NEU1_BOVIN
ID NEU1_BOVIN Reviewed; 125 AA.
AC P01175; A5PJ78; P01188;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 160.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6687626; DOI=10.1038/302342a0;
RA Land H., Grez M., Ruppert S., Schmale H., Rehbein M., Richter D.,
RA Schuetz G.;
RT "Deduced amino acid sequence from the bovine oxytocin-neurophysin I
RT precursor cDNA.";
RL Nature 302:342-344(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6709064; DOI=10.1038/308554a0;
RA Ruppert S., Scherer G., Schuetz G.;
RT "Recent gene conversion involving bovine vasopressin and oxytocin precursor
RT genes suggested by nucleotide sequence.";
RL Nature 308:554-557(1984).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-125.
RX PubMed=6209133; DOI=10.1002/j.1460-2075.1984.tb02139.x;
RA Ivell R., Richter D.;
RT "The gene for the hypothalamic peptide hormone oxytocin is highly expressed
RT in the bovine corpus luteum: biosynthesis, structure and sequence
RT analysis.";
RL EMBO J. 3:2351-2354(1984).
RN [6]
RP PROTEIN SEQUENCE OF 20-28, DISULFIDE BONDS, AND AMIDATION AT GLY-28.
RX PubMed=13129273; DOI=10.1016/s0021-9258(18)49238-1;
RA du Vigneaud V., Ressler C., Trippett S.;
RT "The sequence of amino acids in oxytocin, with a proposal for the structure
RT of oxytocin.";
RL J. Biol. Chem. 205:949-957(1953).
RN [7]
RP PROTEIN SEQUENCE OF 20-28.
RA Tuppy H., Michl H.;
RT "About the chemical structure of oxytocin.";
RL Monatsh. Chem. 84:1011-1020(1953).
RN [8]
RP PROTEIN SEQUENCE OF 32-124.
RX PubMed=670174; DOI=10.1016/s0021-9258(17)34650-1;
RA Schlesinger D.H., Audhya T.K., Walter R.;
RT "Complete amino acid sequence of bovine neurophysin-I. A major secretory
RT product of the posterior pituitary.";
RL J. Biol. Chem. 253:5019-5024(1978).
RN [9]
RP PROTEIN SEQUENCE OF 32-124.
RX PubMed=428540; DOI=10.1016/0014-5793(79)80146-5;
RA Chauvet M.-T., Codogno P., Chauvet J., Acher R.;
RT "Comparison between MSEL- and VLDV-neurophysins. Complete amino acid
RT sequences of porcine and bovine VLDV-neurophysins.";
RL FEBS Lett. 98:37-40(1979).
RN [10]
RP DISULFIDE BONDS.
RX PubMed=2911588; DOI=10.1073/pnas.86.2.429;
RA Burman S., Wellner D., Chait B., Chaudhary T., Breslow E.;
RT "Complete assignment of neurophysin disulfides indicates pairing in two
RT separate domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:429-433(1989).
RN [11] {ECO:0007744|PDB:1XY1, ECO:0007744|PDB:1XY2}
RP X-RAY CRYSTALLOGRAPHY (1.04 ANGSTROMS) OF OXYTOCIN, DISULFIDE BOND, AND
RP AMIDATION AT GLY-28.
RX PubMed=3008332; DOI=10.1126/science.3008332;
RA Wood S.P., Tickle I.J., Treharne A.M., Pitts J.E., Mascarenhas Y., Li J.Y.,
RA Husain J., Cooper S., Blundell T.L., Hruby V.J.;
RT "Crystal structure analysis of deamino-oxytocin: conformational flexibility
RT and receptor binding.";
RL Science 232:633-636(1986).
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the vasopressin/oxytocin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA23450.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA25194.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X00502; CAA25194.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M25648; AAA30680.1; -; mRNA.
DR EMBL; BC141997; AAI41998.1; -; mRNA.
DR EMBL; V00114; CAA23448.1; -; mRNA.
DR EMBL; V00114; CAA23450.1; ALT_INIT; mRNA.
DR EMBL; V00114; CAA23449.1; ALT_SEQ; mRNA.
DR EMBL; X00950; CAA25462.1; -; mRNA.
DR PIR; S07332; NFBO1.
DR RefSeq; NP_789825.1; NM_176855.1.
DR PDB; 1L5C; NMR; -; A=32-123.
DR PDB; 1L5D; NMR; -; A=32-123.
DR PDB; 1XY1; X-ray; 1.04 A; A/B=21-28.
DR PDB; 1XY2; X-ray; 1.20 A; A=21-28.
DR PDB; 2HNU; X-ray; 2.00 A; A/B/C/D/E=38-118.
DR PDB; 2HNV; X-ray; 2.50 A; A/B/C/D/E=38-118.
DR PDB; 2HNW; X-ray; 2.90 A; A/B/C/D/E=38-117.
DR PDB; 2LBH; NMR; -; A/B=32-123.
DR PDB; 2LBN; NMR; -; A=32-123.
DR PDBsum; 1L5C; -.
DR PDBsum; 1L5D; -.
DR PDBsum; 1XY1; -.
DR PDBsum; 1XY2; -.
DR PDBsum; 2HNU; -.
DR PDBsum; 2HNV; -.
DR PDBsum; 2HNW; -.
DR PDBsum; 2LBH; -.
DR PDBsum; 2LBN; -.
DR AlphaFoldDB; P01175; -.
DR BMRB; P01175; -.
DR SMR; P01175; -.
DR STRING; 9913.ENSBTAP00000010554; -.
DR PaxDb; P01175; -.
DR PRIDE; P01175; -.
DR Ensembl; ENSBTAT00000010554; ENSBTAP00000010554; ENSBTAG00000008026.
DR GeneID; 280888; -.
DR KEGG; bta:280888; -.
DR CTD; 5020; -.
DR VEuPathDB; HostDB:ENSBTAG00000008026; -.
DR VGNC; VGNC:32515; OXT.
DR eggNOG; ENOG502S2CT; Eukaryota.
DR GeneTree; ENSGT00390000004511; -.
DR HOGENOM; CLU_125770_1_0_1; -.
DR InParanoid; P01175; -.
DR OMA; YIQNCPP; -.
DR OrthoDB; 1548839at2759; -.
DR TreeFam; TF333018; -.
DR Reactome; R-BTA-388479; Vasopressin-like receptors.
DR Reactome; R-BTA-416476; G alpha (q) signalling events.
DR EvolutionaryTrace; P01175; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000008026; Expressed in diaphragm and 50 other tissues.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
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:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IDA:CACAO.
DR GO; GO:0043207; P:response to external biotic stimulus; IDA:AgBase.
DR GO; GO:0032094; P:response to food; IDA:AgBase.
DR GO; GO:0009612; P:response to mechanical stimulus; IDA: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 3D-structure; Amidation; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Hormone; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:13129273, ECO:0000269|Ref.7"
FT PEPTIDE 20..28
FT /note="Oxytocin"
FT /id="PRO_0000020491"
FT CHAIN 32..125
FT /note="Neurophysin 1"
FT /id="PRO_0000020492"
FT MOD_RES 28
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:13129273,
FT ECO:0000269|PubMed:3008332"
FT DISULFID 20..25
FT /evidence="ECO:0000269|PubMed:2911588,
FT ECO:0000269|PubMed:3008332"
FT DISULFID 41..85
FT /evidence="ECO:0007744|PDB:1L5C, ECO:0007744|PDB:1L5D,
FT ECO:0007744|PDB:2HNU, ECO:0007744|PDB:2HNV,
FT ECO:0007744|PDB:2HNW, ECO:0007744|PDB:2LBN"
FT DISULFID 44..58
FT /evidence="ECO:0007744|PDB:1L5C, ECO:0007744|PDB:1L5D,
FT ECO:0007744|PDB:2HNU, ECO:0007744|PDB:2HNV,
FT ECO:0007744|PDB:2HNW, ECO:0007744|PDB:2LBN"
FT DISULFID 52..75
FT /evidence="ECO:0007744|PDB:1L5C, ECO:0007744|PDB:1L5D,
FT ECO:0007744|PDB:2HNU, ECO:0007744|PDB:2HNV,
FT ECO:0007744|PDB:2HNW, ECO:0007744|PDB:2LBN"
FT DISULFID 59..65
FT /evidence="ECO:0007744|PDB:1L5C, ECO:0007744|PDB:1L5D,
FT ECO:0007744|PDB:2HNU, ECO:0007744|PDB:2HNV,
FT ECO:0007744|PDB:2HNW, ECO:0007744|PDB:2LBN"
FT DISULFID 92..104
FT /evidence="ECO:0007744|PDB:1L5C, ECO:0007744|PDB:1L5D,
FT ECO:0007744|PDB:2HNU, ECO:0007744|PDB:2HNV,
FT ECO:0007744|PDB:2HNW, ECO:0007744|PDB:2LBN"
FT DISULFID 98..116
FT /evidence="ECO:0007744|PDB:1L5C, ECO:0007744|PDB:1L5D,
FT ECO:0007744|PDB:2HNU, ECO:0007744|PDB:2HNV,
FT ECO:0007744|PDB:2HNW, ECO:0007744|PDB:2LBN"
FT DISULFID 105..110
FT /evidence="ECO:0007744|PDB:1L5C, ECO:0007744|PDB:1L5D,
FT ECO:0007744|PDB:2HNU, ECO:0007744|PDB:2HNV,
FT ECO:0007744|PDB:2HNW, ECO:0007744|PDB:2LBN"
FT CONFLICT 124
FT /note="Q -> L (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1L5C"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2HNU"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2HNU"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:2HNU"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:2HNU"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:2HNU"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:2HNU"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:2HNU"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:2HNU"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2HNU"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2HNU"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2HNU"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:2HNU"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:2HNU"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1L5D"
SQ SEQUENCE 125 AA; 12665 MW; 3B4E4E79A0B7F032 CRC64;
MAGSSLACCL LGLLALTSAC YIQNCPLGGK RAVLDLDVRT CLPCGPGGKG RCFGPSICCG
DELGCFVGTA EALRCQEENY LPSPCQSGQK PCGSGGRCAA AGICCSPDGC HEDPACDPEA
AFSQH
