PACR_RAT
ID PACR_RAT Reviewed; 523 AA.
AC P32215; Q63414;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Pituitary adenylate cyclase-activating polypeptide type I receptor;
DE Short=PACAP type I receptor;
DE Short=PACAP-R-1;
DE Short=PACAP-R1;
DE Flags: Precursor;
GN Name=Adcyap1r1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=8392197; DOI=10.1073/pnas.90.13.6345;
RA Wank S.A., Pisegna J.R.;
RT "Molecular cloning and functional expression of the pituitary adenylate
RT cyclase-activating polypeptide type I receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6345-6349(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7687425; DOI=10.1006/bbrc.1993.1795;
RA Hosoya M., Onda H., Ogi K., Masuda Y., Miyamoto Y., Ohtaki T., Okazaki H.,
RA Arimura A., Fujino M.;
RT "Molecular cloning and functional expression of rat cDNAs encoding the
RT receptor for pituitary adenylate cyclase activating polypeptide (PACAP).";
RL Biochem. Biophys. Res. Commun. 194:133-143(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=8394723; DOI=10.1016/0896-6273(93)90188-w;
RA Hashimoto H., Ishihara T., Shigemoto R., Mori K., Nagata S.;
RT "Molecular cloning and tissue distribution of a receptor for pituitary
RT adenylate cyclase-activating polypeptide.";
RL Neuron 11:333-342(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=8396727; DOI=10.1038/365170a0;
RA Spengler D., Waeber C., Pantaloni C., Holsboer F., Bockaert J.,
RA Seeburg P.H., Journot L.;
RT "Differential signal transduction by five splice variants of the PACAP
RT receptor.";
RL Nature 365:170-175(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Olfactory bulb;
RX PubMed=8394834; DOI=10.1016/0014-5793(93)80202-6;
RA Morrow J.A., Lutz E.M., West K.M., Fink G., Harmar A.J.;
RT "Molecular cloning and expression of a cDNA encoding a receptor for
RT pituitary adenylate cyclase activating polypeptide (PACAP).";
RL FEBS Lett. 329:99-105(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 115-523.
RC STRAIN=Wistar;
RA Svoboda M., Ciccarelli E., Tastenoy M., Christophe J.;
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This is a receptor for PACAP-27 and PACAP-38. The activity of
CC this receptor is mediated by G proteins which activate adenylyl
CC cyclase. May regulate the release of adrenocorticotropin, luteinizing
CC hormone, growth hormone, prolactin, epinephrine, and catecholamine. May
CC play a role in spermatogenesis and sperm motility. Causes smooth muscle
CC relaxation and secretion in the gastrointestinal tract.
CC -!- SUBUNIT: Interacts (via N-terminal extracellular domain) with ADCYAP1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=HIP-HOP1;
CC IsoId=P32215-1; Sequence=Displayed;
CC Name=HOP1;
CC IsoId=P32215-2; Sequence=VSP_002005, VSP_002006;
CC Name=HOP2;
CC IsoId=P32215-3; Sequence=VSP_002005, VSP_002007;
CC Name=HIP;
CC IsoId=P32215-4; Sequence=VSP_002008;
CC Name=PACAP-R;
CC IsoId=P32215-5; Sequence=VSP_002009;
CC -!- TISSUE SPECIFICITY: Hypothalamus, anterior pituitary, adrenal medulla,
CC testicular germ cells.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; D16465; BAA03932.1; -; mRNA.
DR EMBL; L16680; AAA41792.1; -; mRNA.
DR EMBL; D14908; BAA03608.1; -; mRNA.
DR EMBL; D14909; BAA03609.1; -; mRNA.
DR EMBL; Z23272; CAA80810.1; -; mRNA.
DR EMBL; Z23273; CAA80811.1; -; mRNA.
DR EMBL; Z23274; CAA80812.1; -; mRNA.
DR EMBL; Z23275; CAA80813.1; -; mRNA.
DR EMBL; Z23279; CAA80817.1; -; mRNA.
DR EMBL; Z23282; CAA80821.1; -; mRNA.
DR EMBL; Z23282; CAA80820.1; -; mRNA.
DR EMBL; L16506; AAA02990.1; -; mRNA.
DR EMBL; Z22735; CAA80429.1; -; mRNA.
DR PIR; JN0616; JN0616.
DR PIR; S33449; S33449.
DR PIR; S36114; S36114.
DR PIR; S39060; S39060.
DR PIR; S39061; S39061.
DR RefSeq; NP_001257508.1; NM_001270579.1. [P32215-1]
DR RefSeq; NP_001257509.1; NM_001270580.1. [P32215-4]
DR RefSeq; NP_001257510.1; NM_001270581.1. [P32215-5]
DR RefSeq; NP_001257511.1; NM_001270582.1. [P32215-5]
DR RefSeq; NP_001257512.1; NM_001270583.1. [P32215-3]
DR RefSeq; NP_598195.1; NM_133511.2. [P32215-2]
DR RefSeq; XP_017447918.1; XM_017592429.1. [P32215-2]
DR RefSeq; XP_017447919.1; XM_017592430.1. [P32215-2]
DR RefSeq; XP_017447920.1; XM_017592431.1. [P32215-5]
DR AlphaFoldDB; P32215; -.
DR SMR; P32215; -.
DR STRING; 10116.ENSRNOP00000016175; -.
DR ChEMBL; CHEMBL1075233; -.
DR GuidetoPHARMACOLOGY; 370; -.
DR GlyGen; P32215; 3 sites.
DR iPTMnet; P32215; -.
DR PhosphoSitePlus; P32215; -.
DR PaxDb; P32215; -.
DR PRIDE; P32215; -.
DR Ensembl; ENSRNOT00000016175; ENSRNOP00000016175; ENSRNOG00000012098. [P32215-1]
DR Ensembl; ENSRNOT00000035722; ENSRNOP00000030759; ENSRNOG00000012098. [P32215-2]
DR Ensembl; ENSRNOT00000043851; ENSRNOP00000044267; ENSRNOG00000012098. [P32215-5]
DR Ensembl; ENSRNOT00000046192; ENSRNOP00000050048; ENSRNOG00000012098. [P32215-4]
DR GeneID; 24167; -.
DR KEGG; rno:24167; -.
DR UCSC; RGD:2038; rat. [P32215-1]
DR CTD; 117; -.
DR RGD; 2038; Adcyap1r1.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000157362; -.
DR HOGENOM; CLU_002753_4_4_1; -.
DR InParanoid; P32215; -.
DR OMA; TMHSDCI; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P32215; -.
DR TreeFam; TF315710; -.
DR Reactome; R-RNO-420092; Glucagon-type ligand receptors. [P32215-4]
DR PRO; PR:P32215; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000012098; Expressed in frontal cortex and 15 other tissues.
DR Genevisible; P32215; RN.
DR GO; GO:0005923; C:bicellular tight junction; IDA:RGD.
DR GO; GO:0005901; C:caveola; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0008179; F:adenylate cyclase binding; IDA:RGD.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0042923; F:neuropeptide binding; IDA:RGD.
DR GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR GO; GO:0001634; F:pituitary adenylate cyclase-activating polypeptide receptor activity; TAS:Reactome.
DR GO; GO:0031267; F:small GTPase binding; IDA:RGD.
DR GO; GO:0004999; F:vasoactive intestinal polypeptide receptor activity; IEA:InterPro.
DR GO; GO:0007202; P:activation of phospholipase C activity; IDA:RGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0019933; P:cAMP-mediated signaling; IDA:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0046545; P:development of primary female sexual characteristics; IEP:RGD.
DR GO; GO:0033555; P:multicellular organismal response to stress; IEP:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IDA:RGD.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IMP:RGD.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:RGD.
DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; IDA:RGD.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR002285; GPCR_2_PACAP_1_rcpt.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR01156; PACAPRECEPTR.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Spermatogenesis; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..523
FT /note="Pituitary adenylate cyclase-activating polypeptide
FT type I receptor"
FT /id="PRO_0000012843"
FT TOPO_DOM 20..154
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..177
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..204
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..226
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..252
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..290
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..308
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..331
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..440
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..460
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 124..138
FT /note="Important for ligand binding and specificity"
FT /evidence="ECO:0000250"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70205"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70205"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..62
FT /evidence="ECO:0000250"
FT DISULFID 53..117
FT /evidence="ECO:0000250"
FT DISULFID 76..133
FT /evidence="ECO:0000250"
FT VAR_SEQ 348
FT /note="L -> F (in isoform HOP1 and isoform HOP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002005"
FT VAR_SEQ 349..404
FT /note="Missing (in isoform PACAP-R)"
FT /evidence="ECO:0000305"
FT /id="VSP_002009"
FT VAR_SEQ 349..377
FT /note="Missing (in isoform HOP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002007"
FT VAR_SEQ 349..376
FT /note="Missing (in isoform HOP1)"
FT /evidence="ECO:0000305"
FT /id="VSP_002006"
FT VAR_SEQ 377..404
FT /note="Missing (in isoform HIP)"
FT /evidence="ECO:0000305"
FT /id="VSP_002008"
FT CONFLICT 449
FT /note="F -> L (in Ref. 1; AAA41792)"
FT /evidence="ECO:0000305"
FT CONFLICT 510..511
FT /note="QL -> HV (in Ref. 6; AAA02990/CAA80429)"
FT /evidence="ECO:0000305"
FT CONFLICT 515..516
FT /note="SL -> TV (in Ref. 6; AAA02990/CAA80429)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 59637 MW; 038CA413EED37E44 CRC64;
MARVLQLSLT ALLLPVAIAM HSDCIFKKEQ AMCLERIQRA NDLMGLNESS PGCPGMWDNI
TCWKPAQVGE MVLVSCPEVF RIFNPDQVWM TETIGDSGFA DSNSLEITDM GVVGRNCTED
GWSEPFPHYF DACGFDDYEP ESGDQDYYYL SVKALYTVGY STSLATLTTA MVILCRFRKL
HCTRNFIHMN LFVSFMLRAI SVFIKDWILY AEQDSSHCFV STVECKAVMV FFHYCVVSNY
FWLFIEGLYL FTLLVETFFP ERRYFYWYTI IGWGTPTVCV TVWAVLRLYF DDAGCWDMND
STALWWVIKG PVVGSIMVNF VLFIGIIIIL VQKLQSPDMG GNESSIYLTN LRLRVPKKTR
EDPLPVPSDQ HSPPFLSCVQ KCYCKPQRAQ QHSCKMSELS TITLRLARST LLLIPLFGIH
YTVFAFSPEN VSKRERLVFE LGLGSFQGFV VAVLYCFLNG EVQAEIKRKW RSWKVNRYFT
MDFKHRHPSL ASSGVNGGTQ LSILSKSSSQ LRMSSLPADN LAT
