ID NEU4_ONCKE Reviewed; 158 AA. AC P16042; Q91174; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 02-SEP-2026, entry version 95. DE RecName: Full=Vasotocin-neurophysin VT 2; DE Contains: DE RecName: Full=Vasotocin; DE Short=VT; DE Contains: DE RecName: Full=Neurophysin VT 2; DE Flags: Precursor; OS Oncorhynchus keta (Chum salmon) (Salmo keta). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes; OC Salmonidae; Salmoninae; Oncorhynchus. OX NCBI_TaxID=8018; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=2298304; DOI=10.1016/0014-5793(90)80129-7; RA Heierhorst J., Mahlmann S., Morley S.D., Coe I.R., Sherwood N.M., RA Richter D.; RT "Molecular cloning of two distinct vasotocin precursor cDNAs from chum RT salmon (Oncorhynchus keta) suggests an ancient gene duplication."; RL FEBS Lett. 260:301-304(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Tsugaruishi; TISSUE=Brain; RX PubMed=2045542; DOI=10.1007/bf00571256; RA Hyodo S., Kato Y., Ono M., Urano A.; RT "Cloning and sequence analyses of cDNAs encoding vasotocin and isotocin RT precursors of chum salmon, Oncorhynchus keta: evolutionary relationships of RT neurohypophysial hormone precursors."; RL J. Comp. Physiol. B 160:601-608(1991). CC -!- FUNCTION: Vasotocin is an antidiuretic hormone. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- PTM: Seven disulfide bonds are present in neurophysin. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the vasopressin/oxytocin family. {ECO:0000305}. 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; X17328; CAA35206.1; -; mRNA. DR EMBL; D10943; BAA01737.1; ALT_SEQ; mRNA. DR PIR; B34132; B34132. DR AlphaFoldDB; P16042; -. DR SMR; P16042; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0030141; C:secretory granule; IEA:TreeGrafter. DR GO; GO:0005185; F:neurohypophyseal hormone activity; IEA:InterPro. 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:SF13; VASOPRESSIN-NEUROPHYSIN 2-COPEPTIN PRECURSOR; 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 2: Evidence at transcript level; KW Amidation; Cleavage on pair of basic residues; Disulfide bond; Hormone; KW Secreted; Signal. FT SIGNAL 1..19 FT PEPTIDE 20..28 FT /note="Vasotocin" FT /id="PRO_0000020568" FT CHAIN 32..158 FT /note="Neurophysin VT 2" FT /id="PRO_0000020569" FT MOD_RES 28 FT /note="Glycine amide" FT /evidence="ECO:0000250" FT DISULFID 20..25 FT /evidence="ECO:0000250|UniProtKB:P01175" 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..105 FT /evidence="ECO:0000250|UniProtKB:P01175" FT DISULFID 99..117 FT /evidence="ECO:0000250|UniProtKB:P01175" FT DISULFID 106..111 FT /evidence="ECO:0000250|UniProtKB:P01175" SQ SEQUENCE 158 AA; 16670 MW; F8002437A89611C4 CRC64; MPHSTLLLCV IGLLAFSSAC YIQNCPRGGK RALQDTGIRQ CMTCGPGDQG HCFGPSICCG EGLGCWMGSP ETARCFEENY LPTPCQTGGR PCGSDAGRCA APGVCCDSES CVLDPDCLSE SRYHSPADHS AGATSDSPGE LLLRLLHFAT RGQSEYKQ //