Lin7c lin-7 homolog C, crumbs cell polarity complex component [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Lin7cprovided by MGI
Official Full Name: lin-7 homolog C, crumbs cell polarity complex componentprovided by MGI
Primary source: MGI:MGI:1330839
See related: Ensembl:ENSMUSG00000027162 AllianceGenome:MGI:1330839
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Veli3; LIN-7C; MALS-3; LIN-7-C; D2Ertd520e; 9130007B12Rik
Summary: Predicted to enable cytoskeletal protein binding activity; protein domain specific binding activity; and protein-macromolecule adaptor activity. Acts upstream of or within neurotransmitter secretion. Is active in glutamatergic synapse. Is expressed in brain; brainstem nucleus; and midbrain ventricular layer. Orthologous to human LIN7C (lin-7 homolog C, crumbs cell polarity complex component). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Broad expression in CNS E18 (RPKM 9.9), whole brain E14.5 (RPKM 7.2) and 21 other tissues See more
Orthologs: human all
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Genomic context

Location:: 2 E3; 2 56.65 cM

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	2	NC_000068.8 (109721205..109731348)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	2	NC_000068.7 (109890878..109900937)

Chromosome 2 - NC_000068.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Data show that CASK expression and the appropriate localization of DLG1 and LIN7c are not essential for either epithelial polarity or intestinal homeostasis in vivo.
Title: CASK deletion in intestinal epithelia causes mislocalization of LIN7C and the DLG1/Scrib polarity complex without affecting cell polarity.
MALS-3 plays a role in maintaining apicobasal polarity and is required for normal neurogenesis in the developing cortex.
Title: MALS-3 regulates polarity and early neurogenesis in the developing cerebral cortex.
MALS-3 mediates stable assembly of the crumbs tight junction complex and the discs large basolateral complex, and these complexes are disrupted in renal epithelia from MALS-3 knockout mice.
Title: Renal defects associated with improper polarization of the CRB and DLG polarity complexes in MALS-3 knockout mice.
These findings suggest that Mpp4 coordinates Psd95/Veli3 assembly and maintenance at synaptic membranes. Mpp4 is a critical recruitment factor to organize scaffolds at the photoreceptor synapse.
Title: Mpp4 recruits Psd95 and Veli3 towards the photoreceptor synapse.
analysis of structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins
Title: A unified assembly mode revealed by the structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins.
Association of Veli3 with either MPP4 or MPP5 suggests that the MAGUKs recruit Veli3 and its binding partners to different cellular regions of the retina where they may participate in the organization of specialized intercellular junctions.
Title: Membrane-associated guanylate kinase proteins MPP4 and MPP5 associate with Veli3 at distinct intercellular junctions of the neurosensory retina.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Targeted (2) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH136482 (e-PCR)
- UniSTS:210466

AW125731 (e-PCR)
- UniSTS:165188

AU022189 (e-PCR)
- UniSTS:167328

AI303698 (e-PCR)
- UniSTS:178673

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables L27 domain binding	IEA Inferred from Electronic Annotation more info
enables L27 domain binding	ISO Inferred from Sequence Orthology more info
enables PDZ domain binding	ISO Inferred from Sequence Orthology more info
enables cytoskeletal protein binding	IEA Inferred from Electronic Annotation more info
enables cytoskeletal protein binding	ISO Inferred from Sequence Orthology more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein domain specific binding	ISO Inferred from Sequence Orthology more info
enables protein-macromolecule adaptor activity	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in exocytosis	IEA Inferred from Electronic Annotation more info
involved_in morphogenesis of an epithelial sheet	IEA Inferred from Electronic Annotation more info
involved_in morphogenesis of an epithelial sheet	ISO Inferred from Sequence Orthology more info
involved_in neurotransmitter secretion	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within neurotransmitter secretion	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein transport	IEA Inferred from Electronic Annotation more info
involved_in regulation of synaptic assembly at neuromuscular junction	IBA Inferred from Biological aspect of Ancestor more info
involved_in synaptic vesicle transport	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
part_of MPP7-DLG1-LIN7 complex	IBA Inferred from Biological aspect of Ancestor more info
part_of MPP7-DLG1-LIN7 complex	IEA Inferred from Electronic Annotation more info
part_of MPP7-DLG1-LIN7 complex	ISO Inferred from Sequence Orthology more info
is_active_in basolateral plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in basolateral plasma membrane	IEA Inferred from Electronic Annotation more info
located_in bicellular tight junction	IEA Inferred from Electronic Annotation more info
is_active_in cell-cell junction	IBA Inferred from Biological aspect of Ancestor more info
located_in cell-cell junction	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
is_active_in glutamatergic synapse	IDA Inferred from Direct Assay more info	PubMed
is_active_in glutamatergic synapse	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
located_in postsynaptic density membrane	IEA Inferred from Electronic Annotation more info
located_in presynapse	IEA Inferred from Electronic Annotation more info
is_active_in synapse	IBA Inferred from Biological aspect of Ancestor more info
is_active_in synapse	IDA Inferred from Direct Assay more info	PubMed
located_in synapse	IDA Inferred from Direct Assay more info	PubMed
is_active_in synapse	ISO Inferred from Sequence Orthology more info
located_in transport vesicle membrane	TAS Traceable Author Statement more info

General protein information

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Preferred Names: protein lin-7 homolog C

Names: lin 7 homolog c; lin-7 homolog C; mammalian lin-seven protein 3; vertebrate homolog of C. elegans Lin-7 type 3; vertebrate lin-7 homolog 3

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_011699.4 → NP_035829.1 protein lin-7 homolog C

See identical proteins and their annotated locations for NP_035829.1

Status: VALIDATED

Source sequence(s)

AL845423

Consensus CDS

CCDS16509.1

UniProtKB/Swiss-Prot

O88952

UniProtKB/TrEMBL

Q3UX93

Related

ENSMUSP00000028583.8, ENSMUST00000028583.8

Conserved Domains (2) summary

cd00992
Location:91 → 172

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam02828
Location:14 → 66

L27; L27 domain