ID U3JDR5_FICAL Unreviewed; 517 AA.
AC U3JDR5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=ADCYAP receptor type I {ECO:0000313|Ensembl:ENSFALP00000000919.1};
GN Name=ADCYAP1R1 {ECO:0000313|Ensembl:ENSFALP00000000919.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000000919.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000000919.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000000919.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000256|ARBA:ARBA00005314}.
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DR RefSeq; XP_016151725.1; XM_016296239.1.
DR STRING; 59894.ENSFALP00000000919; -.
DR Ensembl; ENSFALT00000000924.2; ENSFALP00000000919.1; ENSFALG00000000871.2.
DR Ensembl; ENSFALT00000028172.1; ENSFALP00000016716.1; ENSFALG00000000871.2.
DR GeneID; 101805967; -.
DR CTD; 117; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000157362; -.
DR OMA; HLRSCVQ; -.
DR OrthoDB; 5344559at2759; -.
DR Proteomes; UP000016665; Chromosome 2.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0004999; F:vasoactive intestinal polypeptide receptor activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..517
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040717238"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..141
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 156..453
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
SQ SEQUENCE 517 AA; 58781 MW; F8C8F6FB47A700CA CRC64;
MAINWKVCFF SLVLLPVVAA THSNCIIKKE QETCLEKIRR ATALNPLNDS SPGCPGMWDN
ITCWKPASVG EIVFVKCPAL FRFIISEDGW EVDNLGQTHA GDYDLLESTA QSLLGDISRN
CTEDGWSEPF PHYYDACGFD ENETESDNQD YYYLSVKALY TVGYSTSLVS LTTAMVILCR
FRKLHCTRNF IHMNLFVSFI LRAISVFIKD GVLYAEQDGN HCFISTVECK AVMVFFHYCV
MSNYFWLFIE GLYLFTLLVE TFFPERRYFY WYTIIGWGTP TICVTVWAVL RLHFDDTGCW
DMNDNTALWW VIKGPVVGSI MINFVLFIGI IVILVQKLQS PDIGGNESSI YFTLPLPPRC
SCSPCPGHLR SCVQKCYCKP KRANQHSCKM SELSTITLRL ARSTLLLIPL FGIHYTVFAF
SPENVSKRER LVFELGLGSF QGFVVAVLYC FLNGEVQSEI KRKWRSWKVN RYFAVDFKHR
HPSLASSGVN GGTQLSILSK SSSQIRMSSI NAENLAT
//
