ID A0A452HVQ6_9SAUR Unreviewed; 484 AA.
AC A0A452HVQ6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000019164.1};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000019164.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000019164.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Forms serotonin (5-hydroxytryptamine/5-HT3)-activated cation-
CC selective channel complexes, which when activated cause fast,
CC depolarizing responses in neurons. {ECO:0000256|ARBA:ARBA00037540}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671,
CC ChEBI:CHEBI:29108; Evidence={ECO:0000256|ARBA:ARBA00036634};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00034430};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC ChEBI:CHEBI:29101; Evidence={ECO:0000256|ARBA:ARBA00036239};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC {ECO:0000256|RuleBase:RU000687}.
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DR AlphaFoldDB; A0A452HVQ6; -.
DR STRING; 38772.ENSGAGP00000019164; -.
DR Ensembl; ENSGAGT00000021838.1; ENSGAGP00000019164.1; ENSGAGG00000014172.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:InterPro.
DR GO; GO:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR CDD; cd19011; LGIC_ECD_5-HT3A; 1.
DR CDD; cd19063; LGIC_TM_5-HT3; 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; IPR008132; 5HT3_rcpt.
DR InterPro; IPR008133; 5HT3_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:SF52; 5-HYDROXYTRYPTAMINE RECEPTOR 3A; 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; PR01709; 5HT3ARECEPTR.
DR PRINTS; PR01708; 5HT3RECEPTOR.
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 Ion channel {ECO:0000256|RuleBase:RU000687};
KW Ion transport {ECO:0000256|RuleBase:RU000687};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Signal {ECO:0000256|RuleBase:RU000687};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000687};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU000687}; Transport {ECO:0000256|RuleBase:RU000687}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT CHAIN 24..484
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT /id="PRO_5022268061"
FT TRANSMEM 248..271
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 283..304
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 310..332
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 458..481
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 41..247
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 254..473
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
SQ SEQUENCE 484 AA; 56157 MW; 762144F5285F257B CRC64;
MIPSALWAFL ALLLFTFRFQ SEAARKGNNR TLNSAKPALL QLSDYLLTHY RKGVRPVQDW
RRTTNVAIDV MVYAILSVDE KNQVLTTYIW YRQHWIDEFL RWNPEDFDNI TQMSLPTQSI
WVPDILINEF VDVGKSPDIP YVYVRYHGEV QNLKPIQVMT ACSLDIYNFP FDVQNCSLTF
TSWLHNIRDI NISLWRQPEL VKFDKSVFMN QGEWELLYVL SHFQEFSVKG SDSYAEMKFY
VVIRRRPLFY AVSLLLPSVF LMVMDIVGFY LPPDSGERVS FKITLLLGYS VFLIIVSDTL
PATAIGTPLI GVYFVVCMAL LVISLTETIL IVRLVHKQDL QPHVPNWVKH LVLERATILL
CIRDRKKFYP SRTQSSDISQ HPENNDSTAR LNHYGCENLR EYERVAGARP LPAQGESSPV
VASILQEISA IRQFLEKRDE FRDIAREWLQ VGYVLDVLLF RVYLVAVLAY SITLGTLWSV
WQYA
//
