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Pituitary adenylate cyclase-activating polypeptide (PACAP) [Cleaved into: PACAP-related peptide (PRP-48); Pituitary adenylate cyclase-activating polypeptide 27 (PACAP-27) (PACAP27); Pituitary adenylate cyclase-activating polypeptide 38 (PACAP-38) (PACAP38)]

 PACA_HUMAN              Reviewed;         176 AA.
P18509; B2R7N4; Q52LQ0;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 3.
25-OCT-2017, entry version 158.
RecName: Full=Pituitary adenylate cyclase-activating polypeptide;
Short=PACAP;
Contains:
RecName: Full=PACAP-related peptide;
AltName: Full=PRP-48;
Contains:
RecName: Full=Pituitary adenylate cyclase-activating polypeptide 27;
Short=PACAP-27;
Short=PACAP27;
Contains:
RecName: Full=Pituitary adenylate cyclase-activating polypeptide 38;
Short=PACAP-38;
Short=PACAP38;
Flags: Precursor;
Name=ADCYAP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-54.
TISSUE=Testis;
PubMed=1739432; DOI=10.1089/dna.1992.11.21;
Ohkubo S., Kimura C., Ogi K., Okazaki K., Hosoya M., Onda H.,
Miyata A., Arimura A., Fujino M.;
"Primary structure and characterization of the precursor to human
pituitary adenylate cyclase activating polypeptide.";
DNA Cell Biol. 11:21-30(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-54.
PubMed=1730060; DOI=10.1016/0167-4781(92)90488-L;
Hosoya M., Kimura C., Ogi K., Ohkubo S., Miyamoto Y., Kugoh H.,
Shimizu M., Onda H., Oshimura M., Arimura A., Fujino M.;
"Structure of the human pituitary adenylate cyclase activating
polypeptide (PACAP) gene.";
Biochim. Biophys. Acta 1129:199-206(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-54.
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 114-176, AND AMIDATION AT LEU-158 AND
LYS-169.
PubMed=2302217; DOI=10.1016/0006-291X(90)91914-E;
Kimura C., Ohkubo S., Ogi K., Hosoya M., Itoh Y., Onda H., Miyata A.,
Jiang L., Dahl R.R., Stibbs H.H., Arimura A., Fujino M.;
"A novel peptide which stimulates adenylate cyclase: molecular cloning
and characterization of the ovine and human cDNAs.";
Biochem. Biophys. Res. Commun. 166:81-89(1990).
[6]
FUNCTION.
PubMed=23800469; DOI=10.1126/scisignal.2003993;
Emery A.C., Eiden M.V., Mustafa T., Eiden L.E.;
"Rapgef2 Connects GPCR-Mediated cAMP Signals to ERK Activation in
Neuronal and Endocrine Cells.";
Sci. Signal. 6:RA51-RA51(2013).
[7]
STRUCTURE BY NMR OF 132-169.
PubMed=8504103; DOI=10.1021/bi00073a016;
Wray V., Kakoschke C., Nokihara K., Naruse S.;
"Solution structure of pituitary adenylate cyclase activating
polypeptide by nuclear magnetic resonance spectroscopy.";
Biochemistry 32:5832-5841(1993).
[8]
STRUCTURE BY NMR OF 132-158.
PubMed=1483839;
Inooka H., Endo S., Kitada C., Mizuta E., Fujino M.;
"Pituitary adenylate cyclase activating polypeptide (PACAP) with 27
residues. Conformation determined by 1H NMR and CD spectroscopies and
distance geometry in 25% methanol solution.";
Int. J. Pept. Protein Res. 40:456-464(1992).
[9]
STRUCTURE BY NMR OF 132-152, AND FUNCTION.
PubMed=11175907; DOI=10.1038/84159;
Inooka H., Ohtaki T., Kitahara O., Ikegami T., Endo S., Kitada C.,
Ogi K., Onda H., Fujino M., Shirakawa M.;
"Conformation of a peptide ligand bound to its G-protein coupled
receptor.";
Nat. Struct. Biol. 8:161-165(2001).
[10]
STRUCTURE BY NMR OF 137-169 IN COMPLEX WITH ADCYAP1R1, AND MUTAGENESIS
OF VAL-150; LYS-151; LYS-152; TYR-153; VAL-157 AND LEU-158.
PubMed=17470806; DOI=10.1073/pnas.0611397104;
Sun C., Song D., Davis-Taber R.A., Barrett L.W., Scott V.E.,
Richardson P.L., Pereda-Lopez A., Uchic M.E., Solomon L.R., Lake M.R.,
Walter K.A., Hajduk P.J., Olejniczak E.T.;
"Solution structure and mutational analysis of pituitary adenylate
cyclase-activating polypeptide binding to the extracellular domain of
PAC1-RS.";
Proc. Natl. Acad. Sci. U.S.A. 104:7875-7880(2007).
[11]
VARIANT GLY-54.
PubMed=11968092; DOI=10.1002/humu.9034;
Gu H.F.;
"Genetic variation screening and association studies of the adenylate
cyclase activating polypeptide 1 (ADCYAP1) gene in patients with type
2 diabetes.";
Hum. Mutat. 19:572-573(2002).
-!- FUNCTION: Binding to its receptor activates G proteins and
stimulates adenylate cyclase in pituitary cells. Promotes neuron
projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway.
In chromaffin cells, induces long-lasting increase of
intracellular calcium concentrations and neuroendocrine secretion
(By similarity). Involved in the control of glucose homeostasis,
induces insulin secretion by pancreatic beta cells (By
similarity). {ECO:0000250|UniProtKB:O70176,
ECO:0000250|UniProtKB:P13589, ECO:0000269|PubMed:11175907,
ECO:0000269|PubMed:23800469}.
-!- SUBUNIT: Interacts with ADCYAP1R1 (via N-terminal extracellular
domain). {ECO:0000269|PubMed:17470806}.
-!- INTERACTION:
P41586-3:ADCYAP1R1; NbExp=2; IntAct=EBI-8588930, EBI-15635217;
P10909:CLU; NbExp=4; IntAct=EBI-8588930, EBI-1104674;
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; S83513; AAB21470.1; -; mRNA.
EMBL; X60435; CAA42962.1; -; Genomic_DNA.
EMBL; AK313050; BAG35881.1; -; mRNA.
EMBL; BC093837; AAH93837.1; -; mRNA.
EMBL; BC101803; AAI01804.1; -; mRNA.
CCDS; CCDS11825.1; -.
PIR; I84638; I84638.
RefSeq; NP_001093203.1; NM_001099733.1.
RefSeq; NP_001108.2; NM_001117.4.
UniGene; Hs.531719; -.
UniGene; Hs.727476; -.
PDB; 1GEA; NMR; -; A=132-152.
PDB; 2D2P; NMR; -; A=132-169.
PDB; 2JOD; NMR; -; B=137-169.
PDBsum; 1GEA; -.
PDBsum; 2D2P; -.
PDBsum; 2JOD; -.
ProteinModelPortal; P18509; -.
SMR; P18509; -.
BioGrid; 106629; 26.
DIP; DIP-60936N; -.
IntAct; P18509; 4.
MINT; MINT-2801501; -.
STRING; 9606.ENSP00000411658; -.
BindingDB; P18509; -.
ChEMBL; CHEMBL5692; -.
iPTMnet; P18509; -.
PhosphoSitePlus; P18509; -.
BioMuta; ADCYAP1; -.
DMDM; 71159615; -.
PaxDb; P18509; -.
PeptideAtlas; P18509; -.
PRIDE; P18509; -.
DNASU; 116; -.
Ensembl; ENST00000450565; ENSP00000411658; ENSG00000141433.
Ensembl; ENST00000579794; ENSP00000462647; ENSG00000141433.
GeneID; 116; -.
KEGG; hsa:116; -.
UCSC; uc010dkg.4; human.
CTD; 116; -.
DisGeNET; 116; -.
EuPathDB; HostDB:ENSG00000141433.12; -.
GeneCards; ADCYAP1; -.
HGNC; HGNC:241; ADCYAP1.
HPA; HPA065887; -.
MIM; 102980; gene.
neXtProt; NX_P18509; -.
OpenTargets; ENSG00000141433; -.
PharmGKB; PA24564; -.
eggNOG; ENOG410IWIZ; Eukaryota.
eggNOG; ENOG4111FZG; LUCA.
GeneTree; ENSGT00530000063592; -.
HOVERGEN; HBG018069; -.
InParanoid; P18509; -.
KO; K05262; -.
OMA; RYRQRIR; -.
OrthoDB; EOG091G0J1P; -.
PhylomeDB; P18509; -.
TreeFam; TF332804; -.
Reactome; R-HSA-187024; NGF-independant TRKA activation.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-420092; Glucagon-type ligand receptors.
SABIO-RK; P18509; -.
SIGNOR; P18509; -.
EvolutionaryTrace; P18509; -.
GeneWiki; Pituitary_adenylate_cyclase-activating_peptide; -.
GenomeRNAi; 116; -.
PRO; PR:P18509; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000141433; -.
CleanEx; HS_ADCYAP1; -.
Genevisible; P18509; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
GO; GO:0005184; F:neuropeptide hormone activity; IDA:UniProtKB.
GO; GO:0051428; F:peptide hormone receptor binding; IDA:UniProtKB.
GO; GO:0016521; F:pituitary adenylate cyclase activating polypeptide activity; IDA:BHF-UCL.
GO; GO:0031858; F:pituitary adenylate cyclase-activating polypeptide receptor binding; IEA:Ensembl.
GO; GO:0005102; F:receptor binding; IPI:BHF-UCL.
GO; GO:0005057; F:signal transducer activity, downstream of receptor; IEA:Ensembl.
GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc.
GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
GO; GO:0019933; P:cAMP-mediated signaling; IMP:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; TAS:ProtInc.
GO; GO:0001821; P:histamine secretion; IEA:Ensembl.
GO; GO:0030073; P:insulin secretion; ISS:UniProtKB.
GO; GO:0002865; P:negative regulation of acute inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0002878; P:negative regulation of acute inflammatory response to non-antigenic stimulus; IEA:Ensembl.
GO; GO:0045786; P:negative regulation of cell cycle; IEA:Ensembl.
GO; GO:0060253; P:negative regulation of glial cell proliferation; IEA:Ensembl.
GO; GO:0034260; P:negative regulation of GTPase activity; IEA:Ensembl.
GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0043267; P:negative regulation of potassium ion transport; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
GO; GO:0007218; P:neuropeptide signaling pathway; IDA:UniProtKB.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0021983; P:pituitary gland development; IEA:Ensembl.
GO; GO:0010579; P:positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0071651; P:positive regulation of chemokine (C-C motif) ligand 5 production; IDA:CACAO.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0060124; P:positive regulation of growth hormone secretion; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0090274; P:positive regulation of somatostatin secretion; IEA:Ensembl.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; IDA:UniProtKB.
GO; GO:0070445; P:regulation of oligodendrocyte progenitor proliferation; IEA:Ensembl.
GO; GO:0060078; P:regulation of postsynaptic membrane potential; IEA:Ensembl.
GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0042594; P:response to starvation; IEA:Ensembl.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
InterPro; IPR000532; Glucagon_GIP_secretin_VIP.
Pfam; PF00123; Hormone_2; 2.
PRINTS; PR00275; GLUCAGON.
SMART; SM00070; GLUCA; 2.
PROSITE; PS00260; GLUCAGON; 1.
1: Evidence at protein level;
3D-structure; Amidation; Cleavage on pair of basic residues;
Complete proteome; Hormone; Neurogenesis; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 24 {ECO:0000255}.
PROPEP 25 79
/FTId=PRO_0000011486.
PEPTIDE 82 129 PACAP-related peptide.
/FTId=PRO_0000011487.
PEPTIDE 132 169 Pituitary adenylate cyclase-activating
polypeptide 38.
/FTId=PRO_0000011488.
PEPTIDE 132 158 Pituitary adenylate cyclase-activating
polypeptide 27.
/FTId=PRO_0000011489.
PROPEP 173 176
/FTId=PRO_0000011490.
REGION 150 158 Important for receptor binding.
MOD_RES 158 158 Leucine amide.
{ECO:0000269|PubMed:2302217}.
MOD_RES 169 169 Lysine amide.
{ECO:0000269|PubMed:2302217}.
VARIANT 54 54 D -> G (in dbSNP:rs2856966).
{ECO:0000269|PubMed:11968092,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:1730060,
ECO:0000269|PubMed:1739432}.
/FTId=VAR_014597.
MUTAGEN 150 150 V->G: Strongly reduced affinity for
ADCYAP1R1. {ECO:0000269|PubMed:17470806}.
MUTAGEN 151 151 K->E: Strongly reduced affinity for
ADCYAP1R1. {ECO:0000269|PubMed:17470806}.
MUTAGEN 152 152 K->E: Strongly reduced affinity for
ADCYAP1R1. {ECO:0000269|PubMed:17470806}.
MUTAGEN 153 153 Y->A: Strongly reduced affinity for
ADCYAP1R1. {ECO:0000269|PubMed:17470806}.
MUTAGEN 157 157 V->A: Strongly reduced affinity for
ADCYAP1R1. {ECO:0000269|PubMed:17470806}.
MUTAGEN 158 158 L->A: Strongly reduced affinity for
ADCYAP1R1. {ECO:0000269|PubMed:17470806}.
STRAND 135 139 {ECO:0000244|PDB:1GEA}.
HELIX 140 150 {ECO:0000244|PDB:1GEA}.
HELIX 153 160 {ECO:0000244|PDB:2JOD}.
SEQUENCE 176 AA; 18835 MW; 696DD57D2A510E1D CRC64;
MTMCSGARLA LLVYGIIMHS SVYSSPAAAG LRFPGIRPEE EAYGEDGNPL PDFDGSEPPG
AGSPASAPRA AAAWYRPAGR RDVAHGILNE AYRKVLDQLS AGKHLQSLVA RGVGGSLGGG
AGDDAEPLSK RHSDGIFTDS YSRYRKQMAV KKYLAAVLGK RYKQRVKNKG RRIAYL


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