LNIR, Nectin cell adhesion molecule 4, PVRL4, Ig superfamily receptor LNIR, Poliovirus receptor-related protein 4, NECTIN4, Poliovirus Receptor-Related 4, Nectin-4, Nectin 4, PRR4, EDSS1


Nectins and Nectin-like molecules (Necl) are families of cellular adhesion molecules[1] involved in Ca2+-independent cellular adhesion.Nectins are ubiquitously expressed and have adhesive roles in a wide range of tissues such as the adherens junction of epithelia or the chemical synapse of the neuronal tissue.So far four nectins have been identified in humans, namely nectin-1, nectin-2, nectin-3 and nectin-4. These four family members have also been found in most other well studied mammals. Also, five Necls have been identified, these are: Necl-1, Necl-2, Necl-3, Necl-4 and Necl-5.Necl-4 Seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with NECTIN1. Does not act as receptor for alpha-herpesvirus entry into cells. Acts as a receptor for measles virus.

KO Status

RenMab: F2 (-/-)

Drug Information

Launched drug: 1
Drug in clinical trials: 1
Latest Research Phase: Approved

Drug Name





Clinical Trials

Enfortumab vedotin

AGS-M6, AGS-22ME, ASG-22CE, ASG-22ME, AGS-22M6E, ASG-22M6E, AGS-22C3, DLE8519RWM


Agensys, Seattle Genetics

Solid tumours, Kidney Neoplasms, Carcinoma, Carcinoma, Transitional Cell, Urinary Bladder Neoplasms, Urethral Neoplasms, Urologic Neoplasms, Ureteral Neoplasms

Nectin4/FAP-targeted CAR-T cell therapy (The Sixth Affiliated Hospital of Wenzhou Medical University)

Phase 1 Clinical

Wenzhou Medical University






Nectin-4, a new serological breast cancer marker, is a substrate for tumor necrosis factor-alpha-converting enzyme (TACE)/ADAM-17

Fabre-Lafay S., Garrido-Urbani S., Reymond N., Goncalves A., Dubreuil P., Lopez M.,

J. Biol. Chem. 280:19543-19550(2005)

Nectin-4 is a new histological and serological tumor associated marker for breast cancer

Fabre-Lafay S., Monville F., Garrido-Urbani S., Berruyer-Pouyet C., Ginestier C., Reymond N., Finetti P., Sauvan R., Adelaide J., Geneix J., Lecocq E., Popovici C., Dubreuil P., Viens P., Goncalves A., Charafe-Jauffret E., Jacquemier J., Birnbaum D., Lopez M.,

BMC Cancer 7:73-73(2007)

Adherens junction protein nectin-4 is the epithelial receptor for measles virus

Muhlebach M.D., Mateo M., Sinn P.L., Prufer S., Uhlig K.M., Leonard V.H., Navaratnarajah C.K., Frenzke M., Wong X.X., Sawatsky B., Ramachandran S., McCray P.B. Jr., Cichutek K., von Messling V., Lopez M., Cattaneo R.,

Nature 480:530-533(2011)

Nectin ectodomain structures reveal a canonical adhesive interface

Harrison O.J., Vendome J., Brasch J., Jin X., Hong S., Katsamba P.S., Ahlsen G., Troyanovsky R.B., Troyanovsky S.M., Honig B., Shapiro L.,

Nat. Struct. Mol. Biol. 19:906-915(2012)

Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4

Zhang X., Lu G., Qi J., Li Y., He Y., Xu X., Shi J., Zhang C.W., Yan J., Gao G.F.,

Nat. Struct. Mol. Biol. 20:67-72(2013)

Mutations in PVRL4, encoding cell adhesion molecule nectin-4, cause ectodermal dysplasia-syndactyly syndrome

Brancati F., Fortugno P., Bottillo I., Lopez M., Josselin E., Boudghene-Stambouli O., Agolini E., Bernardini L., Bellacchio E., Iannicelli M., Rossi A., Dib-Lachachi A., Stuppia L., Palka G., Mundlos S., Stricker S., Kornak U., Zambruno G., Dallapiccola B.,

Am. J. Hum. Genet. 87:265-273(2010)

Nectin4/PRR4, a new afadin-associated member of the nectin family that trans-interacts with nectin1/PRR1 through V domain interaction

Reymond N., Fabre S., Lecocq E., Adelaide J., Dubreuil P., Lopez M.,

J. Biol. Chem. 276:43205-43215(2001)

Complete sequencing and characterization of 21,243 full-length human cDNAs

Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Sugano S.,

Nat. Genet. 36:40-45(2004)

The DNA sequence and biological annotation of human chromosome 1

Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Bentley D.R.,

Nature 441:315-321(2006)

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)

The MGC Project Team,

Genome Res. 14:2121-2127(2004)