain contains a tandem repeat of five laminin G domains.hich are critical for heparin-binding and cell attachment activity . Laminin alpha4 is distributed in a variety of tissues including peripheral nerves.orsal root ganglion.keletal muscle and capillaries; in the neuromuscular junction.t is required for synaptic specialisation . The structure of the laminin-G domain has been predicted to resemble that of pentraxin . Laminin G domains can vary in their function.nd a variety of binding functions have been ascribed to different LamG modules. For example.he laminin alpha1 and alpha2 chains each have five C-teminal laminin G domains.here only domains LG4 and LG5 contain binding sites for heparin.ulphatides and the cell surface receptor dystroglycan . Laminin G-containing proteins appear to have a wide variety of roles in cell adhesion.ignalling.igration.ssembly and differentiation. This entry represents one subtype of laminin G domains.hich is sometimes found in association with thrombospondin-type laminin G domains ().
  IPR012680:Laminin G, subdomain 2
Cadherins are a family of adhesion molecules that mediate Ca2+-dependent cell-cell adhesion in all solid tissues of the organism which modulate a wide variety of processes including cell polarisation and migration . Cadherin-mediated cell-cell junctions are formed as a result of interaction between extracellular domains of identical cadherins.hich are located on the membranes of the neighbouring cells. The stability of these adhesive junctions is ensured by binding of the intracellular cadherin domain with the actin cytoskeleton. There are a number of different isoforms distributed in a tissue-specific manner in a wide variety of organisms. Cells containing different cadherins tend to segregate in vitro.hile those that contain the same cadherins tend to preferentially aggregate together. This observation is linked to the finding that cadherin expression causes morphological changes involving the positional segregation of cells into layers.uggesting they may play an important role in the sorting of different cell types during morphogenesis.istogenesis and regeneration. They may also be involved in the regulation of tight and gap junctions.nd in the control of intercellular spacing. Cadherins are evolutionary related to the desmogleins which are component of intercellular desmosome junctions involved in the interaction of plaque proteins.Structurally.adherins comprise a number of domains: classically.hese include a signal sequence; a propeptide of around 130 residues; a single transmembrane domain and five tandemly repeated extracellular cadherin domains. of which are cadherin repeats.nd the fifth contains 4 conserved cysteines and a N-terminal cytoplasmic domain . However.roteins are designated as members of the broadly defined cadherin family if they have one or more cadherin repeats. A cadherin repeat is an independently folding sequence of approximately 110 amino acids that contains motifs with the conserved sequences DRE.XNDNAPXF.nd DXD. Crystal structures have revealed that multiple cadherin domains form Ca2+-dependent rod-like structures with a conserved Ca2+-binding pocket at thedomain-domain interface. Cadherins depend on calcium for their function: calcium ions bind to specific residues in each cadherin repeat to ensure its proper folding.o confer rigidity upon the extracellular domain and is essential for cadherin adhesive function and for protection against protease digestion.
  IPR002126:Cadherin
This domain has been termed the GPS domain (for GPCR proteolytic site).ecause it contains a cleavage site in latrophilin . However this region in latrophilin is found in many otherwise unrelated cell surface receptors . There is no evidence currently that this domain provides a cleavage site in any of the other receptors. However the peptide bond that is cleaved in latrophilin is between Leu and Thr residues that are conserved in some of the other receptors GPS domains are about 50 residues long and contain either 2 or 4 cysteine residues that are likely to form disulphide bridges. Based on conservation of these cysteines the following pairing can be predicted.
  IPR000203:GPS
This domain is found in the extracellular part of some hormone receptors including the calcitonin receptor; corticotropin releasing factor receptor 1; diuretic hormone receptor; glucagon-like peptide 1 receptor; and parathyroid hormone peptide receptor.
  IPR001879:Hormone receptor, extracellular
Laminins are the major noncollagenous components of basement membranesthat mediate cell adhesion.rowth migration.nd differentiation. They arecomposed of distinct but related alpha.eta and gamma chains. The threechains form a cross-shaped molecule that consist of a long arm and three shortglobular arms. The long arm consist of a coiled coil structure contributed byall three chains and cross-linked by interchain disulphide bonds.Beside different types of globular domains each subunit contains.n its firsthalf.onsecutive repeats of about 60 amino acids in length that include eightconserved cysteines . The tertiary structure .f this domain isremotely similar in its N-terminal to that of the EGF-like module (see ). It is known as a LE or laminin-type EGF-like domain. Thenumber of copies of the LE domain in the different forms of laminins is highlyvariable; from 3 up to 22 copies have been found.A schematic representation of the topology of the four disulphide bonds inthe LE domain is shown below.In mouse laminin gamma-1 chain.he seventh LE domain has been shown to be theonly one that binds with a high affinity to nidogen . The binding-sites arelocated on the surface within the loops C1-C3 and C5-C6 . Longconsecutive arrays of LE domains in laminins form rod-like elements of limitedflexibility .hich determine the spacing in the formation of lamininnetworks of basement membranes .
  IPR002049:EGF-like, laminin
A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF)has been shown to be present.n a moreor less conserved form.n a large number of other.ostly animal proteins. The list of proteins currently known tocontain one or more copies of an EGF-like pattern is large and varied. The functional significance of EGF domains inwhat appear to be unrelated proteins is not yet clear. However. common feature is that these repeats are found inthe extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandinG/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphidebonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet.Subdomains between the conserved cysteines vary in length.
  IPR006209:EGF-like
Epidermal growth factors and transforming growth factors belong to a general class of proteins that share a repeat pattern involving a number of conserved Cys residues. Growth factors are involved in cell recognition and division . The repeating pattern.specially of cysteines (the so-called EGF repeat).s thought to be important to the 3D structure of the proteins.nd hence its recognition by receptors and other molecules. The type 1 EGF signature includes six conserved cysteines believed to be involved in disulphide bond formation. The EGF motif is found frequently in nature.articularly in extracellular proteins.
  IPR006210:EGF
Lectins and glucanases exhibit the common property of reversibly binding to specific complex carbohydrates. The lectins/glucanases are a diverse group of proteins found in a wide range of species from prokaryotes to humans. The different family members all contain a concanavalin A-like domain.hich consists of a sandwich of 12-14 beta strands in two sheets with a complex topology. Members of this family are diverse.nd include the lectins: legume lectins.ereal lectins.iral lectins.nd animal lectins. Plant lectins function in the storage and transport of carbohydrates in seeds.he binding of nitrogen-fixing bacteria to root hairs.he inhibition of fungal growth or insect feeding.nd in hormonally regulated plant growth . Protein members include concanavalin A (Con A).avin.solectin I.ectin IV.oybean agglutinin and lentil lectin. Animal lectins include the galectins.hich are S-type lactose-binding and IgE-binding proteins such as S-lectin.LC protein.alectin1.alectin2.alectin3 CRD.nd Congerin I . Other members with a Con A-like domain include the glucanases and xylanases. Bacterial and fungal beta-glucanases.uch as Bacillus 1-3.-4-beta-glucanse.arry out the acid catalysis of beta-glucans found in microorganisms and plants . Similarly.appa-Carrageenase degrades kappa-carrageenans from marine red algae cell walls . Xylanase and cellobiohydrolase I degrade hemicellulose and cellulose.espectively . There are many Con A-like domains found in proteins involved in cell recognition and adhesion. For example.everal viral and bacterial toxins carry Con A-like domains. Examples include the Clostridium neurotoxins responsible for the neuroparalytic effects of botulism and tetanus . The Pseudomonas exotoxin A. virulence factor which is highly toxic to eukaryotic cells.ausing the arrest of protein synthesis.ontains a Con A-like domain involved in receptor binding . Cholerae neuraminidase can bind to cell surfaces.ossibly through their Con A-like domains.here they function as part of a mucinase complex to degrade the mucin layer of the gastrointestinal tract . The rotaviral outer capsid protein.P4.as a Con A-like sialic acid binding domain.hich functions in cell attachment and membrane penetration . Con A-like domains also play a role in cell recognition in eukaryotes. Proteins containing a Con A-like domain include the sex hormone-binding globulins which transport sex steroids in blood and regulate their access to target tissues .aminins which are large heterotrimeric glycoproteins involved in basement membrane architecture and function .eurexins which are expressed in hundreds of isoforms on the neuronal cell surface.here they may function as cell recognition molecules and sialidases that are found in both microorganisms and animals.nd function in cell adhesion and signal transduction . Other proteins containing a Con A-like domain include pentraxins and calnexins. The pentraxin PTX3 is a TNFalpha-induced.ecreted protein of adipose cells produced during inflammation . The calnexin family of molecular chaperones is conserved among plants.ungi.nd animals. Family members include Calnexin. type-I integral membrane protein in the endoplasmic reticulum which coordinates the processing of newly synthesized N-linked glycoproteins with their productive folding.almegin. type-I membrane protein expressed mainly in the spermatids of the testis.nd calreticulin. soluble ER lumenal paralog .
  IPR008985:Concanavalin A-like lectin/glucanase
Lectins and glucanases exhibit the common property of reversibly binding to specific complex carbohydrates. The lectins/glucanases are a diverse group of proteins found in a wide range of species from prokaryotes to humans. The different family members all contain a concanavalin A-like domain.hich consists of a sandwich of 12-14 beta strands in two sheets with a complex topology. Members of this family are diverse.nd include the lectins: legume lectins.ereal lectins.iral lectins.nd animal lectins. Plant lectins function in the storage and transport of carbohydrates in seeds.he binding of nitrogen-fixing bacteria to root hairs.he inhibition of fungal growth or insect feeding.nd in hormonally regulated plant growth . Protein members include concanavalin A (Con A).avin.solectin I.ectin IV.oybean agglutinin and lentil lectin. Animal lectins include the galectins.hich are S-type lactose-binding and IgE-binding proteins such as S-lectin.LC protein.alectin1.alectin2.alectin3 CRD.nd Congerin I . Other members with a Con A-like domain include the glucanases. Bacterial and fungal beta-glucanases.uch as Bacillus 1-3.-4-beta-glucanse.arry out the acid catalysis of beta-glucans found in microorganisms and plants . Similarly.appa-Carrageenase degrades kappa-carrageenans from marine red algae cell walls . This entry differs from () by omitting the xylanases and glycosyl hydrolases.
  IPR013320:Concanavalin A-like lectin/glucanase, subgroup
IPR000832:7tm_2 
Evalue:-91.1739273071289 
Location:2536-2778IPR012680:Laminin_G_2 
Evalue:-37.8538703918457 
Location:1543-1702IPR002126:CA 
Evalue:-31.3665315444204 
Location:673-754IPR002126:CA 
Evalue:-29.3467874862247 
Location:455-543IPR002126:Cadherin 
Evalue:-29.236572265625 
Location:550-642IPR002126:CA 
Evalue:-27.9208187539524 
Location:983-1065IPR002126:CA 
Evalue:-27.2924298239021 
Location:880-959IPR002126:CA 
Evalue:-26.7695510786217 
Location:347-431IPR002126:Cadherin 
Evalue:-23.443696975708 
Location:1072-1160IPR000203:GPS 
Evalue:-22.5686359405518 
Location:2476-2529IPR001791:LamG 
Evalue:-22.2518119729938 
Location:1785-1924IPR002126:Cadherin 
Evalue:-20.1674919128418 
Location:761-849IPR001879:HRM 
Evalue:-19.6382713317871 
Location:2126-2183IPR006209:EGF 
Evalue:-9.26760578155518 
Location:1726-1757IPR006209:EGF 
Evalue:-8.38721656799316 
Location:1985-2019IPR002049:Laminin_EGF 
Evalue:-8.28399658203125 
Location:2077-2110IPR006209:EGF 
Evalue:-8.187087059021 
Location:1479-1513IPR006209:EGF 
Evalue:-7.36653137207031 
Location:1439-1470IPR006209:EGF 
Evalue:-5.67778062820435 
Location:1950-1981IPR006209:EGF 
Evalue:-3.44369745254517 
Location:1379-1432IPR002126:Cadherin 
Evalue:-1.20760834217072 
Location:1179-1266IPR002126:CADHERIN 
Evalue:0 
Location:856-869IPR008985:ConA_like_lec_gl 
Evalue:0 
Location:5-14IPR000832:G_PROTEIN_RECEP_F2_1 
Evalue:0 
Location:0-0
SequencesProtein: CELR3_HUMAN (3312 aa)
mRNA: AY714129 NM_001407
Local Annotation
Synapse Ontology
all
sdb:0004 Presynaptic compartment  (Evidence:domains)
Any process that modulates the physical form of a synapse, the junction between a neuron and a target (neuron, muscle, or secretory cell).
sdb:0033 regulation of synapse structure  (Evidence:domains)
The formation of a synapse.
sdb:0034 synaptogenesis  (Evidence:domains)
KO assignmentK04602
  Level 3 annotation:
    cadherin, EGF LAG seven-pass G-type receptor 3 (flamingo)
  Level 2 annotation:
    G-protein coupled receptors
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 47 residues, 48637834-48637972Exon2: 47 residues, 48638654-48638791Exon3: 20 residues, 48639067-48639122Exon4: 67 residues, 48639312-48639509Exon5: 44 residues, 48640851-48640978Exon6: 33 residues, 48641058-48641151Exon7: 25 residues, 48642078-48642148Exon8: 37 residues, 48642308-48642415Exon9: 34 residues, 48642498-48642594Exon10: 28 residues, 48642874-48642952Exon11: 40 residues, 48643043-48643157Exon12: 51 residues, 48643429-48643577Exon13: 29 residues, 48643660-48643743Exon14: 53 residues, 48644085-48644238Exon15: 57 residues, 48644316-48644481Exon16: 52 residues, 48644681-48644833Exon17: 13 residues, 48645072-48645105Exon18: 39 residues, 48645410-48645521Exon19: 48 residues, 48645687-48645827Exon20: 55 residues, 48645913-48646072Exon21: 297 residues, 48652110-48652996Exon22: 69 residues, 48653760-48653961Exon23: 55 residues, 48654287-48654446Exon24: 38 residues, 48654794-48654904Exon25: 51 residues, 48655172-48655321Exon26: 41 residues, 48655403-48655520Exon27: 44 residues, 48655990-48656117Exon28: 28 residues, 48656652-48656732Exon29: 39 residues, 48657152-48657265Exon30: 60 residues, 48657471-48657646Exon31: 98 residues, 48657798-48658086Exon32: 44 residues, 48658178-48658305Exon33: 58 residues, 48658526-48658694Exon34: 57 residues, 48659199-48659365Exon35: 54 residues, 48660277-48660433Exon36: 67 residues, 48660702-48660898Exon37: 72 residues, 48661155-48661365Exon38: 33 residues, 48661557-48661652Exon39: 36 residues, 48662916-48663018Exon40: 63 residues, 48663328-48663512Exon41: 42 residues, 48663795-48663916Exon42: 49 residues, 48664013-48664155Exon43: 59 residues, 48664313-48664485Exon44: 41 residues, 48664873-48664990Exon45: 64 residues, 48665438-48665624Exon46: 58 residues, 48666055-48666225Exon47: 44 residues, 48666314-48666440Exon48: 56 residues, 48666725-48666889Exon49: 54 residues, 48667480-48667638Exon50: 31 residues, 48667742-48667831Exon51: 40 residues, 48668172-48668288Exon52: 77 residues, 48668576-48668802Exon53: 219 residues, 48669134-48669785Exon54: 1221 residues, 48671323-48674982Exon55: 60 residues, 48675536-48675710Exon56: 43 residues, 48684860-48684985Exon57: 2 residues, -Jump to CELR3_HUMANExon1: 590 residues, 48648900-48650669Exon2: 297 residues, 48652110-48652996Exon3: 69 residues, 48653760-48653961Exon4: 55 residues, 48654287-48654446Exon5: 38 residues, 48654794-48654904Exon6: 51 residues, 48655172-48655321Exon7: 41 residues, 48655403-48655520Exon8: 43 residues, 48655990-48656114Exon9: 28 residues, 48656652-48656732Exon10: 39 residues, 48657152-48657265Exon11: 60 residues, 48657471-48657646Exon12: 71 residues, 48657879-48658086Exon13: 44 residues, 48658178-48658305Exon14: 58 residues, 48658526-48658694Exon15: 57 residues, 48659199-48659365Exon16: 54 residues, 48660277-48660433Exon17: 67 residues, 48660702-48660898Exon18: 72 residues, 48661155-48661365Exon19: 33 residues, 48661557-48661652Exon20: 36 residues, 48662916-48663018Exon21: 63 residues, 48663328-48663512Exon22: 42 residues, 48663795-48663916Exon23: 49 residues, 48664013-48664155Exon24: 59 residues, 48664313-48664485Exon25: 41 residues, 48664873-48664990Exon26: 64 residues, 48665438-48665624Exon27: 58 residues, 48666055-48666225Exon28: 44 residues, 48666314-48666440Exon29: 56 residues, 48666725-48666889Exon30: 54 residues, 48667480-48667638Exon31: 31 residues, 48667742-48667831Exon32: 40 residues, 48668172-48668288Exon33: 77 residues, 48668576-48668802Exon34: 219 residues, 48669134-48669785Exon35: 1345 residues, 48671323-48675352Exon36: 2 residues, -Jump to CELR3_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4601 48530128-48569231 ~-39K 25651(PFKFB4)(-)Loci: 4602 48611435-48622102 ~-11K 25656(UQCRC1)(-)Loci: 4603 48637834-48684985 ~-47K 25658(CELSR3)(-)Loci: 4604 48686283-48698338 ~-12K 25669(NCKIPSD)(-)Loci: 4605 48762098-48860265 ~-98K 25672(-)Loci: 4606 49133551-49145603 ~-12K 25699(LAMB2)(-)Loci: 4607 49429215-49435016 ~-6K 25713(AMT)(-)Loci: 3354 49566925-49683976 ~-117K 25718(BSN)(+)Loci: 4608 49921309-49942261 ~-21K 25739(-)Loci: 4609 50330243-50333903 ~-4K 25774(HYAL2)(-)Loci: 4600 48420266-48441746 ~-21K 25634(PLXNB1)(-)Link out to UCSC