V2R_HUMAN
ID V2R_HUMAN Reviewed; 371 AA.
AC P30518; C5HF20; O43192; Q3MJD3; Q9UCV9;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Vasopressin V2 receptor;
DE Short=V2R;
DE AltName: Full=AVPR V2;
DE AltName: Full=Antidiuretic hormone receptor;
DE AltName: Full=Renal-type arginine vasopressin receptor;
GN Name=AVPR2; Synonyms=ADHR, DIR, DIR3, V2R;
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 [GENOMIC DNA].
RX PubMed=1415251;
RA Seibold A., Brabet P., Rosenthal W., Birnbaumer M.;
RT "Structure and chromosomal localization of the human antidiuretic hormone
RT receptor gene.";
RL Am. J. Hum. Genet. 51:1078-1083(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=1534149; DOI=10.1038/357333a0;
RA Birnbaumer M., Seibold A., Gilbert S., Ishido M., Barberis C.,
RA Antaramian A., Brabet P., Rosenthal W.;
RT "Molecular cloning of the receptor for human antidiuretic hormone.";
RL Nature 357:333-335(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7913579;
RA Wildin R.S., Antush M.J., Bennett R.L., Schoof J.M., Scott C.R.;
RT "Heterogeneous AVPR2 gene mutations in congenital nephrogenic diabetes
RT insipidus.";
RL Am. J. Hum. Genet. 55:266-277(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=8735975; DOI=10.1016/0196-9781(96)00009-5;
RA Fay M.J., Du J., Yu X., North W.G.;
RT "Evidence for expression of vasopressin V2 receptor mRNA in human lung.";
RL Peptides 17:477-481(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung carcinoma, and Mammary cancer;
RX PubMed=9581826;
RA North W.G., Fay M.J., Longo K.A., Du J.;
RT "Expression of all known vasopressin receptor subtypes by small cell tumors
RT implies a multifaceted role for this neuropeptide.";
RL Cancer Res. 58:1866-1871(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=19440390; DOI=10.1371/journal.pone.0005573;
RA Boselt I., Rompler H., Hermsdorf T., Thor D., Busch W., Schulz A.,
RA Schoneberg T.;
RT "Involvement of the V2 vasopressin receptor in adaptation to limited water
RT supply.";
RL PLoS ONE 4:E5573-E5573(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Warren C.N., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 307-371.
RX PubMed=8882880; DOI=10.1007/s004390050264;
RA Oksche A., Moeller A., Dickson J., Rosendahl W., Rascher W., Bichet D.G.,
RA Rosenthal W.;
RT "Two novel mutations in the aquaporin-2 and the vasopressin V2 receptor
RT genes in patients with congenital nephrogenic diabetes insipidus.";
RL Hum. Genet. 98:587-589(1996).
RN [11]
RP PALMITOYLATION AT CYS-341 AND CYS-342, AND MUTAGENESIS OF CYS-341 AND
RP CYS-342.
RX PubMed=9224808; DOI=10.1124/mol.52.1.21;
RA Sadeghi H.M., Innamorati G., Dagarag M., Birnbaumer M.;
RT "Palmitoylation of the V2 vasopressin receptor.";
RL Mol. Pharmacol. 52:21-29(1997).
RN [12]
RP INTERACTION WITH TMEM147.
RX PubMed=21056967; DOI=10.1124/mol.110.067363;
RA Rosemond E., Rossi M., McMillin S.M., Scarselli M., Donaldson J.G.,
RA Wess J.;
RT "Regulation of M(3) muscarinic receptor expression and function by
RT transmembrane protein 147.";
RL Mol. Pharmacol. 79:251-261(2011).
RN [13]
RP INTERACTION WITH ARRDC4, IDENTIFICATION IN A COMPLEX WITH HGS AND ARRDC4,
RP AND SUBCELLULAR LOCATION.
RX PubMed=23236378; DOI=10.1371/journal.pone.0050557;
RA Shea F.F., Rowell J.L., Li Y., Chang T.H., Alvarez C.E.;
RT "Mammalian alpha arrestins link activated seven transmembrane receptors to
RT Nedd4 family e3 ubiquitin ligases and interact with beta arrestins.";
RL PLoS ONE 7:E50557-E50557(2012).
RN [14]
RP VARIANT XNDI ASP-132.
RX PubMed=1356229; DOI=10.1038/359233a0;
RA Rosenthal W., Seibold A., Antaramian A., Lonergan M., Arthus M.-F.,
RA Hendy G.N., Birnbaumer M., Bichet D.G.;
RT "Molecular identification of the gene responsible for congenital
RT nephrogenic diabetes insipidus.";
RL Nature 359:233-235(1992).
RN [15]
RP VARIANTS XNDI CYS-185; CYS-203 AND CYS-205.
RX PubMed=1303271; DOI=10.1038/ng1092-99;
RA van den Ouweland A.M.W., Dreesen J.C.F.M., Verdijk M., Knoers N.V.A.M.,
RA Monnens L.A.H., Rocchi M., van Oost B.A.;
RT "Mutations in the vasopressin type 2 receptor gene (AVPR2) associated with
RT nephrogenic diabetes insipidus.";
RL Nat. Genet. 2:99-102(1992).
RN [16]
RP VARIANTS XNDI SER-128; CYS-181; ARG-286 AND 247-ARG--GLY-250 DEL.
RX PubMed=1303257; DOI=10.1038/ng1092-103;
RA Pan Y., Metzenberg A., Das S., Jing B., Gitschier J.;
RT "Mutations in the V2 vasopressin receptor gene are associated with X-linked
RT nephrogenic diabetes insipidus.";
RL Nat. Genet. 2:103-106(1992).
RN [17]
RP VARIANTS XNDI PRO-143 AND VAL-277 DEL.
RX PubMed=8267567; DOI=10.1006/bbrc.1993.2578;
RA Tsukaguchi H., Matsubara H., Aritaki S., Kimura T., Abe S., Inada M.;
RT "Two novel mutations in the vasopressin V2 receptor gene in unrelated
RT Japanese kindreds with nephrogenic diabetes insipidus.";
RL Biochem. Biophys. Res. Commun. 197:1000-1010(1993).
RN [18]
RP VARIANT XNDI TRP-113.
RX PubMed=8479490; DOI=10.1056/nejm199305273282105;
RA Holtzman E.J., Harris H.W. Jr., Kolakowski L.F. Jr., Guay-Woodford L.M.,
RA Botelho B., Ausiello D.A.;
RT "A molecular defect in the vasopressin V2-receptor gene causing nephrogenic
RT diabetes insipidus.";
RL N. Engl. J. Med. 328:1534-1537(1993).
RN [19]
RP VARIANT XNDI HIS-137.
RX PubMed=8514744; DOI=10.1016/s0021-9258(19)38614-4;
RA Rosenthal W., Antaramian A., Gilbert S., Birnbaumer M.;
RT "Nephrogenic diabetes insipidus. A V2 vasopressin receptor unable to
RT stimulate adenylyl cyclase.";
RL J. Biol. Chem. 268:13030-13033(1993).
RN [20]
RP VARIANTS XNDI MET-88; CYS-106; ARG-112; TRP-113; PHE-126; SER-128; HIS-137;
RP SER-164; LEU-167; CYS-181; CYS-202 AND PRO-285.
RX PubMed=8037205;
RA Bichet D.G., Birnbaumer M., Lonergan M., Arthus M.-F., Rosenthal W.,
RA Goodyer P., Nivet H., Benoit S., Giampietro P., Simonetti S., Fish A.,
RA Whitley C.B., Jaeger P., Gertner J., New M., Dibona F.J., Kaplan B.S.,
RA Robertson G.L., Hendy G.N., Fujiwara T.M., Morgan K.;
RT "Nature and recurrence of AVPR2 mutations in X-linked nephrogenic diabetes
RT insipidus.";
RL Am. J. Hum. Genet. 55:278-286(1994).
RN [21]
RP VARIANTS XNDI PRO-44 AND THR-167.
RX PubMed=7999078; DOI=10.1006/bbrc.1994.2700;
RA Oksche A., Dickson J., Schuelein R., Hansjoerg W.S., Mueller M.,
RA Rascher W., Birnbaumer M., Rosenthal W.;
RT "Two novel mutations in the vasopressin V2 receptor gene in patients with
RT congenital nephrogenic diabetes insipidus.";
RL Biochem. Biophys. Res. Commun. 205:552-557(1994).
RN [22]
RP VARIANTS XNDI CYS-280 AND PRO-292.
RX PubMed=7987330; DOI=10.1093/hmg/3.8.1429;
RA Wenkert D., Merendino J.J. Jr., Shenker A., Thambi N., Robertson G.L.,
RA Moses A.M., Spiegel A.M.;
RT "Novel mutations in the V2 vasopressin receptor gene of patients with X-
RT linked nephrogenic diabetes insipidus.";
RL Hum. Mol. Genet. 3:1429-1430(1994).
RN [23]
RP VARIANTS XNDI SER-128; VAL-277 DEL AND LEU-286.
RX PubMed=7833930; DOI=10.1093/hmg/3.9.1685;
RA Faa V., Ventruto M.L., Loche S., Bozzola M., Podda R., Cao A.,
RA Rosatelli M.C.;
RT "Mutations in the vasopressin V2-receptor gene in three families of Italian
RT descent with nephrogenic diabetes insipidus.";
RL Hum. Mol. Genet. 3:1685-1686(1994).
RN [24]
RP VARIANT XNDI ARG-80.
RX PubMed=8045948; DOI=10.1210/jcem.79.2.8045948;
RA Yuasa H., Ito M., Oiso Y., Kurokawa M., Watanabe T., Oda Y., Ishizuka T.,
RA Tani N., Ito S., Shibata A., Saito H.;
RT "Novel mutations in the V2 vasopressin receptor gene in two pedigrees with
RT congenital nephrogenic diabetes insipidus.";
RL J. Clin. Endocrinol. Metab. 79:361-365(1994).
RN [25]
RP VARIANT XNDI TRP-113.
RX PubMed=7984150; DOI=10.1210/mend.8.7.7984150;
RA Birnbaumer M., Gilbert S., Rosenthal W.;
RT "An extracellular congenital nephrogenic diabetes insipidus mutation of the
RT vasopressin receptor reduces cell surface expression, affinity for ligand,
RT and coupling to the Gs/adenylyl cyclase system.";
RL Mol. Endocrinol. 8:886-894(1994).
RN [26]
RP VARIANT XNDI CYS-280.
RX PubMed=8078903; DOI=10.1073/pnas.91.18.8457;
RA Friedman E., Bale A.E., Carson E., Boson W.L., Nordenskjoeld M., Ritzen M.,
RA Ferriera P.C., Jammal A., De Marco L.;
RT "Nephrogenic diabetes insipidus: an X chromosome-linked dominant
RT inheritance pattern with a vasopressin type 2 receptor gene that is
RT structurally normal.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:8457-8461(1994).
RN [27]
RP VARIANTS XNDI PRO-143; CYS-202 AND VAL-277 DEL.
RX PubMed=7560098; DOI=10.1172/jci118252;
RA Tsukaguchi H., Matsubara H., Taketani S., Mori Y., Seido T., Inada M.;
RT "Binding-, intracellular transport-, and biosynthesis-defective mutants of
RT vasopressin type 2 receptor in patients with X-linked nephrogenic diabetes
RT insipidus.";
RL J. Clin. Invest. 96:2043-2050(1995).
RN [28]
RP VARIANTS XNDI PRO-43; GLU-107 AND SER-322.
RX PubMed=9402087; DOI=10.1681/asn.v8121855;
RA Vargas-Poussou R., Forestier L., Dautzenberg M.D., Niaudet P., Dechaux M.,
RA Antignac C.;
RT "Mutations in the vasopressin V2 receptor and aquaporin-2 genes in 12
RT families with congenital nephrogenic diabetes insipidus.";
RL J. Am. Soc. Nephrol. 8:1855-1862(1997).
RN [29]
RP VARIANTS XNDI HIS-137; VAL-277 DEL AND PRO-309.
RX PubMed=9452109; DOI=10.1002/humu.1380110188;
RA Shoji Y., Takahashi T., Suzuki Y., Suzuki T., Komatsu K., Hirono H.,
RA Shoji Y., Yokoyama T., Kito H., Takada G.;
RT "Mutational analyses of AVPR2 gene in three Japanese families with X-linked
RT nephrogenic diabetes insipidus: two recurrent mutations, R137H and
RT deltaV278, caused by the hypermutability at CpG dinucleotides.";
RL Hum. Mutat. Suppl. 1:S278-S283(1998).
RN [30]
RP VARIANTS XNDI ARG-112; LYS-317 AND SER-323.
RX PubMed=10694923;
RA Szalai C., Triga D., Czinner A.;
RT "C112R, W323S, N317K mutations in the vasopressin V2 receptor gene in
RT patients with nephrogenic diabetes insipidus.";
RL Hum. Mutat. 12:137-138(1998).
RN [31]
RP VARIANTS XNDI HIS-137 AND CYS-181.
RX PubMed=9711877;
RX DOI=10.1002/(sici)1098-1004(1998)12:3<196::aid-humu7>3.0.co;2-f;
RA Schoeneberg T., Schulz A., Biebermann H., Grueters A., Grimm T.,
RA Huebschmann K., Filler G., Gudermann T., Schultz G.;
RT "V2 vasopressin receptor dysfunction in nephrogenic diabetes insipidus
RT caused by different molecular mechanisms.";
RL Hum. Mutat. 12:196-205(1998).
RN [32]
RP VARIANTS XNDI LYS-46; VAL-105 AND PHE-130.
RX PubMed=10770218; DOI=10.1210/jcem.85.4.6507;
RA Pasel K., Schulz A., Timmermann K., Linnemann K., Hoeltzenbein M.,
RA Jaaskelainen J., Gruters A., Filler G., Schoneberg T.;
RT "Functional characterization of the molecular defects causing nephrogenic
RT diabetes insipidus in eight families.";
RL J. Clin. Endocrinol. Metab. 85:1703-1710(2000).
RN [33]
RP CHARACTERIZATION OF VARIANTS XNDI ASN-204; CYS-205 AND ASP-206.
RX PubMed=11026555; DOI=10.1016/s0303-7207(00)00236-7;
RA Postina R., Ufer E., Pfeiffer R., Knoers N.V., Fahrenholz F.;
RT "Misfolded vasopressin V2 receptors caused by extracellular point mutations
RT entail congenital nephrogenic diabetes insipidus.";
RL Mol. Cell. Endocrinol. 164:31-39(2000).
RN [34]
RP VARIANT XNDI CYS-104.
RX PubMed=11232028; DOI=10.1210/jcem.86.1.7165;
RA Inaba S., Hatakeyama H., Taniguchi N., Miyamori I.;
RT "The property of a novel V2 receptor mutant in a patient with nephrogenic
RT diabetes insipidus.";
RL J. Clin. Endocrinol. Metab. 86:381-385(2001).
RN [35]
RP VARIANTS XNDI CYS-106 AND LEU-287.
RX PubMed=11916004; DOI=10.1007/s100380200002;
RA Chen C.H., Chen W.Y., Liu H.L., Liu T.T., Tsou A.P., Lin C.Y., Chao T.,
RA Qi Y., Hsiao K.J.;
RT "Identification of mutations in the arginine vasopressin receptor 2 gene
RT causing nephrogenic diabetes insipidus in Chinese patients.";
RL J. Hum. Genet. 47:66-73(2002).
RN [36]
RP VARIANTS NSIAD CYS-137 AND LEU-137.
RX PubMed=15872203; DOI=10.1056/nejmoa042743;
RA Feldman B.J., Rosenthal S.M., Vargas G.A., Fenwick R.G., Huang E.A.,
RA Matsuda-Abedini M., Lustig R.H., Mathias R.S., Portale A.A., Miller W.L.,
RA Gitelman S.E.;
RT "Nephrogenic syndrome of inappropriate antidiuresis.";
RL N. Engl. J. Med. 352:1884-1890(2005).
RN [37]
RP VARIANTS XNDI ASP-122 AND HIS-137.
RX PubMed=16845277; DOI=10.1097/01.gim.0000223554.46981.7a;
RA Carroll P., Al-Mojalli H., Al-Abbad A., Al-Hassoun I., Al-Hamed M.,
RA Al-Amr R., Butt A.I., Meyer B.F.;
RT "Novel mutations underlying nephrogenic diabetes insipidus in Arab
RT families.";
RL Genet. Med. 8:443-447(2006).
RN [38]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-247.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Receptor for arginine vasopressin. The activity of this
CC receptor is mediated by G proteins which activate adenylate cyclase.
CC Involved in renal water reabsorption. {ECO:0000269|PubMed:19440390}.
CC -!- SUBUNIT: Interacts with ARRDC4 (PubMed:23236378). Identified in a
CC complex containing at least ARRDC4, V2R and HGS (PubMed:23236378).
CC Interacts with TMEM147 (PubMed:21056967). {ECO:0000269|PubMed:21056967,
CC ECO:0000269|PubMed:23236378}.
CC -!- INTERACTION:
CC P30518; Q8NCT1: ARRDC4; NbExp=2; IntAct=EBI-11675746, EBI-11673273;
CC P30518; P21964: COMT; NbExp=3; IntAct=EBI-11675746, EBI-372265;
CC P30518; Q8IVJ1: SLC41A1; NbExp=3; IntAct=EBI-11675746, EBI-12266234;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23236378};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P30518-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30518-2; Sequence=VSP_036990, VSP_036991;
CC -!- TISSUE SPECIFICITY: Kidney.
CC -!- DISEASE: Nephrogenic syndrome of inappropriate antidiuresis (NSIAD)
CC [MIM:300539]: Characterized by an inability to excrete a free water
CC load, with inappropriately concentrated urine and resultant
CC hyponatremia, hypoosmolarity, and natriuresis.
CC {ECO:0000269|PubMed:15872203}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Diabetes insipidus, nephrogenic, X-linked (XNDI) [MIM:304800]:
CC A disorder caused by the inability of the renal collecting ducts to
CC absorb water in response to arginine vasopressin. Characterized by
CC excessive water drinking (polydipsia), excessive urine excretion
CC (polyuria), persistent hypotonic urine, and hypokalemia.
CC {ECO:0000269|PubMed:10694923, ECO:0000269|PubMed:10770218,
CC ECO:0000269|PubMed:11026555, ECO:0000269|PubMed:11232028,
CC ECO:0000269|PubMed:11916004, ECO:0000269|PubMed:1303257,
CC ECO:0000269|PubMed:1303271, ECO:0000269|PubMed:1356229,
CC ECO:0000269|PubMed:16845277, ECO:0000269|PubMed:7560098,
CC ECO:0000269|PubMed:7833930, ECO:0000269|PubMed:7984150,
CC ECO:0000269|PubMed:7987330, ECO:0000269|PubMed:7999078,
CC ECO:0000269|PubMed:8037205, ECO:0000269|PubMed:8045948,
CC ECO:0000269|PubMed:8078903, ECO:0000269|PubMed:8267567,
CC ECO:0000269|PubMed:8479490, ECO:0000269|PubMed:8514744,
CC ECO:0000269|PubMed:9402087, ECO:0000269|PubMed:9452109,
CC ECO:0000269|PubMed:9711877}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Vasopressin/oxytocin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L22206; AAA03651.1; -; Genomic_DNA.
DR EMBL; Z11687; CAA77746.1; -; mRNA.
DR EMBL; U04357; AAC09005.1; -; Genomic_DNA.
DR EMBL; AF030626; AAB86428.1; -; mRNA.
DR EMBL; AF101727; AAD16444.1; -; mRNA.
DR EMBL; AF032388; AAB87678.1; -; mRNA.
DR EMBL; AY242131; AAO92298.1; -; mRNA.
DR EMBL; FJ411207; ACR39021.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72783.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72784.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72785.1; -; Genomic_DNA.
DR EMBL; BC101484; AAI01485.1; -; mRNA.
DR EMBL; BC112181; AAI12182.1; -; mRNA.
DR CCDS; CCDS14735.1; -. [P30518-1]
DR CCDS; CCDS55539.1; -. [P30518-2]
DR PIR; I51865; I51865.
DR RefSeq; NP_000045.1; NM_000054.4. [P30518-1]
DR RefSeq; NP_001139623.1; NM_001146151.1. [P30518-2]
DR RefSeq; XP_006724891.1; XM_006724828.3.
DR PDB; 4JQI; X-ray; 2.60 A; V=343-371.
DR PDB; 6NI2; EM; 4.00 A; V=343-368.
DR PDB; 6U1N; EM; 4.00 A; R=343-371.
DR PDB; 7BB6; EM; 4.20 A; A=3-371.
DR PDB; 7BB7; EM; 4.40 A; A=3-371.
DR PDB; 7DF9; X-ray; 3.17 A; V=346-368.
DR PDB; 7DFA; X-ray; 2.54 A; V=346-368.
DR PDB; 7DFB; X-ray; 3.28 A; V=346-368.
DR PDB; 7DFC; X-ray; 2.49 A; V=346-367.
DR PDB; 7DW9; EM; 2.60 A; R=1-371.
DR PDB; 7KH0; EM; 2.80 A; R=1-371.
DR PDBsum; 4JQI; -.
DR PDBsum; 6NI2; -.
DR PDBsum; 6U1N; -.
DR PDBsum; 7BB6; -.
DR PDBsum; 7BB7; -.
DR PDBsum; 7DF9; -.
DR PDBsum; 7DFA; -.
DR PDBsum; 7DFB; -.
DR PDBsum; 7DFC; -.
DR PDBsum; 7DW9; -.
DR PDBsum; 7KH0; -.
DR AlphaFoldDB; P30518; -.
DR SMR; P30518; -.
DR BioGRID; 107035; 285.
DR ELM; P30518; -.
DR IntAct; P30518; 4.
DR STRING; 9606.ENSP00000351805; -.
DR BindingDB; P30518; -.
DR ChEMBL; CHEMBL1790; -.
DR DrugBank; DB09059; Atosiban.
DR DrugBank; DB00872; Conivaptan.
DR DrugBank; DB00618; Demeclocycline.
DR DrugBank; DB00035; Desmopressin.
DR DrugBank; DB14642; Lypressin.
DR DrugBank; DB05091; M0002.
DR DrugBank; DB05838; OPC-51803.
DR DrugBank; DB02638; Terlipressin.
DR DrugBank; DB06212; Tolvaptan.
DR DrugBank; DB00067; Vasopressin.
DR DrugCentral; P30518; -.
DR GuidetoPHARMACOLOGY; 368; -.
DR TCDB; 9.A.14.10.3; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P30518; 1 site.
DR iPTMnet; P30518; -.
DR PhosphoSitePlus; P30518; -.
DR SwissPalm; P30518; -.
DR BioMuta; AVPR2; -.
DR DMDM; 267256; -.
DR MassIVE; P30518; -.
DR PaxDb; P30518; -.
DR PeptideAtlas; P30518; -.
DR PRIDE; P30518; -.
DR TopDownProteomics; P30518-2; -. [P30518-2]
DR Antibodypedia; 17443; 310 antibodies from 32 providers.
DR DNASU; 554; -.
DR Ensembl; ENST00000337474.5; ENSP00000338072.5; ENSG00000126895.16. [P30518-1]
DR Ensembl; ENST00000370049.1; ENSP00000359066.1; ENSG00000126895.16. [P30518-2]
DR Ensembl; ENST00000646375.2; ENSP00000496396.1; ENSG00000126895.16. [P30518-1]
DR GeneID; 554; -.
DR KEGG; hsa:554; -.
DR MANE-Select; ENST00000646375.2; ENSP00000496396.1; NM_000054.7; NP_000045.1.
DR UCSC; uc004fjh.5; human. [P30518-1]
DR CTD; 554; -.
DR DisGeNET; 554; -.
DR GeneCards; AVPR2; -.
DR GeneReviews; AVPR2; -.
DR HGNC; HGNC:897; AVPR2.
DR HPA; ENSG00000126895; Tissue enhanced (adipose).
DR MalaCards; AVPR2; -.
DR MIM; 300538; gene.
DR MIM; 300539; phenotype.
DR MIM; 304800; phenotype.
DR neXtProt; NX_P30518; -.
DR OpenTargets; ENSG00000126895; -.
DR Orphanet; 223; Nephrogenic diabetes insipidus.
DR Orphanet; 93606; Nephrogenic syndrome of inappropriate antidiuresis.
DR PharmGKB; PA25189; -.
DR VEuPathDB; HostDB:ENSG00000126895; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244882; -.
DR HOGENOM; CLU_009579_15_3_1; -.
DR InParanoid; P30518; -.
DR OMA; RIMMAEL; -.
DR OrthoDB; 291625at2759; -.
DR PhylomeDB; P30518; -.
DR TreeFam; TF106499; -.
DR PathwayCommons; P30518; -.
DR Reactome; R-HSA-388479; Vasopressin-like receptors.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-9036092; Defective AVP does not bind AVPR2 and causes neurohypophyseal diabetes insipidus (NDI).
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; P30518; -.
DR SIGNOR; P30518; -.
DR BioGRID-ORCS; 554; 10 hits in 698 CRISPR screens.
DR GeneWiki; Arginine_vasopressin_receptor_2; -.
DR GenomeRNAi; 554; -.
DR Pharos; P30518; Tclin.
DR PRO; PR:P30518; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P30518; protein.
DR Bgee; ENSG00000126895; Expressed in apex of heart and 105 other tissues.
DR ExpressionAtlas; P30518; baseline and differential.
DR Genevisible; P30518; HS.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0030139; C:endocytic vesicle; IDA:ARUK-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005768; C:endosome; IDA:ARUK-UCL.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0005000; F:vasopressin receptor activity; IDA:ARUK-UCL.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007599; P:hemostasis; TAS:ProtInc.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:ARUK-UCL.
DR GO; GO:0035814; P:negative regulation of renal sodium excretion; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IBA:GO_Central.
DR GO; GO:0001992; P:regulation of systemic arterial blood pressure by vasopressin; IBA:GO_Central.
DR GO; GO:0003092; P:renal water retention; TAS:ProtInc.
DR GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
DR GO; GO:0021537; P:telencephalon development; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001817; Vasoprsn_rcpt.
DR InterPro; IPR000161; Vprsn_rcpt_V2.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00896; VASOPRESSINR.
DR PRINTS; PR00898; VASOPRSNV2R.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Diabetes insipidus;
KW Disease variant; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..371
FT /note="Vasopressin V2 receptor"
FT /id="PRO_0000070208"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..135
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..220
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..293
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..308
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..328
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 341
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:9224808"
FT LIPID 342
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:9224808"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 305..309
FT /note="APFVL -> GCSRG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9581826"
FT /id="VSP_036990"
FT VAR_SEQ 310..371
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9581826"
FT /id="VSP_036991"
FT VARIANT 7
FT /note="T -> S (in dbSNP:rs5196)"
FT /id="VAR_003516"
FT VARIANT 12
FT /note="G -> E (in dbSNP:rs2071126)"
FT /id="VAR_015296"
FT VARIANT 42
FT /note="A -> V (in dbSNP:rs5198)"
FT /id="VAR_011858"
FT VARIANT 43
FT /note="L -> P (in XNDI)"
FT /evidence="ECO:0000269|PubMed:9402087"
FT /id="VAR_015297"
FT VARIANT 44
FT /note="L -> P (in XNDI)"
FT /evidence="ECO:0000269|PubMed:7999078"
FT /id="VAR_003517"
FT VARIANT 46
FT /note="I -> K (in XNDI; dbSNP:rs104894759)"
FT /evidence="ECO:0000269|PubMed:10770218"
FT /id="VAR_015298"
FT VARIANT 53
FT /note="L -> R (in XNDI)"
FT /id="VAR_015299"
FT VARIANT 55
FT /note="N -> D (in XNDI)"
FT /id="VAR_015300"
FT VARIANT 55
FT /note="N -> H (in XNDI)"
FT /id="VAR_015301"
FT VARIANT 59
FT /note="L -> P (in XNDI; dbSNP:rs193922112)"
FT /id="VAR_015302"
FT VARIANT 61
FT /note="A -> V"
FT /id="VAR_015303"
FT VARIANT 62..64
FT /note="Missing (in XNDI)"
FT /id="VAR_003518"
FT VARIANT 62
FT /note="L -> P (in XNDI)"
FT /id="VAR_015304"
FT VARIANT 64
FT /note="R -> W (in dbSNP:rs150351033)"
FT /id="VAR_003519"
FT VARIANT 80
FT /note="H -> R (in XNDI)"
FT /evidence="ECO:0000269|PubMed:8045948"
FT /id="VAR_003520"
FT VARIANT 81
FT /note="L -> F (in XNDI)"
FT /id="VAR_015305"
FT VARIANT 83
FT /note="L -> P (in XNDI)"
FT /id="VAR_015306"
FT VARIANT 83
FT /note="L -> Q (in XNDI)"
FT /id="VAR_015307"
FT VARIANT 84
FT /note="A -> D (in XNDI)"
FT /id="VAR_015308"
FT VARIANT 85
FT /note="D -> N (in XNDI; dbSNP:rs104894754)"
FT /id="VAR_015309"
FT VARIANT 88
FT /note="V -> M (in XNDI)"
FT /evidence="ECO:0000269|PubMed:8037205"
FT /id="VAR_003521"
FT VARIANT 92
FT /note="Q -> R (in XNDI)"
FT /id="VAR_015310"
FT VARIANT 94
FT /note="L -> Q (in XNDI)"
FT /id="VAR_015311"
FT VARIANT 95
FT /note="P -> L (in XNDI)"
FT /id="VAR_015312"
FT VARIANT 99
FT /note="W -> R (in XNDI)"
FT /id="VAR_015313"
FT VARIANT 104
FT /note="R -> C (in XNDI; binding capacity is 10% of wild-
FT type, but binding affinity is stronger than wild-type;
FT dbSNP:rs104894760)"
FT /evidence="ECO:0000269|PubMed:11232028"
FT /id="VAR_015314"
FT VARIANT 105
FT /note="F -> V (in XNDI; dbSNP:rs104894758)"
FT /evidence="ECO:0000269|PubMed:10770218"
FT /id="VAR_015315"
FT VARIANT 106
FT /note="R -> C (in XNDI)"
FT /evidence="ECO:0000269|PubMed:11916004,
FT ECO:0000269|PubMed:8037205"
FT /id="VAR_003522"
FT VARIANT 107
FT /note="G -> E (in XNDI)"
FT /evidence="ECO:0000269|PubMed:9402087"
FT /id="VAR_015316"
FT VARIANT 112
FT /note="C -> R (in XNDI)"
FT /evidence="ECO:0000269|PubMed:10694923,
FT ECO:0000269|PubMed:8037205"
FT /id="VAR_003523"
FT VARIANT 112
FT /note="C -> Y (in XNDI)"
FT /id="VAR_015317"
FT VARIANT 113
FT /note="R -> W (in XNDI; dbSNP:rs28935496)"
FT /evidence="ECO:0000269|PubMed:7984150,
FT ECO:0000269|PubMed:8037205, ECO:0000269|PubMed:8479490"
FT /id="VAR_003524"
FT VARIANT 122
FT /note="G -> D (in XNDI)"
FT /evidence="ECO:0000269|PubMed:16845277"
FT /id="VAR_062591"
FT VARIANT 122
FT /note="G -> R (in XNDI)"
FT /id="VAR_015318"
FT VARIANT 123
FT /note="M -> K (in XNDI)"
FT /id="VAR_015319"
FT VARIANT 126
FT /note="S -> F (in XNDI)"
FT /evidence="ECO:0000269|PubMed:8037205"
FT /id="VAR_003525"
FT VARIANT 127
FT /note="S -> F (in XNDI)"
FT /id="VAR_015320"
FT VARIANT 128
FT /note="Y -> S (in XNDI)"
FT /evidence="ECO:0000269|PubMed:1303257,
FT ECO:0000269|PubMed:7833930, ECO:0000269|PubMed:8037205"
FT /id="VAR_003526"
FT VARIANT 130
FT /note="I -> F (in XNDI; dbSNP:rs796052096)"
FT /evidence="ECO:0000269|PubMed:10770218"
FT /id="VAR_015321"
FT VARIANT 132
FT /note="A -> D (in XNDI; dbSNP:rs104894747)"
FT /evidence="ECO:0000269|PubMed:1356229"
FT /id="VAR_003527"
FT VARIANT 135
FT /note="L -> P (in XNDI; dbSNP:rs1557100610)"
FT /id="VAR_015322"
FT VARIANT 137
FT /note="R -> C (in NSIAD; constitutively active;
FT dbSNP:rs104894761)"
FT /evidence="ECO:0000269|PubMed:15872203"
FT /id="VAR_025901"
FT VARIANT 137
FT /note="R -> H (in XNDI; fails to activate the adenylyl
FT cyclase system; dbSNP:rs104894756)"
FT /evidence="ECO:0000269|PubMed:16845277,
FT ECO:0000269|PubMed:8037205, ECO:0000269|PubMed:8514744,
FT ECO:0000269|PubMed:9452109, ECO:0000269|PubMed:9711877"
FT /id="VAR_003528"
FT VARIANT 137
FT /note="R -> L (in NSIAD; constitutively active;
FT dbSNP:rs104894756)"
FT /evidence="ECO:0000269|PubMed:15872203"
FT /id="VAR_025902"
FT VARIANT 139
FT /note="R -> S"
FT /id="VAR_015323"
FT VARIANT 143
FT /note="R -> P (in XNDI)"
FT /evidence="ECO:0000269|PubMed:7560098,
FT ECO:0000269|PubMed:8267567"
FT /id="VAR_003529"
FT VARIANT 147
FT /note="A -> V (in dbSNP:rs5200)"
FT /id="VAR_003530"
FT VARIANT 163
FT /note="A -> P (in XNDI)"
FT /id="VAR_015324"
FT VARIANT 164
FT /note="W -> S (in XNDI)"
FT /evidence="ECO:0000269|PubMed:8037205"
FT /id="VAR_003531"
FT VARIANT 167
FT /note="S -> L (in XNDI)"
FT /evidence="ECO:0000269|PubMed:8037205"
FT /id="VAR_003532"
FT VARIANT 167
FT /note="S -> T (in XNDI)"
FT /evidence="ECO:0000269|PubMed:7999078"
FT /id="VAR_003533"
FT VARIANT 173
FT /note="P -> S (in XNDI)"
FT /id="VAR_015325"
FT VARIANT 174
FT /note="Q -> L (in XNDI)"
FT /id="VAR_015326"
FT VARIANT 181
FT /note="R -> C (in XNDI; dbSNP:rs104894757)"
FT /evidence="ECO:0000269|PubMed:1303257,
FT ECO:0000269|PubMed:8037205, ECO:0000269|PubMed:9711877"
FT /id="VAR_003534"
FT VARIANT 185
FT /note="G -> C (in XNDI; dbSNP:rs104894748)"
FT /evidence="ECO:0000269|PubMed:1303271"
FT /id="VAR_003535"
FT VARIANT 191
FT /note="D -> G (in XNDI)"
FT /id="VAR_015327"
FT VARIANT 201
FT /note="G -> D (in XNDI; dbSNP:rs104894755)"
FT /id="VAR_015328"
FT VARIANT 202
FT /note="R -> C (in XNDI; dbSNP:rs782806507)"
FT /evidence="ECO:0000269|PubMed:7560098,
FT ECO:0000269|PubMed:8037205"
FT /id="VAR_003536"
FT VARIANT 203
FT /note="R -> C (in XNDI; dbSNP:rs104894750)"
FT /evidence="ECO:0000269|PubMed:1303271"
FT /id="VAR_003537"
FT VARIANT 204
FT /note="T -> N (in XNDI)"
FT /evidence="ECO:0000269|PubMed:11026555"
FT /id="VAR_015329"
FT VARIANT 205
FT /note="Y -> C (in XNDI; dbSNP:rs104894749)"
FT /evidence="ECO:0000269|PubMed:11026555,
FT ECO:0000269|PubMed:1303271"
FT /id="VAR_003538"
FT VARIANT 206
FT /note="V -> D (in XNDI)"
FT /evidence="ECO:0000269|PubMed:11026555"
FT /id="VAR_015330"
FT VARIANT 207
FT /note="T -> N (in XNDI)"
FT /id="VAR_015331"
FT VARIANT 209
FT /note="I -> F (in XNDI)"
FT /id="VAR_015332"
FT VARIANT 214
FT /note="F -> S (in XNDI)"
FT /id="VAR_015333"
FT VARIANT 215
FT /note="V -> M (in dbSNP:rs112109182)"
FT /id="VAR_015334"
FT VARIANT 217
FT /note="P -> T (in XNDI)"
FT /id="VAR_015335"
FT VARIANT 219
FT /note="L -> P (in XNDI)"
FT /id="VAR_015336"
FT VARIANT 219
FT /note="L -> R (in XNDI)"
FT /id="VAR_015337"
FT VARIANT 247..250
FT /note="Missing (in XNDI)"
FT /evidence="ECO:0000269|PubMed:1303257"
FT /id="VAR_003539"
FT VARIANT 247
FT /note="R -> H (in a breast cancer sample; somatic mutation;
FT dbSNP:rs149668713)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035769"
FT VARIANT 252
FT /note="R -> W (in dbSNP:rs61733407)"
FT /id="VAR_015338"
FT VARIANT 272
FT /note="M -> K (in XNDI)"
FT /id="VAR_015339"
FT VARIANT 277
FT /note="V -> A (in XNDI)"
FT /id="VAR_015340"
FT VARIANT 277
FT /note="Missing (in XNDI)"
FT /evidence="ECO:0000269|PubMed:7560098,
FT ECO:0000269|PubMed:7833930, ECO:0000269|PubMed:8267567,
FT ECO:0000269|PubMed:9452109"
FT /id="VAR_003540"
FT VARIANT 280
FT /note="Y -> C (in XNDI; dbSNP:rs104894752)"
FT /evidence="ECO:0000269|PubMed:7987330,
FT ECO:0000269|PubMed:8078903"
FT /id="VAR_003541"
FT VARIANT 282
FT /note="L -> P (in XNDI)"
FT /id="VAR_015341"
FT VARIANT 285
FT /note="A -> P (in XNDI; dbSNP:rs193922122)"
FT /evidence="ECO:0000269|PubMed:8037205"
FT /id="VAR_003542"
FT VARIANT 286
FT /note="P -> L (in XNDI; dbSNP:rs1557100917)"
FT /evidence="ECO:0000269|PubMed:7833930"
FT /id="VAR_003543"
FT VARIANT 286
FT /note="P -> R (in XNDI)"
FT /evidence="ECO:0000269|PubMed:1303257"
FT /id="VAR_003544"
FT VARIANT 286
FT /note="P -> S (in XNDI)"
FT /id="VAR_015342"
FT VARIANT 287
FT /note="F -> L (in XNDI)"
FT /evidence="ECO:0000269|PubMed:11916004"
FT /id="VAR_015343"
FT VARIANT 289
FT /note="L -> P (in XNDI)"
FT /id="VAR_015344"
FT VARIANT 292
FT /note="L -> P (in XNDI)"
FT /evidence="ECO:0000269|PubMed:7987330"
FT /id="VAR_003545"
FT VARIANT 294
FT /note="A -> P (in XNDI)"
FT /id="VAR_015345"
FT VARIANT 309
FT /note="L -> P (in XNDI)"
FT /evidence="ECO:0000269|PubMed:9452109"
FT /id="VAR_003546"
FT VARIANT 309
FT /note="L -> R (in XNDI)"
FT /id="VAR_015346"
FT VARIANT 315
FT /note="S -> R (in XNDI)"
FT /id="VAR_015347"
FT VARIANT 317
FT /note="N -> K (in XNDI)"
FT /evidence="ECO:0000269|PubMed:10694923"
FT /id="VAR_003547"
FT VARIANT 318
FT /note="S -> T"
FT /id="VAR_015348"
FT VARIANT 319
FT /note="C -> R (in XNDI)"
FT /id="VAR_015349"
FT VARIANT 321
FT /note="N -> D (in XNDI)"
FT /id="VAR_015350"
FT VARIANT 321
FT /note="N -> K (in XNDI; dbSNP:rs193922123)"
FT /id="VAR_015351"
FT VARIANT 321
FT /note="N -> Y (in XNDI)"
FT /id="VAR_015352"
FT VARIANT 322
FT /note="P -> H (in XNDI)"
FT /id="VAR_015353"
FT VARIANT 322
FT /note="P -> S (in XNDI)"
FT /evidence="ECO:0000269|PubMed:9402087"
FT /id="VAR_015354"
FT VARIANT 323
FT /note="W -> R (in XNDI)"
FT /id="VAR_015355"
FT VARIANT 323
FT /note="W -> S (in XNDI)"
FT /evidence="ECO:0000269|PubMed:10694923"
FT /id="VAR_003548"
FT VARIANT 352
FT /note="G -> D (in dbSNP:rs146350208)"
FT /id="VAR_015356"
FT MUTAGEN 341
FT /note="C->S: Reduced palmitoylation, reduced cell surface
FT localization but coupling to G protein unaffected."
FT /evidence="ECO:0000269|PubMed:9224808"
FT MUTAGEN 342
FT /note="C->S: Reduced palmitoylation, reduced cell surface
FT localization but coupling to G protein unaffected."
FT /evidence="ECO:0000269|PubMed:9224808"
FT HELIX 34..66
FT /evidence="ECO:0007829|PDB:7DW9"
FT HELIX 73..91
FT /evidence="ECO:0007829|PDB:7DW9"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:7DW9"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:7DW9"
FT HELIX 109..142
FT /evidence="ECO:0007829|PDB:7DW9"
FT TURN 144..148
FT /evidence="ECO:0007829|PDB:7KH0"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:7DW9"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:7DW9"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:7DW9"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:7DW9"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:7DW9"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:7DW9"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:7DW9"
FT HELIX 215..234
FT /evidence="ECO:0007829|PDB:7DW9"
FT HELIX 264..296
FT /evidence="ECO:0007829|PDB:7DW9"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:7KH0"
FT HELIX 305..310
FT /evidence="ECO:0007829|PDB:7DW9"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:7DW9"
FT HELIX 316..328
FT /evidence="ECO:0007829|PDB:7DW9"
FT HELIX 330..337
FT /evidence="ECO:0007829|PDB:7DW9"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:4JQI"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:4JQI"
SQ SEQUENCE 371 AA; 40279 MW; 1F87D20A3C0ECB0D CRC64;
MLMASTTSAV PGHPSLPSLP SNSSQERPLD TRDPLLARAE LALLSIVFVA VALSNGLVLA
ALARRGRRGH WAPIHVFIGH LCLADLAVAL FQVLPQLAWK ATDRFRGPDA LCRAVKYLQM
VGMYASSYMI LAMTLDRHRA ICRPMLAYRH GSGAHWNRPV LVAWAFSLLL SLPQLFIFAQ
RNVEGGSGVT DCWACFAEPW GRRTYVTWIA LMVFVAPTLG IAACQVLIFR EIHASLVPGP
SERPGGRRRG RRTGSPGEGA HVSAAVAKTV RMTLVIVVVY VLCWAPFFLV QLWAAWDPEA
PLEGAPFVLL MLLASLNSCT NPWIYASFSS SVSSELRSLL CCARGRTPPS LGPQDESCTT
ASSSLAKDTS S
