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ACM1_PIG
ID   ACM1_PIG                Reviewed;         460 AA.
AC   P04761;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Muscarinic acetylcholine receptor M1;
GN   Name=CHRM1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=3762692; DOI=10.1038/323411a0;
RA   Kubo T., Fukuda K., Mikami A., Maeda A., Takahashi H., Mishina M., Haga T.,
RA   Haga K., Ichiyama A., Kangawa K., Kojima M., Matsuo H., Hirose T., Numa S.;
RT   "Cloning, sequencing and expression of complementary DNA encoding the
RT   muscarinic acetylcholine receptor.";
RL   Nature 323:411-416(1986).
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   -!- SUBUNIT: Interacts with GPRASP2 (By similarity). Interacts with TMEM147
CC       (By similarity). {ECO:0000250|UniProtKB:P11229}.
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. CHRM1 sub-subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; X04413; CAA28003.1; -; mRNA.
DR   PIR; A24325; A24325.
DR   RefSeq; NP_999199.1; NM_214034.1.
DR   RefSeq; XP_013849645.1; XM_013994191.1.
DR   AlphaFoldDB; P04761; -.
DR   SMR; P04761; -.
DR   STRING; 9823.ENSSSCP00000026844; -.
DR   PaxDb; P04761; -.
DR   PRIDE; P04761; -.
DR   Ensembl; ENSSSCT00015092787; ENSSSCP00015037944; ENSSSCG00015069309.
DR   Ensembl; ENSSSCT00025101968; ENSSSCP00025045084; ENSSSCG00025074060.
DR   Ensembl; ENSSSCT00025102004; ENSSSCP00025045104; ENSSSCG00025074060.
DR   Ensembl; ENSSSCT00030016391; ENSSSCP00030007346; ENSSSCG00030011943.
DR   Ensembl; ENSSSCT00030016402; ENSSSCP00030007353; ENSSSCG00030011943.
DR   Ensembl; ENSSSCT00035060405; ENSSSCP00035024300; ENSSSCG00035045451.
DR   Ensembl; ENSSSCT00035060408; ENSSSCP00035024301; ENSSSCG00035045451.
DR   Ensembl; ENSSSCT00040060497; ENSSSCP00040025407; ENSSSCG00040045082.
DR   Ensembl; ENSSSCT00040060566; ENSSSCP00040025434; ENSSSCG00040045082.
DR   Ensembl; ENSSSCT00045057639; ENSSSCP00045040313; ENSSSCG00045033695.
DR   Ensembl; ENSSSCT00045057669; ENSSSCP00045040337; ENSSSCG00045033695.
DR   Ensembl; ENSSSCT00050014122; ENSSSCP00050005817; ENSSSCG00050010499.
DR   Ensembl; ENSSSCT00050014128; ENSSSCP00050005819; ENSSSCG00050010499.
DR   Ensembl; ENSSSCT00055008469; ENSSSCP00055006696; ENSSSCG00055004285.
DR   Ensembl; ENSSSCT00055008473; ENSSSCP00055006699; ENSSSCG00055004285.
DR   Ensembl; ENSSSCT00060049104; ENSSSCP00060021028; ENSSSCG00060036236.
DR   Ensembl; ENSSSCT00060049109; ENSSSCP00060021030; ENSSSCG00060036236.
DR   Ensembl; ENSSSCT00065009381; ENSSSCP00065003912; ENSSSCG00065007001.
DR   Ensembl; ENSSSCT00065009386; ENSSSCP00065003914; ENSSSCG00065007001.
DR   GeneID; 397099; -.
DR   KEGG; ssc:397099; -.
DR   CTD; 1128; -.
DR   eggNOG; KOG4220; Eukaryota.
DR   HOGENOM; CLU_009579_11_2_1; -.
DR   InParanoid; P04761; -.
DR   OrthoDB; 1245472at2759; -.
DR   TreeFam; TF320495; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; P04761; SS.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; IBA:GO_Central.
DR   GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0007197; P:adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0050890; P:cognition; IEA:InterPro.
DR   GO; GO:0009649; P:entrainment of circadian clock; IMP:AgBase.
DR   GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; IMP:AgBase.
DR   GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR   GO; GO:0007603; P:phototransduction, visible light; IMP:AgBase.
DR   GO; GO:0040012; P:regulation of locomotion; IEA:InterPro.
DR   GO; GO:0046541; P:saliva secretion; IEA:InterPro.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR002228; Musac_Ach_M1_rcpt.
DR   InterPro; IPR000995; Musac_Ach_rcpt.
DR   PANTHER; PTHR24248:SF155; PTHR24248:SF155; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00243; MUSCARINICR.
DR   PRINTS; PR00538; MUSCRINICM1R.
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..460
FT                   /note="Muscarinic acetylcholine receptor M1"
FT                   /id="PRO_0000069018"
FT   TOPO_DOM        1..22
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P11229"
FT   TRANSMEM        23..48
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P11229"
FT   TOPO_DOM        49..62
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P11229"
FT   TRANSMEM        63..84
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P11229"
FT   TOPO_DOM        85..95
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P11229"
FT   TRANSMEM        96..121
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P11229"
FT   TOPO_DOM        122..142
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P11229"
FT   TRANSMEM        143..164
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P11229"
FT   TOPO_DOM        165..185
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P11229"
FT   TRANSMEM        186..209
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P11229"
FT   TOPO_DOM        210..366
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P11229"
FT   TRANSMEM        367..390
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P11229"
FT   TOPO_DOM        391..397
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P11229"
FT   TRANSMEM        398..420
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P11229"
FT   TOPO_DOM        421..460
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P11229"
FT   REGION          225..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         230
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P12657"
FT   MOD_RES         428
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         451
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         455
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         457
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        12
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        98..178
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   460 AA;  51419 MW;  C025C70EA43BC2AD CRC64;
     MNTSAPPAVS PNITVLAPGK GPWQVAFIGI TTGLLSLATV TGNLLVLISF KVNTELKTVN
     NYFLLSLACA DLIIGTFSMN LYTTYLLMGH WALGTLACDL WLALDYVASN ASVMNLLLIS
     FDRYFSVTRP LSYRAKRTPR RAALMIGLAW LVSFVLWAPA ILFWQYLVGE RTVLAGQCYI
     QFLSQPIITF GTAMAAFYLP VTVMCTLYWR IYRETENRAR ELAALQGSET PGKGGGSSSS
     SERSQPGAEG SPETPPGRCC RCCRAPRLLQ AYSWKEEEEE DEGSMESLTS SEGEEPGSEV
     VIKMPMVDPE AQAPAKQPPR SSPNTVKRPT RKGRERAGKG QKPRGKEQLA KRKTFSLVKE
     KKAARTLSAI LLAFIVTWTP YNIMVLVSTF CKDCVPETLW ELGYWLCYVN STINPMCYAL
     CNKAFRDTFR LLLLCRWDKR RWRKIPKRPG SVHRTPSRQC
 
 
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