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Database: UniProt
Entry: M7CJI8_CHEMY
LinkDB: M7CJI8_CHEMY
Original site: M7CJI8_CHEMY 
ID   M7CJI8_CHEMY            Unreviewed;       494 AA.
AC   M7CJI8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   31-JUL-2019, entry version 34.
DE   SubName: Full=Acetylcholine receptor subunit gamma {ECO:0000313|EMBL:EMP41197.1};
GN   ORFNames=UY3_01563 {ECO:0000313|EMBL:EMP41197.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudines; Cryptodira; Durocryptodira; Americhelydia;
OC   Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP41197.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z.,
RA   Li C., White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y.,
RA   Zheng Y., Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M.,
RA   Li Q., Wang J., Zhang H., Yu L., Shigenobu S., Wang J., Liu J.,
RA   Flicek P., Searle S., Wang J., Kuratani S., Yin Y., Aken B., Zhang G.,
RA   Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield
RT   insights into the development and evolution of the turtle-specific
RT   body plan.";
RL   Nat. Genet. 45:701-706(2013).
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane {ECO:0000256|SAAS:SAAS00569352}; Multi-pass membrane
CC       protein {ECO:0000256|SAAS:SAAS00569352}. Cell membrane
CC       {ECO:0000256|SAAS:SAAS00569391}; Multi-pass membrane protein
CC       {ECO:0000256|SAAS:SAAS00569391}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. {ECO:0000256|RuleBase:RU000687,
CC       ECO:0000256|SAAS:SAAS00978283}.
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DR   EMBL; KB497182; EMP41197.1; -; Genomic_DNA.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
DR   GO; GO:0030054; C:cell 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; 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; 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   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   3: Inferred from homology;
KW   Cell junction {ECO:0000256|SAAS:SAAS00458005};
KW   Cell membrane {ECO:0000256|SAAS:SAAS00458000};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031443};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00081591};
KW   Ion channel {ECO:0000256|RuleBase:RU000687,
KW   ECO:0000256|SAAS:SAAS00458066};
KW   Ion transport {ECO:0000256|RuleBase:RU000687,
KW   ECO:0000256|SAAS:SAAS00457919};
KW   Ligand-gated ion channel {ECO:0000256|SAAS:SAAS00172123};
KW   Membrane {ECO:0000256|SAAS:SAAS00978300, ECO:0000256|SAM:Phobius};
KW   Postsynaptic cell membrane {ECO:0000256|SAAS:SAAS00081626};
KW   Receptor {ECO:0000256|SAAS:SAAS00172128, ECO:0000313|EMBL:EMP41197.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW   Synapse {ECO:0000256|SAAS:SAAS00103537};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00978734,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00978768,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU000687,
KW   ECO:0000256|SAAS:SAAS00081549}.
FT   TRANSMEM    216    238       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    250    270       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    282    305       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    458    480       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       53    215       Neur_chan_LBD. {ECO:0000259|Pfam:
FT                                PF02931}.
FT   DOMAIN      222    475       Neur_chan_memb. {ECO:0000259|Pfam:
FT                                PF02932}.
FT   REGION      372    398       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    376    395       Pro-rich. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   494 AA;  55257 MW;  4CBDB5673DDD7A14 CRC64;
     MSGPRVNSRP HSEGPYHPSA AFLFFCPRRS NLQARHPQTP ASAAENFGRT VSEWVDYRLN
     YSNSEFKGIR SLRVPSDMVW LPDIVLENNI DGQFEIAYYA NVLVYPGGAM YWLPPAIYRS
     TCVIEVTYFP FDWQNCSLVF QSQTYSANEV ELQLSINEKT ARPFDEIDID PAAFTENGEW
     VIRHRPAWKV LHPELGREAL GFQEIRFSLI IQRKPLFYII NIIVPCVLIS SLVVLVYFLP
     AQAGGQKCTL SISVLLAQTV FLFLIAQKVP ETSLSVPLIG KYLMFVMGVA TLIVMNCVIV
     LNVSLPTPNT HCMSERLKHV FLEVLPRYLG SALEPMGDPW AAPPARRRSS FAIMLKAEEY
     ILKKPRSEIL GRASGRAPPG PPPVVRDPPP PHPTARETQY GVDVGVTSTL YKNLANAAPE
     IRACVEACTF ITETTREQNA SNAAMENWVL IGKVIDKLCF CAAILLFTIG TLSIFLMGHF
     NQVPDDPFPL QPDP
//
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