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VIP peptides [Cleaved into: Intestinal peptide PHI-42; Intestinal peptide PHI-27 (Peptide histidine isoleucinamide 27); Vasoactive intestinal peptide (VIP) (Vasoactive intestinal polypeptide)]

 VIP_MOUSE               Reviewed;         170 AA.
P32648; Q9D2Z7; Q9QUN1;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
25-OCT-2017, entry version 128.
RecName: Full=VIP peptides;
Contains:
RecName: Full=Intestinal peptide PHI-42;
Contains:
RecName: Full=Intestinal peptide PHI-27;
AltName: Full=Peptide histidine isoleucinamide 27;
Contains:
RecName: Full=Vasoactive intestinal peptide;
Short=VIP;
AltName: Full=Vasoactive intestinal polypeptide;
Flags: Precursor;
Name=Vip;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1851524; DOI=10.1016/0169-328X(91)90005-I;
Lamperti E.D., Rosen K.M., Villa-Komaroff L.;
"Characterization of the gene and messages for vasoactive intestinal
polypeptide (VIP) in rat and mouse.";
Brain Res. Mol. Brain Res. 9:217-231(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cecum;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
STRAIN=C57BL/6J; TISSUE=Spleen;
PubMed=7894056; DOI=10.3109/10425179409039701;
Sena M., Bravo D.T., Agoston D., Waschek J.A.;
"High conservation of upstream regulatory sequences on the human and
mouse vasoactive intestinal peptide (VIP) genes.";
DNA Seq. 5:25-29(1994).
[5]
PROTEIN SEQUENCE OF 119-129 AND 134-152, AND AMIDATION AT ASN-152.
TISSUE=Mast cell;
PubMed=8402943; DOI=10.1006/cimm.1993.1246;
Wershil B.K., Turck C.W., Sreedharan S.P., Yang J., An S., Galli S.J.,
Goetzl E.J.;
"Variants of vasoactive intestinal peptide in mouse mast cells and rat
basophilic leukemia cells.";
Cell. Immunol. 151:369-378(1993).
-!- FUNCTION: VIP causes vasodilation, lowers arterial blood pressure,
stimulates myocardial contractility, increases glycogenolysis and
relaxes the smooth muscle of trachea, stomach and gall bladder.
-!- FUNCTION: PHM-27 is a potent agonist of the calcitonin receptor
CALCR, with similar efficacy as calcitonin (By similarity). PHM
also causes vasodilation. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
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EMBL; AK018599; BAB31301.1; -; mRNA.
EMBL; BC089511; AAH89511.1; -; mRNA.
EMBL; X74297; CAA52350.1; -; Genomic_DNA.
PIR; A60037; A60037.
RefSeq; NP_001300898.1; NM_001313969.1.
RefSeq; NP_035832.1; NM_011702.3.
RefSeq; XP_006512510.1; XM_006512447.1.
UniGene; Mm.98916; -.
ProteinModelPortal; P32648; -.
SMR; P32648; -.
STRING; 10090.ENSMUSP00000019906; -.
PhosphoSitePlus; P32648; -.
PaxDb; P32648; -.
PRIDE; P32648; -.
GeneID; 22353; -.
KEGG; mmu:22353; -.
UCSC; uc007egk.1; mouse.
CTD; 7432; -.
MGI; MGI:98933; Vip.
eggNOG; ENOG410IW68; Eukaryota.
eggNOG; ENOG4111JKK; LUCA.
HOGENOM; HOG000253943; -.
HOVERGEN; HBG018069; -.
InParanoid; P32648; -.
KO; K05264; -.
PhylomeDB; P32648; -.
TreeFam; TF332804; -.
PRO; PR:P32648; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_VIP; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005179; F:hormone activity; IDA:BHF-UCL.
GO; GO:0048255; P:mRNA stabilization; ISS:AgBase.
GO; GO:0010579; P:positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:BHF-UCL.
GO; GO:0070459; P:prolactin secretion; ISS:AgBase.
GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL.
GO; GO:0009966; P:regulation of signal transduction; IMP:MGI.
InterPro; IPR000532; Glucagon_GIP_secretin_VIP.
InterPro; IPR015523; VIP.
PANTHER; PTHR11213:SF5; PTHR11213:SF5; 1.
Pfam; PF00123; Hormone_2; 2.
SMART; SM00070; GLUCA; 2.
PROSITE; PS00260; GLUCAGON; 2.
1: Evidence at protein level;
Amidation; Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Glycoprotein; Hormone; Phosphoprotein;
Reference proteome; Secreted; Signal.
SIGNAL 1 21 {ECO:0000250}.
PROPEP 22 79
/FTId=PRO_0000011462.
PEPTIDE 81 122 Intestinal peptide PHI-42. {ECO:0000250}.
/FTId=PRO_0000011463.
PEPTIDE 81 107 Intestinal peptide PHI-27.
/FTId=PRO_0000011464.
PEPTIDE 125 152 Vasoactive intestinal peptide.
/FTId=PRO_0000011465.
PROPEP 156 170
/FTId=PRO_0000011466.
MOD_RES 76 76 Phosphoserine.
{ECO:0000250|UniProtKB:P01283}.
MOD_RES 107 107 Isoleucine amide. {ECO:0000250}.
MOD_RES 152 152 Asparagine amide.
{ECO:0000269|PubMed:8402943}.
CARBOHYD 133 133 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 35 35 V -> VS (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 122 122 I -> V (in Ref. 5; AA sequence).
{ECO:0000305}.
SEQUENCE 170 AA; 19049 MW; 0164C831F8F5C73D CRC64;
MEARSKPQFL AFLILFSVLF SQSLAWPLFG PPSVVRLDDR MPFEGAGDPD QVSLKADSDI
LQNPLAENGT PYYDVSRNAR HADGVFTSDY SRLLGQISAK KYLESLIGKR ISSSISEDPV
PIKRHSDAVF TDNYTRLRKQ MAVKKYLNSI LNGKRSSEGD SADFLEELEK


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