VIP_MOUSE
ID VIP_MOUSE Reviewed; 170 AA.
AC P32648; Q9D2Z7; Q9QUN1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=VIP peptides;
DE Contains:
DE RecName: Full=Intestinal peptide PHI-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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=7894056; DOI=10.3109/10425179409039701;
RA Sena M., Bravo D.T., Agoston D., Waschek J.A.;
RT "High conservation of upstream regulatory sequences on the human and mouse
RT vasoactive intestinal peptide (VIP) genes.";
RL DNA Seq. 5:25-29(1994).
RN [5]
RP PROTEIN SEQUENCE OF 119-129 AND 134-152, AND AMIDATION AT ASN-152.
RC TISSUE=Mast cell;
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).
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). PHM 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; AK018599; BAB31301.1; -; mRNA.
DR EMBL; BC089511; AAH89511.1; -; mRNA.
DR EMBL; X74297; CAA52350.1; -; Genomic_DNA.
DR PIR; A60037; A60037.
DR RefSeq; NP_001300898.1; NM_001313969.1.
DR RefSeq; NP_035832.1; NM_011702.3.
DR RefSeq; XP_006512510.1; XM_006512447.1.
DR AlphaFoldDB; P32648; -.
DR BMRB; P32648; -.
DR SMR; P32648; -.
DR BioGRID; 204525; 1.
DR STRING; 10090.ENSMUSP00000019906; -.
DR GlyGen; P32648; 1 site.
DR PhosphoSitePlus; P32648; -.
DR PaxDb; P32648; -.
DR PRIDE; P32648; -.
DR ProteomicsDB; 297885; -.
DR DNASU; 22353; -.
DR GeneID; 22353; -.
DR KEGG; mmu:22353; -.
DR UCSC; uc007egk.1; mouse.
DR CTD; 7432; -.
DR MGI; MGI:98933; Vip.
DR eggNOG; ENOG502QVTA; Eukaryota.
DR InParanoid; P32648; -.
DR OrthoDB; 1343108at2759; -.
DR PhylomeDB; P32648; -.
DR TreeFam; TF332804; -.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-420092; Glucagon-type ligand receptors.
DR BioGRID-ORCS; 22353; 2 hits in 71 CRISPR screens.
DR PRO; PR:P32648; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P32648; protein.
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; ISO:MGI.
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:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
DR GO; GO:0019732; P:antifungal humoral response; ISO:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
DR GO; GO:0048242; P:epinephrine secretion; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0007611; P:learning or memory; ISO:MGI.
DR GO; GO:0048255; P:mRNA stabilization; ISS:AgBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043267; P:negative regulation of potassium ion transport; ISO:MGI.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0032812; P:positive regulation of epinephrine secretion; IBA:GO_Central.
DR GO; GO:0060406; P:positive regulation of penile erection; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0009966; P:regulation of signal transduction; IMP:MGI.
DR GO; GO:0001878; P:response to yeast; ISO:MGI.
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 /evidence="ECO:0000250"
FT PROPEP 22..79
FT /id="PRO_0000011462"
FT PEPTIDE 81..122
FT /note="Intestinal peptide PHI-42"
FT /evidence="ECO:0000250"
FT /id="PRO_0000011463"
FT PEPTIDE 81..107
FT /note="Intestinal peptide PHI-27"
FT /id="PRO_0000011464"
FT PEPTIDE 125..152
FT /note="Vasoactive intestinal peptide"
FT /id="PRO_0000011465"
FT PROPEP 156..170
FT /id="PRO_0000011466"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01283"
FT MOD_RES 107
FT /note="Isoleucine amide"
FT /evidence="ECO:0000250"
FT MOD_RES 152
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:8402943"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 35
FT /note="V -> VS (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="I -> V (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 170 AA; 19049 MW; 0164C831F8F5C73D CRC64;
MEARSKPQFL AFLILFSVLF SQSLAWPLFG PPSVVRLDDR MPFEGAGDPD QVSLKADSDI
LQNPLAENGT PYYDVSRNAR HADGVFTSDY SRLLGQISAK KYLESLIGKR ISSSISEDPV
PIKRHSDAVF TDNYTRLRKQ MAVKKYLNSI LNGKRSSEGD SADFLEELEK
