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Database: UniProt
Entry: A0A151WTB6_9HYME
LinkDB: A0A151WTB6_9HYME
Original site: A0A151WTB6_9HYME 
ID   A0A151WTB6_9HYME        Unreviewed;      1104 AA.
AC   A0A151WTB6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Muscarinic acetylcholine receptor DM1 {ECO:0000313|EMBL:KYQ51073.1};
GN   ORFNames=ALC60_09871 {ECO:0000313|EMBL:KYQ51073.1};
OS   Trachymyrmex zeteki.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ51073.1, ECO:0000313|Proteomes:UP000075809};
RN   [1] {ECO:0000313|EMBL:KYQ51073.1, ECO:0000313|Proteomes:UP000075809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ51073.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYQ51073.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex zeteki WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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 AHA1 family.
CC       {ECO:0000256|ARBA:ARBA00006817}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000256|ARBA:ARBA00010663, ECO:0000256|RuleBase:RU000688}.
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DR   EMBL; KQ982762; KYQ51073.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151WTB6; -.
DR   STRING; 64791.A0A151WTB6; -.
DR   Proteomes; UP000075809; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR   GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; IEA:InterPro.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR   CDD; cd15301; 7tmA_mAChR_DM1-like; 1.
DR   CDD; cd08892; SRPBCC_Aha1; 1.
DR   Gene3D; 3.30.530.20; -; 1.
DR   Gene3D; 3.15.10.20; Activator of Hsp90 ATPase Aha1, N-terminal domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 2.
DR   InterPro; IPR036338; Aha1.
DR   InterPro; IPR015310; AHSA1-like_N.
DR   InterPro; IPR013538; ASHA1-like_C.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000995; Musac_Ach_rcpt.
DR   InterPro; IPR023393; START-like_dom_sf.
DR   PANTHER; PTHR24247; 5-HYDROXYTRYPTAMINE RECEPTOR; 1.
DR   PANTHER; PTHR24247:SF268; MUSCARINIC ACETYLCHOLINE RECEPTOR DM1; 1.
DR   Pfam; PF00001; 7tm_1; 2.
DR   Pfam; PF09229; Aha1_N; 1.
DR   Pfam; PF08327; AHSA1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00243; MUSCARINICR.
DR   SMART; SM01000; Aha1_N; 1.
DR   SUPFAM; SSF103111; Activator of Hsp90 ATPase, Aha1; 1.
DR   SUPFAM; SSF55961; Bet v1-like; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW   ECO:0000256|RuleBase:RU000688};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000688};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU000688};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000688};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        545..569
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        581..607
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        619..640
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        661..686
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        706..729
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1014..1035
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1055..1078
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          561..1071
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
FT   REGION          431..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          742..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          850..884
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..491
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..506
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..770
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1104 AA;  125683 MW;  761F1E9592D1B4E8 CRC64;
     MAKWGEGDPR WIVEERPDAT NVNNWHWTEK NACVWSQEKL KEFFVNSKIE GEGVSCKITE
     MEKCEGEAIV NNRKGKLIFF YEWNIVLKWI LDGESSKDIE GKINIPNLSE ENDISEIDIE
     ITLKDSTDEG EKVKQFLHTK GKDAIREKLK KYVSSLKEEF AKGMILPKKD NDKEKENISN
     ITSGFNIKMQ MNAAVTSTNN NKTANCKIST TTIKQNVKFQ CRAGEFYNVL SSIEMVQAFT
     KNPVKLEPKK NGQFELFGGN IHGEFIEITP TKIIQKWRCK QWPSGHFSDV TIDICEKNDH
     TEVNLTQSGV PVSEELSTKE NWDRYRVKLF KISLKKVQLE IREAKRIRQV GRDPAGPDLA
     VQLPSIYSPP HRQASSMPCA LNREVIALHT WRNMHPSTPL PQQQFDRLAR DIELAAFDEE
     SVAIMAVIDE STTTEAVDEE EEEEEEEEGV EEEEEEEGVE EEAEEEGEGE EEEEEEDEDE
     EDDDEEENEG EEVEKGRDRD EKTRNSPSDM NVTPMVEIPG NDSYSISNGL DCGGEPHQYT
     VWERVTIVVI AVILSLTTVV GNIMVMISFK IDKNLQTISN YFLFSLAVAD FAIGLISMPL
     FTVYTVLGYW PLGSHVCDTW LALDYLASNA SVLNLLIISF DRYFSVTRPL TYRAKRTTFR
     AAVMIGSAWG ISLLLWPPWI YAWPYIEGQR TVPTSSCYIQ FIETNHYITF GTAIAAFYVP
     VMIMTILYWR IWKETKKRQK DLPNLQAGKQ DASKRSNSSN SANIARSKDS SAVRRTYSHV
     FPCSDEVLDM EESRRQRSES STADDVSHAT HIAVSYIDKH YPQYKSHRPF SWTWLKMWCI
     AWWHSGRDDE DDDEEIAGPE SSHTGAGYED TLTPLSAETP LPSTVSRCPS LSAIQATGIA
     LDKTAMQHEL YKRPARSVDL RNISSDTIYT ILIKLPSNGG KFSEGTSIRM IHDESVSIHP
     STVTMRRPSQ MPDIRIPLNA KNIPKTLTTG KGILNKQPNK KKKKLQEKKA DRKAAKTLSA
     ILLAFIITWT PYNILVLLKS LTACSWYIPQ VLWDFVYYLC YINSTVNPMC YALGNAAFRR
     TYVRILKCKW QSRNRGGTGA VDRG
//
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