ID H2LBF8_ORYLA Unreviewed; 2079 AA.
AC H2LBF8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=cacna1da {ECO:0000313|Ensembl:ENSORLP00000003230.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000003230.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000003230.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000003230.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000003230.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000003230.2};
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: Membrane {ECO:0000256|RuleBase:RU003808}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
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DR Ensembl; ENSORLT00000003231.2; ENSORLP00000003230.2; ENSORLG00000002583.2.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000154839; -.
DR HOGENOM; CLU_000540_0_1_1; -.
DR TreeFam; TF312805; -.
DR Proteomes; UP000001038; Chromosome 5.
DR Bgee; ENSORLG00000002583; Expressed in sexually immature organism and 6 other cell types or tissues.
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; 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:SF11; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1D; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 103..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 522..540
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 560..583
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 652..671
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 724..751
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 821..839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 851..870
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 937..967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1021..1042
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1062..1089
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1141..1161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1173..1193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1298..1316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1390..1413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1547..1581
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1685..1710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1821..1856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1882..1912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..44
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1705
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1821..1850
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1885..1909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 704
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1035
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 2079 AA; 235634 MW; 44A86A09CF72F9B6 CRC64;
MSSNGPAPDP APAAQEAPPS STPAPAPAPA PKAPPAPPVP HAPATSTIPV GALAQKKRQQ
YAKSKKQGSN ANSRPQRALF CLNLNNPIRR ACISLVEWKP FDIFILIAIF ANCMALAVYI
PFPEDDSNSI NHDLETVEYA FLIIFTIETF LKIIAYGLVM HQNAYVRNGW NMLDFVIVVI
GLFSVVLELL TKEEPKVEGD GANNHPSMHG HGGKPGGFDV KALRAFRVLR PLRLVSGVPS
LQVVLNSIIK AMVPLLHIAL LVLFVIIIYA IIGLELFIGK MHATCYMPGS DLIAEEEPAP
CAISGHGRQC PINGTECREG WHGPNNGITN FDNFLFAMLT VFQCITMEGW TDVLYWVNDA
IGFETPWIYF VSLIILGSFF VLNLVLGVLS GEFSKEREKA KARGDFQKLR EKQQLEEDLK
GYLDWITQAE DIDPDNEDEA DEGKRNRVTL ADLTEKKKGR FGWFSQSSDT HASVPASETE
SVNTENQNGE DEKTPCCGPL CRRWRRWNRF CRRKCRLAVK SVPFYWLVII LVFLNTLTIS
SEHYNQPLWL TQVQDVANKV LLALFTCEML VKMYSLGLQA YFVSLFNRFD CFVVCGGITE
TILVELEIMS PLGISVFRCV RLLRIFKVTR HWQSLSNLVA SLLNSMKSIA SLLLLLFLFI
IIFSLLGMQV FGGKFNFDET QTKRSTFDNF PQALLTVFQI LTGEDWNAVM YDGIMAYGGP
SSTGMIVCFY FIILFICGNY ILLNVFLAIA VDNLADEDEE EFEDNAVEEE DPDVPSGPRP
VISDLVKKEK ITPIPEGSAF FIFSNTNPVR VFCHKLINHH IFTNLILVFI MLSSVSLAAE
DPIRNLSARN IVLGYADYVF TSMFTFEIVL KMTTYGAFLH KGAFCRNYFN LLDLLVVGVS
LVSFGIQSSA ISVVKILRVL RVLRPLRAIN RAKGLKHVVQ CVFVAIRTIG NIMIVTTLLQ
FMFACIGVQL FKGKFYRCTD EAKSSQEVCK GTYIVYKDGD VNQPTMQRRV WHNSDFNFDN
VLMAMMALFT VSTFEGWPAL LYKAIDSNRE NFGPIYNYRV EISIFFIIYI IIIAFFMMNI
FVGFVIVTFQ EQGEKEYKNC ELDKNQRQCV EYALKARPLR RYIPKNPYQY KFWYVVNSTG
FEYIMFVLIM LNTLCLAVQH YGQSALFNYV MDILNMVFTT VFTVEMFLKL IAFKPRLCVP
KKDRMLGYFG DAWNVFDALV VIGSIVDIVL SEIDVSKCGC CSHPTETPQV DEMGNTEDSA
RISITFFRLF RVMRLVKLLS RGEGIRTLLW TFIKSFQALP YVALLIAMLF FIYAVIGMQV
FGKIAMVDGT QINRNNNFQT FPQAVLLLFR CATGEAWQDI MLACMPGKLC DPESDYNIGE
EMTCGSGFAI VYFITFYMLC AFLIINLFVA VIMDNFDYLT RDWSILGPHH LDEFKRIWSE
YDPEAKGRIK HLDVVTLLRR IQPPLGFGKL CPHRVACKRL VAMNMPLNSD GTVMFNATLF
ALVRTALKIK TEGNLEQANE ELRAVIKKIW KRTSMKLLDQ VVPPAGDDEV TVGKFYATFL
IQDYFRKFKK RKEEGLVGAH PSQNNTAIAL QAGLRTLHDI GPEIRRAISC DLQDDDLVDF
IPEEDEEIYR RNGGLFGNHL MNGGHRRSNG HQTNATQRPL QVQPPPHYAH MEQPVGRLSR
ANAMSHPNHR HHHHHHHHRH HNSYGKSPKS TNINLNNANM SSLPNGGHHR YYDHAPPNGY
LGLHRSYYDY IKPRTPQGQR SHRGDGRHPT ICREEEFDED RFSGEYYSGE EFYEHDSMLS
GDRYPAFIWI LRYQNSDTEY ETPKGYHHPD SYYDDDEQPL YHDSRRSPKR RLLPATPQGT
FMPVSLSCTA FSVMAVAGLD SSRAHRLSPT RSTRSWATPP ATPASKDQSP YYTPLIRVDR
PQRDSVSGSQ VSVRKSSWYT DDPEFSQRAY SPVHLQVPPE YHNQYHQKRG SATSLVEAVL
ISEGLGRYAR DPNFVAATKH EIADACEMTI DEMESAASHL LNGGMAPGMN GVNVFPFLTQ
RDYEVQDAGA NYSDEDPETE PRAPYEEDLA DEMICITTL
//
