ID A0A3P9D1D2_9CICH Unreviewed; 2052 AA.
AC A0A3P9D1D2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1D {ECO:0000313|Ensembl:ENSMZEP00005028174.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005028174.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005028174.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005028174.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; ENSMZET00005029070.1; ENSMZEP00005028174.1; ENSMZEG00005020783.1.
DR GeneTree; ENSGT00940000154839; -.
DR Proteomes; UP000265160; LG20.
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; 2.
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:UP000265160};
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 79..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 472..490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 510..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 541..564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 599..618
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 677..701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 784..802
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 814..837
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 857..880
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 901..934
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 984..1005
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1026..1052
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1095..1120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1132..1156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1242..1260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1334..1357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1491..1525
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1999..2023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1999..2017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 654
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 998
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 2052 AA; 231235 MW; 299DCD9D32139072 CRC64;
MTQGDPEKPN ISSRPPVCTT STPAPVGSLA QKKRQQYAKS KKQGGSTSGR PPRALFCLTL
NNPIRRACIS LVEWKPFDIF ILLSIFANCV ALAIYIPFPG DDSNSTNQEL ETVEYAFLII
FTIETFLKII AYGLVMHQNS YVRNGWNMLD FVIVIVGLFS VVLEMITKDA DSGGQSGGKP
GGFDVKALRA FRVLRPLRLV SGVPSLQVVL NSIIKAMVPL LHIALLVLFV IIIYAIIGLE
LFIGKMHATC YMTETGALAE EEPAPCAISG HGRHCLLNGT VCREGWQGPN NGITNFDNFL
FAMLTVFQCI TMEGWTDVLY WMNDAMGFEL PWVYFVSLVI FGSFFVLNLV LGVLSGEFSK
EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEEEGDEEGK RNPSIPTSET
ESVTTDNHNG EEDKSPCCGP LCQKITKSKC SRQWRRWNRF CRRKCRAAVK SVTFYWLVII
LVFLNTLTIS SEHYNQPDWL TEVQDVANKV LLALFTLEML VKMYSLGLQA YFVSLFNRFD
CFVVCGGIVE TILVELAIMS PLGISVLRCV RLLRIFKVTR HWASLSNLVA SLLNSMKSIA
SLLLLLFLFI IIFSLLGMQL FGGKFNFDET VTKRSTFDNF PQALLTVFQI LTGEDWNTVM
YDGIMAYGGP ASSGMVVCIY FIILFICGNY ILLNVFLAIA VDNLADAESL NTKRCDIAES
KDVCDDGTDN DELPEVPSGP RPQRLSELTI KEKIPPIPEG SAFFIFSSTN PFRVFCHKLI
NHQIFTNLIL VFIMLSSVSL AAEDPIRNFS ARNIILGYAD YVFTSMFTFE IFIKMTAFGA
FLHKGAFCRN YFNLLDLLVV GVSLVSFGIQ SSAISVVKIL RVLRVLRPLR AINRAKGLKH
VVQCVFVAIR TIGNIMIVTT LLQFMFACIG VQLFKGKFYR CTDDAKSSPD ECKGTYILYN
NGDTALPMVK ERIWYNSEFN FDNVLMAMMA LFTVSTFEGW PTLLYKAIDS NRENMGPIYN
YRIEISIFFI IYIIIIAFFM MNIFVGFVIV TFQEQGEKEY KNCELDKNQR QCVEYALKAR
PLRRYIPKNP YQYKFWYVVN STGFEYVMFV LIILNTLCLA IQHHGQSHLF NYAMDILNMV
FTGVFTVEMI LKLIAFKPRN YFADAWNTFD ALIVVGSVVD IAITEINNCV PTTFVQVANT
EDSARISITF FRLFRVMRLV KLLSRGEGIR TLLWTFIKSF QALPYVALLI AMLFFIYAVI
GMQVFGKIAM VDGTQINRNN NFQTFPQAVL MLFRCATGEA WQEIMLACMP GKLCDSESDY
NPGEERTCGS GFAIIYFISF YMLCAFLIIN LFVAVIMDNF DYLTRDWSIL GPHHLDEFKR
IWSEYDPEAK GRIKHLDVVT LLRRIQPPLG FGKLCPHRVA CKRLVAMNMP LNSDGTVMFN
ATLFALVRTA LKIKTEGNLE QANEELRAVI KKIWKRTSMK LLDQVVPPAG DDDVTVGKFY
ATFLIQDYFR KFKRRKEQGL VGRRSWERLN TTLALQAGLR TLHDIGPEIR RAISCDLQEE
GLVDENAEEE EEIYRRNGSL FGNHVNHIGG DQQGSSHPTT VTQRPLQILP FSSAASTEPP
QIVRRASSND REGETELNSS PILCNQLHPT THYPHCNSTC VQSPIPSNAN LNNANVPSLL
SMTIARQQKC LIRSRPSSTR NASSTTTYSK GLRTRYYEAY IRYSSGALYP TIRREERGNG
DSDEERGSGE YFSGEEFHED DIMLSNNECH DDAEGDFDLV SRGDCQSESY CDDDQQPIYQ
DSRASPRKWF LPSPQASNRP TFNFECLRRR NSGDGAPPSP SCTALPLHLM QQHVMAVAGL
DASKIHRLSP TRSMRSWATP PASPVSRDFS PSYTPLIQVS LLSSVKRSSW YTDSQDGPPS
QSHSPSRLHL PAECCSHCLQ KRGSANSLVE AVLISEGLGK YARDPKFVSA TKHEIADACE
MTIDEMESAA SNLLNGTMGN GNTGRKESVG SDSHASANIR DHSIRDYSDE EPYVAVKCEE
DLTDEMICIT SL
//
