VIP_BOVIN
ID VIP_BOVIN Reviewed; 170 AA.
AC P81401; Q0VC69; Q8MI77;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
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;
GN Name=VIP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12097482; DOI=10.1523/jneurosci.22-13-05310.2002;
RA Hamelink C., Lee H.-W., Chen Y., Grimaldi M., Eiden L.E.;
RT "Coincident elevation of cAMP and calcium influx by PACAP-27
RT synergistically regulates vasoactive intestinal polypeptide gene
RT transcription through a novel PKA-independent signaling pathway.";
RL J. Neurosci. 22:5310-5320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 81-107, AND AMIDATION AT ILE-107.
RC TISSUE=Duodenum;
RX PubMed=6548446; DOI=10.1111/j.1432-1033.1984.tb08456.x;
RA Carlquist M., Kaiser R., Tatemoto K., Joernvall H., Mutt V.;
RT "A novel form of the polypeptide PHI isolated in high yield from bovine
RT upper intestine. Relationships to other peptides of the glucagon-secretin
RT family.";
RL Eur. J. Biochem. 144:243-247(1984).
RN [4]
RP PROTEIN SEQUENCE OF 125-152, AND AMIDATION AT ASN-152.
RC TISSUE=Intestine;
RX PubMed=520589; DOI=10.1016/0014-5793(79)80587-6;
RA Carlquist M., Mutt V., Joernvall H.;
RT "Isolation and characterization of bovine vasoactive intestinal peptide
RT (VIP).";
RL FEBS Lett. 108:457-460(1979).
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 EMBL; AF503910; AAM28152.1; -; mRNA.
DR EMBL; BC120324; AAI20325.1; -; mRNA.
DR RefSeq; NP_776395.1; NM_173970.3.
DR AlphaFoldDB; P81401; -.
DR SMR; P81401; -.
DR STRING; 9913.ENSBTAP00000017827; -.
DR PaxDb; P81401; -.
DR Ensembl; ENSBTAT00000017827; ENSBTAP00000017827; ENSBTAG00000013400.
DR GeneID; 280956; -.
DR KEGG; bta:280956; -.
DR CTD; 7432; -.
DR VEuPathDB; HostDB:ENSBTAG00000013400; -.
DR VGNC; VGNC:36797; VIP.
DR eggNOG; ENOG502QVTA; Eukaryota.
DR GeneTree; ENSGT00950000183154; -.
DR HOGENOM; CLU_133877_1_0_1; -.
DR InParanoid; P81401; -.
DR OMA; MDRNTRH; -.
DR OrthoDB; 1343108at2759; -.
DR TreeFam; TF332804; -.
DR Reactome; R-BTA-420092; Glucagon-type ligand receptors.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000013400; Expressed in caecum and 40 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IDA:BHF-UCL.
DR GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central.
DR GO; GO:0051428; F:peptide hormone receptor binding; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0048242; P:epinephrine secretion; IBA:GO_Central.
DR GO; GO:0007611; P:learning or memory; IBA:GO_Central.
DR GO; GO:0048255; P:mRNA stabilization; ISS:AgBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0043267; P:negative regulation of potassium ion transport; IBA:GO_Central.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IBA:GO_Central.
DR GO; GO:0032812; P:positive regulation of epinephrine secretion; IBA:GO_Central.
DR GO; GO:0060406; P:positive regulation of penile erection; IBA:GO_Central.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:BHF-UCL.
DR GO; GO:0070459; P:prolactin secretion; ISS:AgBase.
DR GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IBA:GO_Central.
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; Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..79
FT /id="PRO_0000011450"
FT PEPTIDE 81..107
FT /note="Intestinal peptide PHI-27"
FT /id="PRO_0000011451"
FT PROPEP 111..122
FT /id="PRO_0000011452"
FT PEPTIDE 125..152
FT /note="Vasoactive intestinal peptide"
FT /id="PRO_0000011453"
FT PROPEP 156..170
FT /id="PRO_0000011454"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01283"
FT MOD_RES 107
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:6548446"
FT MOD_RES 152
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:520589"
SQ SEQUENCE 170 AA; 19165 MW; 9C6A6049AF7BFF81 CRC64;
METRSKPQLL VFLTLFSVLF SQTLAWPLFG APSALRMGDR IPFEGANEPD QVSLKADTDI
LQDALAENDT PYYDVSRNVR HADGVFTSDY SRLLGQLSAK KYLESLIGKR VSNSISEDQG
PIKRHSDAVF TDNYTRLRKQ MAVKKYLNSI LNGKRSSEGE SPDFLEELEK