Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot P18509 (PACA_HUMAN)

Last modified November 25, 2008. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pituitary adenylate cyclase-activating polypeptide
      Short name=PACAP
Cleaved into the following 3 chains:
    1- Recommended name:
            PACAP-related peptide
        Alternative name(s):
            PRP-48
    2- Recommended name:
            Pituitary adenylate cyclase-activating polypeptide 27
                Short name=PACAP-27
                Short name=PACAP27
    3- Recommended name:
            Pituitary adenylate cyclase-activating polypeptide 38
                Short name=PACAP-38
                Short name=PACAP38
Gene names
Name: ADCYAP1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length176 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Stimulates adenylate cyclase in pituitary cells.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glucagon family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 7955
PRO_0000011486
Peptide82 – 12948PACAP-related peptide
PRO_0000011487
Peptide132 – 16938Pituitary adenylate cyclase-activating polypeptide 38
PRO_0000011488
Peptide132 – 15827Pituitary adenylate cyclase-activating polypeptide 27
PRO_0000011489
Propeptide173 – 1764
PRO_0000011490

Amino acid modifications

Modified residue1581Leucine amide
Modified residue1691Lysine amide

Natural variations

Natural variant541D → G: dbSNP rs2856966.
VAR_014597

Secondary structure

.... 176
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18509-1 [UniParc].

Last modified May 10, 2005. Version 3.
Checksum: 696DD57D2A510E1D

FASTA17618,835
        10         20         30         40         50         60 
MTMCSGARLA LLVYGIIMHS SVYSSPAAAG LRFPGIRPEE EAYGEDGNPL PDFDGSEPPG 

        70         80         90        100        110        120 
AGSPASAPRA AAAWYRPAGR RDVAHGILNE AYRKVLDQLS AGKHLQSLVA RGVGGSLGGG 

       130        140        150        160        170 
AGDDAEPLSK RHSDGIFTDS YSRYRKQMAV KKYLAAVLGK RYKQRVKNKG RRIAYL 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure and characterization of the precursor to human pituitary adenylate cyclase activating polypeptide."
Ohkubo S., Kimura C., Ogi K., Okazaki K., Hosoya M., Onda H., Miyata A., Arimura A., Fujino M.
DNA Cell Biol. 11:21-30(1992) [PubMed: 1739432] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-54.
Tissue: Testis.
[2]"Structure of the human pituitary adenylate cyclase activating polypeptide (PACAP) gene."
Hosoya M., Kimura C., Ogi K., Ohkubo S., Miyamoto Y., Kugoh H., Shimizu M., Onda H., Oshimura M., Arimura A., Fujino M.
Biochim. Biophys. Acta 1129:199-206(1992) [PubMed: 1730060] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-54.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"A novel peptide which stimulates adenylate cyclase: molecular cloning and characterization of the ovine and human cDNAs."
Kimura C., Ohkubo S., Ogi K., Hosoya M., Itoh Y., Onda H., Miyata A., Jiang L., Dahl R.R., Stibbs H.H., Arimura A., Fujino M.
Biochem. Biophys. Res. Commun. 166:81-89(1990) [PubMed: 2302217] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 114-176.
[5]"Solution structure of pituitary adenylate cyclase activating polypeptide by nuclear magnetic resonance spectroscopy."
Wray V., Kakoschke C., Nokihara K., Naruse S.
Biochemistry 32:5832-5841(1993) [PubMed: 8504103] [Abstract]
Cited for: STRUCTURE BY NMR OF 132-169.
[6]"Pituitary adenylate cyclase activating polypeptide (PACAP) with 27 residues. Conformation determined by 1H NMR and CD spectroscopies and distance geometry in 25% methanol solution."
Inooka H., Endo S., Kitada C., Mizuta E., Fujino M.
Int. J. Pept. Protein Res. 40:456-464(1992) [PubMed: 1483839] [Abstract]
Cited for: STRUCTURE BY NMR OF 132-158.
[7]"Genetic variation screening and association studies of the adenylate cyclase activating polypeptide 1 (ADCYAP1) gene in patients with type 2 diabetes."
Gu H.F.
Hum. Mutat. 19:572-573(2002) [PubMed: 11968092] [Abstract]
Cited for: VARIANT GLY-54.
+Additional computationally mapped references.

Cross-references

Sequence databases

S83513 mRNA. Translation: AAB21470.1.
X60435 Genomic DNA. Translation: CAA42962.1.
BC093837 mRNA. Translation: AAH93837.1.
BC101803 mRNA. Translation: AAI01804.1.
PIRI84638.
RefSeqNP_001093203.1.
NP_001108.2.
UniGeneHs.531719

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GEANMR-A132-151[»]
2D2PNMR-A132-169[»]
2JODNMR-B137-169[»]
ModBaseSearch...

PTM databases

PhosphoSiteP18509.

Genome annotation databases

EnsemblENSG00000141433. Homo sapiens. [Contig view]
GeneID116.
KEGGhsa:116.

Organism-specific databases

HGNCHGNC:241. ADCYAP1.
MIM102980. gene.
PharmGKBPA24564.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMP18509.
HOVERGENP18509.

Enzyme and pathway databases

ReactomeREACT_11061. Signalling by NGF.

Gene expression databases

ArrayExpressP18509.
CleanExHS_ADCYAP1.
GermOnlineENSG00000141433. Homo sapiens.

Family and domain databases

InterProIPR000532. Glucagon_GIP_secretin_VIP.
[Graphical view]
PfamPF00123. Hormone_2. 2 hits.
[Graphical view]
PRINTSPR00275. GLUCAGON.
SMARTSM00070. GLUCA. 2 hits.
[Graphical view]
PROSITEPS00260. GLUCAGON. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio449.
SOURCESearch...

Entry information

Entry namePACA_HUMAN
AccessionPrimary (citable) accession number: P18509
Secondary accession number(s): Q52LQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 10, 2005
Last modified: November 25, 2008
This is version 76 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents