NEU2_CAVPO
ID NEU2_CAVPO Reviewed; 144 AA.
AC P10769;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 106.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3803579; DOI=10.1016/0014-5793(87)81294-2;
RA Chauvet M.-T., Rouille Y., Chauvet J., Acher R.;
RT "Guinea pig neurohypophysial hormones. Peculiar processing of the three-
RT domain vasopressin precursor.";
RL FEBS Lett. 210:40-44(1987).
RN [2]
RP PROTEIN SEQUENCE OF 13-144.
RX PubMed=3595848; DOI=10.1016/0014-5793(87)80659-2;
RA Chauvet J., Chauvet M.-T., Acher R.;
RT "Conformation limited proteolysis in the common neurophysin-copeptin
RT precursor shown by trypsin-sepharose chromatographic proteolysis.";
RL FEBS Lett. 217:180-183(1987).
RN [3]
RP PROTEIN SEQUENCE OF 13-105.
RX PubMed=3436704; DOI=10.1111/j.1399-3011.1987.tb03379.x;
RA Chauvet M.-T., Chauvet J., Acher R.;
RT "Guinea pig MSEL-neurophysin. Sequence comparison of eight mammalian MSEL-
RT neurophysins.";
RL Int. J. Pept. Protein Res. 30:676-682(1987).
RN [4]
RP PROTEIN SEQUENCE OF 95-132, AND AMIDATION AT GLY-9.
RX PubMed=3081370; DOI=10.1016/0014-5793(86)80320-9;
RA Chauvet M.-T., Chauvet J., Acher R.;
RT "Guinea pig copeptin. The glycopeptide domain of the vasopressin
RT precursor.";
RL FEBS Lett. 197:169-172(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}.
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DR PIR; A29101; A29101.
DR AlphaFoldDB; P10769; -.
DR SMR; P10769; -.
DR STRING; 10141.ENSCPOP00000015497; -.
DR eggNOG; ENOG502S21K; Eukaryota.
DR HOGENOM; CLU_125770_0_0_1; -.
DR InParanoid; P10769; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005185; F:neurohypophyseal hormone activity; IEA:InterPro.
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 Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW Vasoactive; Vasoconstrictor.
FT PEPTIDE 1..9
FT /note="Arg-vasopressin"
FT /id="PRO_0000020512"
FT CHAIN 13..105
FT /note="Neurophysin 2"
FT /id="PRO_0000020513"
FT PEPTIDE 107..144
FT /note="Copeptin"
FT /id="PRO_0000020514"
FT SITE 9
FT /note="Important for agonist activity on V1aR/AVPR1A"
FT /evidence="ECO:0000250|UniProtKB:P01185"
FT MOD_RES 9
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:3081370"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 1..6
FT DISULFID 22..66
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 25..39
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 33..56
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 40..46
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 73..85
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 79..97
FT /evidence="ECO:0000250|UniProtKB:P01175"
FT DISULFID 86..91
FT /evidence="ECO:0000250|UniProtKB:P01175"
SQ SEQUENCE 144 AA; 15068 MW; CE2B18A162C9ABEA CRC64;
CYFQNCPRGG KRALSDTELR QCLPCGPGGQ GRCFGPSICC ADALGCFVGT AEALRCQEEN
YLPSPCQSGQ KPCGSGGRCA ANGVCCNDES CVIEPECREE FHRPVRAGDR SNVTQLDGPA
GALLLRLMQL AGAPEPQPAA PGGY