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ZACN_CANLF
ID   ZACN_CANLF              Reviewed;         409 AA.
AC   Q866Y9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Zinc-activated ligand-gated ion channel;
DE   AltName: Full=Ligand-gated ion channel zinc-activated 1;
DE   Flags: Precursor;
GN   Name=ZACN; Synonyms=LGICZ, LGICZ1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12381728; DOI=10.1074/jbc.m208814200;
RA   Davies P.A., Wang W., Hales T.G., Kirkness E.F.;
RT   "A novel class of ligand-gated ion channel is activated by Zn2+.";
RL   J. Biol. Chem. 278:712-717(2003).
CC   -!- FUNCTION: Zinc-activated ligand-gated ion channel. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The mouse and rat orthologous proteins do not exist.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       {ECO:0000305}.
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DR   EMBL; AF512523; AAO20972.1; -; Genomic_DNA.
DR   RefSeq; NP_001010955.1; NM_001010955.1.
DR   AlphaFoldDB; Q866Y9; -.
DR   SMR; Q866Y9; -.
DR   STRING; 9612.ENSCAFP00000007487; -.
DR   PaxDb; Q866Y9; -.
DR   GeneID; 483326; -.
DR   KEGG; cfa:483326; -.
DR   CTD; 353174; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   HOGENOM; CLU_672608_0_0_1; -.
DR   InParanoid; Q866Y9; -.
DR   OMA; WATCKSD; -.
DR   OrthoDB; 1001614at2759; -.
DR   TreeFam; TF315605; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR   GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   Gene3D; 1.20.58.390; -; 1.
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; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   PANTHER; PTHR18945; PTHR18945; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   SUPFAM; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Receptor; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Transport; Zinc.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..409
FT                   /note="Zinc-activated ligand-gated ion channel"
FT                   /id="PRO_0000317164"
FT   TOPO_DOM        19..233
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        287..296
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..317
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        318..365
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        387..409
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          325..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..354
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        157..171
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   409 AA;  45529 MW;  D62FFF76C317282E CRC64;
     MAPRLLLLLL AFLRLGTTGP LVQGRGFRSP TVAWPSFFNF NQPQGVQETI QIPNNGSAPL
     LVDVQVFVSN VFNVDILRYT VSSMLLLRLS WVDTRLAWNA SLYPQHAVTL PWDSLWTPGL
     TIQEALWVDW QDQSPRARVG PDGHVDLYLA LTTETNCDFE LLHFPRDQSD CNLSFYALSN
     TVLELEFRAH AVNEIVSVKR EYVVWGLETQ IPPRQLVPCF QVTLRLQNTA LKAIIALLVP
     GEALLLADMC GGLLPLRATE RIAYKVTLLL GYLVFHSSLV QALPSSSSCN PLLIYYFTVL
     LLLLFISTME TVLLAALQAR GHLSARSSPI PTPRGEQQDH GDLGPHPEEA PGVKESRSWA
     EAADHIFFLV YVVGVVCSQF FFIGFWMWAT CKSDPAPGEA IPHGGQPRL
 
 
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