NEU2_RAT
ID NEU2_RAT Reviewed; 168 AA.
AC P01186;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 161.
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-I;
DE Contains:
DE RecName: Full=Copeptin;
DE Flags: Precursor;
GN Name=Avp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=1706187; DOI=10.1089/dna.1991.10.81;
RA Schmitz E., Mohr E., Richter D.;
RT "Rat vasopressin and oxytocin genes are linked by a long interspersed
RT repeated DNA element (LINE): sequence and transcriptional analysis of
RT LINE.";
RL DNA Cell Biol. 10:81-91(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE.
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6315416; DOI=10.1002/j.1460-2075.1983.tb01497.x;
RA Schmale H., Heinsohn S., Richter D.;
RT "Structural organization of the rat gene for the arginine vasopressin-
RT neurophysin precursor.";
RL EMBO J. 2:763-767(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6526016; DOI=10.1002/j.1460-2075.1984.tb02291.x;
RA Schmale H., Ivell R., Breindl M., Darmer D., Richter D.;
RT "The mutant vasopressin gene from diabetes insipidus (Brattleboro) rats is
RT transcribed but the message is not efficiently translated.";
RL EMBO J. 3:3289-3293(1984).
RN [5]
RP AMINO-ACID COMPOSITION OF 24-32, AND AMIDATION AT GLY-32.
RX PubMed=5150741; DOI=10.1016/s0300-9084(71)80199-2;
RA Chauvet J., Chauvet M.-T., Acher R.;
RT "Evolution of neurohypophyseal hormones: isolation of active principles
RT from rabbits and rats.";
RL Biochimie 53:1099-1104(1971).
RN [6]
RP PROTEIN SEQUENCE OF 36-128.
RX PubMed=7036996; DOI=10.1016/0006-291x(81)90493-9;
RA Chauvet M.-T., Chauvet J., Acher R.;
RT "Identification of rat neurophysins: complete amino acid sequences of
RT MSEL- and VLDV-neurophysins.";
RL Biochem. Biophys. Res. Commun. 103:595-603(1981).
RN [7]
RP PROTEIN SEQUENCE OF 36-68.
RX PubMed=891987; DOI=10.1016/0014-5793(77)80478-x;
RA Schlesinger D.H., Pickering B.T., Watkins W.B., Peek J.C., Moore L.G.,
RA Audhya T.K., Walter R.;
RT "A comparative study of partial neurophysin protein sequences of cod,
RT guinea pig, rat and sheep.";
RL FEBS Lett. 80:371-373(1977).
RN [8]
RP PROTEIN SEQUENCE OF 130-168.
RX PubMed=6641941; DOI=10.1016/0014-5793(83)80830-8;
RA Chauvet M.-T., Chauvet J., Acher R.;
RT "The glycopeptide domain of the rat vasopressin precursor.";
RL FEBS Lett. 163:257-260(1983).
RN [9]
RP PROTEIN SEQUENCE OF 130-168.
RX PubMed=3956504; DOI=10.1111/j.1432-1033.1986.tb09558.x;
RA Burbach J.P.H., Seidah N.G., Chretien M.;
RT "Isolation and primary structure of novel neurointermediate pituitary
RT peptides derived from the C-terminal of the rat vasopressin-neurophysin
RT precursor (propressophysin).";
RL Eur. J. Biochem. 156:137-142(1986).
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 -!- SIMILARITY: Belongs to the vasopressin/oxytocin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA42342.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X59496; CAA42086.1; -; Genomic_DNA.
DR EMBL; M25646; AAA42342.1; ALT_INIT; mRNA.
DR EMBL; V01275; CAA24582.1; -; Genomic_DNA.
DR EMBL; V01276; CAA24583.1; -; Genomic_DNA.
DR EMBL; X01637; CAA25795.2; -; Genomic_DNA.
DR PIR; A90982; NVRT2.
DR RefSeq; NP_058688.2; NM_016992.2.
DR AlphaFoldDB; P01186; -.
DR SMR; P01186; -.
DR STRING; 10116.ENSRNOP00000028833; -.
DR GlyGen; P01186; 1 site.
DR PaxDb; P01186; -.
DR Ensembl; ENSRNOT00000028833; ENSRNOP00000028833; ENSRNOG00000021229.
DR GeneID; 24221; -.
DR KEGG; rno:24221; -.
DR UCSC; RGD:2184; rat.
DR CTD; 551; -.
DR RGD; 2184; Avp.
DR eggNOG; ENOG502S21K; Eukaryota.
DR GeneTree; ENSGT00390000004511; -.
DR HOGENOM; CLU_125770_0_0_1; -.
DR InParanoid; P01186; -.
DR OMA; GCVVDSD; -.
DR OrthoDB; 1548839at2759; -.
DR PhylomeDB; P01186; -.
DR TreeFam; TF333018; -.
DR Reactome; R-RNO-388479; Vasopressin-like receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-RNO-879518; Transport of organic anions.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P01186; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000021229; Expressed in testis and 9 other tissues.
DR Genevisible; P01186; RN.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0005185; F:neurohypophyseal hormone activity; IEA:InterPro.
DR GO; GO:0005184; F:neuropeptide hormone activity; IDA:RGD.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0031894; F:V1A vasopressin receptor binding; IDA:RGD.
DR GO; GO:0031895; F:V1B vasopressin receptor binding; IMP:RGD.
DR GO; GO:0031896; F:V2 vasopressin receptor binding; TAS:RGD.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0007625; P:grooming behavior; IMP:RGD.
DR GO; GO:0042538; P:hyperosmotic salinity response; IEP:RGD.
DR GO; GO:0007626; P:locomotory behavior; IMP:RGD.
DR GO; GO:0002125; P:maternal aggressive behavior; IMP:RGD.
DR GO; GO:0042711; P:maternal behavior; IMP:RGD.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; IMP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0007621; P:negative regulation of female receptivity; IMP:RGD.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:0051970; P:negative regulation of transmission of nerve impulse; IMP:RGD.
DR GO; GO:0043084; P:penile erection; IMP:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0032849; P:positive regulation of cellular pH reduction; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; IMP:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IMP:RGD.
DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IDA:RGD.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
DR GO; GO:0070528; P:protein kinase C signaling; ISO:RGD.
DR GO; GO:0035813; P:regulation of renal sodium excretion; IMP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0006939; P:smooth muscle contraction; TAS:RGD.
DR GO; GO:0035176; P:social behavior; IMP:RGD.
DR GO; GO:0001659; P:temperature homeostasis; TAS:RGD.
DR GO; GO:0042310; P:vasoconstriction; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; ISO:RGD.
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; Glycoprotein; Hormone; Reference proteome; Secreted;
KW Signal; Vasoactive; Vasoconstrictor.
FT SIGNAL 1..23
FT PEPTIDE 24..32
FT /note="Arg-vasopressin"
FT /id="PRO_0000020524"
FT CHAIN 36..128
FT /note="Neurophysin 2"
FT /id="PRO_0000020525"
FT PEPTIDE 130..168
FT /note="Copeptin"
FT /id="PRO_0000020526"
FT SITE 32
FT /note="Important for agonist activity on V1aR/AVPR1A"
FT /evidence="ECO:0000250|UniProtKB:P01185"
FT MOD_RES 32
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:5150741"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 24..29
FT DISULFID 45..89
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 48..62
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 56..79
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 63..69
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 96..108
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 102..120
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 109..114
FT /evidence="ECO:0000250|UniProtKB:P01175"
SQ SEQUENCE 168 AA; 17923 MW; DB369FED09A74698 CRC64;
MLAMMLNTTL SACFLSLLAL TSACYFQNCP RGGKRATSDM ELRQCLPCGP GGKGRCFGPS
ICCADELGCF LGTAEALRCQ EENYLPSPCQ SGQKPCGSGG RCAAAGICCS DESCVAEPEC
REGFFRLTRA REQSNATQLD GPARELLLRL VQLAGTQESV DSAKPRVY
