ID A0A3Q1ERM7_9TELE Unreviewed; 2140 AA.
AC A0A3Q1ERM7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000007596.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000007596.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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, hormone
CC or neurotransmitter release, gene expression, cell motility, cell
CC division and cell death. {ECO:0000256|RuleBase:RU003808}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma, T-tubule
CC {ECO:0000256|ARBA:ARBA00024012}. Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004415}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004415}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651}. Cell projection, dendrite
CC {ECO:0000256|ARBA:ARBA00004279}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003808}. Perikaryon
CC {ECO:0000256|ARBA:ARBA00004484}. Postsynaptic density membrane
CC {ECO:0000256|ARBA:ARBA00034112}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1C subfamily. {ECO:0000256|ARBA:ARBA00024028}.
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DR STRING; 80966.ENSAPOP00000007596; -.
DR Ensembl; ENSAPOT00000004686.1; ENSAPOP00000007596.1; ENSAPOG00000009579.1.
DR GeneTree; ENSGT00940000156127; -.
DR InParanoid; A0A3Q1ERM7; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030315; C:T-tubule; IEA:UniProtKB-SubCell.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 6.10.250.2180; -; 1.
DR Gene3D; 6.10.250.2500; -; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR InterPro; IPR031688; CAC1F_C.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR005451; VDCC_L_a1csu.
DR InterPro; IPR005446; VDCC_L_a1su.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR45628; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR PANTHER; PTHR45628:SF10; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1C; 1.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16885; CAC1F_C; 1.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01630; LVDCCALPHA1.
DR PRINTS; PR01635; LVDCCALPHA1C.
DR SMART; SM01062; Ca_chan_IQ; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR602077-1};
KW Calcium channel {ECO:0000256|ARBA:ARBA00022673,
KW ECO:0000256|RuleBase:RU003808};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU003808};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|PIRSR:PIRSR602077-3};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602077-1};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU003808}.
FT TRANSMEM 33..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 521..540
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 591..618
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..783
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 803..823
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 881..910
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1008..1033
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1084..1102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1114..1135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1246..1264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1338..1362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1496..1530
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 316..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1603..1685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1853..1873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1900..1947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1996..2140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1603..1618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1997..2024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2087..2104
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 571
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 979
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 2140 AA; 239442 MW; 0CA8672A8978C0AA CRC64;
MTIFANCVAL AVYIPFPEDD SNATNSNLER VEYLFLIIFT VEAFLKVIAY GLLFHPNAYL
RNGWNLLDFI IVVVGLFSAI LEQATKGDGA APIGGKAAGF DVKALRAFRV LRPLRLVSGV
PSLQVVLNSI IKAMVPLLHI ALLVLFVIII YAIIGLELFM GKMHKSCFDN HTGAIAEKKA
PCAPDNAYGR HCTENGTQCR GGWEGPNDGI TNFDNFAFAM LTVFQCITME GWTDVLYWMQ
DAMGYELPWV YFVSLVIFGS FFVLNLVLGV LSGEFSKERE KAKARGDFQK LREKQQLEED
LKGYLDWITQ AEDIDPENEE EGMDDDKPRN LSMPASENES VNTDNAHGGD VEGETCCTRL
AIRISKSKFS RYSRRWNRLC RRKCRAAVKS QVFYWLVIFL VFLNTLTIAS EHHQQPQWLT
DVQDIANKVL LALFTGEMLL KMYSLGLQAY FVSLFNRFDS FVVCGGILET ILVETKIMSP
LGISVLRCVR LLRIFKITRY WNSLSNLVAS LLNSVRSIAS LLLLLFLFII IFSLLGMQLF
GGKFNFDETR RSTFDNFPQS LLTVFQILTG EDWNSVMYDG IMAYGGPSFP GMLVCIYFII
LFICGNYILL NVFLAIAVDN LADAESLTSA QKEEEEEKER KKLARLASPE KRHDNEKPPL
EEEKKEKIEL KSITSDGETN TATKINMDDC CGDESEEKNP YPANDYIGDD DDDEPEMPVG
PRPRPLSDIQ LKEKAVPMPE ARAFFIFSHT NKFRVLCHKI VNHNIFTNLI LFFILLSSIS
LAAEDPVKND SFRNQILGYA DHVFTGLFTI EIILKMTAYG AFLHKGSFCR NYFNILDLVV
VSVSLISSGI QSSAINVVKI LRVLRVLRPL RAINRAKGLK HVVQCVFVAI RTIGNIVIVT
TLLQFMFACI GVQLFKGKFY SCSDSSKHTQ ADCRGSYIKY KDGDVGKPEK ADRKWENSAF
NFDDVLQGMM ALFAVSTFEG WPGLLYQAID SHAEDVGPIY NYRVVISIFF IIYIIIIAFF
MMNIFVGFVI VTFQEQGEQE YKNCELDKNQ RQCVEYALKA RPLRRYIPKN PYQYKVWYVV
NSTYFEYLMF TLILLNTICL AMQHHGQTKH FNDAMNILNM LFTGLFTVEM ILKLIAFKPR
GYFSDPWNVF DFLIVIGSII DVILSEINPA DSSSSSSSSS SSSSSSSSSS SHPPVVRPMG
LQNSEENARI SITFFRLFRV MRLVKLLSRG EGIRTLLWTF IKSFQALPYV ALLIVMLFFI
YAVIGMQMFG KIALQDHTQI NRNNNFQTFP QAVLLLFRCA TGEAWQEIML ACSPNRTCEK
GSTHENSTDT EDCGSQFAII YFVSFYMLCA FLIINLFVAV IMDNFDYLTR DWSILGPHHL
DEFKRIWAEY DPEAKGRIKH LDVVTLLRRI QPPLGFGKLC PHRVACKRLV SMNMPLNSDG
TVMFNATLFA LVRTALRIKT EGNLEQANEE LRAIVKKIWK RTSMKLLDQV VPPAGDDEVT
VGKFYATFLI QEYFRKFKKR KEQGLVAKVP PKTALSLQAG LRTLHDIGPE IRRAISGDLT
VEEELDKGLK EPVSAASEDD IFRRTGGLFG NHVNYYNQSD GRGSFPQSFT TQRPLHISQK
GSPCEGESPS HEKLMDSTTF TPSSYSSSGS NANINNANNT GMGGVATQGI SRFPSPSIST
VDGHTGQPLT PILLPRSAWC FPPKRTCFYD TLMRSDSSDS RLPIIRRGEG STEETYDESY
ADDREYHEDD HSLSSDMLVY HDETCKQLTP MEDAEEVEER RGGGGWQSPR RVFLCPTSLG
RRSSFHLECL RRQSRPDVSQ KTAVPLHLVH HQALAVAGLS PLLRRSHSPT LFSRLCSTPP
ASPTGQCSDA SYQRVPSLRL EGSNSHEKLN TSLPSVNCGP WYSDSNGNSR GPSPSPTPSM
SASSQRAPRP VSLTVPSLLG KDSSSLSHGS AGSLVEAVLI SEGLGHFAQD PSFIEATKAE
LADACDMTIE EMEHAANNIL NGNSTTNATS STSSTSQHSP NGNLLPFHTA AAAAAAATTT
THRDRVPSLS PSEGGGESGG SRGSIHGPSS IEERQELLAR GRAREEEEEX EEEEEEEEEE
EDEPAGREEG HHRGSVVIGA ARQRNSGLLE DEDMECVTSL
//
