AR_BOMMO
ID AR_BOMMO Reviewed; 361 AA.
AC Q8WPA2;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Allatostatin-A receptor;
DE Short=BAR {ECO:0000303|PubMed:11590150};
GN Name=AR {ECO:0000303|PubMed:11590150};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG44631.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Lyon 200 BA x Lyon 300 AB {ECO:0000312|EMBL:AAG44631.1};
RC TISSUE=Fifth instar larvae {ECO:0000269|PubMed:11590150};
RX PubMed=11590150; DOI=10.1074/jbc.m106675200;
RA Secher T., Lenz C., Cazzamali G., Sorensen G., Williamson M., Hansen G.N.,
RA Svane P., Grimmelikhuijzen C.J.P.;
RT "Molecular cloning of a functional allatostatin gut/brain receptor and an
RT allatostatin preprohormone from the silkworm Bombyx mori.";
RL J. Biol. Chem. 276:47052-47060(2001).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=18725956; DOI=10.1371/journal.pone.0003048;
RA Yamanaka N., Yamamoto S., Zitnan D., Watanabe K., Kawada T., Satake H.,
RA Kaneko Y., Hiruma K., Tanaka Y., Shinoda T., Kataoka H.;
RT "Neuropeptide receptor transcriptome reveals unidentified neuroendocrine
RT pathways.";
RL PLoS ONE 3:E3048-E3048(2008).
CC -!- FUNCTION: Acts as a receptor for A-type allatostatin neuropeptide
CC hormones. {ECO:0000269|PubMed:11590150}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the midgut and, to a lesser extent, in
CC the fore- and hindgut of fifth instar larvae. Also highly expressed in
CC the brain of fourth and fifth instar larvae.
CC {ECO:0000269|PubMed:11590150, ECO:0000269|PubMed:18725956}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF254742; AAG44631.1; -; mRNA.
DR EMBL; AF303370; AAL47056.1; -; Genomic_DNA.
DR EMBL; AF303368; AAL47056.1; JOINED; Genomic_DNA.
DR EMBL; AF303369; AAL47056.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001037035.1; NM_001043570.1.
DR RefSeq; XP_012546689.1; XM_012691235.1.
DR RefSeq; XP_012546690.1; XM_012691236.1.
DR AlphaFoldDB; Q8WPA2; -.
DR SMR; Q8WPA2; -.
DR STRING; 7091.BGIBMGA005708-TA; -.
DR GeneID; 692587; -.
DR KEGG; bmor:692587; -.
DR CTD; 692587; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_6_4_1; -.
DR InParanoid; Q8WPA2; -.
DR OrthoDB; 1294084at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0042562; F:hormone binding; IDA:UniProtKB.
DR GO; GO:0042923; F:neuropeptide binding; IDA:UniProtKB.
DR InterPro; IPR000405; Galanin_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00663; GALANINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..361
FT /note="Allatostatin-A receptor"
FT /id="PRO_0000389519"
FT TOPO_DOM 1..46
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 341..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 361 AA; 40479 MW; 63C2B2846FC3010A CRC64;
MESTEDEFYT ICLNLTAEDP SFGNCNYTTD FENGELLEKV VSRVVPIFFG FIGIVGLVGN
ALVVLVVAAN PGMRSTTNLL IINLAVADLL FVIFCVPFTA TDYVMPRWPF GDWWCKVVQY
FIVVTAHASV YTLVLMSLDR FMAVVHPIAS MSIRTEKNAL LAIACIWVVI LTTAIPVGIC
HGEREYSYFN RNHSSCVFLE ERGYSKLGFQ MSFFLSSYVI PLALISVLYM CMLTRLWKSA
PGGRVSAESR RGRKKVTRMV VVVVVVFAVC WCPIQIILLV KALNKYHITY FTVTAQIVSH
VLAYMNSCVN PVLYAFLSEN FRVAFRKVMY CPPPYNDGFS GRPQATKTTR TGNGNSCHDI
V
