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ACH92_ONCMY
ID   ACH92_ONCMY             Reviewed;         550 AA.
AC   Q68RJ7;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Neuronal acetylcholine receptor subunit alpha-9-II;
DE   AltName: Full=Nicotinic acetylcholine receptor subunit alpha-9-II;
DE            Short=NACHR alpha-9-II;
DE   Flags: Precursor;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Saccule;
RX   PubMed=15283971; DOI=10.1016/j.neuroscience.2004.05.037;
RA   Drescher D.G., Ramakrishnan N.A., Drescher M.J., Chun W., Wang X.,
RA   Myers S.F., Green G.E., Sadrazodi K., Karadaghy A.A., Poopat N.,
RA   Karpenko A.N., Khan K.M., Hatfield J.S.;
RT   "Cloning and characterization of alpha9 subunits of the nicotinic
RT   acetylcholine receptor expressed by saccular hair cells of the rainbow
RT   trout (Oncorhynchus mykiss).";
RL   Neuroscience 127:737-752(2004).
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000305}; Multi-
CC       pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, liver, olfactory mucosa,
CC       pituitary gland and hair cells of the saccule.
CC       {ECO:0000269|PubMed:15283971}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily. {ECO:0000305}.
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DR   EMBL; AY611482; AAT45203.1; -; mRNA.
DR   RefSeq; NP_001117991.1; NM_001124519.1.
DR   AlphaFoldDB; Q68RJ7; -.
DR   SMR; Q68RJ7; -.
DR   Ensembl; ENSOMYT00000009003; ENSOMYP00000008106; ENSOMYG00000004143.
DR   GeneID; 100136255; -.
DR   KEGG; omy:100136255; -.
DR   CTD; 55584; -.
DR   GeneTree; ENSGT00940000156077; -.
DR   OrthoDB; 845098at2759; -.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   Gene3D; 1.20.58.390; -; 2.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR   InterPro; IPR038050; Neuro_actylchol_rec.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR   PANTHER; PTHR18945; PTHR18945; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00254; NICOTINICR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW   Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..550
FT                   /note="Neuronal acetylcholine receptor subunit alpha-9-II"
FT                   /id="PRO_0000000375"
FT   TOPO_DOM        21..233
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        319..528
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        529..549
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          357..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        150..164
FT                   /evidence="ECO:0000250"
FT   DISULFID        214..215
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   550 AA;  61771 MW;  6352395FE46BB997 CRC64;
     MRKMVPVVCF ATMLLQVAHS AQGRYAQQLL TDLMENYSNA LRPVEDTDKA LNVTLQITLS
     QIKDMDERNQ VLIAYLWIRQ TWHDAYLRWN KEDYDGLEVI RIPSSLVWRP DLVLYNKADD
     DFSGPLDTNV VLRYNGEITW DAPAITKSSC VVDVSYFPFD SQECNLTFGS WTYNGNQVDI
     AMGMDSGDLS DFVENVEWEC HGMPATKNVI MYGCCSDPYP DITYTVLLQR RSSFYIFNLL
     LPCFLISFLA PLGFYLPADS GEKVSLGVTV LLALTVFQLM VAESMPPSES VPLIGKYYIA
     TMTMITASTA LTIFIMNIHF CGAEAKPVPH WAKVLIIDYM SKIFFVYEVG ENCATATSSS
     SSSSSSSHFG QDDVHQPNFS SHRQANGKPG GNSGRENQYR HKNPRPQTPG PQRHPKPRHQ
     HHITRDEKNH LSSSKYEGFE SNRNLPLGDC CKEAPPCCPE DEKTAVVAAA VASVTFGPCV
     FCSHGSSLPG VDSKLVRNVE YIANCFREQR ATCAKGAEWK RVAKVMDRFF MWIFFIMVFL
     MSILIIGKAP
 
 
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