ID NEU1_HUMAN Reviewed; 125 AA. AC P01178; Q3MIG0; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 02-SEP-2026, entry version 208. DE RecName: Full=Oxytocin-neurophysin 1 proprotein {ECO:0000305}; DE Short=OT-NPI; DE AltName: Full=pro-oxytocin/neurophysin {ECO:0000250|UniProtKB:P01175}; DE Short=pro-OXT {ECO:0000250|UniProtKB:P01175}; DE Contains: DE RecName: Full=Oxytocin {ECO:0000303|PubMed:3768139}; DE AltName: Full=Ocytocin; DE Contains: DE RecName: Full=Neurophysin 1 {ECO:0000303|PubMed:6574452}; DE Flags: Precursor; GN Name=OXT {ECO:0000312|HGNC:HGNC:8528}; Synonyms=OT; 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 [MRNA], AND FUNCTION. 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 [2] 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Grunwald W.C. Jr., Cool D.R.; RT "Lack of sequence polymorphism in the oxytocin gene of autistic patients."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-110. RX PubMed=2249637; DOI=10.1210/endo-127-6-2990; RA Ivell R., Furuya K., Brackmann B., Dawood Y., Khan-Dawood F.; RT "Expression of the oxytocin and vasopressin genes in human and baboon RT gonadal tissues."; RL Endocrinology 127:2990-2996(1990). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-125. 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 [8] RP PROTEIN SEQUENCE OF 32-125. 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 [9] RP PROTEIN SEQUENCE OF 32-125. RX PubMed=7262323; DOI=10.1016/0014-5793(81)80109-3; RA Schlesinger D.H., Audhya T.K.; RT "A comparative study of mammalian neurophysin protein sequences."; RL FEBS Lett. 128:325-328(1981). RN [10] 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 [11] RP INDUCTION. RX PubMed=2108152; DOI=10.1016/s0021-9258(19)39297-x; RA Richard S., Zingg H.H.; RT "The human oxytocin gene promoter is regulated by estrogens."; RL J. Biol. Chem. 265:6098-6103(1990). RN [12] RP INDUCTION. RX PubMed=1371278; DOI=10.1016/s0021-9258(19)50592-0; RA Adan R.A., Cox J.J., van Kats J.P., Burbach J.P.; RT "Thyroid hormone regulates the oxytocin gene."; RL J. Biol. Chem. 267:3771-3777(1992). RN [13] RP FUNCTION OF OXYTOCIN, 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). RN [14] RP FUNCTION (OXYTOCIN). RX PubMed=6278592; DOI=10.1126/science.6278592; RA Fuchs A.R., Fuchs F., Husslein P., Soloff M.S., Fernstroem M.J.; RT "Oxytocin receptors and human parturition: a dual role for oxytocin in the RT initiation of labor."; RL Science 215:1396-1398(1982). RN [15] RP FUNCTION (OXYTOCIN). RX PubMed=15931222; DOI=10.1038/nature03701; RA Kosfeld M., Heinrichs M., Zak P.J., Fischbacher U., Fehr E.; RT "Oxytocin increases trust in humans."; RL Nature 435:673-676(2005). RN [16] RP FUNCTION (OXYTOCIN). RX PubMed=20538951; DOI=10.1126/science.1189047; RA De Dreu C.K., Greer L.L., Handgraaf M.J., Shalvi S., Van Kleef G.A., RA Baas M., Ten Velden F.S., Van Dijk E., Feith S.W.; RT "The neuropeptide oxytocin regulates parochial altruism in intergroup RT conflict among humans."; RL Science 328:1408-1411(2010). RN [17] RP FUNCTION (OXYTOCIN). RX PubMed=21220339; DOI=10.1073/pnas.1015316108; RA De Dreu C.K., Greer L.L., Van Kleef G.A., Shalvi S., Handgraaf M.J.; RT "Oxytocin promotes human ethnocentrism."; RL Proc. Natl. Acad. Sci. U.S.A. 108:1262-1266(2011). RN [18] RP REVIEW. RX PubMed=36864410; DOI=10.1186/s12884-022-05221-w; RA Buckley S., Uvnaes-Moberg K., Pajalic Z., Luegmair K., RA Ekstroem-Bergstroem A., Dencker A., Massarotti C., Kotlowska A., RA Callaway L., Morano S., Olza I., Magistretti C.M.; RT "Maternal and newborn plasma oxytocin levels in response to maternal RT synthetic oxytocin administration during labour, birth and postpartum - a RT systematic review with implications for the function of the oxytocinergic RT system."; RL BMC Pregnancy Childbirth 23:137-137(2023). RN [19] {ECO:0007744|PDB:7OFG, ECO:0007744|PDB:7OTD} RP STRUCTURE BY NMR OF 20-28 IN COMPLEX WITH COPPER, AND DISULFIDE BOND. RX PubMed=34459989; DOI=10.1007/s00775-021-01897-1; RA Alshanski I., Shalev D.E., Yitzchaik S., Hurevich M.; RT "Determining the structure and binding mechanism of oxytocin-Cu2+ complex RT using paramagnetic relaxation enhancement NMR analysis."; RL J. Biol. Inorg. Chem. 26:809-815(2021). RN [20] {ECO:0007744|PDB:7QVM} RP STRUCTURE BY ELECTRON MICROSCOPY (3.25 ANGSTROMS) OF 20-28 IN COMPLEX WITH RP OXTR; GNAO1; GNB1 AND GNG2, FUNCTION (OXYTOCIN), AND DISULFIDE BONDS. RX PubMed=35851571; DOI=10.1038/s41467-022-31325-0; RA Waltenspuehl Y., Ehrenmann J., Vacca S., Thom C., Medalia O., RA Plueckthun A.; RT "Structural basis for the activation and ligand recognition of the human RT oxytocin receptor."; RL Nat. Commun. 13:4153-4153(2022). RN [21] {ECO:0007744|PDB:7RYC} RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 20-28 IN COMPLEX WITH RP OXTR; GNAS; GNB1 AND GNG2, FUNCTION (OXYTOCIN), AND DISULFIDE BONDS. RX PubMed=35241813; DOI=10.1038/s41594-022-00728-4; RA Meyerowitz J.G., Robertson M.J., Barros-Alvarez X., Panova O., RA Nwokonko R.M., Gao Y., Skiniotis G.; RT "The oxytocin signaling complex reveals a molecular switch for cation RT dependence."; RL Nat. Struct. Mol. Biol. 29:274-281(2022). CC -!- FUNCTION: Precursor of oxytocin, a neurohypophyseal hormone that plays CC a key role in social interactions and neurophysin 1, its carrier CC protein. {ECO:0000269|PubMed:3768139}. CC -!- FUNCTION: [Oxytocin]: Neuropeptide hormone released by the posterior CC pituitary gland that plays a key role in social behavior and other CC biological processes, such as milk ejection (PubMed:15931222, CC PubMed:20538951, PubMed:21220339, PubMed:6278592). Released in response CC to a variety of social cues and acts by binding to oxytocin receptor CC (OXTR), triggering signaling that modulates neural circuits by altering CC ion channel activity, changing intrinsic neuronal properties and CC modifying synaptic transmission (both excitatory and inhibitory) CC (PubMed:18174156, PubMed:35241813, PubMed:35851571). Central release CC (direct secretion in the brain) plays essential roles in social CC behavior, such as maternal care, social cognition and affiliative CC behaviors (PubMed:15931222, PubMed:20538951, PubMed:21220339). CC Stressful and anxiogenic stimuli promote release of oxytocin, which CC acts as a powerful modulator of anxiety- and stress-related behaviors CC (PubMed:15931222, PubMed:20538951, PubMed:21220339). Oxytocin promotes CC altruism by enhancing empathy, trust and social bonding, making people CC more generous (PubMed:15931222, PubMed:20538951, PubMed:21220339). Can CC also favor parochial altruism, a social behavior involving costly CC helping of one's own group (in-group) that often comes with hostility CC or discrimination towards other groups (out-groups) (PubMed:20538951, CC PubMed:21220339). Modulates neural circuits related to reward, fear and CC social approach, encouraging care and cooperation, but can also CC increase guilt or aggression towards out-groups (PubMed:20538951, CC PubMed:21220339). Beyond its role in social behavior, plays a role in CC other processes, such as parturition, lactation or osteoblast CC differentiation, when released peripherally (secreted from the CC posterior pituitary gland into the bloodstream) (PubMed:6278592). CC Required for parturition and milk ejection by triggering and CC strengthening contraction of the smooth muscle of the uterus and CC mammary gland, respectively (PubMed:6278592). Promotes bone mass by CC stimulating bone formation by osteoblasts (By similarity). CC {ECO:0000250|UniProtKB:P35454, ECO:0000269|PubMed:15931222, CC ECO:0000269|PubMed:18174156, ECO:0000269|PubMed:20538951, CC ECO:0000269|PubMed:21220339, ECO:0000269|PubMed:35241813, CC ECO:0000269|PubMed:35851571, ECO:0000269|PubMed:6278592}. CC -!- FUNCTION: [Neurophysin 1]: Carrier protein that binds to and transports CC oxytocin from the hypothalamus to the posterior pituitary gland, CC protecting it from degradation and facilitating its release. CC {ECO:0000250|UniProtKB:P01179}. CC -!- SUBUNIT: [Oxytocin]: Interacts with vasopressin receptors AVPR1A, CC AVPR1B and AVPR2. {ECO:0000269|PubMed:18174156}. CC -!- SUBUNIT: [Neurophysin 1]: Homodimer. {ECO:0000250|UniProtKB:P01175}. CC -!- INTERACTION: CC P01178; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-1762651, EBI-10303987; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle CC {ECO:0000250|UniProtKB:P01179}. Note=The precursor protein (pro-OXT) is CC packaged into neurosecretory granules. {ECO:0000250|UniProtKB:P01179}. CC -!- SUBCELLULAR LOCATION: [Oxytocin]: Secreted CC {ECO:0000250|UniProtKB:P01179}. Cytoplasmic vesicle, secretory vesicle CC {ECO:0000250|UniProtKB:P01179}. Note=Following processing, oxytocin and CC neurophysin 1 are transported to the posterior pituitary and stored in CC neurosecretory granules at the nerve termini until secreted. CC {ECO:0000250|UniProtKB:P01179}. CC -!- SUBCELLULAR LOCATION: [Neurophysin 1]: Secreted CC {ECO:0000250|UniProtKB:P01179}. Cytoplasmic vesicle, secretory vesicle CC {ECO:0000250|UniProtKB:P01179}. Note=Following processing, oxytocin and CC neurophysin 1 are transported to the posterior pituitary and stored in CC neurosecretory granules at the nerve termini until secreted. CC {ECO:0000250|UniProtKB:P01179}. CC -!- INDUCTION: Expression is activated by thyroid hormone and estrogens. CC {ECO:0000269|PubMed:1371278, ECO:0000269|PubMed:2108152}. CC -!- PTM: Synthesized as a large inactive precursor protein (pro-OXT), which CC is cleaved into oxytocin and neurophysin 1 by endopeptidases, such as CC neuroendocrine convertases PCSK1 and PCSK2 (By similarity). Oxytocin is CC then amidated at the C-terminus, completing its activation CC (PubMed:13591312). {ECO:0000250|UniProtKB:P35454, CC ECO:0000269|PubMed:13591312}. CC -!- PTM: [Oxytocin]: Amidated at the C-terminus by alpha-amidating CC monooxygenase (PAM), completing its activation. CC {ECO:0000269|PubMed:13591312}. CC -!- PHARMACEUTICAL: Oxytocin is available under the names Pitocin (Parke- CC Davis) and Syntocinon (Sandoz) (PubMed:36864410). Used to artificially CC speed or induce labor (PubMed:36864410). {ECO:0000303|PubMed:36864410}. CC -!- SIMILARITY: Belongs to the vasopressin/oxytocin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Oxytocin entry; CC URL="https://en.wikipedia.org/wiki/Oxytocin"; 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; M25650; AAA59977.1; -; mRNA. DR EMBL; M11186; AAA98806.1; -; Genomic_DNA. DR EMBL; AY082910; AAL92860.1; -; Genomic_DNA. DR EMBL; AL160414; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC069144; AAH69144.1; -; mRNA. DR EMBL; BC101841; AAI01842.1; -; mRNA. DR EMBL; BC101843; AAI01844.1; -; mRNA. DR EMBL; X03173; CAA26936.1; -; mRNA. DR EMBL; M62611; AAA59979.1; -; mRNA. DR CCDS; CCDS13044.1; -. DR PIR; A94676; NFHU1. DR RefSeq; NP_000906.1; NM_000915.4. DR RefSeq; XP_054179442.1; XM_054323467.1. DR PDB; 7OFG; NMR; -; A=20-28. DR PDB; 7OTD; NMR; -; A=20-28. DR PDB; 7QVM; EM; 3.25 A; L=20-28. DR PDB; 7RYC; EM; 2.90 A; L=20-28. DR AlphaFoldDB; P01178; -. DR EMDB; EMD-14180; -. DR EMDB; EMD-24733; -. DR MDposit; P01178; -. DR SMR; P01178; -. DR BioGRID; 111060; 21. DR FunCoup; P01178; 689. DR IntAct; P01178; 7. DR NDEx; IQUERY-CP-OXT; 4 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000217386; -. DR ChEMBL; CHEMBL5169107; -. DR DrugBank; DB00107; Oxytocin. DR DrugCentral; P01178; -. DR BioMuta; OXT; -. DR DMDM; 128071; -. DR MassIVE; P01178; -. DR PaxDb; 9606-ENSP00000217386; -. DR PeptideAtlas; P01178; -. DR ProteomicsDB; 51341; -. DR Antibodypedia; 7257; 252 antibodies from 37 providers. DR DNASU; 5020; -. DR Ensembl; ENST00000217386.2; ENSP00000217386.2; ENSG00000101405.3. DR GeneID; 5020; -. DR KEGG; hsa:5020; -. DR MANE-Select; ENST00000217386.2; ENSP00000217386.2; NM_000915.4; NP_000906.1. DR AGR; HGNC:8528; -. DR ClinPGx; PA32857; -. DR CTD; 5020; -. DR DisGeNET; 5020; -. DR GeneCards; OXT; -. DR HGNC; HGNC:8528; OXT. DR HPA; ENSG00000101405; Tissue enriched (brain). DR MIM; 167050; gene. DR OpenTargets; ENSG00000101405; -. DR VEuPathDB; HostDB:ENSG00000101405; -. DR eggNOG; ENOG502S2CT; Eukaryota. DR GeneTree; ENSGT00390000004511; -. DR HOGENOM; CLU_125770_1_0_1; -. DR InParanoid; P01178; -. DR OMA; ACVINDP; -. DR OrthoDB; 10056056at2759; -. DR PAN-GO; P01178; 7 GO annotations based on evolutionary models. DR PhylomeDB; P01178; -. DR PathwayCommons; P01178; -. DR Reactome; R-HSA-388479; Vasopressin-like receptors. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR SignaLink; P01178; -. DR SIGNOR; P01178; -. DR Agora; ENSG00000101405; -. DR BioGRID-ORCS; 5020; 11 hits in 1146 CRISPR screens. DR GeneWiki; Neurophysin_I; -. DR GeneWiki; Oxytocin; -. DR GenomeRNAi; 5020; -. DR Pharos; P01178; Tbio. DR PRO; PR:P01178; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; P01178; protein. DR Bgee; ENSG00000101405; Expressed in oocyte and 104 other cell types or tissues. DR ExpressionAtlas; P01178; baseline and differential. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0098992; C:neuronal dense core vesicle; IEA:Ensembl. DR GO; GO:0030141; C:secretory granule; IBA:GO_Central. DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl. DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0005185; F:neurohypophyseal hormone activity; IEA:InterPro. DR GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central. DR GO; GO:0031855; F:oxytocin receptor binding; IBA:GO_Central. DR GO; GO:0042756; P:drinking behavior; IEA:Ensembl. DR GO; GO:0042755; P:eating behavior; IEA:Ensembl. DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl. DR GO; GO:0007625; P:grooming behavior; IEA:Ensembl. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0060179; P:male mating behavior; IEA:Ensembl. DR GO; GO:0002125; P:maternal aggressive behavior; IBA:GO_Central. DR GO; GO:0042711; P:maternal behavior; IEA:Ensembl. DR GO; GO:0007613; P:memory; IEA:Ensembl. DR GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl. DR GO; GO:0035811; P:negative regulation of urine volume; IEA:Ensembl. DR GO; GO:0045777; P:positive regulation of blood pressure; IEA:Ensembl. DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl. DR GO; GO:0045925; P:positive regulation of female receptivity; IEA:Ensembl. DR GO; GO:0060450; P:positive regulation of hindgut contraction; IEA:Ensembl. DR GO; GO:0010701; P:positive regulation of norepinephrine secretion; IEA:Ensembl. DR GO; GO:0045778; P:positive regulation of ossification; IEA:Ensembl. DR GO; GO:0060406; P:positive regulation of penile erection; IEA:Ensembl. DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; IEA:Ensembl. DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl. DR GO; GO:0050806; P:positive regulation of synaptic transmission; IEA:Ensembl. DR GO; GO:0070474; P:positive regulation of uterine smooth muscle contraction; IBA:GO_Central. DR GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl. DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl. DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl. DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0045472; P:response to ether; IEA:Ensembl. DR GO; GO:0032094; P:response to food; IEA:Ensembl. DR GO; GO:0033595; P:response to genistein; IEA:Ensembl. DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl. DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl. DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl. DR GO; GO:0034695; P:response to prostaglandin E; IEA:Ensembl. DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl. DR GO; GO:0009744; P:response to sucrose; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0035176; P:social behavior; IEA:Ensembl. DR GO; GO:0042713; P:sperm ejaculation; IEA:Ensembl. DR FunFam; 2.60.9.10:FF:000001; oxytocin-neurophysin 1; 1. 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:SF2; OXYTOCIN-NEUROPHYSIN 1; 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 PDBsum; 7OFG; -. DR PDBsum; 7OTD; -. DR PDBsum; 7QVM; -. DR PDBsum; 7RYC; -. PE 1: Evidence at protein level; KW 3D-structure; Amidation; Behavior; Cleavage on pair of basic residues; KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; Hormone; KW Pharmaceutical; Proteomics identification; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:13591312" FT PEPTIDE 20..28 FT /note="Oxytocin" FT /evidence="ECO:0000269|PubMed:13591312" FT /id="PRO_0000020495" FT CHAIN 32..125 FT /note="Neurophysin 1" FT /evidence="ECO:0000269|PubMed:6574452, FT ECO:0000269|PubMed:7262323" FT /id="PRO_0000020496" FT BINDING 20 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0000269|PubMed:34459989" FT BINDING 21 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0000269|PubMed:34459989" FT BINDING 22 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0000269|PubMed:34459989" FT BINDING 23 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0000269|PubMed:34459989" FT MOD_RES 28 FT /note="Glycine amide" FT /evidence="ECO:0000269|PubMed:13591312" FT DISULFID 20..25 FT /evidence="ECO:0000269|PubMed:34459989, FT ECO:0000269|PubMed:35241813, ECO:0000269|PubMed:35851571, FT ECO:0007744|PDB:7OFG, ECO:0007744|PDB:7OTD, FT ECO:0007744|PDB:7QVM, ECO:0007744|PDB:7RYC" 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 MUTAGEN 28 FT /note="G->V: Gain of antagonist activity on V1aR/AVPR1A FT (and loss of agonist activity on this receptor). 310-fold FT decrease in affinity for oxytocin receptor (OXTR), 13-fold FT decrease in affinity for V1aR/AVPR1A, and complete loss of FT affinity for V1bR/AVPR1B and V2R/AVPR2." FT /evidence="ECO:0000269|PubMed:18174156" FT CONFLICT 94 FT /note="S -> G (in Ref. 6; AAA59979)" FT /evidence="ECO:0000305" FT CONFLICT 100..101 FT /note="VL -> AA (in Ref. 9; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 100 FT /note="Missing (in Ref. 2; AAA98806)" FT /evidence="ECO:0000305" FT CONFLICT 124 FT /note="Q -> L (in Ref. 9; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 24..27 FT /evidence="ECO:0007829|PDB:7RYC" SQ SEQUENCE 125 AA; 12722 MW; C65BB544731A0E7C CRC64; MAGPSLACCL LGLLALTSAC YIQNCPLGGK RAAPDLDVRK CLPCGPGGKG RCFGPNICCA EELGCFVGTA EALRCQEENY LPSPCQSGQK ACGSGGRCAV LGLCCSPDGC HADPACDAEA TFSQR //