PACA_SHEEP
ID PACA_SHEEP Reviewed; 176 AA.
AC P16613;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Pituitary adenylate cyclase-activating polypeptide;
DE Short=PACAP;
DE Contains:
DE RecName: Full=PACAP-related peptide;
DE AltName: Full=PRP-48;
DE Contains:
DE RecName: Full=Pituitary adenylate cyclase-activating polypeptide 27;
DE Short=PACAP-27;
DE Short=PACAP27;
DE Contains:
DE RecName: Full=Pituitary adenylate cyclase-activating polypeptide 38;
DE Short=PACAP-38;
DE Short=PACAP38;
DE Flags: Precursor;
GN Name=ADCYAP1;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT LYS-169.
RC TISSUE=Hypothalamus;
RX PubMed=2302217; DOI=10.1016/0006-291x(90)91914-e;
RA Kimura C., Ohkubo S., Ogi K., Hosoya M., Itoh Y., Onda H., Miyata A.,
RA Jiang L., Dahl R.R., Stibbs H.H., Arimura A., Fujino M.;
RT "A novel peptide which stimulates adenylate cyclase: molecular cloning and
RT characterization of the ovine and human cDNAs.";
RL Biochem. Biophys. Res. Commun. 166:81-89(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1739432; DOI=10.1089/dna.1992.11.21;
RA Ohkubo S., Kimura C., Ogi K., Okazaki K., Hosoya M., Onda H., Miyata A.,
RA Arimura A., Fujino M.;
RT "Primary structure and characterization of the precursor to human pituitary
RT adenylate cyclase activating polypeptide.";
RL DNA Cell Biol. 11:21-30(1992).
RN [3]
RP PROTEIN SEQUENCE OF 132-158, AND AMIDATION AT LEU-158.
RX PubMed=2383262; DOI=10.1016/0006-291x(90)92140-u;
RA Miyata A., Jiang L., Dahl R.D., Kitada C., Kubo K., Fujino M., Minamino N.,
RA Arimura A.;
RT "Isolation of a neuropeptide corresponding to the N-terminal 27 residues of
RT the pituitary adenylate cyclase activating polypeptide with 38 residues
RT (PACAP38).";
RL Biochem. Biophys. Res. Commun. 170:643-648(1990).
CC -!- FUNCTION: Binding to its receptor activates G proteins and stimulates
CC adenylate cyclase in pituitary cells (By similarity). Promotes neuron
CC projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway (By
CC similarity). In chromaffin cells, induces long-lasting increase of
CC intracellular calcium concentrations and neuroendocrine secretion (By
CC similarity). Involved in the control of glucose homeostasis, induces
CC insulin secretion by pancreatic beta cells (By similarity).
CC {ECO:0000250|UniProtKB:O70176, ECO:0000250|UniProtKB:P13589,
CC ECO:0000250|UniProtKB:P18509, ECO:0000250|UniProtKB:Q29W19}.
CC -!- SUBUNIT: Interacts with ADCYAP1R1 (via N-terminal extracellular
CC domain). {ECO:0000250|UniProtKB:P18509}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
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DR EMBL; M32216; AAA31575.1; -; mRNA.
DR EMBL; S83511; AAB21469.1; -; mRNA.
DR PIR; A34044; A34044.
DR RefSeq; NP_001009776.1; NM_001009776.1.
DR AlphaFoldDB; P16613; -.
DR BMRB; P16613; -.
DR SMR; P16613; -.
DR Ensembl; ENSOART00020014250; ENSOARP00020011753; ENSOARG00020009231.
DR GeneID; 443337; -.
DR KEGG; oas:443337; -.
DR CTD; 116; -.
DR OrthoDB; 1415722at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005184; F:neuropeptide hormone activity; ISS:UniProtKB.
DR GO; GO:0051428; F:peptide hormone receptor binding; ISS:UniProtKB.
DR GO; GO:0016521; F:pituitary adenylate cyclase activating polypeptide activity; IDA:BHF-UCL.
DR GO; GO:0031858; F:pituitary adenylate cyclase-activating polypeptide receptor binding; IEA:InterPro.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0019933; P:cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0030073; P:insulin secretion; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL.
DR InterPro; IPR015550; Glucagon.
DR InterPro; IPR000532; Glucagon_GIP_secretin_VIP.
DR InterPro; IPR039080; PACAP.
DR PANTHER; PTHR11213; PTHR11213; 1.
DR PANTHER; PTHR11213:SF1; PTHR11213:SF1; 1.
DR Pfam; PF00123; Hormone_2; 2.
DR PRINTS; PR00275; GLUCAGON.
DR SMART; SM00070; GLUCA; 2.
DR PROSITE; PS00260; GLUCAGON; 1.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Hormone; Neurogenesis; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..80
FT /id="PRO_0000011506"
FT PEPTIDE 82..129
FT /note="PACAP-related peptide"
FT /id="PRO_0000011507"
FT PEPTIDE 132..169
FT /note="Pituitary adenylate cyclase-activating polypeptide
FT 38"
FT /id="PRO_0000011508"
FT PEPTIDE 132..158
FT /note="Pituitary adenylate cyclase-activating polypeptide
FT 27"
FT /id="PRO_0000011509"
FT PROPEP 173..176
FT /id="PRO_0000011510"
FT REGION 36..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..158
FT /note="Important for receptor binding"
FT /evidence="ECO:0000250"
FT MOD_RES 158
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:2383262"
FT MOD_RES 169
FT /note="Lysine amide"
FT /evidence="ECO:0000269|PubMed:2302217"
SQ SEQUENCE 176 AA; 19459 MW; FBADC68CA56361C2 CRC64;
MTMCSGARLA LLVYGILMHS SVYGSPAASG LRFPGIRPEN EAYDEDGNPQ QDFYDSEPPG
VGSPASALRD AYALYYPAEE RDVAHGILDK AYRKVLDQLS ARRYLQTLMA KGLGGTPGGG
ADDDSEPLSK RHSDGIFTDS YSRYRKQMAV KKYLAAVLGK RYKQRVKNKG RRIPYL
