Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pituitary adenylate cyclase-activating polypeptide

Gene

Adcyap1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binding to its receptor activates G proteins and stimulates adenylate cyclase in pituitary cells (By similarity). Promotes neuron projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • activation of adenylate cyclase activity Source: Reactome
  • ATP metabolic process Source: RGD
  • behavioral fear response Source: RGD
  • cAMP-mediated signaling Source: UniProtKB
  • cellular response to glucocorticoid stimulus Source: RGD
  • histamine secretion Source: RGD
  • negative regulation of acute inflammatory response to antigenic stimulus Source: RGD
  • negative regulation of acute inflammatory response to non-antigenic stimulus Source: RGD
  • negative regulation of cell cycle Source: Ensembl
  • negative regulation of glial cell proliferation Source: RGD
  • negative regulation of GTPase activity Source: RGD
  • negative regulation of muscle cell apoptotic process Source: RGD
  • negative regulation of potassium ion transport Source: RGD
  • neuron projection development Source: UniProtKB
  • neuropeptide signaling pathway Source: UniProtKB
  • ovarian follicle development Source: RGD
  • pituitary gland development Source: RGD
  • positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway Source: BHF-UCL
  • positive regulation of cAMP biosynthetic process Source: RGD
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of chemokine (C-C motif) ligand 5 production Source: Ensembl
  • positive regulation of cytosolic calcium ion concentration Source: RGD
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of growth hormone secretion Source: RGD
  • positive regulation of GTPase activity Source: UniProtKB
  • positive regulation of interleukin-6 production Source: RGD
  • positive regulation of neuron projection development Source: RGD
  • positive regulation of protein kinase activity Source: UniProtKB
  • positive regulation of somatostatin secretion Source: RGD
  • positive regulation of synaptic transmission, glutamatergic Source: RGD
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of vasodilation Source: RGD
  • regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
  • regulation of oligodendrocyte progenitor proliferation Source: RGD
  • regulation of postsynaptic membrane potential Source: RGD
  • regulation of protein localization Source: BHF-UCL
  • response to ethanol Source: RGD
  • response to starvation Source: RGD
  • sensory perception of pain Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Keywords - Biological processi

Neurogenesis

Enzyme and pathway databases

ReactomeiR-RNO-187024. NGF-independant TRKA activation.
R-RNO-418555. G alpha (s) signalling events.
R-RNO-420092. Glucagon-type ligand receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Pituitary adenylate cyclase-activating polypeptide
Short name:
PACAP
Cleaved into the following 3 chains:
Alternative name(s):
PRP-48
Pituitary adenylate cyclase-activating polypeptide 27
Short name:
PACAP-27
Short name:
PACAP27
Pituitary adenylate cyclase-activating polypeptide 38
Short name:
PACAP-38
Short name:
PACAP38
Gene namesi
Name:Adcyap1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi2037. Adcyap1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular space Source: RGD
  • terminal bouton Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Propeptidei25 – 7854PRO_0000011501Add
BLAST
Peptidei81 – 12848PACAP-related peptidePRO_0000011502Add
BLAST
Peptidei131 – 16838Pituitary adenylate cyclase-activating polypeptide 38PRO_0000011503Add
BLAST
Peptidei131 – 15727Pituitary adenylate cyclase-activating polypeptide 27PRO_0000011504Add
BLAST
Propeptidei172 – 1754PRO_0000011505

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei157 – 1571Leucine amideBy similarity
Modified residuei168 – 1681Lysine amide1 Publication

Keywords - PTMi

Amidation, Cleavage on pair of basic residues

Proteomic databases

PaxDbiP13589.

Expressioni

Gene expression databases

ExpressionAtlasiP13589. baseline and differential.
GenevisibleiP13589. RN.

Interactioni

Subunit structurei

Interacts with ADCYAP1R1 (via N-terminal extracellular domain).By similarity

GO - Molecular functioni

  • neuropeptide hormone activity Source: UniProtKB
  • peptide hormone receptor binding Source: UniProtKB
  • pituitary adenylate cyclase activating polypeptide activity Source: BHF-UCL
  • pituitary adenylate cyclase-activating polypeptide receptor binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000063920.

Chemistry

BindingDBiP13589.

Structurei

3D structure databases

ProteinModelPortaliP13589.
SMRiP13589. Positions 131-168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 1579Important for receptor bindingBy similarity

Sequence similaritiesi

Belongs to the glucagon family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IWIZ. Eukaryota.
ENOG4111FZG. LUCA.
GeneTreeiENSGT00530000063592.
HOVERGENiHBG018069.
InParanoidiP13589.
KOiK05262.
OMAiRYRQRIR.
OrthoDBiEOG7M6D8P.
PhylomeDBiP13589.

Family and domain databases

InterProiIPR000532. Glucagon_GIP_secretin_VIP.
[Graphical view]
PfamiPF00123. Hormone_2. 2 hits.
[Graphical view]
PRINTSiPR00275. GLUCAGON.
SMARTiSM00070. GLUCA. 2 hits.
[Graphical view]
PROSITEiPS00260. GLUCAGON. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13589-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTMCSGARLA LLVYGIIMHN SVSCSPAAGL SFPGIRPEEE AYDQDGNPLQ
60 70 80 90 100
DFYDWDPPGA GSPASALRDA YALYYPADRR DVAHEILNEA YRKVLDQLSA
110 120 130 140 150
RKYLQSMVAR GMGENLAAAA VDDRAPLTKR HSDGIFTDSY SRYRKQMAVK
160 170
KYLAAVLGKR YKQRVKNKGR RIAYL
Length:175
Mass (Da):19,557
Last modified:March 1, 1992 - v2
Checksum:i0398946896602B04
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71A → R in CAA56564 (PubMed:7835287).Curated
Sequence conflicti26 – 261P → L in CAA56564 (PubMed:7835287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63006 mRNA. Translation: AAA41791.1.
X80290 mRNA. Translation: CAA56564.1.
PIRiA37786.
RefSeqiNP_058685.1. NM_016989.2.
XP_006245734.1. XM_006245672.2.
XP_006245735.1. XM_006245673.2.
XP_006245736.1. XM_006245674.2.
XP_008765640.1. XM_008767418.1.
XP_008765641.1. XM_008767419.1.
UniGeneiRn.202559.
Rn.37400.

Genome annotation databases

EnsembliENSRNOT00000087405; ENSRNOP00000070007; ENSRNOG00000049882.
GeneIDi24166.
KEGGirno:24166.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63006 mRNA. Translation: AAA41791.1.
X80290 mRNA. Translation: CAA56564.1.
PIRiA37786.
RefSeqiNP_058685.1. NM_016989.2.
XP_006245734.1. XM_006245672.2.
XP_006245735.1. XM_006245673.2.
XP_006245736.1. XM_006245674.2.
XP_008765640.1. XM_008767418.1.
XP_008765641.1. XM_008767419.1.
UniGeneiRn.202559.
Rn.37400.

3D structure databases

ProteinModelPortaliP13589.
SMRiP13589. Positions 131-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000063920.

Chemistry

BindingDBiP13589.

Proteomic databases

PaxDbiP13589.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000087405; ENSRNOP00000070007; ENSRNOG00000049882.
GeneIDi24166.
KEGGirno:24166.

Organism-specific databases

CTDi116.
RGDi2037. Adcyap1.

Phylogenomic databases

eggNOGiENOG410IWIZ. Eukaryota.
ENOG4111FZG. LUCA.
GeneTreeiENSGT00530000063592.
HOVERGENiHBG018069.
InParanoidiP13589.
KOiK05262.
OMAiRYRQRIR.
OrthoDBiEOG7M6D8P.
PhylomeDBiP13589.

Enzyme and pathway databases

ReactomeiR-RNO-187024. NGF-independant TRKA activation.
R-RNO-418555. G alpha (s) signalling events.
R-RNO-420092. Glucagon-type ligand receptors.

Miscellaneous databases

PROiP13589.

Gene expression databases

ExpressionAtlasiP13589. baseline and differential.
GenevisibleiP13589. RN.

Family and domain databases

InterProiIPR000532. Glucagon_GIP_secretin_VIP.
[Graphical view]
PfamiPF00123. Hormone_2. 2 hits.
[Graphical view]
PRINTSiPR00275. GLUCAGON.
SMARTiSM00070. GLUCA. 2 hits.
[Graphical view]
PROSITEiPS00260. GLUCAGON. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and characterization of cDNA for the precursor of rat pituitary adenylate cyclase activating polypeptide (PACAP)."
    Ogi K., Kimura C., Onda H., Arimura A., Fujino M.
    Biochem. Biophys. Res. Commun. 173:1271-1279(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "Cloning and molecular characterization of complementary deoxyribonucleic acid corresponding to a novel form of pituitary adenylate cyclase-activating polypeptide messenger ribonucleic acid in the rat testis."
    Hurley J.D., Gardiner J.V., Jones P.M., Bloom S.R.
    Endocrinology 136:550-557(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Testis.
  3. "Isolation of a novel 38 residue-hypothalamic polypeptide which stimulates adenylate cyclase in pituitary cells."
    Miyata A., Arimura A., Dahl R.R., Minamino N., Uehara A., Jiang A., Culler M.D., Coy D.H.
    Biochem. Biophys. Res. Commun. 164:567-574(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 131-168, AMIDATION AT LYS-168.
  4. "Rapgef2 Connects GPCR-Mediated cAMP Signals to ERK Activation in Neuronal and Endocrine Cells."
    Emery A.C., Eiden M.V., Mustafa T., Eiden L.E.
    Sci. Signal. 6:RA51-RA51(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiPACA_RAT
AccessioniPrimary (citable) accession number: P13589
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: March 1, 1992
Last modified: June 8, 2016
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.