PACA_BOVIN
ID PACA_BOVIN Reviewed; 176 AA.
AC Q29W19;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
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; Synonyms=PACAP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovarian follicle;
RA Sayasith K., Sirois J.;
RT "Characterization of pituitary adenylate cyclase activating polypeptide
RT (PACAP).";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=23800469; DOI=10.1126/scisignal.2003993;
RA Emery A.C., Eiden M.V., Mustafa T., Eiden L.E.;
RT "Rapgef2 Connects GPCR-Mediated cAMP Signals to ERK Activation in Neuronal
RT and Endocrine Cells.";
RL Sci. Signal. 6:RA51-RA51(2013).
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:0000269|PubMed:23800469}.
CC -!- SUBUNIT: Interacts with ADCYAP1R1 (via N-terminal extracellular
CC domain). {ECO:0000250|UniProtKB:P18509}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
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DR EMBL; AY924308; AAY16443.1; -; mRNA.
DR RefSeq; NP_001040020.1; NM_001046555.1.
DR AlphaFoldDB; Q29W19; -.
DR STRING; 9913.ENSBTAP00000027516; -.
DR GeneID; 615187; -.
DR KEGG; bta:615187; -.
DR CTD; 116; -.
DR eggNOG; ENOG502QSGB; Eukaryota.
DR InParanoid; Q29W19; -.
DR OrthoDB; 1415722at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005184; F:neuropeptide hormone activity; IDA: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; IMP:UniProtKB.
DR GO; GO:0030073; P:insulin secretion; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA: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; IDA:UniProtKB.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA: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; 1.
DR PRINTS; PR00275; GLUCAGON.
DR SMART; SM00070; GLUCA; 2.
DR PROSITE; PS00260; GLUCAGON; 1.
PE 2: Evidence at transcript level;
KW Amidation; Cleavage on pair of basic residues; Hormone; Neurogenesis;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..80
FT /evidence="ECO:0000250"
FT /id="PRO_0000240602"
FT PEPTIDE 82..129
FT /note="PACAP-related peptide"
FT /id="PRO_0000240603"
FT PEPTIDE 132..169
FT /note="Pituitary adenylate cyclase-activating polypeptide
FT 38"
FT /id="PRO_0000240604"
FT PEPTIDE 132..158
FT /note="Pituitary adenylate cyclase-activating polypeptide
FT 27"
FT /id="PRO_0000240605"
FT PROPEP 173..176
FT /evidence="ECO:0000250"
FT /id="PRO_0000240606"
FT REGION 98..135
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:0000250|UniProtKB:P18509"
FT MOD_RES 169
FT /note="Lysine amide"
FT /evidence="ECO:0000250|UniProtKB:P18509"
SQ SEQUENCE 176 AA; 19464 MW; 3DCC7A03B493EDF7 CRC64;
MTMCSGARLA LLVYGILMHS SVYGSPAASG LRFPGIRPEN EVYDEDGNPQ QDFYDSESLG
VGSPASALRD AYALYYPAEE RDVAHGILNK AYRKVLDQPS ARRSPADAHG QGLGWDPGGS
ADDDSEPLSK RHSDGIFTDS YSRYRKQMAV KKYLAAVLGK RYKQRVKNKG RRIPYL
