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PACA_HELSU
ID   PACA_HELSU              Reviewed;          56 AA.
AC   P0DJ95;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 18.
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: Fragments;
GN   Name=Adcyap1;
OS   Heloderma suspectum (Gila monster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Anguimorpha; Neoanguimorpha; Helodermatidae; Heloderma.
OX   NCBI_TaxID=8554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=9545315; DOI=10.1074/jbc.273.16.9778;
RA   Pohl M., Wank S.A.;
RT   "Molecular cloning of the helodermin and exendin-4 cDNAs in the lizard.
RT   Relationship to vasoactive intestinal polypeptide/pituitary adenylate
RT   cyclase activating polypeptide and glucagon-like peptide 1 and evidence
RT   against the existence of mammalian homologues.";
RL   J. Biol. Chem. 273:9778-9784(1998).
CC   -!- FUNCTION: Binding to its receptor activates G proteins and stimulates
CC       adenylate cyclase in pituitary cells (By similarity). Promotes neuron
CC       projection development (By similarity). {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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
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DR   AlphaFoldDB; P0DJ95; -.
DR   BMRB; P0DJ95; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0030073; P:insulin secretion; ISS:UniProtKB.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; 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   InterPro; IPR015550; Glucagon.
DR   InterPro; IPR000532; Glucagon_GIP_secretin_VIP.
DR   PANTHER; PTHR11213; PTHR11213; 1.
DR   Pfam; PF00123; Hormone_2; 2.
DR   PRINTS; PR00275; GLUCAGON.
DR   SMART; SM00070; GLUCA; 2.
DR   PROSITE; PS00260; GLUCAGON; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Hormone; Secreted.
FT   PEPTIDE         <1..>23
FT                   /note="PACAP-related peptide"
FT                   /id="PRO_0000414103"
FT   PEPTIDE         24..>56
FT                   /note="Pituitary adenylate cyclase-activating polypeptide
FT                   38"
FT                   /id="PRO_0000414104"
FT   PEPTIDE         24..50
FT                   /note="Pituitary adenylate cyclase-activating polypeptide
FT                   27"
FT                   /id="PRO_0000414105"
FT   REGION          42..50
FT                   /note="Important for receptor binding"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         50
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000250"
FT   NON_CONS        23..24
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         56
SQ   SEQUENCE   56 AA;  6629 MW;  7CBF023B9FD60344 CRC64;
     IFNKAYRKVL GQLSARKYLH SLMHSDGIFT DSYSRYRKQM AVKKYLAAVL GKRYKQ
 
 
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