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Database: UniProt
Entry: A0A151IK00_9HYME
LinkDB: A0A151IK00_9HYME
Original site: A0A151IK00_9HYME 
ID   A0A151IK00_9HYME        Unreviewed;      1278 AA.
AC   A0A151IK00;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Muscarinic acetylcholine receptor DM1 {ECO:0000313|EMBL:KYN03953.1};
GN   ORFNames=ALC62_05254 {ECO:0000313|EMBL:KYN03953.1};
OS   Cyphomyrmex costatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Cyphomyrmex.
OX   NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN03953.1, ECO:0000313|Proteomes:UP000078542};
RN   [1] {ECO:0000313|EMBL:KYN03953.1, ECO:0000313|Proteomes:UP000078542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS0001 {ECO:0000313|EMBL:KYN03953.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN03953.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Cyphomyrmex costatus WGS genome.";
RL   Submitted (MAR-2016) 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; KQ977294; KYN03953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151IK00; -.
DR   SMR; A0A151IK00; -.
DR   STRING; 456900.A0A151IK00; -.
DR   Proteomes; UP000078542; 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:UP000078542};
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        671..695
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        707..733
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        745..766
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        787..812
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        832..855
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1189..1210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1230..1253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          687..1246
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
FT   REGION          551..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          952..975
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1163..1184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..620
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        880..906
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1170..1184
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1278 AA;  144498 MW;  A58AFED90572ED05 CRC64;
     MAKWGEGDPR WIVEERPDAT NVNNWHWTEK NACVWSQEKL KELLINFKIE GEGVSCKVTE
     MEKCEGEAVA NNRKGKLIFF YEWNIVLKWI SDETSNKDIE GKINIPNLSE ENDISEVDIE
     ITLKDSTDEG EKVKQFLHTK GKDAIREKLK KYVSSLKEEF TKGMILPKKD TDKEKENISN
     ITSGFNIKMQ MNAAVTPTNN NKSASKISTT TIKQNVKFQC RADEFYNVLS SIEMVQAFTK
     NPVKLEPKKN GQFELFGGNI HGEFIEITPT KIIQKWRCKQ WPSGHFSDVT IDISEKNDHT
     EVNLTQSGVP VSKIVMRKCR DFQRGALYEG ELGQNNRTDC VQSHAVARAL DFCGSIDELS
     SFSISFGARS AGTRASVSRP ERVEAALNHT CNRSRVRQSV SDSLTGPHVA VDRTSVVVVV
     VGVMTTVSDR CSYSHVPRCR HVSARAPSLT PALRRLPFHP LSPSTHSTRA SIARGCRRDI
     PDLAIQIPSI YSPPHRQASS MPCALNREVI ALHTWRNMHP STPLPQQQFD RLARDIELAA
     FDEESVAIMT VIDESTTTEA VDEEEEGGEE EEEDEESEED EDNNDDDDDG HDDDDHDDDH
     DDDDDDDDED DDDEEENEKE EVEKGRDRYG SVSEDMNVTS MVEIFGNDSN NVSNGLDCGG
     EPHQYALWER VTIVVIAVVL SFTTVGGNIM VMISFKIDKQ LQTISNYFLF SLAVADFAIG
     LISMPLFTLY TVLGYWPLGP YVCDTWLALD YLASNASVLN LLIISFDRYF SVTRPLTYRA
     KRTTVKAAIM IGSAWGISLL LWPPWIYAWP YIEGQRTVPM TSCYIQFIET NHYITFGTAI
     AAFYVPVMIM TFLYWRIWKE TKKRQKDLPN LQAGKQDASK RSNSSDEVII DMEEGRRQRS
     ESSTADDVSH ATHIAVSYID KHYPQYKSHR PFSWTWLKMW CIAWWHSGRD DEDDDEEIAG
     PESSHTGAGY EDTLTPLSAE TPLPSTVSRC PSISAIQATG IALDKTMLHE YKRSARPVDL
     RNISNDTVCD ASILSRNLYL NVYLKFDENK KKNCSEKFSV IIRNKTVIFE IAIESIDSRS
     KIHTTRVSLL QFQIYTILIK LPSNGGKFTE GTSIRMIPDD GSGASRLFRL GGGSVSSPST
     VTMRRPSQMP DIRIPLNAKN IPKAGKGILS KQPNKKKKKL QEKKADRKAA RTLSAILLAF
     IITWTPYNIL VLLKSITACS WYIPQVLWDF VYYLCYINST VNPMCYALGN AAFRRTYVRI
     LKCKWHSRNR GTGAVDRG
//
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