GenomeNet

Database: UniProt
Entry: A0A4D9E8L9_9SAUR
LinkDB: A0A4D9E8L9_9SAUR
Original site: A0A4D9E8L9_9SAUR 
ID   A0A4D9E8L9_9SAUR        Unreviewed;       458 AA.
AC   A0A4D9E8L9;
DT   03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   03-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=LanC-like protein 2 {ECO:0000313|EMBL:TFK04398.1};
GN   ORFNames=DR999_PMT13123 {ECO:0000313|EMBL:TFK04398.1};
OS   Platysternon megacephalum (big-headed turtle).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Platysternidae; Platysternon.
OX   NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK04398.1, ECO:0000313|Proteomes:UP000297703};
RN   [1] {ECO:0000313|EMBL:TFK04398.1, ECO:0000313|Proteomes:UP000297703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DO16091913 {ECO:0000313|EMBL:TFK04398.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TFK04398.1};
RA   Gong S.;
RT   "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TFK04398.1, ECO:0000313|Proteomes:UP000297703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DO16091913 {ECO:0000313|EMBL:TFK04398.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TFK04398.1};
RA   Gong S.;
RT   "The genome sequence of big-headed turtle.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC         ChEBI:CHEBI:17996; Evidence={ECO:0000256|ARBA:ARBA00024167};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic
CC       cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00034104}. Synapse
CC       {ECO:0000256|ARBA:ARBA00034103}. Synaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00034099}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       {ECO:0000256|RuleBase:RU000687}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TFK04398.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QXTE01000139; TFK04398.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4D9E8L9; -.
DR   STRING; 55544.A0A4D9E8L9; -.
DR   Proteomes; UP000297703; Unassembled WGS sequence.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0016594; F:glycine binding; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0022824; F:transmitter-gated monoatomic ion channel activity; IEA:InterPro.
DR   CDD; cd19009; LGIC_ECD_GlyR_alpha; 1.
DR   CDD; cd19060; LGIC_TM_GlyR_alpha; 1.
DR   Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR   Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 1.
DR   InterPro; IPR006028; GABAA/Glycine_rcpt.
DR   InterPro; IPR008127; Glycine_rcpt_A.
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   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945:SF211; GLYCINE RECEPTOR SUBUNIT ALPHA-4; 1.
DR   PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR01673; GLYRALPHA.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR   SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Chloride {ECO:0000256|ARBA:ARBA00023214};
KW   Chloride channel {ECO:0000256|ARBA:ARBA00023173};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR608127-52};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU000687};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU000687};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW   Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW   Reference proteome {ECO:0000313|Proteomes:UP000297703};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU000687};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000687};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU000687};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000687}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   CHAIN           29..458
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT                   /id="PRO_5022248621"
FT   TRANSMEM        256..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        285..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        321..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        429..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          49..256
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          263..359
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
FT   BINDING         238..243
FT                   /ligand="strychnine"
FT                   /ligand_id="ChEBI:CHEBI:90700"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-53"
FT   SITE            297
FT                   /note="Important for obstruction of the ion pore in the
FT                   closed conformation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-51"
FT   DISULFID        173..187
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-52"
FT   DISULFID        234..245
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-52"
SQ   SEQUENCE   458 AA;  52912 MW;  995890DD8532D5A5 CRC64;
     MKTLALGTVS FFVFCLLQEH IPLRLVSGKE EIKSTSTGSG QPMSPSDFLD KLMGKTSGYD
     ARIRPNFKGP PVNVTCNIFI NSFGSVTETT MDYRVNVFLR QQWNDPRLAY REYPDDSLDL
     DPSMLDSIWK PDLFFANEKG ANFHEVTTDN KLLRIFKNGN VLYSIRLTLI LSCPMDLKNF
     PMDIQTCTMQ LESFGYTMND LIFEWLEEQE AVQVAEGLTL PQFILRDEKD LGYCTKYYNT
     GKFTCIEVKF HLERQMGYYL IQMYIPSLLI VILSWVSFWI NMDAAPARVG LGITTVLTMT
     TQSAGSRASL PKVSYVKAID IWMAVCLLFV FAALLEYAAV NFVSRQHKEF MRLRRRQRRQ
     RMEEEVVRES RFYFRGYGLG HCMHVKDGSA VEGPNIYSPP PPTPFLREGE AILRRYVDKA
     KRIDTISRAV FPFTFLVFNI FYWVIYKVLR SEDIHQAP
//
DBGET integrated database retrieval system