NEU2_BOVIN
ID NEU2_BOVIN Reviewed; 166 AA.
AC P01180; Q3SZF1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Vasopressin-neurophysin 2-copeptin;
DE AltName: Full=AVP-NPII;
DE Contains:
DE RecName: Full=Arg-vasopressin;
DE AltName: Full=Arginine-vasopressin;
DE Contains:
DE RecName: Full=Neurophysin 2;
DE AltName: Full=Neurophysin-II;
DE Contains:
DE RecName: Full=Copeptin;
DE Flags: Precursor;
GN Name=AVP;
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=6276766; DOI=10.1038/295299a0;
RA Land H., Schuetz G., Schmale H., Richter D.;
RT "Nucleotide sequence of cloned cDNA encoding bovine arginine vasopressin-
RT neurophysin II precursor.";
RL Nature 295:299-303(1982).
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 (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 20-28, AND AMIDATION AT GLY-28.
RA du Vigneaud V., Lawler H.C., Popenoe E.A.;
RT "Enzymatic cleavage of glycinamide from vasopressin and a proposed
RT structure for this pressor-antidiuretic hormone of the posterior
RT pituitary.";
RL J. Am. Chem. Soc. 75:4880-4881(1953).
RN [6]
RP PROTEIN SEQUENCE OF 20-28.
RX PubMed=13115463; DOI=10.1016/0006-3002(53)90173-5;
RA Acher R., Chauvet J.;
RT "The structure of bovine vasopressin.";
RL Biochim. Biophys. Acta 12:487-488(1953).
RN [7]
RP PROTEIN SEQUENCE OF 32-126.
RX PubMed=3318825; DOI=10.1016/0006-291x(87)90950-8;
RA Burman S., Breslow E., Chait B.T., Chaudhary T.;
RT "Partial assignment of disulfide pairs in neurophysins.";
RL Biochem. Biophys. Res. Commun. 148:827-833(1987).
RN [8]
RP PROTEIN SEQUENCE OF 32-126.
RA Chauvet M.-T., Chauvet J., Acher R.;
RT "The neurohypophysial hormone-binding protein: complete amino-acid sequence
RT of ovine and bovine MSEL-neurophysins.";
RL Eur. J. Biochem. 69:475-485(1976).
RN [9]
RP PROTEIN SEQUENCE OF 32-126.
RX PubMed=1252249; DOI=10.1016/0006-291x(76)91192-x;
RA Wuu T.-C., Crumm S.E.;
RT "Amino acid sequence of bovine neurophysin-II: a reinvestigation.";
RL Biochem. Biophys. Res. Commun. 68:634-639(1976).
RN [10]
RP PRELIMINARY PROTEIN SEQUENCE (FETAL NEUROPHYSIN 2).
RX PubMed=1248642; DOI=10.1016/0014-5793(76)80023-3;
RA Chauvet M.-T., Chauvet J., Acher R.;
RT "Foetal bovine MSEL-neurophysin: comparison with adult homologous
RT neurophysin.";
RL FEBS Lett. 62:89-92(1976).
RN [11]
RP DISULFIDE BONDS IN NEUROPHYSIN 2.
RX PubMed=4564211; DOI=10.1073/pnas.69.11.3350;
RA Schlesinger D.H., Frangione B., Walter R.;
RT "Covalent structure of bovine neurophysin-II: localization of the disulfide
RT bonds.";
RL Proc. Natl. Acad. Sci. U.S.A. 69:3350-3354(1972).
RN [12]
RP PROTEIN SEQUENCE OF 128-166.
RX PubMed=465021; DOI=10.1016/s0006-291x(79)80007-8;
RA Smyth D.G., Massey D.E.;
RT "A new glycopeptide in pig, ox and sheep pituitary.";
RL Biochem. Biophys. Res. Commun. 87:1006-1010(1979).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF NEUROPHYSIN 2.
RX PubMed=2034668; DOI=10.1073/pnas.88.10.4240;
RA Chen L.Q., Rose J.P., Breslow E., Yang D., Chang W.-R., Furey W.F. Jr.,
RA Sax M., Wang B.-C.;
RT "Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 A
RT determined from the single-wavelength anomalous scattering signal of an
RT incorporated iodine atom.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4240-4244(1991).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF NEUROPHYSIN 2.
RC TISSUE=Pituitary;
RX PubMed=8564543; DOI=10.1038/nsb0296-163;
RA Rose J.P., Wu C.-K., Hsiao C.-D., Breslow E., Wang B.-C.;
RT "Crystal structure of the neurophysin-oxytocin complex.";
RL Nat. Struct. Biol. 3:163-169(1996).
CC -!- FUNCTION: Neurophysin 2 specifically binds vasopressin.
CC -!- FUNCTION: Vasopressin has a direct antidiuretic action on the kidney,
CC it also causes vasoconstriction of the peripheral vessels. Acts by
CC binding to vasopressin receptors (V1bR/AVPR1B, V1aR/AVPR1A, and
CC V2R/AVPR2) (By similarity). {ECO:0000250|UniProtKB:P01185}.
CC -!- SUBUNIT: Interacts with vasopressin receptors V1bR/AVPR1B (Ki=85 pM),
CC V1aR/AVPR1A (Ki=0.6 nM) and V2R/AVPR2 (Ki=4.9 nM) (By similarity).
CC Interacts with oxytocin receptor (OXTR) (Ki=110 nM) (By similarity).
CC {ECO:0000250|UniProtKB:P01185}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MISCELLANEOUS: Fetal neurophysin is the major neurophysin present in
CC the neurohypophysis of 7 to 9 month fetuses and its sequence appears to
CC be identical with that of the adult.
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; V00113; CAA23447.1; -; mRNA.
DR EMBL; X00503; CAA25195.1; -; Genomic_DNA.
DR EMBL; M25645; AAA30806.1; -; mRNA.
DR EMBL; BC102897; AAI02898.1; -; mRNA.
DR PIR; S09580; NVBO2.
DR RefSeq; NP_789824.1; NM_176854.2.
DR PDB; 1JK4; X-ray; 2.30 A; A=38-126, B=20-26.
DR PDB; 1JK6; X-ray; 2.40 A; A/C=38-126.
DR PDB; 1NPO; X-ray; 3.00 A; A/C=32-126.
DR PDB; 2BN2; X-ray; 2.80 A; A/C/E/G=32-126.
DR PDBsum; 1JK4; -.
DR PDBsum; 1JK6; -.
DR PDBsum; 1NPO; -.
DR PDBsum; 2BN2; -.
DR AlphaFoldDB; P01180; -.
DR SMR; P01180; -.
DR STRING; 9913.ENSBTAP00000010555; -.
DR PaxDb; P01180; -.
DR GeneID; 280728; -.
DR KEGG; bta:280728; -.
DR CTD; 551; -.
DR eggNOG; ENOG502S21K; Eukaryota.
DR HOGENOM; CLU_125770_0_0_1; -.
DR InParanoid; P01180; -.
DR OrthoDB; 1548839at2759; -.
DR TreeFam; TF333018; -.
DR EvolutionaryTrace; P01180; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0031894; F:V1A vasopressin receptor binding; IBA:GO_Central.
DR GO; GO:0042310; P:vasoconstriction; IEA:UniProtKB-KW.
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; Glycoprotein; Hormone;
KW Reference proteome; Secreted; Signal; Vasoactive; Vasoconstrictor.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:13115463, ECO:0000269|Ref.5"
FT PEPTIDE 20..28
FT /note="Arg-vasopressin"
FT /id="PRO_0000020509"
FT CHAIN 32..126
FT /note="Neurophysin 2"
FT /id="PRO_0000020510"
FT PEPTIDE 128..166
FT /note="Copeptin"
FT /id="PRO_0000020511"
FT SITE 28
FT /note="Important for agonist activity on V1aR/AVPR1A"
FT /evidence="ECO:0000250|UniProtKB:P01185"
FT MOD_RES 28
FT /note="Glycine amide"
FT /evidence="ECO:0000269|Ref.5"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 20..25
FT /evidence="ECO:0000269|PubMed:4564211"
FT DISULFID 41..85
FT /evidence="ECO:0000269|PubMed:4564211"
FT DISULFID 44..58
FT /evidence="ECO:0000269|PubMed:4564211"
FT DISULFID 52..75
FT /evidence="ECO:0000269|PubMed:4564211"
FT DISULFID 59..65
FT /evidence="ECO:0000269|PubMed:4564211"
FT DISULFID 92..104
FT /evidence="ECO:0000269|PubMed:4564211"
FT DISULFID 98..116
FT /evidence="ECO:0000269|PubMed:4564211"
FT DISULFID 105..110
FT /evidence="ECO:0000269|PubMed:4564211"
FT VARIANT 120
FT /note="V -> I (in 30% of the molecules)"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:1JK4"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:2BN2"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1JK4"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1JK4"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1JK4"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1JK4"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1JK4"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1JK4"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:1JK4"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1JK4"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1JK4"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1JK4"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1JK4"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1JK4"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1JK6"
SQ SEQUENCE 166 AA; 17325 MW; 0441DC255288D8F6 CRC64;
MPDATLPACF LSLLAFTSAC YFQNCPRGGK RAMSDLELRQ CLPCGPGGKG RCFGPSICCG
DELGCFVGTA EALRCQEENY LPSPCQSGQK PCGSGGRCAA AGICCNDESC VTEPECREGV
GFPRRVRAND RSNATLLDGP SGALLLRLVQ LAGAPEPAEP AQPGVY
