NEU4_ONCKE
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 25-MAY-2022, entry version 88.
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:0005185; F:neurohypophyseal hormone activity; IEA:InterPro.
DR Gene3D; 2.60.9.10; -; 1.
DR InterPro; IPR000981; Neurhyp_horm.
DR InterPro; IPR036387; Neurhyp_horm_dom_sf.
DR InterPro; IPR022423; Neurohypophysial_hormone_CS.
DR PANTHER; PTHR11681; PTHR11681; 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; SSF49606; 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
