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   24-JAN-2024, entry version 157.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyCosmos; P70205; 3 sites, No reported glycans.
DR   GlyGen; P70205; 3 sites.
DR   iPTMnet; P70205; -.
DR   PhosphoSitePlus; P70205; -.
DR   SwissPalm; P70205; -.
DR   MaxQB; P70205; -.
DR   PaxDb; 10090-ENSMUSP00000063784; -.
DR   ProteomicsDB; 294242; -.
DR   Antibodypedia; 4280; 344 antibodies from 32 providers.
DR   DNASU; 11517; -.
DR   Ensembl; ENSMUST00000070736.12; ENSMUSP00000063784.6; ENSMUSG00000029778.13.
DR   GeneID; 11517; -.
DR   KEGG; mmu:11517; -.
DR   UCSC; uc009cat.2; mouse.
DR   AGR; MGI:108449; -.
DR   CTD; 117; -.
DR   MGI; MGI:108449; Adcyap1r1.
DR   VEuPathDB; HostDB:ENSMUSG00000029778; -.
DR   eggNOG; KOG4564; Eukaryota.
DR   GeneTree; ENSGT00940000157362; -.
DR   InParanoid; P70205; -.
DR   OrthoDB; 5344559at2759; -.
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 75 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 180 other cell types or tissues.
DR   ExpressionAtlas; P70205; baseline and differential.
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:0005768; C:endosome; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:receptor complex; 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: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:1901032; P:negative regulation of response to reactive oxygen species; 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   CDD; cd15987; 7tmB1_PACAP-R1; 1.
DR   Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
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   PANTHER; PTHR45620; PDF RECEPTOR-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR45620:SF12; PITUITARY ADENYLATE CYCLASE-ACTIVATING POLYPEPTIDE TYPE I RECEPTOR; 1.
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; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   SUPFAM; SSF111418; Hormone receptor domain; 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.
DR   Genevisible; P70205; MM.
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
//