V2116_MOUSE
ID V2116_MOUSE Reviewed; 856 AA.
AC E9Q6I0; D7URW5;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Vomeronasal type-2 receptor 116 {ECO:0000312|MGI:MGI:3646674};
DE AltName: Full=Vomeronasal type-2 receptor P5 {ECO:0000303|PubMed:20596023};
DE Flags: Precursor;
GN Name=Vmn2r116 {ECO:0000312|Ensembl:ENSMUSP00000128106,
GN ECO:0000312|MGI:MGI:3646674}; Synonyms=V2rp5 {ECO:0000312|EMBL:BAJ10472.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAJ10472.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAJ10472.1};
RX PubMed=20596023; DOI=10.1038/nature09142;
RA Haga S., Hattori T., Sato T., Sato K., Matsuda S., Kobayakawa R.,
RA Sakano H., Yoshihara Y., Kikusui T., Touhara K.;
RT "The male mouse pheromone ESP1 enhances female sexual receptive behaviour
RT through a specific vomeronasal receptor.";
RL Nature 466:118-122(2010).
RN [2] {ECO:0000312|Ensembl:ENSMUSP00000128106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000128106};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305}
RP FUNCTION.
RX DOI=10.1351/pac200779040775;
RA Haga S., Kimoto H., Touhara K.;
RT "Molecular characterization of vomeronasal sensory neurons responding to a
RT male-specific peptide in tear fluid: sexual communication in mice.";
RL Pure Appl. Chem. 79:775-783(2007).
RN [4] {ECO:0000305}
RP INTERACTION WITH ESP1.
RX PubMed=23576433; DOI=10.1074/jbc.m112.436782;
RA Yoshinaga S., Sato T., Hirakane M., Esaki K., Hamaguchi T.,
RA Haga-Yamanaka S., Tsunoda M., Kimoto H., Shimada I., Touhara K.,
RA Terasawa H.;
RT "Structure of the mouse sex peptide pheromone ESP1 reveals a molecular
RT basis for specific binding to the class C G-protein-coupled vomeronasal
RT receptor.";
RL J. Biol. Chem. 288:16064-16072(2013).
CC -!- FUNCTION: Receptor for the Esp1 pheromone. Mediates the response to
CC Esp1 which enhances female sexual receptive behavior (lordosis) upon
CC male mounting, resulting in successful copulation.
CC {ECO:0000269|PubMed:20596023, ECO:0000269|PubMed:23576433,
CC ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the vomeronasal organ.
CC {ECO:0000269|PubMed:20596023}.
CC -!- DISRUPTION PHENOTYPE: No response of neurons in the vomeronasal organ
CC or accessory olfactory bulb to Esp1 and no enhancement of lordosis
CC following exposure to Esp1. {ECO:0000269|PubMed:20596023}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000255}.
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DR EMBL; AB540947; BAJ10472.1; -; mRNA.
DR EMBL; CT485617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS50009.1; -.
DR RefSeq; NP_001098050.1; NM_001104580.1.
DR AlphaFoldDB; E9Q6I0; -.
DR SMR; E9Q6I0; -.
DR IntAct; E9Q6I0; 1.
DR STRING; 10090.ENSMUSP00000128106; -.
DR GlyGen; E9Q6I0; 1 site.
DR PaxDb; E9Q6I0; -.
DR PRIDE; E9Q6I0; -.
DR Ensembl; ENSMUST00000164856; ENSMUSP00000128106; ENSMUSG00000090966.
DR GeneID; 619697; -.
DR KEGG; mmu:619697; -.
DR UCSC; uc009vbt.1; mouse.
DR CTD; 619697; -.
DR MGI; MGI:3646674; Vmn2r116.
DR VEuPathDB; HostDB:ENSMUSG00000090966; -.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT00950000183069; -.
DR HOGENOM; CLU_005389_5_0_1; -.
DR InParanoid; E9Q6I0; -.
DR OMA; LIRWKIS; -.
DR OrthoDB; 546292at2759; -.
DR PhylomeDB; E9Q6I0; -.
DR TreeFam; TF340115; -.
DR BioGRID-ORCS; 619697; 5 hits in 68 CRISPR screens.
DR ChiTaRS; Vmn2r116; mouse.
DR PRO; PR:E9Q6I0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; E9Q6I0; protein.
DR ExpressionAtlas; E9Q6I0; baseline and differential.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0016503; F:pheromone receptor activity; IGI:MGI.
DR GO; GO:0045925; P:positive regulation of female receptivity; IGI:MGI.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR Gene3D; 2.10.50.30; -; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR000337; GPCR_3.
DR InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR InterPro; IPR038550; GPCR_3_9-Cys_sf.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR000068; GPCR_3_Ca_sens_rcpt-rel.
DR InterPro; IPR017979; GPCR_3_CS.
DR InterPro; IPR004073; GPCR_3_vmron_rcpt_2.
DR InterPro; IPR028082; Peripla_BP_I.
DR PANTHER; PTHR24061; PTHR24061; 1.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF07562; NCD3G; 1.
DR PRINTS; PR00248; GPCRMGR.
DR PRINTS; PR01535; VOMERONASL2R.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Pheromone response; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..856
FT /note="Vomeronasal type-2 receptor 116"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424696"
FT TOPO_DOM 19..586
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 608..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..658
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 659..679
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 680..690
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..745
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 746..766
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 767..778
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 800..806
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 807..827
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 828..856
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 856 AA; 97704 MW; E9E246C276AF9761 CRC64;
MFTLIFLFLF LNIPLLVADF ISPRCFWKMK QNEYRDRHHG TGCIFLILAI QQPVKKEYFS
HILNIQTHTE NHKYALALAF SIYEINRNPD LLPNMSLIFI FSADSCEWES ELSLIRFGLQ
NSDNLPNYLC EELTKCILAL TNMNWATTVT LHTILSNFLS DQLLHITYGT FHPALSDHEK
FPYLHQMASD HTSLALALVS FIIHFGWNWV GLVISDSDQG IQFLSYLRRE MEKYTLCFAF
VNMIPLNINL YMSRAEVYYN QIMTSSTNVV IIYGDTDSTL AVSFRMWESL GIQRLWITTS
QWDVSPSMKD FTFGNKYGTF AFEQHHSEIS GFKHFVQTLN SVKCPDEYLV KLEWMHFNCE
VSASKCKTLK NCSSNHSLKW LMVHTFDMAF IEESYYIYNA VYAFAHVLHQ FTFQKFDNLP
KDNGKEHNYS CKKLYSYLRK NHFINPVGDR VSMNQRDKLQ EEYDIVYIWN FPQGLGLRVK
IGMFSPYFPN GQQVHLSEDM LKWARGSTQV PTSMCSADCG PGSRKFRMDG MAACCFHCKP
CPENEISNET NVDNCVQCPE DQYANTEQNH CIRKAVVFLS YEEPLGVALS LLSLCFSAFT
TVVLGIFVKH HNTPIVKANN RTLTYLLLIS LIFCFLCPLL FIGHPNSATC ILQQLTFGVV
FTVSLSTVLA KTITVVLAFK IIASQRMMKY FLISGAINYI IPICILIQVI VCAVWLRASP
PSVDIDAHSE HGQIIIVCHK GSVNAFYCVL GYLAILAFGS FTLAFLSRNL PGAFNEAKSI
TFSMLVFCSV WVTFIPVYHS TKGKVMVAVE IFSTLASSAG MLGCIFVPKC YTILFRQDQN
SLEMIRVKSS SNVHVS
