ID   VIP_RABIT               Reviewed;          72 AA.
AC   P32649;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=VIP peptides;
DE   Contains:
DE     RecName: Full=Intestinal peptide PHI-27;
DE     AltName: Full=Peptide histidine isoleucinamide 27;
DE   Contains:
DE     RecName: Full=Vasoactive intestinal peptide;
DE              Short=VIP;
DE     AltName: Full=Vasoactive intestinal polypeptide;
DE   Flags: Precursor; Fragment;
GN   Name=VIP;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-27 AND 45-72, AND AMIDATION AT ILE-27 AND ASN-72.
RC   TISSUE=Small intestine;
RX   PubMed=2342988; DOI=10.1016/0196-9781(90)90120-t;
RA   Gossen D., Buscail L., Cauvin A., Gourlet P., de Neef P., Rathe J.,
RA   Robberecht P., Vandermeers-Piret M.C., Vandermeers A., Christophe J.;
RT   "Amino acid sequence of VIP, PHI and secretin from the rabbit small
RT   intestine.";
RL   Peptides 11:123-128(1990).
CC   -!- FUNCTION: VIP causes vasodilation, lowers arterial blood pressure,
CC       stimulates myocardial contractility, increases glycogenolysis and
CC       relaxes the smooth muscle of trachea, stomach and gall bladder.
CC   -!- FUNCTION: PHM-27 is a potent agonist of the calcitonin receptor CALCR,
CC       with similar efficacy as calcitonin (By similarity). PHI also causes
CC       vasodilation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: X's at positions 28 to 44 were included by homology with
CC       the human precursor sequence.
CC   -!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
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DR   PIR; B60415; VRRB.
DR   BMRB; P32649; -.
DR   STRING; 9986.ENSOCUP00000000447; -.
DR   InParanoid; P32649; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:UniProt.
DR   GO; GO:0048255; P:mRNA stabilization; ISS:AgBase.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:UniProt.
DR   GO; GO:0070459; P:prolactin secretion; ISS:AgBase.
DR   GO; GO:0032880; P:regulation of protein localization; IEA:UniProt.
DR   InterPro; IPR015550; Glucagon.
DR   InterPro; IPR000532; Glucagon_GIP_secretin_VIP.
DR   InterPro; IPR015523; VIP.
DR   PANTHER; PTHR11213; PTHR11213; 1.
DR   PANTHER; PTHR11213:SF5; PTHR11213:SF5; 1.
DR   Pfam; PF00123; Hormone_2; 2.
DR   SMART; SM00070; GLUCA; 2.
DR   PROSITE; PS00260; GLUCAGON; 2.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Hormone; Reference proteome; Secreted.
FT   PEPTIDE         1..27
FT                   /note="Intestinal peptide PHI-27"
FT                   /id="PRO_0000011469"
FT   PEPTIDE         45..72
FT                   /note="Vasoactive intestinal peptide"
FT                   /id="PRO_0000011470"
FT   MOD_RES         27
FT                   /note="Isoleucine amide"
FT                   /evidence="ECO:0000269|PubMed:2342988"
FT   MOD_RES         72
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000269|PubMed:2342988"
FT   NON_TER         1
FT   NON_TER         72
SQ   SEQUENCE   72 AA;  8198 MW;  EF03B1F0E5C1CA3A CRC64;
     HADGVFTSDF SRLLGQLSAK KYLESLIXXX XXXXXXXXXX XXXXHSDAVF TDNYTRLRKQ
     MAVKKYLNSI LN