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0UNC5C_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameUNC5C
DescriptionNetrin receptor unc5c precursor (unc-5 homolog c) (unc-5 homolog 3).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005042 netrin receptor activity (TAS)
0007411 axon guidance (TAS)
0007420 brain development (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 unassigned to SynO:
This is a domain of unknown function.resent in ZO-1 and Unc5-like netrin receptors. It is also found in different variants of ankyrin.hich are responsible for attaching integral membrane proteins to cytoskeletal elements.
  IPR000906:ZU5
The death domain (DD) is a homotypic protein interaction module composed of a bundle of six alpha-helices. DD is related in sequence and structure to the death effector domain (DED.ee ) and the caspase recruitment domain (CARD.ee ).hich work in similar pathways and show similar interaction properties . DD bind each other forming oligomers. Mammals have numerous and diverse DD-containing proteins . Within these proteins.he DD domains can be found in combination with other domains.ncluding: CARDs.EDs.nkyrin repeats ().aspase-like folds.inase domains.eucine zippers ().eucine-rich repeats (LRR) ().IR domains ().nd ZU5 domains () .Some DD-containing proteins are involved in the regulation of apoptosis and inflammation through their activation of caspases and NF-kappaB.hich typically involves interactions with TNF (tumour necrosis factor) cytokine receptors . In humans.ight of the over 30 known TNF receptors contain DD in their cytoplasmic tails; several of these TNF receptors use caspase activation as a signalling mechanism. The DD mediates self-association of these receptors.hus giving the signal to downstream events that lead to apoptosis. Other DD-containing proteins.uch as ankyrin.yD88 and pelle.re probably not directly involved in cell death signalling. DD-containing proteins also have links to innate immunity.ommunicating with Toll family receptors through bipartite adapter proteins such as MyD88 .
  IPR000488:Death
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents I-set domains.hich are found in several cell adhesion molecules.ncluding vascular (VCAM).ntercellular (ICAM).eural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules.s well as junction adhesion molecules (JAM). I-set domains are also present in several other diverse protein families.ncluding several tyrosine-protein kinase receptors.he hemolymph protein hemolin.he muscle proteins titin.elokin.nd twitchin.he neuronal adhesion molecule axonin-1 .nd the signalling molecule semaphorin 4D that is involved in axonal guidance.mmune function and angiogenesis .
  IPR013098:Immunoglobulin I-set
This repeat was first described in 1986 by Lawler and Hynes . It was found in the thrombospondin protein where it is repeated 3 times. Now a number of proteins involved in the complement pathway (properdin.6.7.8A.8B.9) as well as extracellular matrix protein like mindin.-spondin .CO-spondin and even the circumsporozoite surface protein 2 and TRAP proteins of Plasmodium .ontain one or more instance of this repeat.It has been involved in cell-cell interraction.nhibition of angiogenesis andapoptosis . The intron-exon organisation of the properdin gene confirms the hypothesis that the repeat might have evolved by a process involving exon shuffling .A study of properdin structure provides some information about the structure ofthe thrombospondin type I repeat .
  IPR000884:Thrombospondin, type I
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents a subtype of the immunoglobulin domain.nd is found in a diverse range of protein families that includes glycoproteins.ibroblast growth factor receptors.ascular endothelial growth factor receptors.nterleukin-6 receptor.nd neural cell adhesion molecules. It also includes proteins that are classified as unassigned proteinase inhibitors belonging to MEROPS inhibitor families I2.17 and I43 .
  IPR003598:Immunoglobulin subtype 2
The TSP1 (thrombospondin 1) repeat was first identified in thethrombospondin protein.here it is repeated 3 times . The domain is ~60 amino acid residues in length and is characterised by a highly conserved W-S-X-W motif and six cysteine residues. TSP1 repeats have been identified in a number of proteins including: the complement pathwayproteins properdin.6.7.8A.8B and C9; extracellular matrix proteins.ncluding mindin.DAMTS and F-spondin; Plasmodium TRAP proteins; and G protein-coupled receptors.uch as the brain-specific angiogenesis inhibitors. The domains have a number of functions.ncluding effects on cell attachment.otility.roliferation.he activities of extracellularproteases.nd inhibition of angiogenesis.ontributing to vascular homeostasis. A study of the structure of properdin indicates that the TSP1 repeat contains two amphipathic turn regions and a hydrophilic beta-strand .
  IPR008085:Thrombospondin, subtype 1
The death domain (DD) is a conserved region of about 80 residues found on death receptors.nd which is required for death signalling.s well as a variety of non-apoptotic functions . Proteins containing this domain include the low affinity neurotrophin receptor p73.as.ADD (Fas-associated death domain protein).NF-1 (tumour necrosis factor receptor-1).elle protein kinase.nd the Tube adaptor protein .The induction of apoptosis also relies on the presence of a second domain.alled the death effector domain. The death effector domain (DED) occurs in proteins that regulate programmed cell death.ncluding both pro- and anti-apoptotic proteins; many of these proteins are also involved in controlling cellular activation and proliferation pathways . Proteins containing this domain include FADD (DED N-terminal.D C-terminal).EA-15 (phosphoproteins enriched in astrocytes 15kDa).aspases and FLIP.The induction of apoptosis results in the activation of caspases. family of aspartyl-specific cysteine proteases that are the main executioners of apoptosis. For example.he DED of FADD recruits two DED-containing caspases.aspase-8 and caspase-10.o form the death-inducing signal complex.hich initiates apoptosis. Proteins containing the caspase recruitment domain (CARD) are involved in the recruitment and activation of caspases during apoptosis . Other CARD proteins participate in NF-kappaB signalling pathways associated with innate or adaptive immune responses. Proteins containing CARD include Raidd.PAF-1 (apoptotic protease activating factor 1).rocaspase 9 and iceberg (inhibitor of interleukin-1-beta generation).The DD shows strong structural similarity to both DED and CARD. They all display a 6-helical closed bundle fold.ith greek key topology and an internal psuedo two-fold symmetry. However.espite their overall similarity in topology.ach domain forms specialised interactions.ypically only with members of its own subfamily.or example DED with DED.Please be aware that some of the proteins hit by the SSF signature may be false positives.
  IPR011029:DEATH-like
This entry represents domains with an immunoglobulin-like (Ig-like) fold.hich consists of a beta-sandwich of seven or more strands in two sheets with a Greek-key topology. Ig-like domains are one of the most common protein modules found in animals.ccurring in a variety of different proteins. These domains are often involved in interactions.ommonly with other Ig-like domains via their beta-sheets . Domains within this fold-family share the same structure.ut can diverge with respect to their sequence. Based on sequence.g-like domains can be classified as V-set domains (antibody variable domain-like).1-set domains (antibody constant domain-like).2-set domains.nd I-set domains (antibody intermediate domain-like). Proteins can contain more than one of these types of Ig-like domains. For example.n the human T-cell receptor antigen CD2.omain 1 (D1) is a V-set domain.hile domain 2 (D2) is a C2-set domain.oth domains having the same Ig-like fold .Domains with an Ig-like fold can be found in many.iverse proteins in addition to immunoglobulin molecules. For example.g-like domains occur in several different types of receptors (such as various T-cell antigen receptors).everal cell adhesion molecules.HC class I and II antigens.s well as the hemolymph protein hemolin.nd the muscle proteins titin.elokin and twitchin.
  IPR013783:Immunoglobulin-like fold
IPR000906:ZU5 
Evalue:-58.1191864013672 
Location:528-631IPR000488:DEATH 
Evalue:-23.1804560644581 
Location:838-929IPR000884:TSP1 
Evalue:-12.0705810742857 
Location:263-314IPR013098:I-set 
Evalue:-9.31875896453857 
Location:167-257IPR000884:TSP1 
Evalue:-6.13667713987954 
Location:319-368IPR013783:Ig-like_fold 
Evalue:0 
Location:62-125IPR000488:DEATH_DOMAIN 
Evalue:0 
Location:0-0
SequencesProtein: UNC5C_HUMAN (931 aa)
mRNA: NM_003728
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
KO assignmentK07521
  Level 3 annotation:
    unc-5 homolog (C. elegans)
  Level 2 annotation:
    Axon guidance
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 288 residues, 96308711-96309573Exon2: 61 residues, 96310327-96310506Exon3: 57 residues, 96323070-96323235Exon4: 52 residues, 96325220-96325370Exon5: 80 residues, 96342904-96343138Exon6: 58 residues, 96346801-96346970Exon7: 31 residues, 96356297-96356385Exon8: 117 residues, 96359142-96359487Exon9: 66 residues, 96360158-96360350Exon10: 57 residues, 96382602-96382767Exon11: 58 residues, 96385150-96385318Exon12: 62 residues, 96390660-96390841Exon13: 36 residues, 96418432-96418536Exon14: 50 residues, 96441779-96441923Exon15: 76 residues, 96475583-96475805Exon16: 94 residues, 96688907-96689185Exon17: 2 residues, -Jump to UNC5C_HUMAN