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

 NECT2_MOUSE             Reviewed;         530 AA.
P32507; Q62096;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 2.
07-JUN-2017, entry version 160.
RecName: Full=Nectin-2;
AltName: Full=Herpes virus entry mediator B;
Short=Herpesvirus entry mediator B;
Short=HveB;
AltName: Full=Murine herpes virus entry protein B;
Short=mHveB;
AltName: Full=Nectin cell adhesion molecule 2 {ECO:0000250|UniProtKB:Q92692};
AltName: Full=Poliovirus receptor homolog;
AltName: Full=Poliovirus receptor-related protein 2;
AltName: CD_antigen=CD112;
Flags: Precursor;
Name=Nectin2 {ECO:0000250|UniProtKB:Q92692};
Synonyms=Mph, Pvr, Pvrl2, Pvs;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
PubMed=1560525;
Morrison M.E., Racaniello V.R.;
"Molecular cloning and expression of a murine homolog of the human
poliovirus receptor gene.";
J. Virol. 66:2807-2813(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=8132569;
Aoki J., Koike S., Ise I., Sato-Yoshida Y., Nomoto A.;
"Amino acid residues on human poliovirus receptor involved in
interaction with poliovirus.";
J. Biol. Chem. 269:8431-8438(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
STRAIN=FVB/N; TISSUE=Colon;
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).
[4]
CHARACTERIZATION.
PubMed=10196354;
Shukla D., Rowe C.L., Dong Y., Racaniello V.R., Spear P.G.;
"The murine homolog (Mph) of human herpesvirus entry protein B (HveB)
mediates entry of pseudorabies virus but not herpes simplex virus
types 1 and 2.";
J. Virol. 73:4493-4497(1999).
[5]
INTERACTION WITH NECTIN3.
PubMed=10744716; DOI=10.1074/jbc.275.14.10291;
Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M.,
Nishimura M., Tachibana K., Mizoguchi A., Takai Y.;
"Nectin-3: a new member of immunoglobulin-like cell adhesion molecules
that shows homophilic and heterophilic cell-cell adhesion
activities.";
J. Biol. Chem. 275:10291-10299(2000).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128; ASN-138 AND ASN-315.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401 AND SER-424, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 32-250, SUBUNIT, DISULFIDE
BONDS, GLYCOSYLATION AT ASN-128 AND ASN-138, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=22902367; DOI=10.1038/nsmb.2366;
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.;
"Nectin ectodomain structures reveal a canonical adhesive interface.";
Nat. Struct. Mol. Biol. 19:906-915(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. Probable cell
adhesion protein. {ECO:0000250|UniProtKB:Q92692}.
-!- SUBUNIT: Can form trans-heterodimers with NECTIN3
(PubMed:10744716, PubMed:22902367). 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 (By
similarity). {ECO:0000250|UniProtKB:Q92692,
ECO:0000269|PubMed:10744716, ECO:0000269|PubMed:22902367}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q92692}; Single-pass type I membrane
protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Beta;
IsoId=P32507-1; Sequence=Displayed;
Name=Alpha;
IsoId=P32507-2; Sequence=VSP_002630, VSP_002631;
-!- TISSUE SPECIFICITY: Brain, spinal cord, spleen, kidney, heart and
liver.
-!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M80206; AAA39734.1; -; mRNA.
EMBL; D26107; BAA05103.1; -; mRNA.
EMBL; BC059941; AAH59941.1; -; mRNA.
CCDS; CCDS20913.1; -. [P32507-1]
CCDS; CCDS52063.1; -. [P32507-2]
PIR; A38211; HLMSP3.
PIR; A53437; A53437.
RefSeq; NP_001153196.1; NM_001159724.1. [P32507-2]
RefSeq; NP_033016.3; NM_008990.3. [P32507-1]
UniGene; Mm.4341; -.
PDB; 4FMK; X-ray; 2.56 A; A=32-250.
PDB; 4FN0; X-ray; 3.35 A; A/B/C=32-250.
PDB; 4FS0; X-ray; 3.25 A; A=32-250.
PDBsum; 4FMK; -.
PDBsum; 4FN0; -.
PDBsum; 4FS0; -.
ProteinModelPortal; P32507; -.
SMR; P32507; -.
DIP; DIP-59964N; -.
IntAct; P32507; 3.
STRING; 10090.ENSMUSP00000074898; -.
iPTMnet; P32507; -.
PhosphoSitePlus; P32507; -.
SwissPalm; P32507; -.
MaxQB; P32507; -.
PaxDb; P32507; -.
PeptideAtlas; P32507; -.
PRIDE; P32507; -.
Ensembl; ENSMUST00000075447; ENSMUSP00000074898; ENSMUSG00000062300. [P32507-1]
Ensembl; ENSMUST00000108450; ENSMUSP00000104089; ENSMUSG00000062300. [P32507-2]
GeneID; 19294; -.
KEGG; mmu:19294; -.
UCSC; uc009fnd.2; mouse. [P32507-1]
UCSC; uc009fne.3; mouse. [P32507-2]
CTD; 5819; -.
MGI; MGI:97822; Nectin2.
eggNOG; ENOG410IIB8; Eukaryota.
eggNOG; ENOG4111FZM; LUCA.
GeneTree; ENSGT00880000137893; -.
HOGENOM; HOG000237277; -.
HOVERGEN; HBG019169; -.
InParanoid; P32507; -.
KO; K06531; -.
OMA; TVNLRCA; -.
OrthoDB; EOG091G0CPW; -.
PhylomeDB; P32507; -.
TreeFam; TF331051; -.
Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-MMU-418990; Adherens junctions interactions.
Reactome; R-MMU-420597; Nectin/Necl trans heterodimerization.
ChiTaRS; Pvrl2; mouse.
PRO; PR:P32507; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000062300; -.
CleanEx; MM_PVRL2; -.
Genevisible; P32507; MM.
GO; GO:0043296; C:apical junction complex; IDA:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0044291; C:cell-cell contact zone; IDA:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:HGNC.
GO; GO:0005915; C:zonula adherens; IDA:BHF-UCL.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC.
GO; GO:0004872; F:receptor activity; IBA:GO_Central.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0001675; P:acrosome assembly; IMP:MGI.
GO; GO:0044406; P:adhesion of symbiont to host; ISO:MGI.
GO; GO:0032990; P:cell part morphogenesis; IMP:MGI.
GO; GO:0008037; P:cell recognition; IBA:GO_Central.
GO; GO:0044782; P:cilium organization; IMP:MGI.
GO; GO:0046814; P:coreceptor-mediated virion attachment to host cell; ISO:MGI.
GO; GO:0007010; P:cytoskeleton organization; IMP:MGI.
GO; GO:0051654; P:establishment of mitochondrion localization; IMP:MGI.
GO; GO:0009566; P:fertilization; IMP:MGI.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; ISO:MGI.
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:HGNC.
GO; GO:0002891; P:positive regulation of immunoglobulin mediated immune response; ISO:MGI.
GO; GO:0033005; P:positive regulation of mast cell activation; ISO:MGI.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:MGI.
GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; ISO:MGI.
GO; GO:0046596; P:regulation of viral entry into host cell; ISO:MGI.
GO; GO:0030382; P:sperm mitochondrion organization; IMP:MGI.
GO; GO:0007286; P:spermatid development; IMP:BHF-UCL.
GO; GO:0007289; P:spermatid nucleus differentiation; IMP:MGI.
GO; GO:0042271; P:susceptibility to natural killer cell mediated cytotoxicity; ISO:MGI.
GO; GO:0060370; P:susceptibility to T cell mediated cytotoxicity; ISO:MGI.
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; 3.
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;
Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 530 Nectin-2.
/FTId=PRO_0000015137.
TOPO_DOM 32 351 Extracellular. {ECO:0000255}.
TRANSMEM 352 372 Helical. {ECO:0000255}.
TOPO_DOM 373 530 Cytoplasmic. {ECO:0000255}.
DOMAIN 32 147 Ig-like V-type.
DOMAIN 153 247 Ig-like C2-type 1.
DOMAIN 252 337 Ig-like C2-type 2.
MOD_RES 401 401 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 128 128 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:22902367}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:22902367}.
CARBOHYD 315 315 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
DISULFID 54 131 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:22902367}.
DISULFID 174 229 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:22902367}.
DISULFID 274 320 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 339 467 ESPSTAGAGATGGIIGGIIAAIIATAVAGTGILICRQQRKE
QRLQAADEEEELEGPPSYKPPTPKAKLEEPEMPSQLFTLGA
SEHSPVKTPYFDAGVSCADQEMPRYHELPTLEERSGPLLLG
ATGLGP -> DTPQASRDVGPLVWGAVGGTLLVLLLAGGFL
ALILLRGRRRRKSPGGGGNDGDRGSYDPKTQVFGNGGPVFW
RSASPEPMRPDGREEDEEEEEEMKAEEGLMLPPHESPKDDM
ESHLDGSLISRRAVYV (in isoform Alpha).
{ECO:0000303|PubMed:1560525}.
/FTId=VSP_002630.
VAR_SEQ 468 530 Missing (in isoform Alpha).
{ECO:0000303|PubMed:1560525}.
/FTId=VSP_002631.
STRAND 35 37 {ECO:0000244|PDB:4FMK}.
STRAND 40 45 {ECO:0000244|PDB:4FMK}.
STRAND 50 52 {ECO:0000244|PDB:4FMK}.
STRAND 54 56 {ECO:0000244|PDB:4FN0}.
STRAND 63 70 {ECO:0000244|PDB:4FMK}.
STRAND 76 81 {ECO:0000244|PDB:4FMK}.
TURN 82 84 {ECO:0000244|PDB:4FMK}.
STRAND 85 87 {ECO:0000244|PDB:4FMK}.
TURN 95 97 {ECO:0000244|PDB:4FMK}.
STRAND 98 100 {ECO:0000244|PDB:4FMK}.
STRAND 104 106 {ECO:0000244|PDB:4FN0}.
HELIX 108 111 {ECO:0000244|PDB:4FS0}.
STRAND 116 118 {ECO:0000244|PDB:4FMK}.
HELIX 123 125 {ECO:0000244|PDB:4FMK}.
STRAND 127 136 {ECO:0000244|PDB:4FMK}.
STRAND 139 151 {ECO:0000244|PDB:4FMK}.
STRAND 154 159 {ECO:0000244|PDB:4FMK}.
STRAND 165 167 {ECO:0000244|PDB:4FMK}.
STRAND 169 181 {ECO:0000244|PDB:4FMK}.
STRAND 184 188 {ECO:0000244|PDB:4FMK}.
STRAND 194 201 {ECO:0000244|PDB:4FMK}.
STRAND 208 216 {ECO:0000244|PDB:4FMK}.
HELIX 220 222 {ECO:0000244|PDB:4FMK}.
STRAND 226 232 {ECO:0000244|PDB:4FMK}.
STRAND 236 238 {ECO:0000244|PDB:4FS0}.
STRAND 240 245 {ECO:0000244|PDB:4FMK}.
SEQUENCE 530 AA; 57318 MW; 0ED71BFA2B231BBE CRC64;
MARAAVLPPS RLSPTLPLLP LLLLLLQETG AQDVRVRVLP EVRGRLGGTV ELPCHLLPPT
TERVSQVTWQ RLDGTVVAAF HPSFGVDFPN SQFSKDRLSF VRARPETNAD LRDATLAFRG
LRVEDEGNYT CEFATFPNGT RRGVTWLRVI AQPENHAEAQ EVTIGPQSVA VARCVSTGGR
PPARITWISS LGGEAKDTQE PGIQAGTVTI ISRYSLVPVG RADGVKVTCR VEHESFEEPI
LLPVTLSVRY PPEVSISGYD DNWYLGRSEA ILTCDVRSNP EPTDYDWSTT SGVFPASAVA
QGSQLLVHSV DRMVNTTFIC TATNAVGTGR AEQVILVRES PSTAGAGATG GIIGGIIAAI
IATAVAGTGI LICRQQRKEQ RLQAADEEEE LEGPPSYKPP TPKAKLEEPE MPSQLFTLGA
SEHSPVKTPY FDAGVSCADQ EMPRYHELPT LEERSGPLLL GATGLGPSLL VPPGPNVVEG
VSLSLEDEEE DDEEEDFLDK INPIYDALSY PSPSDSYQSK DFFVSRAMYV


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