Reviewed, UniProtKB/Swiss-Prot Q96NY8 (PVRL4_HUMAN)

Names and origin

Protein names

Recommended name:
    Poliovirus receptor-related protein 4
Alternative name(s):
    Nectin-4
    Ig superfamily receptor LNIR
Cleaved into the following chain:
    1- Recommended name:
            Processed poliovirus receptor-related protein 4

Gene names

Name:	PVRL4
Synonyms:	LNIR, PRR4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	510 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with PVRL2/nectin-1. Does not act as receptor for alpha-herpesvirus entry into cells.
Subunit structure	Self-associates. Interacts via its Ig-like V-type domain with PVRL1/nectin-1 Ig-like V-type domain. Interacts via its C-terminus with MLLT4. Ref.1 Ref.6
Subcellular location	Cell membrane; Single-pass type I membrane protein Potential. Cell junction › adherens junction. Note: Colocalizes with MLLT4 at cadherin-based adherens junctions. Processed poliovirus receptor-related protein 4: Secreted. Note: The secreted form is found in breast tumor patients. Ref.1
Tissue specificity	Predominantly expressed in placenta. Not detected in normal breast epithelium but expressed in breast carcinoma. Ref.1 Ref.8
Post-translational modification	The soluble form is produced by proteolytic cleavage at the cell surface (shedding), probably by ADAM17/TACE.
Sequence similarities	Belongs to the nectin family. Contains 2 Ig-like C2-type (immunoglobulin-like) domains. Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cell membrane Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	adherens junction Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Potential
	Chain	32 – 510	479	Poliovirus receptor-related protein 4		PRO_0000297673
	Chain	32 – ?		Processed poliovirus receptor-related protein 4		PRO_0000311086
Regions
	Topological domain	32 – 349	318	Extracellular Potential
	Transmembrane	350 – 370	21	Potential
	Topological domain	371 – 510	140	Cytoplasmic Potential
	Domain	32 – 144	113	Ig-like V-type 1
	Domain	148 – 237	90	Ig-like C2-type 1
	Domain	248 – 331	84	Ig-like C2-type 2
Amino acid modifications
	Glycosylation	281	1	N-linked (GlcNAc...) Potential
	Disulfide bond	171 ↔ 223		By similarity
	Disulfide bond	270 ↔ 315		By similarity
Natural variations
	Natural variant	53	1	F → L: dbSNP rs3737786.		VAR_034669
Experimental info
	Sequence conflict	35	1	E → G in BAB55344. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q96NY8-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: DCF5E1D794F227FA	FASTA	510	55,454
	10 20 30 40 50 60 MPLSLGAEMW GPEAWLLLLL LLASFTGRCP AGELETSDVV TVVLGQDAKL PCFYRGDSGE 70 80 90 100 110 120 QVGQVAWARV DAGEGAQELA LLHSKYGLHV SPAYEGRVEQ PPPPRNPLDG SVLLRNAVQA 130 140 150 160 170 180 DEGEYECRVS TFPAGSFQAR LRLRVLVPPL PSLNPGPALE EGQGLTLAAS CTAEGSPAPS 190 200 210 220 230 240 VTWDTEVKGT TSSRSFKHSR SAAVTSEFHL VPSRSMNGQP LTCVVSHPGL LQDQRITHIL 250 260 270 280 290 300 HVSFLAEASV RGLEDQNLWH IGREGAMLKC LSEGQPPPSY NWTRLDGPLP SGVRVDGDTL 310 320 330 340 350 360 GFPPLTTEHS GIYVCHVSNE FSSRDSQVTV DVLDPQEDSG KQVDLVSASV VVVGVIAALL 370 380 390 400 410 420 FCLLVVVVVL MSRYHRRKAQ QMTQKYEEEL TLTRENSIRR LHSHHTDPRS QPEESVGLRA 430 440 450 460 470 480 EGHPDSLKDN SSCSVMSEEP EGRSYSTLTT VREIETQTEL LSPGSGRAEE EEDQDEGIKQ 490 500 510 AMNHFVQENG TLRAKPTGNG IYINGRGHLV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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) [PubMed: 11544254] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH MLLT4 AND PVRL1.
[2]	"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. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[3]	"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. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
[6]	"Prominent role of the Ig-like V domain in trans-interactions of nectins. Nectin3 and nectin 4 bind to the predicted C-C'-C'-D beta-strands of the nectin1 V domain." Fabre S., Reymond N., Cocchi F., Menotti L., Dubreuil P., Campadelli-Fiume G., Lopez M. J. Biol. Chem. 277:27006-27013(2002) [PubMed: 12011057] [Abstract] Cited for: INTERACTION WITH PVLR1.
[7]	"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) [PubMed: 15784625] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[8]	"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) [PubMed: 17474988] [Abstract] Cited for: TISSUE SPECIFICITY.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF426163 mRNA. Translation: AAL23958.1. AK027753 mRNA. Translation: BAB55344.1. AL591806 Genomic DNA. Translation: CAI15376.1. CH471121 Genomic DNA. Translation: EAW52665.1. BC010423 mRNA. Translation: AAH10423.1.
IPI	IPI00043992.
RefSeq	NP_112178.2.
UniGene	Hs.492490
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q96NY8.
Proteomic databases
PRIDE	Q96NY8.
Genome annotation databases
Ensembl	ENSG00000143217. Homo sapiens. [Contig view]
GeneID	81607.
KEGG	hsa:81607.
Organism-specific databases
GeneCards	GC01M159307.
HGNC	HGNC:19688. PVRL4.
HPA	HPA010775.
MIM	609607. gene.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q96NY8.
OMA	Q96NY8. RYHRRKA.
Gene expression databases
ArrayExpress	Q96NY8.
Bgee	Q96NY8.
CleanEx	HS_PRR4. HS_PVRL4.
Family and domain databases
InterPro	IPR013162. CD80_C2-set. IPR013151. Ig. IPR007110. Ig-like. IPR013783. Ig-like_fold. IPR003599. Ig_sub. IPR003598. Ig_sub2. IPR013106. Ig_V-set. [Graphical view]
Gene3D	G3DSA:2.60.40.10. Ig-like_fold. 2 hits.
Pfam	PF08205. C2-set_2. 1 hit. PF00047. ig. 1 hit. PF07686. V-set. 1 hit. [Graphical view]
SMART	SM00409. IG. 1 hit. SM00408. IGc2. 1 hit. [Graphical view]
PROSITE	PS50835. IG_LIKE. 3 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	71924.
SOURCE	Search...

Entry information

Entry name

PVRL4_HUMAN

Accession

Primary (citable) accession number: Q96NY8
Secondary accession number(s): Q96K15

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 21, 2007
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)