NEU1_SHEEP
ID NEU1_SHEEP Reviewed; 125 AA.
AC P13389; P01188;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Oxytocin-neurophysin 1;
DE Short=OT-NPI;
DE Contains:
DE RecName: Full=Oxytocin;
DE AltName: Full=Ocytocin;
DE Contains:
DE RecName: Full=Neurophysin 1;
DE Flags: Precursor;
GN Name=OXT;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Corpus luteum;
RX PubMed=2798140; DOI=10.1093/nar/17.19.7990;
RA Jones D.S.C., Flint A.P.F.;
RT "Nucleotide sequence of a full length cDNA clone encoding the oxytocin-
RT neurophysin I precursor isolated from the ovine corpus luteum.";
RL Nucleic Acids Res. 17:7990-7990(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Ovary;
RX PubMed=2095591; DOI=10.1071/rd9900703;
RA Ivell R., Hunt N., Abend N., Brackman B., Nollmeyer D., Lamsa J.C.,
RA McCracken J.A.;
RT "Structure and ovarian expression of the oxytocin gene in sheep.";
RL Reprod. Fertil. Dev. 2:703-711(1990).
RN [3]
RP PROTEIN SEQUENCE OF 20-28, AND AMIDATION AT GLY-28.
RA Acher R., Chauvet J., Lenci M.T.;
RT "Purification and structure of sheep oxytocin and vasopressin.";
RL C. R. Hebd. Seances Acad. Sci., D, Sci. Nat. 248:1435-1438(1959).
CC -!- FUNCTION: Neurophysin 1 specifically binds oxytocin.
CC -!- FUNCTION: Oxytocin causes contraction of the smooth muscle of the
CC uterus and of the mammary gland. Acts by binding to oxytocin receptor
CC (OXTR) (By similarity). {ECO:0000250|UniProtKB:P01178}.
CC -!- SUBUNIT: Interacts with oxytocin receptor (Ki=1.5 nM) (By similarity).
CC Interacts with vasopressin V1aR/AVPR1A (Ki=37 nM), V1bR/AVPR1B (Ki=222
CC nM), and V2R/AVPR2 receptors (Ki=823 nM) (By similarity).
CC {ECO:0000250|UniProtKB:P01178}.
CC -!- SIMILARITY: Belongs to the vasopressin/oxytocin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA34186.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X16052; CAA34184.1; -; mRNA.
DR EMBL; X16052; CAA34185.1; ALT_SEQ; mRNA.
DR EMBL; X16052; CAA34186.1; ALT_INIT; mRNA.
DR EMBL; X55131; CAA38924.1; -; Genomic_DNA.
DR PIR; S06086; NFSH1.
DR RefSeq; NP_001009801.1; NM_001009801.2.
DR AlphaFoldDB; P13389; -.
DR BMRB; P13389; -.
DR SMR; P13389; -.
DR Ensembl; ENSOART00020009373; ENSOARP00020007743; ENSOARG00020006060.
DR GeneID; 443390; -.
DR KEGG; oas:443390; -.
DR CTD; 5020; -.
DR OrthoDB; 1548839at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR GO; GO:0005185; F:neurohypophyseal hormone activity; IEA:InterPro.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0043207; P:response to external biotic stimulus; ISS:AgBase.
DR GO; GO:0032094; P:response to food; ISS:AgBase.
DR GO; GO:0009612; P:response to mechanical stimulus; ISS:AgBase.
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 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Hormone; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|Ref.3"
FT PEPTIDE 20..28
FT /note="Oxytocin"
FT /id="PRO_0000020505"
FT CHAIN 32..125
FT /note="Neurophysin 1"
FT /id="PRO_0000020506"
FT MOD_RES 28
FT /note="Glycine amide"
FT /evidence="ECO:0000269|Ref.3"
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 CONFLICT 48
FT /note="G -> A (in Ref. 1; CAA34184/CAA34186)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="C -> S (in Ref. 1; CAA34184/CAA34186)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 125 AA; 12635 MW; 3B4C05141422E432 CRC64;
MAGSSLACCL LGLLALTSAC YIQNCPLGGK RAVLDLDVRT CLPCGPGGKG RCFGPSICCG
DELGCFVGTA EALRCREENY LPSPCQSGQK PCGSGGRCAA AGICCSPDGC HADPACDPEA
AFSQH
