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