P13589 (PACA_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pituitary adenylate cyclase-activating polypeptide
Short name=PACAP

Cleaved into the following 3 chains:

1. PACAP-related peptide
   Alternative name(s):
   PRP-48
2. Pituitary adenylate cyclase-activating polypeptide 27
   Short name=PACAP-27
   Short name=PACAP27
3. Pituitary adenylate cyclase-activating polypeptide 38
   Short name=PACAP-38
   Short name=PACAP38

Gene names

Name:

Adcyap1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	175 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binding to its receptor activates G proteins and stimulates adenylate cyclase in pituitary cells By similarity.
Subunit structure	Interacts with ADCYAP1R1 (via N-terminal extracellular domain) By similarity.
Subcellular location	Secreted.
Sequence similarities	Belongs to the glucagon family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hormone
PTM	Amidation Cleavage on pair of basic residues
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP metabolic process Inferred from direct assay PubMed 18563302. Source: RGD behavioral fear response Inferred from direct assay PubMed 17641738. Source: RGD cellular response to glucocorticoid stimulus Inferred from expression pattern PubMed 17884294. Source: RGD elevation of cytosolic calcium ion concentration Inferred from direct assay PubMed 18198219. Source: RGD histamine secretion Inferred from direct assay PubMed 17660849. Source: RGD negative regulation of Rho GTPase activity Inferred from direct assay PubMed 15870074. Source: RGD negative regulation of acute inflammatory response to antigenic stimulus Inferred from direct assay PubMed 17698245. Source: RGD negative regulation of acute inflammatory response to non-antigenic stimulus Inferred from direct assay PubMed 20229361. Source: RGD negative regulation of cell cycle Inferred from electronic annotation. Source: Compara negative regulation of glial cell proliferation Inferred from direct assay PubMed 15870074. Source: RGD negative regulation of muscle cell apoptotic process Inferred from direct assay PubMed 16891268. Source: RGD negative regulation of potassium ion transport Inferred from direct assay PubMed 17498241. Source: RGD neuropeptide signaling pathway Non-traceable author statement PubMed 11959368. Source: RGD ovarian follicle development Inferred from direct assay PubMed 20138961. Source: RGD pituitary gland development Inferred from expression pattern PubMed 18160680. Source: RGD positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway Inferred from direct assay PubMed 9603988. Source: BHF-UCL positive regulation of cell proliferation Inferred from direct assay PubMed 15968088. Source: RGD positive regulation of growth hormone secretion Inferred from direct assay PubMed 18198219. Source: RGD positive regulation of interleukin-6 production Inferred from direct assay PubMed 16888221. Source: RGD positive regulation of neuron projection development Inferred from direct assay PubMed 18541665. Source: RGD positive regulation of somatostatin secretion Inferred from direct assay PubMed 17660849. Source: RGD positive regulation of synaptic transmission, glutamatergic Inferred from direct assay PubMed 16483357. Source: RGD positive regulation of vasodilation Inferred from direct assay PubMed 19220306. Source: RGD regulation of G-protein coupled receptor protein signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB regulation of oligodendrocyte progenitor proliferation Inferred from direct assay PubMed 16989910. Source: RGD regulation of postsynaptic membrane potential Inferred from direct assay PubMed 18727050. Source: RGD regulation of protein localization Inferred from direct assay PubMed 9603988. Source: BHF-UCL response to ethanol Inferred from expression pattern PubMed 16820725. Source: RGD response to starvation Inferred from expression pattern PubMed 16888191. Source: RGD sensory perception of pain Inferred from direct assay PubMed 19091468. Source: RGD
Cellular_component	cytosol Traceable author statement. Source: Reactome extracellular space Inferred from direct assay PubMed 17698245. Source: RGD terminal bouton Inferred from direct assay PubMed 9792613. Source: RGD
Molecular_function	peptide hormone receptor binding Inferred from sequence or structural similarity. Source: UniProtKB pituitary adenylate cyclase activating polypeptide activity Inferred from direct assay PubMed 9603988. Source: BHF-UCL pituitary adenylate cyclase-activating polypeptide receptor binding Inferred from direct assay PubMed 8238511. Source: RGD receptor signaling protein activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Propeptide	25 – 78	54			PRO_0000011501
	Peptide	81 – 128	48	PACAP-related peptide		PRO_0000011502
	Peptide	131 – 168	38	Pituitary adenylate cyclase-activating polypeptide 38 Ref.1 Ref.3		PRO_0000011503
	Peptide	131 – 157	27	Pituitary adenylate cyclase-activating polypeptide 27 Ref.1		PRO_0000011504
	Propeptide	172 – 175	4			PRO_0000011505
Regions
	Region	149 – 157	9	Important for receptor binding By similarity
Amino acid modifications
	Modified residue	157	1	Leucine amide
	Modified residue	168	1	Lysine amide
Experimental info
	Sequence conflict	7	1	A → R in CAA56564. Ref.2
	Sequence conflict	26	1	P → L in CAA56564. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P13589 [UniParc]. Last modified March 1, 1992. Version 2. Checksum: 0398946896602B04	FASTA	175	19,557
	10 20 30 40 50 60 MTMCSGARLA LLVYGIIMHN SVSCSPAAGL SFPGIRPEEE AYDQDGNPLQ DFYDWDPPGA 70 80 90 100 110 120 GSPASALRDA YALYYPADRR DVAHEILNEA YRKVLDQLSA RKYLQSMVAR GMGENLAAAA 130 140 150 160 170 VDDRAPLTKR HSDGIFTDSY SRYRKQMAVK KYLAAVLGKR YKQRVKNKGR RIAYL

References

[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M63006 mRNA. Translation: AAA41791.1. X80290 mRNA. Translation: CAA56564.1.
IPI	IPI00202558.
PIR	A37786.
RefSeq	NP_058685.1. NM_016989.2.
UniGene	Rn.202559.
3D structure databases
ProteinModelPortal	P13589.
SMR	P13589. Positions 131-168.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000073432; ENSRNOP00000063920; ENSRNOG00000049882.
GeneID	24166.
KEGG	rno:24166.
Organism-specific databases
CTD	116.
RGD	2037. Adcyap1.
Phylogenomic databases
GeneTree	ENSGT00530000063592.
HOVERGEN	HBG018069.
KO	K05262.
Enzyme and pathway databases
Reactome	REACT_111984. Signal Transduction.
Gene expression databases
Genevestigator	P13589.
Family and domain databases
InterPro	IPR000532. Glucagon_GIP_secretin_VIP. [Graphical view]
Pfam	PF00123. Hormone_2. 2 hits. [Graphical view]
PRINTS	PR00275. GLUCAGON.
SMART	SM00070. GLUCA. 2 hits. [Graphical view]
PROSITE	PS00260. GLUCAGON. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P13589.
NextBio	602473.

Entry information

Entry name

PACA_RAT

Accession

Primary (citable) accession number: P13589

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	March 1, 1992
Last modified:	April 3, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program