NEUV_PELLE
ID NEUV_PELLE Reviewed; 141 AA.
AC P11858;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Vasotocin-neurophysin VT;
DE Short=VT;
DE Contains:
DE RecName: Full=Hydrin-2;
DE AltName: Full=Hydrin II;
DE Contains:
DE RecName: Full=Vasotocin;
DE Contains:
DE RecName: Full=Neurophysin VT;
DE Flags: Precursor;
OS Pelophylax lessonae (Pool frog) (Rana lessonae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX NCBI_TaxID=45623;
RN [1]
RP PROTEIN SEQUENCE, AND AMIDATION AT GLY-9.
RX PubMed=3501288; DOI=10.1016/0006-291x(87)90401-3;
RA Michel G., Chauvet J., Chauvet M.-T., Acher R.;
RT "One-step processing of the amphibian vasotocin precursor: structure of a
RT frog (Rana esculenta) 'big' neurophysin.";
RL Biochem. Biophys. Res. Commun. 149:538-544(1987).
RN [2]
RP PROTEIN SEQUENCE OF 13-141.
RX PubMed=3258254; DOI=10.1016/0014-5793(88)80645-8;
RA Chauvet J., Michel G., Chauvet M.-T., Acher R.;
RT "An amphibian two-domain 'big' neurophysin: conformational homology with
RT the mammalian MSEL-neurophysin/copeptin intermediate precursor shown by
RT trypsin-sepharose proteolysis.";
RL FEBS Lett. 230:77-80(1988).
RN [3]
RP PROTEIN SEQUENCE OF 1-10.
RX PubMed=2787509; DOI=10.1073/pnas.86.14.5272;
RA Rouille Y., Michel G., Chauvet M.-T., Chauvet J., Acher R.;
RT "Hydrins, hydroosmotic neurohypophysial peptides: osmoregulatory adaptation
RT in amphibians through vasotocin precursor processing.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5272-5275(1989).
CC -!- FUNCTION: Vasotocin is an antidiuretic hormone.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Seven disulfide bonds are present in neurophysin.
CC -!- SIMILARITY: Belongs to the vasopressin/oxytocin family. {ECO:0000305}.
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DR PIR; A27482; A27482.
DR PIR; A33900; A33900.
DR AlphaFoldDB; P11858; -.
DR SMR; P11858; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005185; F:neurohypophyseal hormone activity; IEA:InterPro.
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; Secreted.
FT PEPTIDE 1..10
FT /note="Hydrin-2"
FT /id="PRO_0000020541"
FT PEPTIDE 1..9
FT /note="Vasotocin"
FT /id="PRO_0000020542"
FT CHAIN 13..141
FT /note="Neurophysin VT"
FT /id="PRO_0000020543"
FT MOD_RES 9
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:3501288"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 1..6
FT /evidence="ECO:0000250|UniProtKB:P01175"
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 141 AA; 15322 MW; 0142C4C7880E954F CRC64;
CYIQNCPRGG KRSYPDTEVR QCIPCGPGNR GNCFGPNICC GEDLGCYIGT PETLRCVEEN
YLPSPCEAGG KPCGAGGRCA APGVCCNDQS CTMDSSCLDE DSERQRVSPD QNMTQMNGSA
SDLLLRLMHM ANRQQQQTKH Y