VIP_RAT
ID VIP_RAT Reviewed; 170 AA.
AC P01283; Q9QUN1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=VIP peptides;
DE Contains:
DE RecName: Full=Intestinal peptide PHV-42;
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2159586; DOI=10.1016/0169-328x(90)90036-d;
RA Giladi E., Shani Y., Gozes I.;
RT "The complete structure of the rat VIP gene.";
RL Brain Res. Mol. Brain Res. 7:261-267(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-170, AND AMIDATION AT ILE-107 AND ASN-152.
RC TISSUE=Brain cortex;
RX PubMed=3838518; DOI=10.1016/0014-5793(85)80953-4;
RA Nishizawa M., Hayakawa Y., Yanaihara N., Okamoto H.;
RT "Nucleotide sequence divergence and functional constraint in VIP precursor
RT mRNA evolution between human and rat.";
RL FEBS Lett. 183:55-59(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 78-155.
RX PubMed=1851524; DOI=10.1016/0169-328x(91)90005-i;
RA Lamperti E.D., Rosen K.M., Villa-Komaroff L.;
RT "Characterization of the gene and messages for vasoactive intestinal
RT polypeptide (VIP) in rat and mouse.";
RL Brain Res. Mol. Brain Res. 9:217-231(1991).
RN [4]
RP PROTEIN SEQUENCE OF 134-152, AND AMIDATION AT ASN-152.
RX PubMed=3379062; DOI=10.1016/s0021-9258(19)76511-9;
RA Goetzl E.J., Sreedharan S.P., Turck C.W.;
RT "Structurally distinctive vasoactive intestinal peptides from rat
RT basophilic leukemia cells.";
RL J. Biol. Chem. 263:9083-9086(1988).
RN [5]
RP PROTEIN SEQUENCE OF 134-152.
RX PubMed=8402943; DOI=10.1006/cimm.1993.1246;
RA Wershil B.K., Turck C.W., Sreedharan S.P., Yang J., An S., Galli S.J.,
RA Goetzl E.J.;
RT "Variants of vasoactive intestinal peptide in mouse mast cells and rat
RT basophilic leukemia cells.";
RL Cell. Immunol. 151:369-378(1993).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
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DR EMBL; X02341; CAA26200.1; -; mRNA.
DR PIR; A60053; VRRT.
DR RefSeq; NP_446443.1; NM_053991.1.
DR AlphaFoldDB; P01283; -.
DR BMRB; P01283; -.
DR SMR; P01283; -.
DR STRING; 10116.ENSRNOP00000025477; -.
DR BindingDB; P01283; -.
DR GlyGen; P01283; 1 site.
DR iPTMnet; P01283; -.
DR PhosphoSitePlus; P01283; -.
DR PaxDb; P01283; -.
DR ABCD; P01283; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000025477; ENSRNOP00000025477; ENSRNOG00000018808.
DR GeneID; 117064; -.
DR KEGG; rno:117064; -.
DR UCSC; RGD:621647; rat.
DR CTD; 7432; -.
DR RGD; 621647; Vip.
DR eggNOG; ENOG502QVTA; Eukaryota.
DR GeneTree; ENSGT00950000183154; -.
DR HOGENOM; CLU_133877_1_0_1; -.
DR InParanoid; P01283; -.
DR OMA; MDRNTRH; -.
DR OrthoDB; 1343108at2759; -.
DR PhylomeDB; P01283; -.
DR Reactome; R-RNO-420092; Glucagon-type ligand receptors.
DR PRO; PR:P01283; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018808; Expressed in jejunum and 8 other tissues.
DR ExpressionAtlas; P01283; baseline and differential.
DR Genevisible; P01283; RN.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0048255; P:mRNA stabilization; ISS:AgBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0043267; P:negative regulation of potassium ion transport; IDA:RGD.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:RGD.
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; IDA:RGD.
DR GO; GO:0032812; P:positive regulation of epinephrine secretion; IBA:GO_Central.
DR GO; GO:0060406; P:positive regulation of penile erection; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0009966; P:regulation of signal transduction; ISO:RGD.
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 Glycoprotein; Hormone; Phosphoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT PROPEP 22..79
FT /id="PRO_0000011471"
FT PEPTIDE 81..122
FT /note="Intestinal peptide PHV-42"
FT /evidence="ECO:0000250"
FT /id="PRO_0000011472"
FT PEPTIDE 81..107
FT /note="Intestinal peptide PHI-27"
FT /id="PRO_0000011473"
FT PEPTIDE 125..152
FT /note="Vasoactive intestinal peptide"
FT /id="PRO_0000011474"
FT PROPEP 156..170
FT /id="PRO_0000011475"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 107
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:3838518"
FT MOD_RES 152
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:3379062,
FT ECO:0000269|PubMed:3838518"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 170 AA; 19079 MW; 202AEE82EBBD190B CRC64;
MESRSKPQFL AILTLFSVLF SQSLAWPLYG PPSSVRLDDR LQFEGAGDPD QVSLKADSDI
LQNALAENDT PYYDVSRNAR HADGVFTSDY SRLLGQISAK KYLESLIGKR ISSSISEDPV
PVKRHSDAVF TDNYTRLRKQ MAVKKYLNSI LNGKRSSEGD SPDFLEELEK
