CAC1A_APIME
ID CAC1A_APIME Reviewed; 1904 AA.
AC C9D7C2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Voltage-dependent calcium channel type A subunit alpha-1;
DE AltName: Full=Cacophony protein;
GN Name=CAC;
OS Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=7460;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yang Z., Qiao M., Jin Y.;
RT "Coding region for CAC.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC of calcium ions into excitable cells and are also involved in a variety
CC of calcium-dependent processes, including muscle contraction,
CC neurotransmitter release, gene expression, cell motility, cell division
CC and cell death. {ECO:0000250|UniProtKB:O00555,
CC ECO:0000250|UniProtKB:P91645}.
CC -!- SUBUNIT: Interacts with CATSPER1 and CATSPER2, leading to suppress T-
CC type calcium channel activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O00555}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:O00555}.
CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids at every third position.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1I subfamily. {ECO:0000305}.
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DR EMBL; GQ202019; ACV86997.1; -; mRNA.
DR RefSeq; NP_001159376.1; NM_001165904.1.
DR AlphaFoldDB; C9D7C2; -.
DR SMR; C9D7C2; -.
DR STRING; 7460.GB51897-PA; -.
DR PaxDb; C9D7C2; -.
DR EnsemblMetazoa; NM_001165904; NP_001159376; GeneID_408764.
DR GeneID; 408764; -.
DR KEGG; ame:408764; -.
DR CTD; 12285; -.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; C9D7C2; -.
DR PhylomeDB; C9D7C2; -.
DR Proteomes; UP000005203; Unplaced.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 2.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR SMART; SM01062; Ca_chan_IQ; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Calcium channel; Calcium transport; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..1904
FT /note="Voltage-dependent calcium channel type A subunit
FT alpha-1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000404525"
FT TOPO_DOM 30..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..187
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..225
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..259
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..283
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..322
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..419
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..444
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..587
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 588..602
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..622
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 623..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 631..649
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 650..658
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 659..677
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 678..696
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..716
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 717..769
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 770..794
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..895
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 896..914
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 915..930
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 931..950
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 951..962
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 963..981
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 982..994
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 995..1013
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1014..1032
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1033..1052
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1053..1141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1142..1166
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1167..1221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1222..1250
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1251..1255
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1256..1275
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1276..1283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1284..1302
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1303..1309
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1310..1328
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1329..1347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1348..1367
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1368..1431
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1432..1456
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1457..1904
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 155..447
FT /note="I"
FT REPEAT 554..797
FT /note="II"
FT REPEAT 890..1177
FT /note="III"
FT REPEAT 1214..1470
FT /note="IV"
FT DOMAIN 1476..1511
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1430..1471
FT /note="Phenylalkylamine binding"
FT /evidence="ECO:0000250"
FT REGION 1652..1694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1710..1788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1870..1904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1754..1768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1772..1787
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1890..1904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1489
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1491
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1493
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1495
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT SITE 402
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 748
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1117
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1405
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 993
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1904 AA; 215891 MW; CBE8C7AE704FF84B CRC64;
MLGGVGGRHM STRRRGSSPL VRGGAGLTGY AGPGASGNSN DVAAIPPDMQ RYAGRRRRAV
TTSDHKSCAL VQTRIKLGDI MLAAQEAAQR DPGYASQYRR RPRLAGLSFG DWTSFGGEVP
GLVDMAPGRD QGGGAGGGGG GGKGTTSLFI LSEDNCIRKH TRFIIEWPPF EYAVLLTIIA
NCVVLALEEH LPKQDKTILA QKLEATEIYF LGIFCVEASL KILALGFVLH RGSYLRNIWN
IMDFFVVVTG FITAFSQGIE LDMDLRTLRA IRVLRPLKLV SGIPSLQVVL KSIIKAMAPL
LQIGLLVLFA IVIFAIIGLE FYSGTLHKTC YSIRDINVIV KEGEQASPCN TDNKSEAPFG
AHVCDANIST CMDHWEGPNF GITSFDNIGF AMLTVFQCIT MEGWTAILYW TNDALGSTYN
WIYFIPLIVL GSFFMLNLVL GVLSGEFAKE REKVENRQSF LKLRRQQQLE HELYCYLNWI
CKAEEVILAE ERTTEEEKKH ILEGRKRAEA KKKKLGKSKS TDTEEEEGDD DQDDGELSSS
TKEKGPCKQF WLAEKRFRYW IRKSVKSQKF YWFVIVLVFF NTVCVAVEHY GQPQWLTDFL
YFAEFVFLAL FMLEMFIKVY ALGPRTYFDS SFNRFDCVVI SGSIFEVIWS EVKSGSFGLS
VLRALRLLRI FKVTKYWKSL RNLVISLLSS MRSIISLLFL LFLFILIFAL LGMQLFGGQF
NFDSGTPPTN FNTFPIALLT VFQILTGEDW NEVMYQGIES QGGHKKGMIY SLYFIVLVLF
GNYTLLNVFL AIAVDNLANA QELSAAENEE EEEDKQKQAQ EIEKEIQSLQ NPKDGGAPKV
EICPPNGKGG KQSSEEEKKQ DEDDDTGPKP MLPYSSMFIL SPTNPVRRAA HWVVNLRYFD
FFIMVVISLS SIALAAEDPV WEDSPRNEVL NYFDYAFTGV FTVEMILKII DLGIILHPGS
YLREFWNIMD AVVVICAAVS FAFDMTGSSA GQNLSTIKSL RVLRVLRPLK TIKRVPKLKA
VFDCVVNSLK NVINILIVYI LFQFIFAVIA VQLFNGKFFY CSDESKYTQQ DCQGQYFVFE
DGALLPEPKK REWQSQFFHY DNVMAAMLTL FAVQTGEGWP QILQNSMAAT YEDKGPIQNF
RIEMSIFYIV YFIVFPFFFV NIFVALIIIT FQEQGEAELQ DGEIDKNQKS CIDFTIQARP
LERYMPKERN SVKYKIWRIV VSTPFEYFIM GLIVLNTVLL MMKFHRQSDA YKNTLKYMNM
CFTGMFTVEC ILKIAAFGVR NFFKDAWNTF DFITVIGSIV DALVIEFGEN FINVGFLRLF
RAARLIKLLR QGYTIRILLW TFVQSFKALP YVCLLIAMLF FIYAIIGMQV FGNIALDADT
SITKHNNFQS FIQGLMLLFR CATGEAWPNI MLSCVKGRPC DAKAGKQEGG CGSNIAYAYF
VSFIFFCSFL MLNLFVAVIM DNFDYLTRDS SILGAHHLDE FVRIWAEYDP NATGKIHYTE
MYDMLKNMDP PLGFGNKCPN RLAYKKLIRM NMPVDVDLKV NFTTTLFALI RENLNIKVRR
ASERNQANEE LRDTIRSIWP LQAKKMLDLL IPRNEEIGRG KMTVGKIYVC LLILESWRTT
RFGQIESAGQ PIMELQDVVV SDSRAGSLES LTHTGKRLHP PVQPVRHPSR SPSLRHSPGR
PGYDHHGHYY HEGPGFSDTV SNVVEIQRHT HHPHPSQYNH RHRMRGPWSA STSPARTPSP
IHHIDRGRHY GTTSLEQRSR SPSPIGGRQP PHTHQHYHRH HPHQHSYPVL VTRRGRGRRL
PPTPNKPSTL QLKPANINFP KLNASPTHGS HIHVPIPAGM QHPPPGQHLP PMQPSHCPLS
FEQAVAMGRG GRLLPSPVPN GYKPQPQAKQ RTPRHSDSDE DDWC
