VIP_CAVPO
ID VIP_CAVPO Reviewed; 72 AA.
AC P04566;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 03-AUG-2022, entry version 76.
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 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 OF 1-27 AND 45-72, AND AMIDATION AT ILE-27 AND ASN-72.
RX PubMed=2340294; DOI=10.1016/0167-4838(90)90248-e;
RA Buscail L., Cauvin A., Gourlet P., Gossen D., de Neef P., Rathe J.,
RA Robberecht P., Vandermeers-Piret M.-C., Vandermeers A., Christophe J.;
RT "Purification and amino acid sequence of vasoactive intestinal peptide,
RT peptide histidine isoleucinamide (1-27) and secretin from the small
RT intestine of guinea pig.";
RL Biochim. Biophys. Acta 1038:355-359(1990).
RN [2]
RP PROTEIN SEQUENCE OF 45-72.
RX PubMed=3748846; DOI=10.1016/0196-9781(86)90158-0;
RA Eng J., Du B.-H., Raufman J.-P., Yalow R.S.;
RT "Purification and amino acid sequences of dog, goat and guinea pig VIPs.";
RL Peptides 7 Suppl. 1:17-20(1986).
RN [3]
RP PROTEIN SEQUENCE OF 45-72, AND AMIDATION AT ASN-72.
RX PubMed=4004849; DOI=10.1016/0006-291x(85)91052-6;
RA Du B.-H., Eng J., Hulmes J.D., Chang M., Pan Y.-C.E., Yalow R.S.;
RT "Guinea pig has a unique mammalian VIP.";
RL Biochem. Biophys. Res. Commun. 128:1093-1098(1985).
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: PHI also causes vasodilation.
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; A26175; VRGP.
DR STRING; 10141.ENSCPOP00000002714; -.
DR BindingDB; P04566; -.
DR InParanoid; P04566; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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:0045732; P:positive regulation of protein catabolic process; IEA:UniProt.
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 PRINTS; PR00275; GLUCAGON.
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_0000011455"
FT PEPTIDE 45..72
FT /note="Vasoactive intestinal peptide"
FT /id="PRO_0000011456"
FT MOD_RES 27
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:2340294"
FT MOD_RES 72
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:2340294,
FT ECO:0000269|PubMed:4004849"
FT NON_TER 1
FT NON_TER 72
SQ SEQUENCE 72 AA; 8261 MW; D7B696E02C3C63FD CRC64;
HADGVFTSDY SRLLGQLSAR KYLESLIXXX XXXXXXXXXX XXXXHSDALF TDTYTRLRKQ
MAMKKYLNSV LN