|CD111||PRR1 (poliovirus receptor-related 1 protein), PVRL1, Nectin 1, Hve C1|
|Molecule Type||Antigen Expression||Molecular Weight|
Min / Max
|Non-lineage Restricted Molecule|
Type 1 glycoprotein
|75 / 75|
|CD111, an intracellular adhesion molecule, is expressed on multiple cell types in the brain, spinal cord, trachea, prostate, placenta, skin, kidney, lung, pancreas, thyroid, and liver. CD111 is expressed on cell lines of different lineages, including myeloid cells, and neuronal cells. It is found in the plasma membrane, intra-cellularly, and in vesicle-like structures. CD111 is expressed on CD33+, CD14+ and CD41+ cells. It is also found on CD34 + stem cells, myelomonocytic cells, precursors of red cells and platelets and outside the hematopoietic lineage in erythroid lineages, fibroblastic cells, neuronal cells epithelial cells, and endothelial cells. CD111 is a component of the adherens junction and is 1 of several receptors for herpes simplex viruses types 1 and 2.|
|MOLECULAR FAMILY NAME: Belongs to the immunoglobulin gene family.|
CD111 is a single-pass type-1 glycoprotein. It contains an extracellular domain which contains 2 Ig-like C2-type domains and 1 Ig-like V-type domain and has 8 potential N-glycosylation sites, a transmembrane domain and a cytoplasmic domain. CD111 was originally identified as a transmembrane molecule related to the CD155 molecule and named poliovirus receptor related 1 (PRR1). CD111 belongs to a new family of immunoglobulin-like molecules that includes 4 members, CD111 (nectin-1), CD112 (nectin-2), CD113 (nectin-3) and CD155 (nectin-like 5). CD111 shows approximately 30% homology with CD112 and CD113. The gene encodes at least 2 different transmembrane isoforms sharing identical ectodomains but different transmembrane and cytosolic regions. The 2 corresponding transcripts of 5.9 kb and 3.5 kb are detectable in several tissues. Apparent Mr of the long form of CD111 is 75 kDa.
Alternative splicing yields 3 different isoforms, 1554 bp and 1377 bp long, that splices at position 1003 in the ectodomain. Transmembrane and cytoplasmic sequences are unrelated. The long isoform is the predominant expressed form (518 aa) and the shorter isoform (459 aa) is also observed.
CD111 has 8 potential N-glycosylation sites.
|The extracellular region of CD111 binds the related nectins, CD112, CD113, nectin-4 and CD155 (poliovirus ligand). It can interact with nectin-1 on the same or on other cells (i.e. cis- and trans-homo-interaction). CD111 is a receptor for the α herpes viruses HSV-1 and 2 and pseudorabies virus PRV. |
LIGANDS AND MOLECULES ASSOCIATED WITH CD111
|CD111 is an adhesion molecule involved in the formation of adherens junctions between epithelial cells, cell physiology and trans-interacts with nectin 3. An isoform of CD111 localizes specifically at the adherens junctions via its cytoplasmic interaction with the scaffold F-actin cytokeleton binding protein through afadin. The extracellular portion interacts with the other nectin family members, CD112, CD113 and CD155. This interaction is mediated by a sequence located to the C terminal end of CD111, A/ExYV, and the PDZ domain of afadin. This sequence is also found in CD112 and nectin 3 and represents a specific consensus in the family which is also named the nectin family. The function of CD111 on hematopietic cells is not known.|
BIOCHEMICAL ACTIVITY: No information.
DISEASE RELEVANCE AND FUNCTION OF CD111 IN INTACT ANIMAL
CD111 is associated with cleft lip/palate ectodermal dysplasia syndrome, ectodermal dysplasia, and Margarita Island type Zlotogora-Ogur syndrome. CD111 is a receptor for the α herpes viruses HSV-1 and 2 and pseudorabies. The soluble chimeric CD111-Fc fusin protein and antibody against CD111 blocks virus entry in vitro. The R1.302 monoclonal antibody recognizes the V-type domain of the molecule and blocks virus entry and cell to cell spreading. CD111 may function in homophilic and intracellular adhesion and as a coreceptor for HSV-1 and HSV-2 during infection of epithelial cells on mucosal surfaces. CD111 is a pan-a herpesvirus entry receptor, also named HveC / HlgR, as it mediates entry of many HSV1 and HSV2 strains, bovine herpesvirus 1 (BHV-1) and porcine pseudorabies virus (PRV). The V domain of CD111 interacts with the glycoprotein D of the virus and is sufficient to confer susceptibility to a herpesvirus infection. CD111 is involved in cell to cell spreading of the virus. Murine CD111 also acts as a HSV, BHV-2 and PrV receptor and binds to the to the viral glycoprotein D. Glycoprotein D interaction is weaker than with human CD111.
|MOLECULAR INTERACTIONS -|
PROTEINS AND DNA ELEMENTS WHICH REGULATE TRANSCRIPTION OF CD111: No information.
SUBSTRATES: No information.
ENZYMES WHICH MODIFY CD111: No information.
Database accession numbers
Revised June 25, 2008