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 27-MAR-2024, entry version 228. 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"; 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; 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-22872; -. DR SMR; P01185; -. DR BioGRID; 107032; 48. 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; 375 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 central diabetes insipidus. 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:0042310; P:vasoconstriction; IEA:UniProtKB-KW. DR GO; GO:0046718; P:viral entry into host cell; IDA:UniProtKB. 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. DR Genevisible; P01185; HS. 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 Reference proteome; Secreted; Signal; 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)" 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)" 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 //