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Database: UniProt
Entry: A0A0R4IQX8_DANRE
LinkDB: A0A0R4IQX8_DANRE
Original site: A0A0R4IQX8_DANRE 
ID   A0A0R4IQX8_DANRE        Unreviewed;      1933 AA.
AC   A0A0R4IQX8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-2017, entry version 15.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=cacna1da {ECO:0000313|Ensembl:ENSDARP00000137557,
GN   ECO:0000313|ZFIN:ZDB-GENE-030616-135};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000137557, ECO:0000313|Proteomes:UP000000437};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000137557, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000137557,
RC   ECO:0000313|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J.,
RA   Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P.,
RA   Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G.,
RA   Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D.,
RA   Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K.,
RA   Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C.,
RA   Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J.,
RA   Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S.,
RA   Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A.,
RA   Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D.,
RA   Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z.,
RA   Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J.,
RA   Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C.,
RA   Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C.,
RA   Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000137557}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000137557};
RG   Ensembl;
RL   Submitted (NOV-2015) to UniProtKB.
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. The isoform alpha-1C
CC       gives rise to L-type calcium currents. Long-lasting (L-type)
CC       calcium channels belong to the 'high-voltage activated' (HVA)
CC       group. They are blocked by dihydropyridines (DHP),
CC       phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA
CC       (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-
CC       GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).
CC       Calcium channels containing the alpha-1C subunit play an important
CC       role in excitation-contraction coupling in the heart. Binding of
CC       calmodulin or CABP1 at the same regulatory sites results in an
CC       opposit effects on the channel function.
CC       {ECO:0000256|RuleBase:RU003808}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSDARP00000137557}.
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DR   EMBL; BX248521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX571969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01048890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01065553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01065554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01065555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FQ323136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSDART00000168288; ENSDARP00000137557; ENSDARG00000102773.
DR   ZFIN; ZDB-GENE-030616-135; cacna1da.
DR   GeneTree; ENSGT00830000128247; -.
DR   OMA; LIQVERP; -.
DR   Reactome; R-DRE-422356; Regulation of insulin secretion.
DR   Reactome; R-DRE-5576892; Phase 0 - rapid depolarisation.
DR   Reactome; R-DRE-5576893; Phase 2 - plateau phase.
DR   Proteomes; UP000000437; Chromosome 11.
DR   ExpressionAtlas; A0A0R4IQX8; baseline.
DR   GO; GO:0009925; C:basal plasma membrane; IDA:ZFIN.
DR   GO; GO:0016021; C:integral component of membrane; ISS:ZFIN.
DR   GO; GO:0097470; C:ribbon synapse; IDA:ZFIN.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:ZFIN.
DR   GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; IMP:ZFIN.
DR   GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:ZFIN.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:ZFIN.
DR   GO; GO:0050808; P:synapse organization; IGI:ZFIN.
DR   InterPro; IPR031688; CAC1F_C.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005452; LVDCC_a1dsu.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF139; PTHR10037:SF139; 2.
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.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU003808};
KW   Calcium channel {ECO:0000256|RuleBase:RU003808};
KW   Calcium transport {ECO:0000256|RuleBase:RU003808};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21   1933       Voltage-dependent L-type calcium channel
FT                                subunit alpha. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5006451583.
FT   TRANSMEM     82    105       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    160    181       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    193    215       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    357    375       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    395    418       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    487    507       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    561    586       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    680    698       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    710    733       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    797    830       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    880    901       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    922    948       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1002   1020       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1032   1052       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1127   1145       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1219   1242       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1376   1410       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1933 AA;  220948 MW;  9251361D0A9FD0F5 CRC64;
     MLDFVIVVIG LFSVVLEVLT KEGGEKEEVG ENLSAHGHGG KPGGFDVKAL RAFRVLRPLR
     LVSGVPSLQV VLNSIIKAMV PLLHIALLVL FVIIIYAIIG LELFIGKMHA SCYFQGTDIL
     EDEPAPCAVN GHGRTCPING TLCKEGWQGP NGGITNFDNF MFAMLTVFQC ITMEGWTDVL
     YWMNDAMGLE LPWVYFVSLV IFGSFFVLNL VLGVLSGEFS KEREKAKARG DFQKLREKQQ
     LEEDLKGYLD WITQAEDIDP ENEEEEEESK RNRVTLASLM EKKKKGFGWF SQSSDTHASM
     PASETESMNT ENEKGEDEKA TCCGPTCQKI SKSKFSRRWR RWNRLCRRNC RLAVKSVPFY
     WLVIILVFLN TLTISSEHYN QPMWLTQVQD VANKVLLAMF TCEMLVKMYS LGLQAYFVSL
     FNRFDCFVVC GGITETILVE FEIMSPLGIS VFRCVRLLRI FKVTRHWASL SNLVASLLNS
     MKSIASLLLL LFLFIIIFSL LGMQVFGGKF NFDETQTKRS TFDNFPQALL TVFQILTGED
     WNAVMYDGIM AYGGPSSSGM IVCIYFIILF ICGNYILLNV FLAIAVDNLA DAESLNTDDT
     KKPDEIDEIE DEAKAGEEDE KDNAEEDEEE PDVPAGPRPK ISELVKKEKI TPIPEGSAFF
     IFSNTNPVRV ACHKLINHHI FTNLILVFIM LSSASLAAED PIRNFSARNI ILGYFDYAFT
     AIFTVEIVLK MTTYGAFLHK GAFCRNYFNL LDLLVVGVSL VSFGIQSSAI SVVKILRVLR
     VLRPLRAINR AKGLKHVVQC VFVAIRTIGN IMIVTTLLQF MFACIGVQLF KGKFYRCNDE
     AKSSPEECKG TYIMYKEGDV NQPIIQKRHW HNSDFNFDNV LMAMMALFTV STFEGWPALL
     YKAIDSNREN MGPIYNYRVE ISIFFIIYII IIAFFMMNIF VGFVIVTFQE QGEKEYKNCE
     LDKNQRQCVE YALKARPLRR YIPKNPYQYK FWYVVNSTGF EYIMFVLILL NTICLAVQHY
     GQSELFNYVM DILNMVFTAV FTVEMVLKLI AFKPRHYFTD AWNTFDALIV VGSVVDIAIT
     EVNNTEDSAR ISITFFRLFR VMRLVKLLSR GEGIRTLLWT FIKSFQALPY VALLIAMLFF
     IYAVIGMQVF GKIAMVDHTQ INRNNNFQTF PQAVLLLFRC ATGEAWQEIM LACMPGKLCD
     PESDYNPGEE MTCGSSFAII YFITFYMLCA FLIINLFVAV IMDNFDYLTR DWSILGPHHL
     DEFKRIWSEY DPEAKGRIKH LDVVTLLRRI QPPLGFGKLC PHRVACKRLV AMNMPLNSDG
     TVMFNATLFA LVRTALKIKT EGNLEQANEE LRAVIKKIWK RTSMKLLDQV VPPAGDDEVT
     VGKFYATFLI QDYFRKFKKR KEEGLVGVHP AQNNTAIALQ AGLRTLHDIG PEIRRAISCD
     LQDDELVDFI PEEDEEIYRR NGGLFGNHIN HINGDPRRSS GHQTNATQRP LQVQPPPHYV
     HMEQPVGRLG RANAMAQQNH HRHHHHHHHH HHHNNSYNKS PKSTNINLNN ANVSSLPNGG
     HNRYYEHAPA NGYPGSYYGE YDKPRTPHGQ RRRYYETYIR SQGSDRRRPT IRREEEYEED
     RYSGEYYSGE EFYEDDSMLS GDRYPNSDQE YETPRGYHHP DSYYEDDEQP LYHDSHRSPK
     RRLLPPTPQG KNRRPSFNFE CLRRQSSQDD LPHQRTALPL HLMQHQVMAV AGLDSSRAHR
     LSPTRSTRSW ASPPPTPASK DRTPYYTPLI RVDRPLRDSA SSSHSSIRKS SWYTDDPEYQ
     QRNFSPVHLQ VPPEYRNQYL QKRGSATSLV EAVLISEGLG RYAKDPKFVA ATKHEIADAC
     EMTIDEMESA ASHLLNGGIT PVVNGVNVFP ILGHRDYELQ DVSASYSDEE PEPEPRPRYE
     EDLADEMICI TTL
//
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