PVRIG_HUMAN
ID PVRIG_HUMAN Reviewed; 326 AA.
AC Q6DKI7; D6W5U9; Q9BVK3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Transmembrane protein PVRIG;
DE AltName: Full=CD112 receptor;
DE Short=CD112R;
DE AltName: Full=Poliovirus receptor-related immunoglobulin domain-containing protein;
GN Name=PVRIG; Synonyms=C7orf15;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-81.
RC TISSUE=Lymph, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION.
RX PubMed=16926269; DOI=10.1152/physiolgenomics.00284.2005;
RA Wilson M.D., Cheung J., Martindale D.W., Scherer S.W., Koop B.F.;
RT "Comparative analysis of the paired immunoglobulin-like receptor (PILR)
RT locus in six mammalian genomes: duplication, conversion, and the birth of
RT new genes.";
RL Physiol. Genomics 27:201-218(2006).
RN [4]
RP FUNCTION AS NECTIN2 RECEPTOR, INTERACTION WITH NECTIN2, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, INDUCTION, PHOSPHORYLATION AT TYR-233, AND
RP MUTAGENESIS OF TYR-233 AND TYR-293.
RX PubMed=26755705; DOI=10.1084/jem.20150785;
RA Zhu Y., Paniccia A., Schulick A.C., Chen W., Koenig M.R., Byers J.T.,
RA Yao S., Bevers S., Edil B.H.;
RT "Identification of CD112R as a novel checkpoint for human T cells.";
RL J. Exp. Med. 213:167-176(2016).
CC -!- FUNCTION: Cell surface receptor for NECTIN2. May act as a coinhibitory
CC receptor that suppresses T-cell receptor-mediated signals. Following
CC interaction with NECTIN2, inhibits T-cell proliferation. Competes with
CC CD226 for NECTIN2-binding. {ECO:0000269|PubMed:26755705}.
CC -!- SUBUNIT: Interacts with NECTIN2, hence competing with CD226.
CC {ECO:0000269|PubMed:26755705}.
CC -!- INTERACTION:
CC Q6DKI7; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-17964309, EBI-2804156;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26755705};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in some types of immune cells. Expressed
CC at low levels on the surface of freshly isolated T-cells and natural
CC killer (NK) cells, predominantly on CD8+ T-cells (mainly
CC memory/effector, but not naive cells) and on both CD16+ and CD16- NK
CC cells. T-cell expression levels are variable among individuals. Not
CC detected in B-cells, naive or helper T-cells, monocytes, nor
CC neutrophils (at protein level). Not detected in dendritic cells.
CC {ECO:0000269|PubMed:26755705}.
CC -!- INDUCTION: In T-cells, up-regulated by activation induced by treatment
CC with anti-CD3 and anti-CD28 antibodies. {ECO:0000269|PubMed:26755705}.
CC -!- MISCELLANEOUS: Was named PVRIG for the homology observed between its
CC second exon and the variable immunoglobulin domain of the polio virus
CC receptor (PVR/CD155) and polio virus receptor-like (PVRL) genes.
CC {ECO:0000305|PubMed:16926269}.
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DR EMBL; CH471091; EAW76566.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76567.1; -; Genomic_DNA.
DR EMBL; BC001129; AAH01129.1; -; mRNA.
DR EMBL; BC073861; AAH73861.1; -; mRNA.
DR EMBL; BC107873; AAI07874.1; -; mRNA.
DR CCDS; CCDS5690.1; -.
DR RefSeq; NP_076975.2; NM_024070.3.
DR RefSeq; XP_011514877.1; XM_011516575.2.
DR AlphaFoldDB; Q6DKI7; -.
DR SMR; Q6DKI7; -.
DR BioGRID; 299834; 22.
DR IntAct; Q6DKI7; 11.
DR STRING; 9606.ENSP00000316675; -.
DR iPTMnet; Q6DKI7; -.
DR PhosphoSitePlus; Q6DKI7; -.
DR BioMuta; PVRIG; -.
DR DMDM; 74736413; -.
DR jPOST; Q6DKI7; -.
DR MassIVE; Q6DKI7; -.
DR PaxDb; Q6DKI7; -.
DR PeptideAtlas; Q6DKI7; -.
DR PRIDE; Q6DKI7; -.
DR ProteomicsDB; 66232; -.
DR Antibodypedia; 30659; 200 antibodies from 23 providers.
DR DNASU; 79037; -.
DR Ensembl; ENST00000317271.2; ENSP00000316675.2; ENSG00000213413.2.
DR GeneID; 79037; -.
DR KEGG; hsa:79037; -.
DR UCSC; uc003uuf.2; human.
DR CTD; 79037; -.
DR DisGeNET; 79037; -.
DR GeneCards; PVRIG; -.
DR HGNC; HGNC:32190; PVRIG.
DR HPA; ENSG00000213413; Tissue enhanced (intestine, lymphoid tissue).
DR MIM; 617012; gene.
DR neXtProt; NX_Q6DKI7; -.
DR OpenTargets; ENSG00000213413; -.
DR PharmGKB; PA162400434; -.
DR VEuPathDB; HostDB:ENSG00000213413; -.
DR eggNOG; KOG4433; Eukaryota.
DR GeneTree; ENSGT00390000017799; -.
DR HOGENOM; CLU_862017_0_0_1; -.
DR InParanoid; Q6DKI7; -.
DR OMA; INTSFCP; -.
DR OrthoDB; 1391646at2759; -.
DR PhylomeDB; Q6DKI7; -.
DR TreeFam; TF343319; -.
DR PathwayCommons; Q6DKI7; -.
DR SignaLink; Q6DKI7; -.
DR BioGRID-ORCS; 79037; 12 hits in 1060 CRISPR screens.
DR ChiTaRS; PVRIG; human.
DR GenomeRNAi; 79037; -.
DR Pharos; Q6DKI7; Tbio.
DR PRO; PR:Q6DKI7; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q6DKI7; protein.
DR Bgee; ENSG00000213413; Expressed in granulocyte and 98 other tissues.
DR Genevisible; Q6DKI7; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IMP:UniProtKB.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IMP:UniProtKB.
DR InterPro; IPR034452; TM_PVRIG.
DR PANTHER; PTHR39220; PTHR39220; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..326
FT /note="Transmembrane protein PVRIG"
FT /id="PRO_0000337142"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 296..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 233
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:26755705"
FT VARIANT 81
FT /note="N -> D (in dbSNP:rs2906645)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_043624"
FT MUTAGEN 233
FT /note="Y->F: Reduced phosphorylation."
FT /evidence="ECO:0000269|PubMed:26755705"
FT MUTAGEN 293
FT /note="Y->F: No effect on global phosphorylation."
FT /evidence="ECO:0000269|PubMed:26755705"
SQ SEQUENCE 326 AA; 34344 MW; 7D9DF363C523F9CD CRC64;
MRTEAQVPAL QPPEPGLEGA MGHRTLVLPW VLLTLCVTAG TPEVWVQVRM EATELSSFTI
RCGFLGSGSI SLVTVSWGGP NGAGGTTLAV LHPERGIRQW APARQARWET QSSISLILEG
SGASSPCANT TFCCKFASFP EGSWEACGSL PPSSDPGLSA PPTPAPILRA DLAGILGVSG
VLLFGCVYLL HLLRRHKHRP APRLQPSRTS PQAPRARAWA PSQASQAALH VPYATINTSC
RPATLDTAHP HGGPSWWASL PTHAAHRPQG PAAWASTPIP ARGSFVSVEN GLYAQAGERP
PHTGPGLTLF PDPRGPRAME GPLGVR
