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Protein

Pituitary adenylate cyclase-activating polypeptide

Gene

ADCYAP1

Organism
Homo sapiens (Human)
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. Promotes neuron projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway.2 Publications

GO - Molecular functioni

  • neuropeptide hormone activity Source: UniProtKB
  • peptide hormone receptor binding Source: UniProtKB
  • pituitary adenylate cyclase activating polypeptide activity Source: BHF-UCL
  • receptor binding Source: BHF-UCL
  • signal transducer activity, downstream of receptor Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hormone

Keywords - Biological processi

Neurogenesis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000141433-MONOMER.
ReactomeiR-HSA-187024. NGF-independant TRKA activation.
R-HSA-418555. G alpha (s) signalling events.
R-HSA-420092. Glucagon-type ligand receptors.
SABIO-RKP18509.
SIGNORiP18509.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:241. ADCYAP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi150V → G: Strongly reduced affinity for ADCYAP1R1. 1 Publication1
Mutagenesisi151K → E: Strongly reduced affinity for ADCYAP1R1. 1 Publication1
Mutagenesisi152K → E: Strongly reduced affinity for ADCYAP1R1. 1 Publication1
Mutagenesisi153Y → A: Strongly reduced affinity for ADCYAP1R1. 1 Publication1
Mutagenesisi157V → A: Strongly reduced affinity for ADCYAP1R1. 1 Publication1
Mutagenesisi158L → A: Strongly reduced affinity for ADCYAP1R1. 1 Publication1

Organism-specific databases

DisGeNETi116.
OpenTargetsiENSG00000141433.
PharmGKBiPA24564.

Chemistry databases

ChEMBLiCHEMBL5692.

Polymorphism and mutation databases

BioMutaiADCYAP1.
DMDMi71159615.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000001148625 – 79Add BLAST55
PeptideiPRO_000001148782 – 129PACAP-related peptideAdd BLAST48
PeptideiPRO_0000011488132 – 169Pituitary adenylate cyclase-activating polypeptide 38Add BLAST38
PeptideiPRO_0000011489132 – 158Pituitary adenylate cyclase-activating polypeptide 27Add BLAST27
PropeptideiPRO_0000011490173 – 1764

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei158Leucine amide1 Publication1
Modified residuei169Lysine amide1 Publication1

Keywords - PTMi

Amidation, Cleavage on pair of basic residues

Proteomic databases

PaxDbiP18509.
PeptideAtlasiP18509.
PRIDEiP18509.

PTM databases

iPTMnetiP18509.
PhosphoSitePlusiP18509.

Expressioni

Gene expression databases

BgeeiENSG00000141433.
CleanExiHS_ADCYAP1.
GenevisibleiP18509. HS.

Organism-specific databases

HPAiCAB010005.

Interactioni

Subunit structurei

Interacts with ADCYAP1R1 (via N-terminal extracellular domain).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CLUP109094EBI-8588930,EBI-1104674

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi106629. 26 interactors.
DIPiDIP-60936N.
IntActiP18509. 3 interactors.
MINTiMINT-2801501.
STRINGi9606.ENSP00000411658.

Chemistry databases

BindingDBiP18509.

Structurei

Secondary structure

1176
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi135 – 139Combined sources5
Helixi140 – 150Combined sources11
Helixi153 – 160Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GEANMR-A132-152[»]
2D2PNMR-A132-169[»]
2JODNMR-B137-169[»]
ProteinModelPortaliP18509.
SMRiP18509.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18509.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni150 – 158Important for receptor binding9

Sequence similaritiesi

Belongs to the glucagon family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IWIZ. Eukaryota.
ENOG4111FZG. LUCA.
GeneTreeiENSGT00530000063592.
HOVERGENiHBG018069.
InParanoidiP18509.
KOiK05262.
OMAiRYRQRIR.
OrthoDBiEOG091G0J1P.
PhylomeDBiP18509.
TreeFamiTF332804.

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.

P18509-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTMCSGARLA LLVYGIIMHS SVYSSPAAAG LRFPGIRPEE EAYGEDGNPL
60 70 80 90 100
PDFDGSEPPG AGSPASAPRA AAAWYRPAGR RDVAHGILNE AYRKVLDQLS
110 120 130 140 150
AGKHLQSLVA RGVGGSLGGG AGDDAEPLSK RHSDGIFTDS YSRYRKQMAV
160 170
KKYLAAVLGK RYKQRVKNKG RRIAYL
Length:176
Mass (Da):18,835
Last modified:May 10, 2005 - v3
Checksum:i696DD57D2A510E1D
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01459754D → G.4 PublicationsCorresponds to variant rs2856966dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83513 mRNA. Translation: AAB21470.1.
X60435 Genomic DNA. Translation: CAA42962.1.
AK313050 mRNA. Translation: BAG35881.1.
BC093837 mRNA. Translation: AAH93837.1.
BC101803 mRNA. Translation: AAI01804.1.
CCDSiCCDS11825.1.
PIRiI84638.
RefSeqiNP_001093203.1. NM_001099733.1.
NP_001108.2. NM_001117.4.
UniGeneiHs.531719.
Hs.727476.

Genome annotation databases

EnsembliENST00000450565; ENSP00000411658; ENSG00000141433.
ENST00000579794; ENSP00000462647; ENSG00000141433.
GeneIDi116.
KEGGihsa:116.
UCSCiuc010dkg.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83513 mRNA. Translation: AAB21470.1.
X60435 Genomic DNA. Translation: CAA42962.1.
AK313050 mRNA. Translation: BAG35881.1.
BC093837 mRNA. Translation: AAH93837.1.
BC101803 mRNA. Translation: AAI01804.1.
CCDSiCCDS11825.1.
PIRiI84638.
RefSeqiNP_001093203.1. NM_001099733.1.
NP_001108.2. NM_001117.4.
UniGeneiHs.531719.
Hs.727476.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GEANMR-A132-152[»]
2D2PNMR-A132-169[»]
2JODNMR-B137-169[»]
ProteinModelPortaliP18509.
SMRiP18509.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106629. 26 interactors.
DIPiDIP-60936N.
IntActiP18509. 3 interactors.
MINTiMINT-2801501.
STRINGi9606.ENSP00000411658.

Chemistry databases

BindingDBiP18509.
ChEMBLiCHEMBL5692.

PTM databases

iPTMnetiP18509.
PhosphoSitePlusiP18509.

Polymorphism and mutation databases

BioMutaiADCYAP1.
DMDMi71159615.

Proteomic databases

PaxDbiP18509.
PeptideAtlasiP18509.
PRIDEiP18509.

Protocols and materials databases

DNASUi116.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000450565; ENSP00000411658; ENSG00000141433.
ENST00000579794; ENSP00000462647; ENSG00000141433.
GeneIDi116.
KEGGihsa:116.
UCSCiuc010dkg.4. human.

Organism-specific databases

CTDi116.
DisGeNETi116.
GeneCardsiADCYAP1.
HGNCiHGNC:241. ADCYAP1.
HPAiCAB010005.
MIMi102980. gene.
neXtProtiNX_P18509.
OpenTargetsiENSG00000141433.
PharmGKBiPA24564.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IWIZ. Eukaryota.
ENOG4111FZG. LUCA.
GeneTreeiENSGT00530000063592.
HOVERGENiHBG018069.
InParanoidiP18509.
KOiK05262.
OMAiRYRQRIR.
OrthoDBiEOG091G0J1P.
PhylomeDBiP18509.
TreeFamiTF332804.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000141433-MONOMER.
ReactomeiR-HSA-187024. NGF-independant TRKA activation.
R-HSA-418555. G alpha (s) signalling events.
R-HSA-420092. Glucagon-type ligand receptors.
SABIO-RKP18509.
SIGNORiP18509.

Miscellaneous databases

EvolutionaryTraceiP18509.
GeneWikiiPituitary_adenylate_cyclase-activating_peptide.
GenomeRNAii116.
PROiP18509.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000141433.
CleanExiHS_ADCYAP1.
GenevisibleiP18509. HS.

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...

Entry informationi

Entry nameiPACA_HUMAN
AccessioniPrimary (citable) accession number: P18509
Secondary accession number(s): B2R7N4, Q52LQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 10, 2005
Last modified: November 30, 2016
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.