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mup-4 Transmembrane matrix receptor MUP-4 [ Caenorhabditis elegans ]

Gene ID: 176060, updated on 9-Dec-2024

Summary

Official Symbol
mup-4
Official Full Name
Transmembrane matrix receptor MUP-4
Primary source
WormBase:WBGene00003497
Locus tag
CELE_K07D8.1
See related
AllianceGenome:WB:WBGene00003497
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Caenorhabditis elegans (strain: Bristol N2)
Lineage
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary
Predicted to enable calcium ion binding activity. Predicted to be involved in cell adhesion. Located in hemidesmosome. Part of hemidesmosome associated protein complex. Is expressed in body wall musculature; hypodermis; pharynx; touch receptor neurons; and vulval cell. Human ortholog(s) of this gene implicated in multiple epiphyseal dysplasia 5; osteoarthritis; and osteochondrodysplasia. Orthologous to human MATN2 (matrilin 2) and MATN3 (matrilin 3). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

See mup-4 in Genome Data Viewer
Location:
chromosome: III
Exon count:
20
Sequence:
Chromosome: III; NC_003281.10 (7479680..7489105, complement)

Chromosome III - NC_003281.10Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene putative fumarate hydratase, mitochondrial Neighboring gene tRNA-synt_2 domain-containing protein Neighboring gene ncRNA Neighboring gene ncRNA

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Gene Ontology Provided by WormBase

Function Evidence Code Pubs
enables calcium ion binding IEA
Inferred from Electronic Annotation
more info
 
enables protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
Process Evidence Code Pubs
involved_in cell adhesion IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
located_in anchoring junction IEA
Inferred from Electronic Annotation
more info
 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
 
located_in cytoskeleton IEA
Inferred from Electronic Annotation
more info
 
located_in hemidesmosome IDA
Inferred from Direct Assay
more info
PubMed 
located_in hemidesmosome IEA
Inferred from Electronic Annotation
more info
 
part_of hemidesmosome associated protein complex IDA
Inferred from Direct Assay
more info
PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
 

General protein information

Preferred Names
Transmembrane matrix receptor MUP-4
NP_498645.1
  • Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_003281.10 Reference assembly

    Range
    7479680..7489105 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_066244.7NP_498645.1  Transmembrane matrix receptor MUP-4 [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_498645.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    Q21281, Q964N4
    Conserved Domains (7) summary
    smart00179
    Location:920954
    EGF_CA; Calcium-binding EGF-like domain
    smart00200
    Location:14951619
    SEA; Domain found in sea urchin sperm protein, enterokinase, agrin
    pfam06247
    Location:8931082
    Plasmod_Pvs28; Plasmodium ookinete surface protein Pvs28
    pfam07645
    Location:17721810
    EGF_CA; Calcium-binding EGF domain
    pfam12947
    Location:823851
    EGF_3; EGF domain
    cl00057
    Location:436604
    vWFA; Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of ...
    cl21504
    Location:873902
    EGF_CA; Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the ...