ID A0A384DC08_URSMA Unreviewed; 741 AA.
AC A0A384DC08;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Neuronal acetylcholine receptor subunit beta-3 {ECO:0000313|RefSeq:XP_008704558.2};
GN Name=CHRNB3 {ECO:0000313|RefSeq:XP_008704558.2};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008704558.2};
RN [1] {ECO:0000313|RefSeq:XP_008704558.2}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008704558.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC extensive change in conformation that affects all subunits and leads to
CC opening of an ion-conducting channel across the plasma membrane.
CC {ECO:0000256|ARBA:ARBA00003328}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034104}. 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}.
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DR RefSeq; XP_008704558.2; XM_008706336.2.
DR KEGG; umr:103677101; -.
DR OrthoDB; 5489962at2759; -.
DR Proteomes; UP000261680; Unplaced.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR CDD; cd19026; LGIC_ECD_nAChR_B3; 1.
DR CDD; cd19064; LGIC_TM_nAChR; 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; 2.
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 NCBIfam; TIGR00860; LIC; 1.
DR PANTHER; PTHR18945:SF75; NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT BETA-3; 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; PR00254; NICOTINICR.
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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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 Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_008704558.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000261680};
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 TRANSMEM 517..540
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 552..570
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 582..604
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 712..737
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 313..515
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 523..729
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT REGION 88..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 83312 MW; 3E29A81D37DE6FD2 CRC64;
MRESWGVCQP GASEEVAVAL SPPSHRPALN LQLSIPKVSS SDAQLGRGTL DGPPWTHLIF
GLPSAIWKSG PHGVLDFVPR GLPCSPPALT QPLERARSDS APCGPAQGRR GRQPSLPAAL
LHRHLLRFGG RAGRRWHFDP ALILRCEARA SFPRPDDLGS QRLQPFPRIP QAPPERSTAR
RPAKRRGPTA VKQEAAQSAV GQHLCGGRGH RGMEPRAQEP SFNPCLLTPP IFGFDPDPFL
YASSAQDAAA AAQEPQQLTE TRTTLRSLPM LCGARRAMDP VRWSPLAQPP VRLLTPARRP
AAAGFSSIAE SEDALLRHLF QGYQKWVRPV LNSNDTIKVY FGLKISQLVD VDEKNQLMTT
NVWLKQEWTD YQLRWNPDEY GGIRSIKVPS ESLWLPDIVL FENADGRFEG SLMTKVIVRW
NGTVVWTPPA SYKSSCTMDV TFFPFDRQNC SMKFGSWTYD GTMVDLVLIN ENVDRKDFFD
NGEWEILNAK GLKGSRRDGV YAYPFITYSF VLRRLPLFYT LFLIVPCLGL SFLTVLVFYL
PSDEGEKLSL STSVLVSLTV FLLVIEEIIP SSSKVIPLIG EYLLFIMVFV TLSIIVTVFV
INVHHRSSST YHPMAPWVKT LFLQKLPALL CMKDHVDRYS FPDKDESQPV VKGKALEKRK
QRRVSEGEAV LVAFLEKAAE SIRYISRHVK KQHFINQVVQ DWKFVAQVLD RIFLWLFLVV
SVTGSVLIFT PALRMWLRSS H
//
