CDH3 (gene)

From Wikipedia, the free encyclopedia
Jump to: navigation, search
CDH3
Available structures
PDB Human UniProt search: PDBe RCSB
Identifiers
Aliases CDH3, CDHP, HJMD, PCAD, cadherin 3
External IDs HomoloGene: 20425 GeneCards: 1001
RNA expression pattern
PBB GE CDH3 203256 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001793
NM_001317195
NM_001317196

n/a

RefSeq (protein)

NP_001784.2
NP_001304124.1
NP_001304125.1

n/a

Location (UCSC) Chr 16: 68.64 – 68.72 Mb n/a
PubMed search [1] n/a
Wikidata
View/Edit Human

Cadherin-3, also known as P-Cadherin, is a protein that in humans is encoded by the CDH3 gene.[1][2]

Function[edit]

This gene is a classical cadherin from the cadherin superfamily. The encoded protein is a calcium-dependent cell-cell adhesion glycoprotein composed of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. This gene is located in a six-cadherin cluster in a region on the long arm of chromosome 16 that is involved in loss of heterozygosity events in breast and prostate cancer. In addition, aberrant expression of this protein is observed in cervical adenocarcinomas.

Clinical significance[edit]

Mutations in this gene have been associated with congential hypotrichosis with juvenile macular dystrophy.[2]

Interactions[edit]

CDH3 (gene) has been shown to interact with:

See also[edit]

References[edit]

  1. ^ Kaupmann K, Becker-Follmann J, Scherer G, Jockusch H, Starzinski-Powitz A (Oct 1992). "The gene for the cell adhesion molecule M-cadherin maps to mouse chromosome 8 and human chromosome 16q24.1-qter and is near the E-cadherin (uvomorulin) locus in both species". Genomics 14 (2): 488–90. doi:10.1016/S0888-7543(05)80247-2. PMID 1427864. 
  2. ^ a b "Entrez Gene: CDH3 cadherin 3, type 1, P-cadherin (placental)". 
  3. ^ a b c d Klingelhöfer J, Troyanovsky RB, Laur OY, Troyanovsky S (Aug 2000). "Amino-terminal domain of classic cadherins determines the specificity of the adhesive interactions". Journal of Cell Science. 113 ( Pt 16): 2829–36. PMID 10910767. 
  4. ^ a b Schmeiser K, Grand RJ (Apr 1999). "The fate of E- and P-cadherin during the early stages of apoptosis". Cell Death and Differentiation 6 (4): 377–86. doi:10.1038/sj.cdd.4400504. PMID 10381631. 
  5. ^ Lehtonen S, Lehtonen E, Kudlicka K, Holthöfer H, Farquhar MG (Sep 2004). "Nephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrin". The American Journal of Pathology 165 (3): 923–36. doi:10.1016/S0002-9440(10)63354-8. PMC 1618613. PMID 15331416. 

Further reading[edit]

External links[edit]