PACR_HUMAN
ID PACR_HUMAN Reviewed; 468 AA.
AC P41586; A8K1Y1; B7ZLA7; B8ZZK3; Q17S10;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 195.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM N).
RC TISSUE=Pituitary;
RX PubMed=7902709; DOI=10.1006/bbrc.1993.2423;
RA Ogi K., Miyamoto Y., Masuda Y., Habata Y., Hosoya M., Ohtaki T., Masuo Y.,
RA Onda H., Fujino M.;
RT "Molecular cloning and functional expression of a cDNA encoding a human
RT pituitary adenylate cyclase activating polypeptide receptor.";
RL Biochem. Biophys. Res. Commun. 196:1511-1521(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM N).
RC TISSUE=Brain;
RA King M., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM N).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM N-HOP1).
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 418-468.
RC TISSUE=Placenta;
RX PubMed=7851900; DOI=10.1006/geno.1994.1560;
RA Stoffel M., Espinosa R., Trabb J.B., le Beau M.M., Bell G.I.;
RT "Human type I pituitary adenylate cyclase activating polypeptide receptor
RT (ADCYAP1R): localization to chromosome band 7p14 and integration into the
RT cytogenetic, physical and genetic map of chromosome 7.";
RL Genomics 23:697-699(1994).
RN [9]
RP ALTERNATIVE SPLICING.
RX PubMed=10583729; DOI=10.1046/j.1365-2826.1999.00411.x;
RA Dautzenberg F.M., Mevenkamp G., Wille S., Hauger R.L.;
RT "N-terminal splice variants of the type I PACAP receptor: isolation,
RT characterization and ligand binding/selectivity determinants.";
RL J. Neuroendocrinol. 11:941-949(1999).
RN [10]
RP STRUCTURE BY NMR OF 22-143 IN COMPLEX WITH ADCYAP1, MUTAGENESIS OF VAL-114;
RP GLU-125; PRO-128; GLU-138 AND TYR-139, AND DISULFIDE BONDS.
RX PubMed=17470806; DOI=10.1073/pnas.0611397104;
RA Sun C., Song D., Davis-Taber R.A., Barrett L.W., Scott V.E.,
RA Richardson P.L., Pereda-Lopez A., Uchic M.E., Solomon L.R., Lake M.R.,
RA Walter K.A., Hajduk P.J., Olejniczak E.T.;
RT "Solution structure and mutational analysis of pituitary adenylate cyclase-
RT activating polypeptide binding to the extracellular domain of PAC1-RS.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7875-7880(2007).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 26-140, MUTAGENESIS OF GLU-125,
RP AND DISULFIDE BONDS.
RX PubMed=21625560; DOI=10.1371/journal.pone.0019682;
RA Kumar S., Pioszak A., Zhang C., Swaminathan K., Xu H.E.;
RT "Crystal structure of the PAC1R extracellular domain unifies a consensus
RT fold for hormone recognition by class B G-protein coupled receptors.";
RL PLoS ONE 6:E19682-E19682(2011).
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:0000269|PubMed:17470806}.
CC -!- INTERACTION:
CC P41586-2; P05067: APP; NbExp=3; IntAct=EBI-17241711, EBI-77613;
CC P41586-2; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-17241711, EBI-12837904;
CC P41586-3; P18509: ADCYAP1; NbExp=2; IntAct=EBI-15635217, EBI-8588930;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=N;
CC IsoId=P41586-1; Sequence=Displayed;
CC Name=N-HOP1;
CC IsoId=P41586-2; Sequence=VSP_042671;
CC Name=S;
CC IsoId=P41586-3; Sequence=VSP_042670;
CC Name=S-HOP1;
CC IsoId=P41586-4; Sequence=VSP_042670, VSP_042671;
CC Name=VS;
CC IsoId=P41586-5; Sequence=VSP_042669, VSP_042670;
CC -!- TISSUE SPECIFICITY: Most abundant in the brain, low expression in the
CC lung, liver, thymus, spleen, pancreas and placenta.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA04466.1; Type=Erroneous initiation; Evidence={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; D17516; BAA04466.1; ALT_INIT; mRNA.
DR EMBL; AB065700; BAC05923.1; -; Genomic_DNA.
DR EMBL; AY366498; AAQ72806.1; -; mRNA.
DR EMBL; AK290046; BAF82735.1; -; mRNA.
DR EMBL; AC006466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117116; AAI17117.1; -; mRNA.
DR EMBL; BC136267; AAI36268.1; -; mRNA.
DR EMBL; BC143679; AAI43680.1; -; mRNA.
DR EMBL; CH471073; EAW93978.1; -; Genomic_DNA.
DR EMBL; U09216; AAA19323.1; -; Genomic_DNA.
DR CCDS; CCDS5433.1; -. [P41586-1]
DR CCDS; CCDS56480.1; -. [P41586-2]
DR CCDS; CCDS56481.1; -. [P41586-3]
DR PIR; JN0902; JN0902.
DR RefSeq; NP_001109.2; NM_001118.4. [P41586-1]
DR RefSeq; NP_001186564.1; NM_001199635.1. [P41586-2]
DR RefSeq; NP_001186565.1; NM_001199636.1.
DR RefSeq; NP_001186566.1; NM_001199637.1. [P41586-3]
DR RefSeq; XP_005249675.1; XM_005249618.4. [P41586-5]
DR RefSeq; XP_016867226.1; XM_017011737.1. [P41586-4]
DR PDB; 2JOD; NMR; -; A=22-143.
DR PDB; 3N94; X-ray; 1.80 A; A=26-140.
DR PDB; 6LPB; EM; 3.90 A; R=21-417.
DR PDB; 6M1H; EM; 3.60 A; A=23-438.
DR PDB; 6M1I; EM; 3.50 A; A=23-438.
DR PDB; 6P9Y; EM; 3.01 A; R=19-468.
DR PDB; 7JQD; X-ray; 2.70 A; A=18-143.
DR PDBsum; 2JOD; -.
DR PDBsum; 3N94; -.
DR PDBsum; 6LPB; -.
DR PDBsum; 6M1H; -.
DR PDBsum; 6M1I; -.
DR PDBsum; 6P9Y; -.
DR PDBsum; 7JQD; -.
DR AlphaFoldDB; P41586; -.
DR SMR; P41586; -.
DR BioGRID; 106630; 3.
DR DIP; DIP-42467N; -.
DR IntAct; P41586; 3.
DR MINT; P41586; -.
DR STRING; 9606.ENSP00000483721; -.
DR BindingDB; P41586; -.
DR ChEMBL; CHEMBL5399; -.
DR GuidetoPHARMACOLOGY; 370; -.
DR TCDB; 9.A.14.4.8; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P41586; 5 sites.
DR iPTMnet; P41586; -.
DR PhosphoSitePlus; P41586; -.
DR BioMuta; ADCYAP1R1; -.
DR DMDM; 1171986; -.
DR MassIVE; P41586; -.
DR MaxQB; P41586; -.
DR PeptideAtlas; P41586; -.
DR PRIDE; P41586; -.
DR ProteomicsDB; 55465; -. [P41586-1]
DR ProteomicsDB; 55466; -. [P41586-2]
DR ProteomicsDB; 55467; -. [P41586-3]
DR ProteomicsDB; 55468; -. [P41586-4]
DR ProteomicsDB; 55469; -. [P41586-5]
DR ABCD; P41586; 41 sequenced antibodies.
DR Antibodypedia; 4280; 293 antibodies from 32 providers.
DR DNASU; 117; -.
DR Ensembl; ENST00000304166.9; ENSP00000306620.4; ENSG00000078549.15. [P41586-1]
DR Ensembl; ENST00000396211.6; ENSP00000379514.2; ENSG00000078549.15. [P41586-2]
DR Ensembl; ENST00000409363.5; ENSP00000387335.1; ENSG00000078549.15. [P41586-3]
DR Ensembl; ENST00000614107.4; ENSP00000483721.1; ENSG00000078549.15. [P41586-2]
DR GeneID; 117; -.
DR KEGG; hsa:117; -.
DR MANE-Select; ENST00000304166.9; ENSP00000306620.4; NM_001118.5; NP_001109.2.
DR UCSC; uc003tca.3; human. [P41586-1]
DR CTD; 117; -.
DR DisGeNET; 117; -.
DR GeneCards; ADCYAP1R1; -.
DR HGNC; HGNC:242; ADCYAP1R1.
DR HPA; ENSG00000078549; Tissue enriched (brain).
DR MIM; 102981; gene.
DR neXtProt; NX_P41586; -.
DR OpenTargets; ENSG00000078549; -.
DR PharmGKB; PA24565; -.
DR VEuPathDB; HostDB:ENSG00000078549; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000157362; -.
DR HOGENOM; CLU_002753_4_4_1; -.
DR InParanoid; P41586; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P41586; -.
DR TreeFam; TF315710; -.
DR PathwayCommons; P41586; -.
DR Reactome; R-HSA-187024; NGF-independant TRKA activation.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-420092; Glucagon-type ligand receptors.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; P41586; -.
DR SIGNOR; P41586; -.
DR BioGRID-ORCS; 117; 11 hits in 1061 CRISPR screens.
DR ChiTaRS; ADCYAP1R1; human.
DR EvolutionaryTrace; P41586; -.
DR GeneWiki; ADCYAP1R1; -.
DR GenomeRNAi; 117; -.
DR Pharos; P41586; Tchem.
DR PRO; PR:P41586; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P41586; protein.
DR Bgee; ENSG00000078549; Expressed in cortical plate and 127 other tissues.
DR ExpressionAtlas; P41586; baseline and differential.
DR Genevisible; P41586; HS.
DR GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
DR GO; GO:0005901; C:caveola; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0008179; F:adenylate cyclase binding; IEA:Ensembl.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0042923; F:neuropeptide binding; IEA:Ensembl.
DR GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0004999; F:vasoactive intestinal polypeptide receptor activity; IEA:InterPro.
DR GO; GO:0007202; P:activation of phospholipase C activity; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0046545; P:development of primary female sexual characteristics; IEA:Ensembl.
DR GO; GO:0033555; P:multicellular organismal response to stress; IEA:Ensembl.
DR GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IEA:Ensembl.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; IEA:Ensembl.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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 3D-structure; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..468
FT /note="Pituitary adenylate cyclase-activating polypeptide
FT type I receptor"
FT /id="PRO_0000012841"
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..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..385
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..405
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 125..139
FT /note="Important for ligand binding and specificity"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70205"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70205"
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 CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..63
FT DISULFID 54..118
FT DISULFID 77..134
FT VAR_SEQ 53..88
FT /note="Missing (in isoform VS)"
FT /evidence="ECO:0000305"
FT /id="VSP_042669"
FT VAR_SEQ 89..109
FT /note="Missing (in isoform S, isoform S-HOP1 and isoform
FT VS)"
FT /evidence="ECO:0000305"
FT /id="VSP_042670"
FT VAR_SEQ 348
FT /note="Y -> YFSCVQKCYCKPQRAQQHSCKMSELSTIT (in isoform N-
FT HOP1 and isoform S-HOP1)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042671"
FT MUTAGEN 114
FT /note="V->A: Reduced affinity for ADCYAP1."
FT /evidence="ECO:0000269|PubMed:17470806"
FT MUTAGEN 125
FT /note="E->R: Reduced affinity for ADCYAP1."
FT /evidence="ECO:0000269|PubMed:17470806,
FT ECO:0000269|PubMed:21625560"
FT MUTAGEN 128
FT /note="P->A: Reduced affinity for ADCYAP1."
FT /evidence="ECO:0000269|PubMed:17470806"
FT MUTAGEN 138
FT /note="E->R: Reduced affinity for ADCYAP1."
FT /evidence="ECO:0000269|PubMed:17470806"
FT MUTAGEN 139
FT /note="Y->A: Strongly reduced affinity for ADCYAP1."
FT /evidence="ECO:0000269|PubMed:17470806"
FT HELIX 26..47
FT /evidence="ECO:0007829|PDB:3N94"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2JOD"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6M1I"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:3N94"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:3N94"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:3N94"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:6M1I"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:3N94"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:6P9Y"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:6P9Y"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6M1I"
FT HELIX 186..210
FT /evidence="ECO:0007829|PDB:6P9Y"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:6M1I"
FT HELIX 224..255
FT /evidence="ECO:0007829|PDB:6P9Y"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:6P9Y"
FT HELIX 276..288
FT /evidence="ECO:0007829|PDB:6P9Y"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:6P9Y"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:6M1I"
FT HELIX 303..336
FT /evidence="ECO:0007829|PDB:6P9Y"
FT HELIX 347..362
FT /evidence="ECO:0007829|PDB:6P9Y"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:6P9Y"
FT TURN 367..371
FT /evidence="ECO:0007829|PDB:6P9Y"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:6P9Y"
FT HELIX 379..385
FT /evidence="ECO:0007829|PDB:6P9Y"
FT TURN 386..391
FT /evidence="ECO:0007829|PDB:6P9Y"
FT HELIX 392..400
FT /evidence="ECO:0007829|PDB:6P9Y"
FT HELIX 405..416
FT /evidence="ECO:0007829|PDB:6P9Y"
FT CONFLICT P41586-2:350
FT /note="Missing (in Ref. 7; AAI43680)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 53314 MW; BB515B84E9F28977 CRC64;
MAGVVHVSLA ALLLLPMAPA MHSDCIFKKE QAMCLEKIQR ANELMGFNDS SPGCPGMWDN
ITCWKPAHVG EMVLVSCPEL FRIFNPDQVW ETETIGESDF GDSNSLDLSD MGVVSRNCTE
DGWSEPFPHY FDACGFDEYE SETGDQDYYY LSVKALYTVG YSTSLVTLTT AMVILCRFRK
LHCTRNFIHM NLFVSFMLRA ISVFIKDWIL YAEQDSNHCF ISTVECKAVM VFFHYCVVSN
YFWLFIEGLY LFTLLVETFF PERRYFYWYT IIGWGTPTVC VTVWATLRLY FDDTGCWDMN
DSTALWWVIK GPVVGSIMVN FVLFIGIIVI LVQKLQSPDM GGNESSIYLR LARSTLLLIP
LFGIHYTVFA FSPENVSKRE RLVFELGLGS FQGFVVAVLY CFLNGEVQAE IKRKWRSWKV
NRYFAVDFKH RHPSLASSGV NGGTQLSILS KSSSQIRMSG LPADNLAT
