PACR_BOVIN
ID PACR_BOVIN Reviewed; 513 AA.
AC Q29627;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC TISSUE=Brain;
RX PubMed=8049255; DOI=10.1016/0167-4781(94)90181-3;
RA Miyamoto Y., Habata Y., Ohtaki T., Masuda Y., Ogi K., Onda H., Fujino M.;
RT "Cloning and expression of a complementary DNA encoding the bovine receptor
RT for pituitary adenylate cyclase-activating polypeptide (PACAP).";
RL Biochim. Biophys. Acta 1218:297-307(1994).
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 (By similarity).
CC {ECO:0000250}.
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=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=Long;
CC IsoId=Q29627-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q29627-2; Sequence=VSP_002004;
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; D17290; BAA04122.1; -; mRNA.
DR EMBL; D17290; BAA04123.1; -; mRNA.
DR PIR; S47631; S47631.
DR RefSeq; NP_783646.1; NM_175715.2. [Q29627-1]
DR RefSeq; XP_010802598.1; XM_010804296.1. [Q29627-1]
DR RefSeq; XP_010802600.1; XM_010804298.1. [Q29627-2]
DR AlphaFoldDB; Q29627; -.
DR SMR; Q29627; -.
DR STRING; 9913.ENSBTAP00000026333; -.
DR PaxDb; Q29627; -.
DR PRIDE; Q29627; -.
DR Ensembl; ENSBTAT00000084591; ENSBTAP00000059289; ENSBTAG00000020247. [Q29627-2]
DR GeneID; 319095; -.
DR KEGG; bta:319095; -.
DR CTD; 117; -.
DR VEuPathDB; HostDB:ENSBTAG00000020247; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000157362; -.
DR HOGENOM; CLU_002753_4_4_1; -.
DR InParanoid; Q29627; -.
DR OrthoDB; 651627at2759; -.
DR TreeFam; TF315710; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000020247; Expressed in prefrontal cortex and 90 other tissues.
DR ExpressionAtlas; Q29627; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR GO; GO:0004999; F:vasoactive intestinal polypeptide receptor activity; IEA:InterPro.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
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; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..513
FT /note="Pituitary adenylate cyclase-activating polypeptide
FT type I receptor"
FT /id="PRO_0000012840"
FT TOPO_DOM 38..172
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..195
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..222
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..270
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..308
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..326
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..349
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..430
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..450
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 142..156
FT /note="Important for ligand binding and specificity"
FT /evidence="ECO:0000250"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70205"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70205"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..80
FT /evidence="ECO:0000250"
FT DISULFID 71..135
FT /evidence="ECO:0000250"
FT DISULFID 94..151
FT /evidence="ECO:0000250"
FT VAR_SEQ 366..393
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8049255"
FT /id="VSP_002004"
SQ SEQUENCE 513 AA; 58785 MW; 9A45753210CE9817 CRC64;
MRGGRHWPEP PCRLRSVMAS IAQVSLAALL LLPMATAMHS DCIFKKEQAM CLEKIQRVND
LMGLNDSSPG CPGMWDNITC WKPAHVGEMV LVSCPELFRI FNPDQVWETE TIGEFGFADS
KSLDLSDMRV VSRNCTEDGW SEPFPHYFDA CGFEEYESET GDQDYYYLSV KALYTVGYST
SLVTLTTAMV ILCRFRKLHC TRNFIHMNLF VSFMLRAISV FIKDWILYAE QDSNHCFVST
VECKAVMVFF HYCVVSNYFW LFIEGLYLFT LLVETFFPER RYFYWYIIIG WGTPTVCVSV
WAMLRLYFDD TGCWDMNDNT ALWWVIKGPV VGSIMVNFVL FIGIIVILVQ KLQSPDMGGN
ESSIYFSCVQ KCYCKPQRAQ QHSCKMSELS TITLRLARST LLLIPLFGIH YTVFAFSPEN
VSKRERLVFE LGLGSFQGFV VAVLYCFLNG EVQAEIKRKW RSWKVNRYFT MDFKHRHPSL
ASSGVNGGTQ LSILSKSSSQ IRMSGLPADN LAT
