ID NEU2_HUMAN Reviewed; 164 AA.
AC P01185; A0AV35; O14935;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 02-OCT-2024, entry version 231.
DE RecName: Full=Vasopressin-neurophysin 2-copeptin;
DE AltName: Full=AVP-NPII;
DE Contains:
DE RecName: Full=Arg-vasopressin;
DE AltName: Full=Arginine-vasopressin;
DE Contains:
DE RecName: Full=Neurophysin 2;
DE AltName: Full=Neurophysin-II;
DE Contains:
DE RecName: Full=Copeptin;
DE Flags: Precursor;
GN Name=AVP; Synonyms=ARVP, VP;
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=2991279; DOI=10.1016/s0021-9258(17)39236-0;
RA Sausville E., Carney D., Battey J.;
RT "The human vasopressin gene is linked to the oxytocin gene and is
RT selectively expressed in a cultured lung cancer cell line.";
RL J. Biol. Chem. 260:10236-10241(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3768139; DOI=10.1515/bchm3.1986.367.2.695;
RA Rehbein M., Hillers M., Mohr E., Ivell R., Morley S., Schmale H.,
RA Richter D.;
RT "The neurohypophyseal hormones vasopressin and oxytocin. Precursor
RT structure, synthesis and regulation.";
RL Biol. Chem. Hoppe-Seyler 367:695-704(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=4065330; DOI=10.1016/0014-5793(85)80069-7;
RA Mohr E., Hillers M., Ivell R., Haulica I.D., Richter D.;
RT "Expression of the vasopressin and oxytocin genes in human hypothalami.";
RL FEBS Lett. 193:12-16(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT NDI VAL-48.
RX PubMed=1740104; DOI=10.1002/j.1460-2075.1992.tb05022.x;
RA Bahnsen U., Oosting P., Swaab D.F., Nahke P., Richter D., Schmale H.;
RT "A missense mutation in the vasopressin-neurophysin precursor gene
RT cosegregates with human autosomal dominant neurohypophyseal diabetes
RT insipidus.";
RL EMBO J. 11:19-23(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-119.
RC TISSUE=Lung carcinoma;
RA Du J., North W.G.;
RT "A missense mutation in the vasopressin mRNA with human small-cell lung
RT carcinoma.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP PROTEIN SEQUENCE OF 20-28, AND AMIDATION AT GLY-28.
RX PubMed=13591312; DOI=10.3181/00379727-98-24154;
RA Light A., du Vigneaud V.;
RT "On the nature of oxytocin and vasopressin from human pituitary.";
RL Proc. Soc. Exp. Biol. Med. 98:692-696(1958).
RN [9]
RP PROTEIN SEQUENCE OF 32-124.
RX PubMed=6574452; DOI=10.1073/pnas.80.10.2839;
RA Chauvet M.-T., Hurpet D., Chauvet J., Acher R.;
RT "Identification of human neurophysins: complete amino acid sequences of
RT MSEL- and VLDV-neurophysins.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:2839-2843(1983).
RN [10]
RP PROTEIN SEQUENCE OF 126-164.
RX PubMed=7271787; DOI=10.1016/s0006-291x(81)80258-6;
RA Seidah N.G., Benjannet S., Chretien M.;
RT "The complete sequence of a novel human pituitary glycopeptide homologous
RT to pig posterior pituitary glycopeptide.";
RL Biochem. Biophys. Res. Commun. 100:901-907(1981).
RN [11]
RP FUNCTION, AND INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL
RP FUNCTION).
RX PubMed=33713620; DOI=10.1016/j.cell.2021.02.053;
RA Yeung M.L., Teng J.L.L., Jia L., Zhang C., Huang C., Cai J.P., Zhou R.,
RA Chan K.H., Zhao H., Zhu L., Siu K.L., Fung S.Y., Yung S., Chan T.M.,
RA To K.K., Chan J.F., Cai Z., Lau S.K.P., Chen Z., Jin D.Y., Woo P.C.Y.,
RA Yuen K.Y.;
RT "Soluble ACE2-mediated cell entry of SARS-CoV-2 via interaction with
RT proteins related to the renin-angiotensin system.";
RL Cell 0:0-0(2021).
RN [12]
RP VARIANT NDI THR-19.
RX PubMed=8370682; DOI=10.1210/jcem.77.3.8370682;
RA McLeod J.F., Kovacs L., Gaskill M.B., Rittig S., Bradley G.S.,
RA Robertson G.L.;
RT "Familial neurohypophyseal diabetes insipidus associated with a signal
RT peptide mutation.";
RL J. Clin. Endocrinol. Metab. 77:599A-599G(1993).
RN [13]
RP VARIANT NDI GLU-78 DEL.
RX PubMed=8103767; DOI=10.1210/jcem.77.3.8103767;
RA Yuasa H., Ito M., Nagasaki H., Oiso Y., Miyamoto S., Sasaki N., Saito H.;
RT "Glu-47, which forms a salt bridge between neurophysin-II and arginine
RT vasopressin, is deleted in patients with familial central diabetes
RT insipidus.";
RL J. Clin. Endocrinol. Metab. 77:600-604(1993).
RN [14]
RP VARIANT NDI THR-19.
RX PubMed=8514868; DOI=10.1172/jci116494;
RA Ito M., Oiso Y., Murase T., Kondo K., Saito H., Chinzei T., Racchi M.,
RA Lively M.O.;
RT "Possible involvement of inefficient cleavage of preprovasopressin by
RT signal peptidase as a cause for familial central diabetes insipidus.";
RL J. Clin. Invest. 91:2565-2571(1993).
RN [15]
RP VARIANT NDI LEU-55.
RX PubMed=8045958; DOI=10.1210/jcem.79.2.8045958;
RA Repaske D.R., Browning J.E.;
RT "A de novo mutation in the coding sequence for neurophysin-II (Pro24-->Leu)
RT is associated with onset and transmission of autosomal dominant
RT neurohypophyseal diabetes insipidus.";
RL J. Clin. Endocrinol. Metab. 79:421-427(1994).
RN [16]
RP VARIANT NDI TRP-93.
RX PubMed=7714110; DOI=10.1210/jcem.80.4.7714110;
RA Nagasaki H., Ito M., Yuasa H., Saito H., Fukase M., Hamada K., Ishikawa E.,
RA Katakami H., Oiso Y.;
RT "Two novel mutations in the coding region for neurophysin-II associated
RT with familial central diabetes insipidus.";
RL J. Clin. Endocrinol. Metab. 80:1352-1356(1995).
RN [17]
RP VARIANTS NDI PHE-17; THR-19; VAL-19; ARG-45; CYS-51; GLY-78; PRO-81;
RP ARG-88; SER-88; SER-92 AND CYS-96.
RX PubMed=8554046;
RA Rittig S., Robertson G.L., Siggaard C., Kovacs L., Gregersen N., Nyborg J.,
RA Pedersen E.B.;
RT "Identification of 13 new mutations in the vasopressin-neurophysin II gene
RT in 17 kindreds with familial autosomal dominant neurohypophyseal diabetes
RT insipidus.";
RL Am. J. Hum. Genet. 58:107-117(1996).
RN [18]
RP VARIANT NDI VAL-54.
RX PubMed=9360520; DOI=10.1210/jcem.82.11.4231;
RA Gagliardi P.C., Bernasconi S., Repaske D.R.;
RT "Autosomal dominant neurohypophyseal diabetes insipidus associated with a
RT missense mutation encoding Gly23-->Val in neurophysin II.";
RL J. Clin. Endocrinol. Metab. 82:3643-3646(1997).
RN [19]
RP VARIANT NDI THR-19.
RX PubMed=9580132; DOI=10.1210/jcem.83.3.4658;
RA Calvo B., Bilbao J.R., Urrutia I., Eizaguirre J., Gaztambide S.,
RA Castano L.;
RT "Identification of a novel nonsense mutation and a missense substitution in
RT the vasopressin-neurophysin II gene in two Spanish kindreds with familial
RT neurohypophyseal diabetes insipidus.";
RL J. Clin. Endocrinol. Metab. 83:995-997(1998).
RN [20]
RP VARIANTS NDI PHE-87 AND TYR-92.
RX PubMed=9814475; DOI=10.1210/jcem.83.11.5278;
RA Grant F.D., Ahmadi A., Hosley C.M., Majzoub J.A.;
RT "Two novel mutations of the vasopressin gene associated with familial
RT diabetes insipidus and identification of an asymptomatic carrier infant.";
RL J. Clin. Endocrinol. Metab. 83:3958-3964(1998).
RN [21]
RP VARIANT NDI LEU-26.
RX PubMed=10369876; DOI=10.1093/hmg/8.7.1303;
RA Willcutts M.D., Felner E., White P.C.;
RT "Autosomal recessive familial neurohypophyseal diabetes insipidus with
RT continued secretion of mutant weakly active vasopressin.";
RL Hum. Mol. Genet. 8:1303-1307(1999).
RN [22]
RP VARIANT NDI ARG-54.
RX PubMed=10487710; DOI=10.1210/jcem.84.9.5979;
RA Calvo B., Bilbao J.R., Rodriguez A., Rodriguez-Arnao M.D., Castano L.;
RT "Molecular analysis in familial neurohypophyseal diabetes insipidus: early
RT diagnosis of an asymptomatic carrier.";
RL J. Clin. Endocrinol. Metab. 84:3351-3354(1999).
RN [23]
RP VARIANTS NDI ARG-116 AND GLY-116.
RX PubMed=11017955;
RA Abbes A.P., Bruggeman B., van den Akker E.L.T., de Groot M.R.,
RA Franken A.A.M., Drexhage V.R., Engel H.;
RT "Identification of two distinct mutations at the same nucleotide position,
RT concomitantly with a novel polymorphism in the vasopressin-neurophysin II
RT gene (AVP-NP II) in two Dutch families with familial neurohypophyseal
RT diabetes insipidus.";
RL Clin. Chem. 46:1699-1702(2000).
RN [24]
RP VARIANT NDI TYR-59.
RX PubMed=11150885; DOI=10.1159/000023573;
RA Skordis N., Patsalis P.C., Hettinger J.A., Kontou M., Herakleous E.,
RA Krishnamani M.R., Phillips J.A. III;
RT "A novel arginine vasopressin-neurophysin II mutation causes autosomal
RT dominant neurohypophyseal diabetes insipidus and morphologic pituitary
RT changes.";
RL Horm. Res. 53:239-245(2000).
RN [25]
RP VARIANT NDI TYR-105.
RX PubMed=10677561; DOI=10.3892/ijmm.5.3.229;
RA Fujii H., Iida S., Moriwaki K.;
RT "Familial neurohypophyseal diabetes insipidus associated with a novel
RT mutation in the vasopressin-neurophysin II gene.";
RL Int. J. Mol. Med. 5:229-234(2000).
RN [26]
RP VARIANT NDI PRO-97.
RX PubMed=11748489; DOI=10.1055/s-2001-18994;
RA Mundschenk J., Rittig S., Siggaard C., Hensen J., Lehnert H.;
RT "A new mutation of the arginine vasopressin-neurophysin II gene in a family
RT with autosomal dominant neurohypophyseal diabetes insipidus.";
RL Exp. Clin. Endocrinol. Diabetes 109:406-409(2001).
RN [27]
RP VARIANT NDI GLY-116, AND CHARACTERIZATION OF VARIANT NDI GLY-116.
RX PubMed=11443218; DOI=10.1210/jcem.86.7.7686;
RA Nijenhuis M., van den Akker E.L.T., Zalm R., Franken A.A.M., Abbes A.P.,
RA Engel H., de Wied D., Burbach J.P.H.;
RT "Familial neurohypophysial diabetes insipidus in a large Dutch kindred:
RT effect of the onset of diabetes on growth in children and cell biological
RT defects of the mutant vasopressin prohormone.";
RL J. Clin. Endocrinol. Metab. 86:3410-3420(2001).
RN [28]
RP VARIANT NDI GLY-98.
RX PubMed=11161827; DOI=10.1006/mgme.2000.3117;
RA DiMeglio L.A., Gagliardi P.C., Browning J.E., Quigley C.A., Repaske D.R.;
RT "A missense mutation encoding cys(67) --> gly in neurophysin ii is
RT associated with early onset autosomal dominant neurohypophyseal diabetes
RT insipidus.";
RL Mol. Genet. Metab. 72:39-44(2001).
RN [29]
RP VARIANTS NDI ARG-54; TYR-92 AND ARG-105.
RX PubMed=11980620; DOI=10.1530/eje.0.1460649;
RA Rutishauser J., Kopp P., Gaskill M.B., Kotlar T.J., Robertson G.L.;
RT "Clinical and molecular analysis of three families with autosomal dominant
RT neurohypophyseal diabetes insipidus associated with a novel and recurrent
RT mutations in the vasopressin-neurophysin II gene.";
RL Eur. J. Endocrinol. 146:649-656(2002).
RN [30]
RP VARIANT NDI SER-92.
RX PubMed=12012274; DOI=10.1055/s-2002-29091;
RA Bullmann C., Kotzka J., Grimm T., Heppner C., Jockenhovel F., Krone W.,
RA Muller-Wieland D.;
RT "Identification of a novel mutation in the arginine vasopressin-neurophysin
RT II gene in familial central diabetes insipidus.";
RL Exp. Clin. Endocrinol. Diabetes 110:134-137(2002).
RN [31]
RP VARIANT NDI HIS-21.
RX PubMed=12107248; DOI=10.1210/jcem.87.7.8677;
RA Rittig S., Siggaard C., Ozata M., Yetkin I., Gregersen N., Pedersen E.B.,
RA Robertson G.L.;
RT "Autosomal dominant neurohypophyseal diabetes insipidus due to substitution
RT of histidine for tyrosine-2 in the vasopressin moiety of the hormone
RT precursor.";
RL J. Clin. Endocrinol. Metab. 87:3351-3355(2002).
RN [32]
RP VARIANT NDI PHE-104.
RX PubMed=12359138; DOI=10.1016/s1096-7192(02)00118-x;
RA Santiprabhob J., Browning J.E., Repaske D.R.;
RT "A missense mutation encoding Cys73Phe in neurophysin II is associated with
RT autosomal dominant neurohypophyseal diabetes insipidus.";
RL Mol. Genet. Metab. 77:112-118(2002).
RN [33]
RP VARIANT NDI THR-19.
RX PubMed=12519420; DOI=10.1046/j.1365-2265.2003.01667.x;
RA Boson W.L., Sarubi J.C., D'Alva C.B., Friedman E., Faria D., De Marco L.,
RA Wajchenberg B.;
RT "A signal peptide mutation of the arginine vasopressin gene in monozygotic
RT twins.";
RL Clin. Endocrinol. (Oxf.) 58:108-110(2003).
RN [34]
RP VARIANT NDI PRO-99.
RX PubMed=14510916; DOI=10.1046/j.1365-2265.2003.01834.x;
RA Elias P.C.L., Elias L.L.K., Torres N., Moreira A.C., Antunes-Rodrigues J.,
RA Castro M.;
RT "Progressive decline of vasopressin secretion in familial autosomal
RT dominant neurohypophyseal diabetes insipidus presenting a novel mutation in
RT the vasopressin-neurophysin II gene.";
RL Clin. Endocrinol. (Oxf.) 59:511-518(2003).
RN [35]
RP VARIANT NDI PHE-58.
RX PubMed=12931042; DOI=10.1159/000072526;
RA Wolf M.T.F., Doetsch J., Metzler M., Holder M., Repp R., Rascher W.;
RT "A new missense mutation of the vasopressin-neurophysin II gene in a family
RT with neurohypophyseal diabetes insipidus.";
RL Horm. Res. 60:143-147(2003).
RN [36]
RP VARIANT NDI SER-98.
RX PubMed=15538939; DOI=10.1530/eje.0.1510605;
RA Baglioni S., Corona G., Maggi M., Serio M., Peri A.;
RT "Identification of a novel mutation in the arginine vasopressin-neurophysin
RT II gene affecting the sixth intrachain disulfide bridge of the neurophysin
RT II moiety.";
RL Eur. J. Endocrinol. 151:605-611(2004).
RN [37]
RP VARIANTS NDI THR-19; VAL-19; ARG-54; ALA-67; GLY-78; GLU-78 DEL; ASP-96;
RP CYS-96; GLY-104 AND TRP-116.
RX PubMed=14673472; DOI=10.1038/sj.ejhg.5201086;
RA Christensen J.H., Siggaard C., Corydon T.J., deSanctis L., Kovacs L.,
RA Robertson G.L., Gregersen N., Rittig S.;
RT "Six novel mutations in the arginine vasopressin gene in 15 kindreds with
RT autosomal dominant familial neurohypophyseal diabetes insipidus give
RT further insight into the pathogenesis.";
RL Eur. J. Hum. Genet. 12:44-51(2004).
RN [38]
RP FUNCTION OF VASOPRESSIN, MUTAGENESIS OF GLY-28, AND SUBUNIT.
RX PubMed=18174156; DOI=10.1074/jbc.m706477200;
RA Dutertre S., Croker D., Daly N.L., Andersson A., Muttenthaler M.,
RA Lumsden N.G., Craik D.J., Alewood P.F., Guillon G., Lewis R.J.;
RT "Conopressin-T from Conus tulipa reveals an antagonist switch in
RT vasopressin-like peptides.";
RL J. Biol. Chem. 283:7100-7108(2008).
CC -!- FUNCTION: [Neurophysin 2]: Specifically binds vasopressin.
CC -!- FUNCTION: [Arg-vasopressin]: Has a direct antidiuretic action on the
CC kidney, it also causes vasoconstriction of the peripheral vessels. Acts
CC by binding to vasopressin receptors (V1bR/AVPR1B, V1aR/AVPR1A, and
CC V2R/AVPR2) (PubMed:18174156). {ECO:0000269|PubMed:18174156}.
CC -!- SUBUNIT: Interacts with vasopressin receptors V1bR/AVPR1B (Ki=85 pM),
CC V1aR/AVPR1A (Ki=0.6 nM) and V2R/AVPR2 (Ki=4.9 nM) (PubMed:18174156).
CC Interacts with oxytocin receptor (OXTR) (Ki=110 nM) (PubMed:18174156).
CC {ECO:0000269|PubMed:18174156}.
CC -!- SUBUNIT: [Arg-vasopressin]: (Microbial infection) May interact with
CC SARS coronavirus-2/SARS-CoV-2; they may form a complex with secreted
CC ACE2. {ECO:0000269|PubMed:33713620}.
CC -!- INTERACTION:
CC P01185; O43741: PRKAB2; NbExp=3; IntAct=EBI-6858021, EBI-1053424;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DISEASE: Diabetes insipidus, neurohypophyseal (NDI) [MIM:125700]: A
CC disease characterized by persistent thirst, polydipsia and polyuria.
CC Affected individuals are apparently normal at birth, but
CC characteristically develop symptoms of vasopressin deficiency during
CC childhood. {ECO:0000269|PubMed:10369876, ECO:0000269|PubMed:10487710,
CC ECO:0000269|PubMed:10677561, ECO:0000269|PubMed:11017955,
CC ECO:0000269|PubMed:11150885, ECO:0000269|PubMed:11161827,
CC ECO:0000269|PubMed:11443218, ECO:0000269|PubMed:11748489,
CC ECO:0000269|PubMed:11980620, ECO:0000269|PubMed:12012274,
CC ECO:0000269|PubMed:12107248, ECO:0000269|PubMed:12359138,
CC ECO:0000269|PubMed:12519420, ECO:0000269|PubMed:12931042,
CC ECO:0000269|PubMed:14510916, ECO:0000269|PubMed:14673472,
CC ECO:0000269|PubMed:15538939, ECO:0000269|PubMed:1740104,
CC ECO:0000269|PubMed:7714110, ECO:0000269|PubMed:8045958,
CC ECO:0000269|PubMed:8103767, ECO:0000269|PubMed:8370682,
CC ECO:0000269|PubMed:8514868, ECO:0000269|PubMed:8554046,
CC ECO:0000269|PubMed:9360520, ECO:0000269|PubMed:9580132,
CC ECO:0000269|PubMed:9814475}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the vasopressin/oxytocin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Vasopressin entry;
CC URL="https://en.wikipedia.org/wiki/Vasopressin";
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DR EMBL; M11166; AAA98772.1; -; Genomic_DNA.
DR EMBL; M25647; AAA61291.1; -; mRNA.
DR EMBL; X03172; CAA26935.1; -; mRNA.
DR EMBL; X62890; CAA44681.1; -; Genomic_DNA.
DR EMBL; AF031476; AAB86629.1; -; mRNA.
DR EMBL; AL160414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X62891; CAA44682.1; -; Genomic_DNA.
DR EMBL; BC126196; AAI26197.1; -; mRNA.
DR EMBL; BC126224; AAI26225.1; -; mRNA.
DR CCDS; CCDS13045.1; -.
DR PIR; A39269; A39269.
DR PIR; B94676; NVHU2.
DR RefSeq; NP_000481.2; NM_000490.4.
DR RefSeq; XP_011527569.1; XM_011529267.1.
DR PDB; 7BB6; EM; 4.20 A; H=20-28.
DR PDB; 7BB7; EM; 4.40 A; H=20-28.
DR PDB; 7DW9; EM; 2.60 A; C=20-28.
DR PDB; 7KH0; EM; 2.80 A; L=20-28.
DR PDB; 7R0C; EM; 4.73 A; B=20-28.
DR PDBsum; 7BB6; -.
DR PDBsum; 7BB7; -.
DR PDBsum; 7DW9; -.
DR PDBsum; 7KH0; -.
DR PDBsum; 7R0C; -.
DR AlphaFoldDB; P01185; -.
DR EMDB; EMD-12128; -.
DR EMDB; EMD-12129; -.
DR EMDB; EMD-14221; -.
DR EMDB; EMD-22872; -.
DR SMR; P01185; -.
DR BioGRID; 107032; 50.
DR IntAct; P01185; 21.
DR STRING; 9606.ENSP00000369647; -.
DR GlyCosmos; P01185; 1 site, No reported glycans.
DR GlyGen; P01185; 1 site.
DR iPTMnet; P01185; -.
DR PhosphoSitePlus; P01185; -.
DR BioMuta; AVP; -.
DR DMDM; 128083; -.
DR MassIVE; P01185; -.
DR PaxDb; 9606-ENSP00000369647; -.
DR PeptideAtlas; P01185; -.
DR ProteomicsDB; 51342; -.
DR Antibodypedia; 7264; 352 antibodies from 31 providers.
DR DNASU; 551; -.
DR Ensembl; ENST00000380293.3; ENSP00000369647.3; ENSG00000101200.5.
DR GeneID; 551; -.
DR KEGG; hsa:551; -.
DR MANE-Select; ENST00000380293.3; ENSP00000369647.3; NM_000490.5; NP_000481.2.
DR AGR; HGNC:894; -.
DR CTD; 551; -.
DR DisGeNET; 551; -.
DR GeneCards; AVP; -.
DR HGNC; HGNC:894; AVP.
DR HPA; ENSG00000101200; Tissue enriched (brain).
DR MalaCards; AVP; -.
DR MIM; 125700; phenotype.
DR MIM; 192340; gene.
DR neXtProt; NX_P01185; -.
DR OpenTargets; ENSG00000101200; -.
DR Orphanet; 30925; Hereditary arginine vasopressin deficiency.
DR PharmGKB; PA25186; -.
DR VEuPathDB; HostDB:ENSG00000101200; -.
DR eggNOG; ENOG502S21K; Eukaryota.
DR GeneTree; ENSGT00390000004511; -.
DR HOGENOM; CLU_125770_0_0_1; -.
DR InParanoid; P01185; -.
DR OMA; GCVVDSD; -.
DR OrthoDB; 5398672at2759; -.
DR PhylomeDB; P01185; -.
DR TreeFam; TF333018; -.
DR PathwayCommons; P01185; -.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR Reactome; R-HSA-388479; Vasopressin-like receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
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-5619099; Defective AVP does not bind AVPR1A,B and causes neurohypophyseal diabetes insipidus (NDI).
DR Reactome; R-HSA-879518; Transport of organic anions.
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 SignaLink; P01185; -.
DR SIGNOR; P01185; -.
DR BioGRID-ORCS; 551; 17 hits in 1146 CRISPR screens.
DR GeneWiki; Vasopressin; -.
DR GenomeRNAi; 551; -.
DR Pharos; P01185; Tbio.
DR PRO; PR:P01185; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P01185; protein.
DR Bgee; ENSG00000101200; Expressed in hypothalamus and 102 other cell types or tissues.
DR ExpressionAtlas; P01185; baseline and differential.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098992; C:neuronal dense core vesicle; IEA:Ensembl.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0005185; F:neurohypophyseal hormone activity; IEA:InterPro.
DR GO; GO:0005184; F:neuropeptide hormone activity; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0031894; F:V1A vasopressin receptor binding; IPI:UniProtKB.
DR GO; GO:0031895; F:V1B vasopressin receptor binding; IEA:Ensembl.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
DR GO; GO:0007625; P:grooming behavior; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0002125; P:maternal aggressive behavior; IEA:Ensembl.
DR GO; GO:0042711; P:maternal behavior; IEA:Ensembl.
DR GO; GO:0050891; P:multicellular organismal-level water homeostasis; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0007621; P:negative regulation of female receptivity; IEA:Ensembl.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
DR GO; GO:0051970; P:negative regulation of transmission of nerve impulse; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0032849; P:positive regulation of cellular pH reduction; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; IEA:Ensembl.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IEA:Ensembl.
DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
DR GO; GO:0070528; P:protein kinase C signaling; IDA:UniProtKB.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR GO; GO:0046718; P:symbiont entry into host cell; IDA:UniProtKB.
DR GO; GO:0042310; P:vasoconstriction; IEA:UniProtKB-KW.
DR GO; GO:0006833; P:water transport; TAS:ProtInc.
DR Gene3D; 2.60.9.10; Neurohypophysial hormone domain; 1.
DR InterPro; IPR000981; Neurhyp_horm.
DR InterPro; IPR036387; Neurhyp_horm_dom_sf.
DR InterPro; IPR022423; Neurohypophysial_hormone_CS.
DR PANTHER; PTHR11681; NEUROPHYSIN; 1.
DR PANTHER; PTHR11681:SF9; VASOPRESSIN-NEUROPHYSIN 2-COPEPTIN; 1.
DR Pfam; PF00220; Hormone_4; 1.
DR Pfam; PF00184; Hormone_5; 1.
DR PIRSF; PIRSF001815; Nonapeptide_hormone_precursor; 1.
DR PRINTS; PR00831; NEUROPHYSIN.
DR SMART; SM00003; NH; 1.
DR SUPFAM; SSF49606; Neurophysin II; 1.
DR PROSITE; PS00264; NEUROHYPOPHYS_HORM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Cleavage on pair of basic residues;
KW Diabetes insipidus; Direct protein sequencing; Disease variant;
KW Disulfide bond; Glycoprotein; Hormone; Host-virus interaction;
KW Proteomics identification; Reference proteome; Secreted; Signal;
KW Vasoactive; Vasoconstrictor.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:13591312"
FT PEPTIDE 20..28
FT /note="Arg-vasopressin"
FT /evidence="ECO:0000269|PubMed:13591312"
FT /id="PRO_0000020515"
FT CHAIN 32..124
FT /note="Neurophysin 2"
FT /evidence="ECO:0000269|PubMed:6574452"
FT /id="PRO_0000020516"
FT PEPTIDE 126..164
FT /note="Copeptin"
FT /evidence="ECO:0000269|PubMed:7271787"
FT /id="PRO_0000020517"
FT SITE 28
FT /note="Important for agonist activity on V1aR/AVPR1A"
FT /evidence="ECO:0000269|PubMed:18174156"
FT MOD_RES 28
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:13591312"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 20..25
FT DISULFID 41..85
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 44..58
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 52..75
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 59..65
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 92..104
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 98..116
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 105..110
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT VARIANT 17
FT /note="S -> F (in NDI)"
FT /evidence="ECO:0000269|PubMed:8554046"
FT /id="VAR_004980"
FT VARIANT 19
FT /note="A -> T (in NDI; probably causes insufficient
FT processing of precursor; dbSNP:rs387906511)"
FT /evidence="ECO:0000269|PubMed:12519420,
FT ECO:0000269|PubMed:14673472, ECO:0000269|PubMed:8370682,
FT ECO:0000269|PubMed:8514868, ECO:0000269|PubMed:8554046,
FT ECO:0000269|PubMed:9580132"
FT /id="VAR_004981"
FT VARIANT 19
FT /note="A -> V (in NDI; dbSNP:rs387906512)"
FT /evidence="ECO:0000269|PubMed:14673472,
FT ECO:0000269|PubMed:8554046"
FT /id="VAR_004982"
FT VARIANT 21
FT /note="Y -> H (in NDI; dbSNP:rs121964893)"
FT /evidence="ECO:0000269|PubMed:12107248"
FT /id="VAR_015262"
FT VARIANT 26
FT /note="P -> L (in NDI; weakly active; dbSNP:rs142886338)"
FT /evidence="ECO:0000269|PubMed:10369876"
FT /id="VAR_015263"
FT VARIANT 45
FT /note="G -> R (in NDI)"
FT /evidence="ECO:0000269|PubMed:8554046"
FT /id="VAR_004983"
FT VARIANT 48
FT /note="G -> V (in NDI; dbSNP:rs121964883)"
FT /evidence="ECO:0000269|PubMed:1740104"
FT /id="VAR_004984"
FT VARIANT 51
FT /note="R -> C (in NDI; dbSNP:rs2066120171)"
FT /evidence="ECO:0000269|PubMed:8554046"
FT /id="VAR_004985"
FT VARIANT 52
FT /note="C -> R (in NDI)"
FT /id="VAR_015264"
FT VARIANT 54
FT /note="G -> R (in NDI; dbSNP:rs121964888)"
FT /evidence="ECO:0000269|PubMed:10487710,
FT ECO:0000269|PubMed:11980620, ECO:0000269|PubMed:14673472"
FT /id="VAR_015265"
FT VARIANT 54
FT /note="G -> V (in NDI; dbSNP:rs121964887)"
FT /evidence="ECO:0000269|PubMed:9360520"
FT /id="VAR_015266"
FT VARIANT 55
FT /note="P -> L (in NDI)"
FT /evidence="ECO:0000269|PubMed:8045958"
FT /id="VAR_004986"
FT VARIANT 58
FT /note="C -> F (in NDI)"
FT /evidence="ECO:0000269|PubMed:12931042"
FT /id="VAR_029997"
FT VARIANT 59
FT /note="C -> R (in NDI)"
FT /id="VAR_015267"
FT VARIANT 59
FT /note="C -> Y (in NDI)"
FT /evidence="ECO:0000269|PubMed:11150885"
FT /id="VAR_015268"
FT VARIANT 67
FT /note="V -> A (in NDI; dbSNP:rs28934878)"
FT /evidence="ECO:0000269|PubMed:14673472"
FT /id="VAR_019273"
FT VARIANT 78
FT /note="E -> G (in NDI)"
FT /evidence="ECO:0000269|PubMed:14673472,
FT ECO:0000269|PubMed:8554046"
FT /id="VAR_004988"
FT VARIANT 78
FT /note="Missing (in NDI; dbSNP:rs2066119604)"
FT /evidence="ECO:0000269|PubMed:14673472,
FT ECO:0000269|PubMed:8103767"
FT /id="VAR_004987"
FT VARIANT 81
FT /note="L -> P (in NDI)"
FT /evidence="ECO:0000269|PubMed:8554046"
FT /id="VAR_004989"
FT VARIANT 82
FT /note="P -> L (in dbSNP:rs5195)"
FT /id="VAR_011894"
FT VARIANT 87
FT /note="S -> F (in NDI; dbSNP:rs121964890)"
FT /evidence="ECO:0000269|PubMed:9814475"
FT /id="VAR_015269"
FT VARIANT 88
FT /note="G -> R (in NDI)"
FT /evidence="ECO:0000269|PubMed:8554046"
FT /id="VAR_004990"
FT VARIANT 88
FT /note="G -> S (in NDI; dbSNP:rs121964882)"
FT /evidence="ECO:0000269|PubMed:8554046"
FT /id="VAR_004991"
FT VARIANT 92
FT /note="C -> S (in NDI)"
FT /evidence="ECO:0000269|PubMed:12012274,
FT ECO:0000269|PubMed:8554046"
FT /id="VAR_004992"
FT VARIANT 92
FT /note="C -> Y (in NDI; dbSNP:rs121964891)"
FT /evidence="ECO:0000269|PubMed:11980620,
FT ECO:0000269|PubMed:9814475"
FT /id="VAR_015270"
FT VARIANT 93
FT /note="G -> W (in NDI; dbSNP:rs121964885)"
FT /evidence="ECO:0000269|PubMed:7714110"
FT /id="VAR_004993"
FT VARIANT 96
FT /note="G -> C (in NDI)"
FT /evidence="ECO:0000269|PubMed:14673472,
FT ECO:0000269|PubMed:8554046"
FT /id="VAR_004994"
FT VARIANT 96
FT /note="G -> D (in NDI)"
FT /evidence="ECO:0000269|PubMed:14673472"
FT /id="VAR_019274"
FT VARIANT 96
FT /note="G -> V (in NDI; dbSNP:rs121964886)"
FT /id="VAR_015271"
FT VARIANT 97
FT /note="R -> C (in NDI)"
FT /id="VAR_015272"
FT VARIANT 97
FT /note="R -> P (in NDI)"
FT /evidence="ECO:0000269|PubMed:11748489"
FT /id="VAR_015273"
FT VARIANT 98
FT /note="C -> G (in NDI)"
FT /evidence="ECO:0000269|PubMed:11161827"
FT /id="VAR_015274"
FT VARIANT 98
FT /note="C -> S (in NDI)"
FT /evidence="ECO:0000269|PubMed:15538939"
FT /id="VAR_029998"
FT VARIANT 99
FT /note="A -> P (in NDI)"
FT /evidence="ECO:0000269|PubMed:14510916"
FT /id="VAR_029999"
FT VARIANT 104
FT /note="C -> F (in NDI)"
FT /evidence="ECO:0000269|PubMed:12359138"
FT /id="VAR_015275"
FT VARIANT 104
FT /note="C -> G (in NDI)"
FT /evidence="ECO:0000269|PubMed:14673472"
FT /id="VAR_019275"
FT VARIANT 105
FT /note="C -> R (in NDI)"
FT /evidence="ECO:0000269|PubMed:11980620"
FT /id="VAR_015276"
FT VARIANT 105
FT /note="C -> Y (in NDI)"
FT /evidence="ECO:0000269|PubMed:10677561"
FT /id="VAR_015279"
FT VARIANT 116
FT /note="C -> G (in NDI; strong accumulation in the
FT endoplasmic reticulum and an altered morphology of this
FT organelle; dbSNP:rs74315383)"
FT /evidence="ECO:0000269|PubMed:11017955,
FT ECO:0000269|PubMed:11443218"
FT /id="VAR_015277"
FT VARIANT 116
FT /note="C -> R (in NDI)"
FT /evidence="ECO:0000269|PubMed:11017955"
FT /id="VAR_015278"
FT VARIANT 116
FT /note="C -> W (in NDI)"
FT /evidence="ECO:0000269|PubMed:14673472"
FT /id="VAR_019276"
FT VARIANT 119
FT /note="G -> V (in dbSNP:rs1051744)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_011895"
FT MUTAGEN 28
FT /note="G->V: Gain of antagonist activity on V1aR/AVPR1A
FT (and loss of agonist activity on this receptor). 42-fold
FT decrease in affinity for V1aR/AVPR1A, 2000-fold decrease in
FT affinity for V1bR/AVPR1B, 5-fold decrease in affinity for
FT V2R/AVPR2 and no change in affinity for oxytocin receptor
FT (OXTR)."
FT /evidence="ECO:0000269|PubMed:18174156"
FT CONFLICT 11
FT /note="L -> P (in Ref. 1; AAA98772)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="G -> D (in Ref. 5; AAB86629)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 164 AA; 17325 MW; 8F5EF9834700B9AE CRC64;
MPDTMLPACF LGLLAFSSAC YFQNCPRGGK RAMSDLELRQ CLPCGPGGKG RCFGPSICCA
DELGCFVGTA EALRCQEENY LPSPCQSGQK ACGSGGRCAA FGVCCNDESC VTEPECREGF
HRRARASDRS NATQLDGPAG ALLLRLVQLA GAPEPFEPAQ PDAY
//