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ACM5_PANTR
ID   ACM5_PANTR              Reviewed;         532 AA.
AC   Q5IS53;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Muscarinic acetylcholine receptor M5;
GN   Name=CHRM5;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA   Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA   Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT   "Accelerated evolution of nervous system genes in the origin of Homo
RT   sapiens.";
RL   Cell 119:1027-1040(2004).
CC   -!- FUNCTION: The muscarinic acetylcholine receptor mediates various
CC       cellular responses, including inhibition of adenylate cyclase,
CC       breakdown of phosphoinositides and modulation of potassium channels
CC       through the action of G proteins. Primary transducing effect is Pi
CC       turnover.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Postsynaptic cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Muscarinic acetylcholine receptor subfamily. CHRM5 sub-subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AY665275; AAV74313.1; -; mRNA.
DR   RefSeq; NP_001012444.1; NM_001012442.1.
DR   AlphaFoldDB; Q5IS53; -.
DR   SMR; Q5IS53; -.
DR   STRING; 9598.ENSPTRP00000011746; -.
DR   GeneID; 503515; -.
DR   CTD; 1133; -.
DR   eggNOG; KOG4220; Eukaryota.
DR   InParanoid; Q5IS53; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; IEA:InterPro.
DR   GO; GO:0001696; P:gastric acid secretion; IEA:InterPro.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000502; Musac_Ach_M5_rcpt.
DR   InterPro; IPR000995; Musac_Ach_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00243; MUSCARINICR.
DR   PRINTS; PR00542; MUSCRINICM5R.
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; Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW   Reference proteome; Synapse; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..532
FT                   /note="Muscarinic acetylcholine receptor M5"
FT                   /id="PRO_0000069045"
FT   TOPO_DOM        1..29
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        30..53
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        54..66
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        67..87
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        88..104
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        105..126
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        127..146
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        147..169
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        170..191
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        192..214
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        215..443
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        444..464
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        465..478
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        479..498
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        499..532
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          263..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         501
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         505
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        8
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        103..183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   532 AA;  59873 MW;  4B09E40A3940A8F8 CRC64;
     MEGDSYGNAT TINGTPVNHQ PLERHRLWEV ITIAAVTAVV SLITIVGNVL VMISFKVNSQ
     LKTVNNYYLL SLACADLIIG IFSMNLYTTY ILMGRWALGS LACDLWLALD YVASNASVMN
     LLVISFDRYF SITRPLTYRA KRTPKRAGIM IGLAWLISFI LWAPAILCWQ YLVGKRTVPP
     DECQIQFLSE PTITFGTAIA AFYIPVSVMT ILYCRIYRET EKRTKDLADL QGSVSVTKAE
     KRKPAHRALF RSCFRCPRPT LVQRERNQAS RSSSHRSTSI TGKPSQATGP STNWAKAEEL
     TTCSSYPSSE DEDKPATDPV LQVVYKSQGK ESPGEEFSAE EAEETFVKGQ TDKNDCDSPD
     YFLSPAAAHR PKSQQCVAYK FQLVVKADGT QETNNGCHKV KIMPCSFPVA KEPSTKGLSP
     NLSHQMTKRK RMVLVKERKA AQTLSAILLA FIITWTPYNI MVLVSTFCDK CVPVALWHLG
     YWLCYVNSTV NPICYALCNR TFRKTFKMLL LCQWKKKKVE EKLYWQGNSK LP
 
 
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