PVR_CHLAE
ID PVR_CHLAE Reviewed; 417 AA.
AC P32506;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Poliovirus receptor homolog;
DE AltName: CD_antigen=CD155;
DE Flags: Precursor;
GN Name=PVR; Synonyms=PVS;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND DELTA).
RC TISSUE=Kidney;
RX PubMed=1331508; DOI=10.1128/jvi.66.12.7059-7066.1992;
RA Koike S., Ise I., Sato Y., Yonekawa H., Gotoh O., Nomoto A.;
RT "A second gene for the African green monkey poliovirus receptor that has no
RT putative N-glycosylation site in the functional N-terminal immunoglobulin-
RT like domain.";
RL J. Virol. 66:7059-7066(1992).
CC -!- FUNCTION: Mediates NK cell adhesion and triggers NK cell effector
CC functions. Binds two different NK cell receptors: CD96 and CD226. These
CC interactions accumulates at the cell-cell contact site, leading to the
CC formation of a mature immunological synapse between NK cell and target
CC cell. This may trigger adhesion and secretion of lytic granules and
CC IFN-gamma and activate cytotoxicity of activated NK cells. May also
CC promote NK cell-target cell modular exchange, and PVR transfer to the
CC NK cell (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Can form trans-heterodimers with NECTIN3. The extracellular
CC domain interacts with VTN, CD226 and CD96. The cytoplasmic domain
CC interacts with DYNLT1. Binds with high affinity to TIGIT (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform Alpha]: Cell membrane; Single-pass type
CC I membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform Beta]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform Gamma]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Alpha;
CC IsoId=P32506-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P32506-3; Sequence=Not described;
CC Name=Gamma;
CC IsoId=P32506-4; Sequence=Not described;
CC Name=Delta;
CC IsoId=P32506-2; Sequence=VSP_002622, VSP_002623;
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). The
CC phosphorylated ITIM motif can bind the SH2 domain of several SH2-
CC containing phosphatases (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by Src kinases on tyrosine residues in the ITIM
CC motif upon ligation. Interaction with TIGIT is required for
CC Phosphorylation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
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DR EMBL; D12611; BAA02136.1; -; mRNA.
DR EMBL; D12612; BAA02137.1; -; mRNA.
DR PIR; A44194; A44194.
DR PIR; B44194; B44194.
DR AlphaFoldDB; P32506; -.
DR SMR; P32506; -.
DR MEROPS; I43.001; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Host-virus interaction; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Receptor; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..417
FT /note="Poliovirus receptor homolog"
FT /id="PRO_0000015132"
FT TOPO_DOM 21..343
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..139
FT /note="Ig-like V-type"
FT DOMAIN 145..237
FT /note="Ig-like C2-type 1"
FT DOMAIN 244..328
FT /note="Ig-like C2-type 2"
FT MOD_RES 398
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15151"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 166..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 266..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 386..392
FT /note="EHASASA -> HHQSCHN (in isoform Delta)"
FT /evidence="ECO:0000303|PubMed:1331508"
FT /id="VSP_002622"
FT VAR_SEQ 393..417
FT /note="Missing (in isoform Delta)"
FT /evidence="ECO:0000303|PubMed:1331508"
FT /id="VSP_002623"
SQ SEQUENCE 417 AA; 45465 MW; DA4AD0FE4D2F6E1F CRC64;
MARTMAAAWP PLLLTLLELS WPPPGTGDII VQAPTQVPGF LGDSVTLPCY LQVPGMEETH
VSQLTWSRHG ESGSMAVFHQ TQGPNYSEPK RLEFVAARLG TELRDASLRM FGLRVEDEGN
YTCLFVTFPQ GSRSVDIWLR VLAKPQNTAE VQKVQLTGKP VPVARCVSTG GRPPAHITWH
SDLGGMPNTS QAPGFLSGTV TVTSLWILVP SSQVDGKSVT CKVEHESFEK PQLLTVNLTV
YYPPEVSISG YDNNWYLSQN EATLTCDARS NPEPTGYNWS TTMGPLPPFA VAQGAQLLIR
PVDKPINTTF ICNVTNALGA RQAELTVQVK EGPPSEPSGM SSNIIIFLIL GIVILLTLLG
IGVYFYRSRC SREFLWCHHL SPSSEEHASA SANGYISYSD VSREASSSQD PQTEGTR
