ID   PACA_PELRI              Reviewed;         171 AA.
AC   Q09169; Q9I8R7; Q9I8R8;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Glucagon family neuropeptides;
DE   Contains:
DE     RecName: Full=Growth hormone-releasing factor;
DE              Short=GRF;
DE     AltName: Full=Growth hormone-releasing hormone;
DE              Short=GHRH;
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   Pelophylax ridibundus (Marsh frog) (Rana ridibunda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX   NCBI_TaxID=8406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10813784;
RX   DOI=10.1002/(sici)1096-9861(20000529)421:2<234::aid-cne8>3.0.co;2-s;
RA   Alexandre D., Vaudry H., Jegou S., Anouar Y.;
RT   "Structure and distribution of the mRNAs encoding pituitary adenylate
RT   cyclase-activating polypeptide and growth hormone-releasing hormone-like
RT   peptide in the frog, Rana ridibunda.";
RL   J. Comp. Neurol. 421:234-246(2000).
RN   [2]
RP   PROTEIN SEQUENCE OF 127-164.
RC   TISSUE=Brain;
RX   PubMed=1720095; DOI=10.1210/endo-129-6-3367;
RA   Chartrel N., Tonon M.-C., Vaudry H., Conlon J.M.;
RT   "Primary structure of frog pituitary adenylate cyclase-activating
RT   polypeptide (PACAP) and effects of ovine PACAP on frog pituitary.";
RL   Endocrinology 129:3367-3371(1991).
CC   -!- FUNCTION: Primary role of GRF is to release GH from the pituitary.
CC   -!- FUNCTION: PACAP plays pivotal roles as a neurotransmitter and/or a
CC       neuromodulator. Stimulates adenylate cyclase in pituitary cells.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q09169-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q09169-2; Sequence=VSP_001761;
CC   -!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
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DR   EMBL; AF221632; AAF74570.1; -; mRNA.
DR   EMBL; AF221633; AAF74571.1; -; mRNA.
DR   PIR; A49165; A49165.
DR   AlphaFoldDB; Q09169; -.
DR   SMR; Q09169; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016521; F:pituitary adenylate cyclase activating polypeptide activity; IEA:InterPro.
DR   GO; GO:0031858; F:pituitary adenylate cyclase-activating polypeptide receptor binding; IEA:InterPro.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0030073; P:insulin secretion; IEA:InterPro.
DR   GO; GO:0032879; P:regulation of localization; IEA:UniProt.
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   Alternative splicing; Amidation; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Hormone; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..76
FT                   /id="PRO_0000011516"
FT   PEPTIDE         79..124
FT                   /note="Growth hormone-releasing factor"
FT                   /id="PRO_0000011517"
FT   PEPTIDE         127..164
FT                   /note="Pituitary adenylate cyclase-activating polypeptide
FT                   38"
FT                   /id="PRO_0000011518"
FT   PEPTIDE         127..153
FT                   /note="Pituitary adenylate cyclase-activating polypeptide
FT                   27"
FT                   /id="PRO_0000011519"
FT   PROPEP          168..171
FT                   /id="PRO_0000011520"
FT   MOD_RES         164
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         78..110
FT                   /note="RHADDLLNKAYRNLLGQLSARKYLHTLMAKHLG -> S (in isoform
FT                   2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001761"
SQ   SEQUENCE   171 AA;  19680 MW;  A9F0E841FA840907 CRC64;
     MYRKALLVWL LVYGIMRCTV HSSPTALKYP ALRLEDEVYD EDGNTLPDFA FDNNPIGIGN
     PASVFDDMYS FYYPAEKRHA DDLLNKAYRN LLGQLSARKY LHTLMAKHLG AVSSSLEDDS
     EPLSKRHSDG IFTDSYSRYR KQMAVKKYLA AVLGKRYKQR IKNKGRRVAY L