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Nectin-2 (Herpes virus entry mediator B) (Herpesvirus entry mediator B) (HveB) (Nectin cell adhesion molecule 2) (Poliovirus receptor-related protein 2) (CD antigen CD112)

 NECT2_HUMAN             Reviewed;         538 AA.
Q92692; A8K5L5; O75455; Q6IBI6; Q96J29;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
27-SEP-2017, entry version 182.
RecName: Full=Nectin-2;
AltName: Full=Herpes virus entry mediator B;
Short=Herpesvirus entry mediator B;
Short=HveB;
AltName: Full=Nectin cell adhesion molecule 2 {ECO:0000312|HGNC:HGNC:9707};
AltName: Full=Poliovirus receptor-related protein 2;
AltName: CD_antigen=CD112;
Flags: Precursor;
Name=NECTIN2 {ECO:0000312|HGNC:HGNC:9707}; Synonyms=HVEB, PRR2, PVRL2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA).
PubMed=7622062; DOI=10.1016/0378-1119(95)00180-E;
Eberle F., Dubreuil P., Mattei M.-G., Devilard E., Lopez M.;
"The human PRR2 gene, related to the human poliovirus receptor gene
(PVR), is the true homolog of the murine MPH gene.";
Gene 159:267-272(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), FUNCTION (MICROBIAL
INFECTION), AND INTERACTION WITH HUMAN HERPESVIRUS 1/HHV-1; HUMAN
HERPESVIRUS 2/HHV-2 ABD PSEUDORABIES VIRUS GLYCOPROTEIN D.
PubMed=9657005; DOI=10.1006/viro.1998.9218;
Warner M.S., Geraghty R.J., Martinez W.M., Montgomery R.I.,
Whitbeck J.C., Xu R., Eisenberg R.J., Cohen G.H., Spear P.G.;
"A cell surface protein with herpesvirus entry activity (HveB) confers
susceptibility to infection by mutants of herpes simplex virus type 1,
herpes simplex virus type 2, and pseudorabies virus.";
Virology 246:179-189(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-538.
Yoshiura K., Murray J.C.;
"A transcriptional map in the region of 19q13 derived using direct
sequencing and exon trapping.";
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 449-538.
PubMed=10520737; DOI=10.3109/10425179809086433;
Freitas E.M., Zhang W.J., Lalonde J.P., Tay G.K., Gaudieri S.,
Ashworth L.K., Van Bockxmeer F.M., Dawkins R.L.;
"Sequencing of 42kb of the APO E-C2 gene cluster reveals a new gene:
PEREC1.";
DNA Seq. 9:89-100(1998).
[9]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HHV-1 MUTANT RID1;
HHV-2 AND PRV GLYCOPROTEIN D, AND MUTAGENESIS OF MET-89.
PubMed=11602758; DOI=10.1128/JVI.75.22.11185-11195.2001;
Martinez W.M., Spear P.G.;
"Structural features of nectin-2 (HveB) required for herpes simplex
virus entry.";
J. Virol. 75:11185-11195(2001).
[10]
INTERACTION WITH CD226.
PubMed=15607800; DOI=10.1016/j.molimm.2004.07.028;
Pende D., Bottino C., Castriconi R., Cantoni C., Marcenaro S.,
Rivera P., Spaggiari G.M., Dondero A., Carnemolla B., Reymond N.,
Mingari M.C., Lopez M., Moretta L., Moretta A.;
"PVR (CD155) and Nectin-2 (CD112) as ligands of the human DNAM-1
(CD226) activating receptor: involvement in tumor cell lysis.";
Mol. Immunol. 42:463-469(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
INTERACTION WITH TIGIT.
PubMed=19011627; DOI=10.1038/ni.1674;
Yu X., Harden K., Gonzalez L.C., Francesco M., Chiang E., Irving B.,
Tom I., Ivelja S., Refino C.J., Clark H., Eaton D., Grogan J.L.;
"The surface protein TIGIT suppresses T cell activation by promoting
the generation of mature immunoregulatory dendritic cells.";
Nat. Immunol. 10:48-57(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-410, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-465 AND SER-470 (ISOFORM ALPHA), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
FUNCTION AS PVRIG LIGAND.
PubMed=26755705; DOI=10.1084/jem.20150785;
Zhu Y., Paniccia A., Schulick A.C., Chen W., Koenig M.R., Byers J.T.,
Yao S., Bevers S., Edil B.H.;
"Identification of CD112R as a novel checkpoint for human T cells.";
J. Exp. Med. 213:167-176(2016).
[18]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 32-158, SUBUNIT, DISULFIDE
BOND, AND MUTAGENESIS OF ASN-81.
PubMed=22927415; DOI=10.1073/pnas.1212912109;
Samanta D., Ramagopal U.A., Rubinstein R., Vigdorovich V.,
Nathenson S.G., Almo S.C.;
"Structure of Nectin-2 reveals determinants of homophilic and
heterophilic interactions that control cell-cell adhesion.";
Proc. Natl. Acad. Sci. U.S.A. 109:14836-14840(2012).
-!- FUNCTION: Modulator of T-cell signaling. Can be either a
costimulator of T-cell function, or a coinhibitor, depending on
the receptor it binds to. Upon binding to CD226, stimulates T-cell
proliferation and cytokine production, including that of IL2, IL5,
IL10, IL13, and IFNG. Upon interaction with PVRIG, inhibits T-cell
proliferation. These interactions are competitive
(PubMed:26755705). Probable cell adhesion protein
(PubMed:9657005). {ECO:0000269|PubMed:26755705,
ECO:0000269|PubMed:9657005}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for herpes
simplex virus 1 (HHV-1) mutant Rid1, herpes simplex virus 1 (HHV-
2) and pseudorabies virus (PRV). {ECO:0000269|PubMed:11602758,
ECO:0000269|PubMed:9657005}.
-!- SUBUNIT: Can form trans-heterodimers with NECTIN3 (By similarity).
Interacts with CD226 or with PVRIG; these interactions are
competitive and have a differential functional outcome on T-cell
activation, either positive or negative, respectively. Binds with
low affinity to TIGIT. {ECO:0000250, ECO:0000269|PubMed:15607800,
ECO:0000269|PubMed:19011627, ECO:0000269|PubMed:22927415}.
-!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus
1 (HHV-1) mutant Rid1, herpes simplex virus 1 (HHV-2) and
pseudorabies virus (PRV) envelope glycoprotein D (PubMed:11602758,
PubMed:9657005). {ECO:0000269|PubMed:11602758,
ECO:0000269|PubMed:9657005}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-718419, EBI-718419;
P55196:AFDN; NbExp=2; IntAct=EBI-718419, EBI-365875;
Q15762:CD226; NbExp=2; IntAct=EBI-718419, EBI-4314442;
A8MQ03:CYSRT1; NbExp=4; IntAct=EBI-6979889, EBI-3867333;
P60370:KRTAP10-5; NbExp=3; IntAct=EBI-718419, EBI-10172150;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-718419, EBI-10172290;
P26371:KRTAP5-9; NbExp=3; IntAct=EBI-718419, EBI-3958099;
Q99750:MDFI; NbExp=4; IntAct=EBI-718419, EBI-724076;
Q9NQS3:NECTIN3; NbExp=3; IntAct=EBI-718419, EBI-2826725;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-718419, EBI-945833;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-718419, EBI-747107;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Delta;
IsoId=Q92692-1; Sequence=Displayed;
Name=Alpha;
IsoId=Q92692-2; Sequence=VSP_002628, VSP_002629;
Note=Ref.3 (BAF84019) sequence is in conflict in position:
410:P->L. Contains a phosphoserine at position 470. Contains a
phosphoserine at position 465. {ECO:0000244|PubMed:24275569,
ECO:0000305};
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
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EMBL; X80038; CAA56342.1; -; mRNA.
EMBL; AF058448; AAC23797.1; -; mRNA.
EMBL; AK291330; BAF84019.1; -; mRNA.
EMBL; CR456818; CAG33099.1; -; mRNA.
EMBL; CH471126; EAW57298.1; -; Genomic_DNA.
EMBL; BC003091; AAH03091.1; -; mRNA.
EMBL; AF044968; AAC82348.1; -; Genomic_DNA.
EMBL; AF044962; AAC82348.1; JOINED; Genomic_DNA.
EMBL; AF044963; AAC82348.1; JOINED; Genomic_DNA.
EMBL; AF044964; AAC82348.1; JOINED; Genomic_DNA.
EMBL; AF044966; AAC82348.1; JOINED; Genomic_DNA.
EMBL; AF044967; AAC82348.1; JOINED; Genomic_DNA.
EMBL; AF050154; AAD02503.1; -; Genomic_DNA.
CCDS; CCDS12645.1; -. [Q92692-2]
CCDS; CCDS42576.1; -. [Q92692-1]
PIR; I68093; I68093.
RefSeq; NP_001036189.1; NM_001042724.1. [Q92692-1]
RefSeq; NP_002847.1; NM_002856.2. [Q92692-2]
UniGene; Hs.655455; -.
PDB; 3R0N; X-ray; 1.30 A; A=32-158.
PDB; 4DFH; X-ray; 1.85 A; A/B=32-158.
PDB; 4DFI; X-ray; 1.80 A; A=32-158.
PDB; 4HZA; X-ray; 1.70 A; A/B=32-158.
PDB; 5V52; X-ray; 3.10 A; C/D=32-158.
PDBsum; 3R0N; -.
PDBsum; 4DFH; -.
PDBsum; 4DFI; -.
PDBsum; 4HZA; -.
PDBsum; 5V52; -.
ProteinModelPortal; Q92692; -.
SMR; Q92692; -.
BioGrid; 111777; 41.
DIP; DIP-41043N; -.
IntAct; Q92692; 36.
MINT; MINT-90946; -.
STRING; 9606.ENSP00000252483; -.
iPTMnet; Q92692; -.
PhosphoSitePlus; Q92692; -.
SwissPalm; Q92692; -.
BioMuta; PVRL2; -.
DMDM; 12643789; -.
EPD; Q92692; -.
MaxQB; Q92692; -.
PaxDb; Q92692; -.
PeptideAtlas; Q92692; -.
PRIDE; Q92692; -.
DNASU; 5819; -.
Ensembl; ENST00000252483; ENSP00000252483; ENSG00000130202. [Q92692-1]
Ensembl; ENST00000252485; ENSP00000252485; ENSG00000130202. [Q92692-2]
GeneID; 5819; -.
KEGG; hsa:5819; -.
UCSC; uc002ozv.4; human. [Q92692-1]
CTD; 5819; -.
DisGeNET; 5819; -.
EuPathDB; HostDB:ENSG00000130202.9; -.
GeneCards; NECTIN2; -.
HGNC; HGNC:9707; NECTIN2.
HPA; CAB026138; -.
HPA; HPA012759; -.
HPA; HPA073459; -.
MIM; 600798; gene.
neXtProt; NX_Q92692; -.
OpenTargets; ENSG00000130202; -.
PharmGKB; PA34052; -.
eggNOG; ENOG410IIB8; Eukaryota.
eggNOG; ENOG4111FZM; LUCA.
GeneTree; ENSGT00880000137893; -.
HOGENOM; HOG000237277; -.
HOVERGEN; HBG019169; -.
InParanoid; Q92692; -.
KO; K06531; -.
OMA; TVNLRCA; -.
OrthoDB; EOG091G0CPW; -.
PhylomeDB; Q92692; -.
TreeFam; TF331051; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-418990; Adherens junctions interactions.
Reactome; R-HSA-420597; Nectin/Necl trans heterodimerization.
ChiTaRS; PVRL2; human.
EvolutionaryTrace; Q92692; -.
GeneWiki; PVRL2; -.
GenomeRNAi; 5819; -.
PRO; PR:Q92692; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000130202; -.
CleanEx; HS_PVRL2; -.
ExpressionAtlas; Q92692; baseline and differential.
Genevisible; Q92692; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005913; C:cell-cell adherens junction; IBA:GO_Central.
GO; GO:0044291; C:cell-cell contact zone; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005915; C:zonula adherens; ISS:BHF-UCL.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
GO; GO:0015026; F:coreceptor activity; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0001675; P:acrosome assembly; IEA:Ensembl.
GO; GO:0034332; P:adherens junction organization; TAS:Reactome.
GO; GO:0044406; P:adhesion of symbiont to host; IDA:BHF-UCL.
GO; GO:0032990; P:cell part morphogenesis; IEA:Ensembl.
GO; GO:0008037; P:cell recognition; IBA:GO_Central.
GO; GO:0044782; P:cilium organization; IEA:Ensembl.
GO; GO:0046814; P:coreceptor-mediated virion attachment to host cell; IDA:BHF-UCL.
GO; GO:0007010; P:cytoskeleton organization; IEA:Ensembl.
GO; GO:0051654; P:establishment of mitochondrion localization; IEA:Ensembl.
GO; GO:0009566; P:fertilization; IEA:Ensembl.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IDA:BHF-UCL.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:BHF-UCL.
GO; GO:0002891; P:positive regulation of immunoglobulin mediated immune response; IMP:BHF-UCL.
GO; GO:0033005; P:positive regulation of mast cell activation; IMP:BHF-UCL.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IMP:BHF-UCL.
GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IMP:BHF-UCL.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0046596; P:regulation of viral entry into host cell; IDA:CACAO.
GO; GO:0030382; P:sperm mitochondrion organization; IEA:Ensembl.
GO; GO:0007286; P:spermatid development; ISS:BHF-UCL.
GO; GO:0007289; P:spermatid nucleus differentiation; IEA:Ensembl.
GO; GO:0042271; P:susceptibility to natural killer cell mediated cytotoxicity; IMP:BHF-UCL.
GO; GO:0060370; P:susceptibility to T cell mediated cytotoxicity; IDA:BHF-UCL.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR013162; CD80_C2-set.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR033318; Nectin-2.
PANTHER; PTHR23277:SF101; PTHR23277:SF101; 1.
Pfam; PF08205; C2-set_2; 1.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 2.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction;
Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 538 Nectin-2.
/FTId=PRO_0000015136.
TOPO_DOM 32 360 Extracellular. {ECO:0000255}.
TRANSMEM 361 381 Helical. {ECO:0000255}.
TOPO_DOM 382 538 Cytoplasmic. {ECO:0000255}.
DOMAIN 32 156 Ig-like V-type.
DOMAIN 162 256 Ig-like C2-type 1.
DOMAIN 261 345 Ig-like C2-type 2.
MOD_RES 410 410 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 433 433 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 54 140 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:22927415}.
DISULFID 183 238 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 283 329 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 351 479 NTAGAGATGGIIGGIIAAIIATAVAATGILICRQQRKEQTL
QGAEEDEDLEGPPSYKPPTPKAKLEAQEMPSQLFTLGASEH
SPLKTPYFDAGASCTEQEMPRYHELPTLEERSGPLHPGATS
LGSPIP -> RASPRDVGPLVWGAVGGTLLVLLLLAGGSLA
FILLRVRRRRKSPGGAGGGASGDGGFYDPKAQVLGNGDPVF
WTPVVPGPMEPDGKDEEEEEEEEKAEKGLMLPPPPALEDDM
ESQLDGSLISRRAVYV (in isoform Alpha).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9657005,
ECO:0000303|Ref.4}.
/FTId=VSP_002628.
VAR_SEQ 480 538 Missing (in isoform Alpha).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9657005,
ECO:0000303|Ref.4}.
/FTId=VSP_002629.
MUTAGEN 81 81 N->A: Abolishes homodimerization.
{ECO:0000269|PubMed:22927415}.
MUTAGEN 89 89 M->F: Loss of entry of HHV-1/Rid1 and
HSV-2. No effect on PRV entry.
{ECO:0000269|PubMed:11602758}.
MUTAGEN 89 89 M->I: Increased entry of HHV-1/Rid1 and
HSV-2. {ECO:0000269|PubMed:11602758}.
STRAND 35 37 {ECO:0000244|PDB:3R0N}.
STRAND 40 43 {ECO:0000244|PDB:3R0N}.
STRAND 50 52 {ECO:0000244|PDB:3R0N}.
STRAND 55 58 {ECO:0000244|PDB:3R0N}.
STRAND 64 71 {ECO:0000244|PDB:3R0N}.
HELIX 77 79 {ECO:0000244|PDB:3R0N}.
STRAND 81 86 {ECO:0000244|PDB:3R0N}.
TURN 87 89 {ECO:0000244|PDB:3R0N}.
STRAND 90 92 {ECO:0000244|PDB:3R0N}.
STRAND 95 98 {ECO:0000244|PDB:3R0N}.
HELIX 100 102 {ECO:0000244|PDB:3R0N}.
STRAND 103 107 {ECO:0000244|PDB:3R0N}.
TURN 113 115 {ECO:0000244|PDB:4DFH}.
STRAND 125 127 {ECO:0000244|PDB:3R0N}.
HELIX 132 134 {ECO:0000244|PDB:3R0N}.
STRAND 136 145 {ECO:0000244|PDB:3R0N}.
STRAND 148 157 {ECO:0000244|PDB:3R0N}.
SEQUENCE 538 AA; 57742 MW; 3AE4F83E92F6F624 CRC64;
MARAAALLPS RSPPTPLLWP LLLLLLLETG AQDVRVQVLP EVRGQLGGTV ELPCHLLPPV
PGLYISLVTW QRPDAPANHQ NVAAFHPKMG PSFPSPKPGS ERLSFVSAKQ STGQDTEAEL
QDATLALHGL TVEDEGNYTC EFATFPKGSV RGMTWLRVIA KPKNQAEAQK VTFSQDPTTV
ALCISKEGRP PARISWLSSL DWEAKETQVS GTLAGTVTVT SRFTLVPSGR ADGVTVTCKV
EHESFEEPAL IPVTLSVRYP PEVSISGYDD NWYLGRTDAT LSCDVRSNPE PTGYDWSTTS
GTFPTSAVAQ GSQLVIHAVD SLFNTTFVCT VTNAVGMGRA EQVIFVRETP NTAGAGATGG
IIGGIIAAII ATAVAATGIL ICRQQRKEQT LQGAEEDEDL EGPPSYKPPT PKAKLEAQEM
PSQLFTLGAS EHSPLKTPYF DAGASCTEQE MPRYHELPTL EERSGPLHPG ATSLGSPIPV
PPGPPAVEDV SLDLEDEEGE EEEEYLDKIN PIYDALSYSS PSDSYQGKGF VMSRAMYV


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