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P01282 (VIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
VIP peptides

Cleaved into the following 3 chains:

  1. Intestinal peptide PHV-42
    Alternative name(s):
    Peptide histidine valine 42
  2. Intestinal peptide PHM-27
    Alternative name(s):
    Peptide histidine methioninamide 27
  3. Vasoactive intestinal peptide
    Short name=VIP
    Alternative name(s):
    Vasoactive intestinal polypeptide
Gene names
Name:VIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length170 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder. Ref.13

PHM and PHV also cause vasodilation. PHM-27 is a potent agonist of the calcitonin receptor CALCR, with similar efficacy as calcitonin. Ref.13

Subcellular location

Secreted.

Sequence similarities

Belongs to the glucagon family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionHormone
   PTMAmidation
Cleavage on pair of basic residues
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement PubMed 10096039. Source: ProtInc

body fluid secretion

Traceable author statement PubMed 4035357. Source: ProtInc

learning or memory

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of potassium ion transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 9603988. Source: BHF-UCL

positive regulation of cell proliferation

Traceable author statement PubMed 8389448. Source: ProtInc

positive regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of penile erection

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein catabolic process

Inferred from direct assay PubMed 9603988. Source: BHF-UCL

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

regulation of protein localization

Inferred from direct assay PubMed 9603988. Source: BHF-UCL

regulation of sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

regulation of signal transduction

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionhormone activity

Inferred from direct assay PubMed 9603988. Source: BHF-UCL

neuropeptide hormone activity

Traceable author statement PubMed 10096039. Source: ProtInc

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P01282-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P01282-2)

The sequence of this isoform differs from the canonical sequence as follows:
     113-113: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 7959
PRO_0000011457
Peptide81 – 12242Intestinal peptide PHV-42 Ref.11
PRO_0000011458
Peptide81 – 10727Intestinal peptide PHM-27
PRO_0000011459
Peptide125 – 15228Vasoactive intestinal peptide
PRO_0000011460
Propeptide156 – 17015
PRO_0000011461

Amino acid modifications

Modified residue1071Methionine amide
Modified residue1521Asparagine amide

Natural variations

Alternative sequence1131Missing in isoform 2.
VSP_023256

Experimental info

Sequence conflict96 – 972QL → PP in AAA61286. Ref.8
Sequence conflict1161S → L in AAA61288. Ref.4
Sequence conflict1361R → G in AAA61288. Ref.4

Secondary structure

... 170
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 93EC0177F89508FD

FASTA17019,169
        10         20         30         40         50         60 
MDTRNKAQLL VLLTLLSVLF SQTSAWPLYR APSALRLGDR IPFEGANEPD QVSLKEDIDM 

        70         80         90        100        110        120 
LQNALAENDT PYYDVSRNAR HADGVFTSDF SKLLGQLSAK KYLESLMGKR VSSNISEDPV 

       130        140        150        160        170 
PVKRHSDAVF TDNYTRLRKQ MAVKKYLNSI LNGKRSSEGE SPDFPEELEK 

« Hide

Isoform 2 [UniParc].

Checksum: F325BDFEF47132C3
Show »

FASTA16919,082

References

« Hide 'large scale' references
[1]"Human preprovasoactive intestinal polypeptide contains a novel PHI-27-like peptide, PHM-27."
Itoh N., Obata K., Yanaihara N., Okamoto H.
Nature 304:547-549(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structure of the human vasoactive intestinal polypeptide gene."
Tsukada T., Horovitch S.J., Montminy M.R., Mandel G., Goodman R.H.
DNA 4:293-300(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Vasoactive intestinal peptide: expression of the prohormone in bacterial cells."
Delamarter J.F., Buell G.N., Kawashima E., Polak J.M., Bloom S.R.
Peptides 6 Suppl. 1:95-102(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Structure and expression of the gene encoding the vasoactive intestinal peptide precursor."
Linder S., Barkhem T., Norberg A., Persson H., Schalling M., Hoekfelt T., Magnusson G.
Proc. Natl. Acad. Sci. U.S.A. 84:605-609(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Complete nucleotide sequence of human vasoactive intestinal peptide/PHM-27 gene and its inducible promoter."
Yamagami T., Ohsawa K., Nishizawa M., Inoue C., Gotoh E., Yanaihara N., Yamamoto H., Okamoto H.
Ann. N. Y. Acad. Sci. 527:87-102(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Prostate.
[8]"Structure and expression of the vasoactive intestinal peptide (VIP) gene in a human tumor."
Gozes I., Bodener M., Shani Y., Fridkin M.
Peptides 7:1-6(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-170.
[9]"Diarrhoea in vipoma patients associated with cosecretion of a second active peptide (peptide histidine isoleucine) explained by single coding gene."
Bloom S.R., Delamarter J.F., Kawashima E., Christofides N.D., Buell G., Polak J.M.
Lancet 2:1163-1165(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 50-170 (ISOFORM 1).
Tissue: Pancreatic carcinoma.
[10]"Vasoactive intestinal peptide gene: putative mechanism of information storage at the RNA level."
Gozes I., Giladi E., Shani Y.
J. Neurochem. 48:1136-1141(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 78-155.
[11]"Isolation, characterization, and pharmacological actions of peptide histidine valine 42, a novel prepro-vasoactive intestinal peptide-derived peptide."
Yiangou Y., di Marzo V., Spokes R.A., Panico M., Morris H.R., Bloom S.R.
J. Biol. Chem. 262:14010-14013(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 81-122.
[12]"Isolation and characterization of peptides which act on rat platelets, from a pheochromocytoma."
Kitamura K., Kangawa K., Kawamoto M., Ichiki Y., Matsuo H., Eto T.
Biochem. Biophys. Res. Commun. 185:134-141(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 127-152.
Tissue: Pheochromocytoma.
[13]"Discovery of novel peptide/receptor interactions: identification of PHM-27 as a potent agonist of the human calcitonin receptor."
Ma J.N., Currier E.A., Essex A., Feddock M., Spalding T.A., Nash N.R., Brann M.R., Burstein E.S.
Biochem. Pharmacol. 67:1279-1284(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (PHM-27).
[14]"Structural determination of the vasoactive intestinal peptide by two-dimensional H-NMR spectroscopy."
Theriault Y., Boulanger Y., St Pierre S.
Biopolymers 31:459-464(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF VIP.
+Additional computationally mapped references.

Web resources

Wikipedia

Vasoactive intestinal peptide entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L00157 expand/collapse EMBL AC list , L00154, L00155, L00156 Genomic DNA. Translation: AAA61289.1.
M11553 expand/collapse EMBL AC list , M11549, M11550, M11551, M11552 Genomic DNA. Translation: AAA61284.1.
M36634 mRNA. Translation: AAA61287.1.
M14623 expand/collapse EMBL AC list , M14619, M14620, M14621, M14622 Genomic DNA. Translation: AAA61288.1.
M33027 Genomic DNA. Translation: AAA69515.1.
AL133356 Genomic DNA. Translation: CAI21764.1.
AL133356 Genomic DNA. Translation: CAI21765.1.
BC009794 mRNA. Translation: AAH09794.1.
M36610 expand/collapse EMBL AC list , M36606, M36607, M36608, M36609 Genomic DNA. Translation: AAA61286.1.
M54930 mRNA. Translation: AAA63268.1.
M32162, M31645 Genomic DNA. Translation: AAA61285.1.
PIRVRHU. A23296.
RefSeqNP_003372.1. NM_003381.3.
NP_919416.1. NM_194435.2.
UniGeneHs.53973.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RRHNMR-A125-153[»]
2RRINMR-A125-153[»]
ProteinModelPortalP01282.
SMRP01282. Positions 81-111, 125-153.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113273. 3 interactions.
IntActP01282. 6 interactions.
MINTMINT-1473277.
STRING9606.ENSP00000356213.

Chemistry

BindingDBP01282.
ChEMBLCHEMBL5737.

PTM databases

PhosphoSiteP01282.

Polymorphism databases

DMDM138574.

Proteomic databases

PaxDbP01282.
PRIDEP01282.

Protocols and materials databases

DNASU7432.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367243; ENSP00000356212; ENSG00000146469. [P01282-2]
ENST00000367244; ENSP00000356213; ENSG00000146469. [P01282-1]
GeneID7432.
KEGGhsa:7432.
UCSCuc003qpe.4. human. [P01282-1]
uc003qpf.4. human. [P01282-2]

Organism-specific databases

CTD7432.
GeneCardsGC06P153164.
HGNCHGNC:12693. VIP.
HPACAB018649.
HPA017324.
MIM192320. gene.
neXtProtNX_P01282.
PharmGKBPA37312.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44083.
HOGENOMHOG000253943.
HOVERGENHBG018069.
InParanoidP01282.
KOK05264.
OMAFSHTLAW.
OrthoDBEOG7QVM4H.
PhylomeDBP01282.
TreeFamTF332804.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP01282.
CleanExHS_VIP.
GenevestigatorP01282.

Family and domain databases

InterProIPR000532. Glucagon_GIP_secretin_VIP.
IPR015523. VIP.
[Graphical view]
PANTHERPTHR11213:SF2. PTHR11213:SF2. 1 hit.
PfamPF00123. Hormone_2. 2 hits.
[Graphical view]
SMARTSM00070. GLUCA. 2 hits.
[Graphical view]
PROSITEPS00260. GLUCAGON. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01282.
GeneWikiVasoactive_intestinal_peptide.
GenomeRNAi7432.
NextBio29108.
PROP01282.
SOURCESearch...

Entry information

Entry nameVIP_HUMAN
AccessionPrimary (citable) accession number: P01282
Secondary accession number(s): Q5TCY8, Q5TCY9, Q96QK3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM