PACR_MOUSE
ID PACR_MOUSE Reviewed; 496 AA.
AC P70205;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8664310; DOI=10.1016/0005-2736(96)00056-9;
RA Hashimoto H., Yamamoto K., Hagigara N., Ogawa N., Nishino A., Aino H.,
RA Nogi H., Imanishi K., Matsuda T., Baba A.;
RT "cDNA cloning of a mouse pituitary adenylate cyclase-activating polypeptide
RT receptor.";
RL Biochim. Biophys. Acta 1281:129-133(1996).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462 AND SER-475, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; D82935; BAA11639.1; -; mRNA.
DR CCDS; CCDS20167.1; -.
DR RefSeq; NP_031433.3; NM_007407.4.
DR AlphaFoldDB; P70205; -.
DR SMR; P70205; -.
DR IntAct; P70205; 1.
DR MINT; P70205; -.
DR STRING; 10090.ENSMUSP00000063784; -.
DR GlyGen; P70205; 3 sites.
DR iPTMnet; P70205; -.
DR PhosphoSitePlus; P70205; -.
DR SwissPalm; P70205; -.
DR MaxQB; P70205; -.
DR PaxDb; P70205; -.
DR PRIDE; P70205; -.
DR ProteomicsDB; 294242; -.
DR Antibodypedia; 4280; 293 antibodies from 32 providers.
DR DNASU; 11517; -.
DR Ensembl; ENSMUST00000070736; ENSMUSP00000063784; ENSMUSG00000029778.
DR GeneID; 11517; -.
DR KEGG; mmu:11517; -.
DR UCSC; uc009cat.2; mouse.
DR CTD; 117; -.
DR MGI; MGI:108449; Adcyap1r1.
DR VEuPathDB; HostDB:ENSMUSG00000029778; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000157362; -.
DR InParanoid; P70205; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P70205; -.
DR TreeFam; TF315710; -.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-420092; Glucagon-type ligand receptors.
DR BioGRID-ORCS; 11517; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Adcyap1r1; mouse.
DR PRO; PR:P70205; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P70205; protein.
DR Bgee; ENSMUSG00000029778; Expressed in paraventricular nucleus of hypothalamus and 178 other tissues.
DR ExpressionAtlas; P70205; baseline and differential.
DR Genevisible; P70205; MM.
DR GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0008179; F:adenylate cyclase binding; ISO:MGI.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:MGI.
DR GO; GO:0042923; F:neuropeptide binding; ISO:MGI.
DR GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0004999; F:vasoactive intestinal polypeptide receptor activity; TAS:MGI.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISO:MGI.
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; ISO:MGI.
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:0007186; P:G protein-coupled receptor signaling pathway; TAS:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISO:MGI.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:MGI.
DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; ISO:MGI.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; ISO:MGI.
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 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Differentiation; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Spermatogenesis; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..496
FT /note="Pituitary adenylate cyclase-activating polypeptide
FT type I receptor"
FT /id="PRO_0000012842"
FT TOPO_DOM 21..155
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..178
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..205
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..253
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..291
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..309
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..332
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..413
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..433
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 125..139
FT /note="Important for ligand binding and specificity"
FT /evidence="ECO:0000250"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..63
FT /evidence="ECO:0000250"
FT DISULFID 54..118
FT /evidence="ECO:0000250"
FT DISULFID 77..134
FT /evidence="ECO:0000250"
SQ SEQUENCE 496 AA; 56640 MW; 47B5D51D4209060A CRC64;
MARTLQLSLT ALLLLPMAIA MHSDCIFKKE QAMCLERIQR ANDLMGLNES SPGCPGMWDN
ITCWKPAQIG EMVLVSCPEV FRIFNPDQVW MTETIGDSGF ADSNSLEITD MGVVGRNCTE
DGWSEPFPHY FDACGFDDYE PESGDQDYYY LSVKALYTVG YSTSLVTLTT AMVILCRFRK
LHCTRNFIHM NLFVSFMLRA ISVFIKDWIL YAEQDSSHCF VSTVECKAVM VFFHYCVVSN
YFWLFIEGLY LFTLLVETFF PERRYFYWYT IIGWGTPTVC VTVWAVLRLY FDDAGCWDMN
DSTALWWVIK GPVVGSIMVN FVLFIGIIII LVQKLQSPDM GGNESSIYFS CVQKCYCKPQ
RAQQHSCKMS ELSTITLRLA RSTLLLIPLF GIHYTVFAFS PENVSKRERL VFELGLGSFQ
GFVVAVLYCF LNGEVQAEIK RKWRSWKVNR YFTMDFKHRH PSLASSGVNG GTQLSILSKS
SSQLRMSSLP ADNLAT
