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Database: UniProt
Entry: A0A2K5IA54_COLAP
LinkDB: A0A2K5IA54_COLAP
Original site: A0A2K5IA54_COLAP 
ID   A0A2K5IA54_COLAP        Unreviewed;       529 AA.
AC   A0A2K5IA54;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Neuronal acetylcholine receptor subunit alpha-2 {ECO:0000256|ARBA:ARBA00039992};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000013520.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000013520.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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       Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-2/CHRNA2 sub-
CC       subfamily. {ECO:0000256|ARBA:ARBA00038428}.
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DR   RefSeq; XP_011799979.1; XM_011944589.1.
DR   RefSeq; XP_011799981.1; XM_011944591.1.
DR   AlphaFoldDB; A0A2K5IA54; -.
DR   STRING; 336983.ENSCANP00000013520; -.
DR   Ensembl; ENSCANT00000036433.1; ENSCANP00000013520.1; ENSCANG00000030174.1.
DR   GeneID; 105513661; -.
DR   KEGG; cang:105513661; -.
DR   CTD; 1135; -.
DR   OMA; SSYHWLE; -.
DR   OrthoDB; 5489962at2759; -.
DR   Proteomes; UP000233080; 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; cd19015; LGIC_ECD_nAChR_A2; 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:SF757; NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-2; 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   Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW   Signal {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..26
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   CHAIN           27..529
FT                   /note="Neuronal acetylcholine receptor subunit alpha-2"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT                   /id="PRO_5022266125"
FT   TRANSMEM        266..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        297..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        331..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        503..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          59..264
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          272..520
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
FT   REGION          28..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   529 AA;  59664 MW;  66A2FA9DDAF0DCE6 CRC64;
     MGPSCPAFLS FTKLSLWWLL LTPAGGEEAK RPPPRAPGDP LSSPSPTALP QGGSHTPAED
     RLFKYLFRGY NRWARPVPNT SDVVIVRFGL SIAQLIDVDE KNQMMTTNVW LKQEWSDYKL
     RWNPADFGNI TSLRVPSEMI WIPDIVLYNN ADGEFAVTHM TKAHLFSTGT VHWVPPAIYK
     SSCSIDVTFF PFDQQNCKMK FGSWTYDKAK IDLEQMEQTV DLKDYWESGE WAIVNATGTY
     NSKKYDCCAE IYPDVTYAFV IRRLPLFYTI NLIIPCLLIS CLTVLVFYLP SDCGEKITLC
     ISVLLSLTVF LLLITEIIPS TSLVIPLIGE YLLFTMIFVT LSIVITVFVL NVHHRSPSTH
     TMPRWVRGAL LGCVPRWLLM NRPPPPLELC HPPGLKLSPS YHWLETNVDA EEREVVVEEE
     DRWVCAGHVA PSVGTLCSHG HLHSGASGPK AEAVLQEGEL LLSPRMRKAL EGVHYIADHL
     RSEDADSSVK EDWKYVAMVI DRIFLWLFII VCFLGTIGLF LPPFLAGMI
//
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