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Database: UniProt
Entry: A0A140LFX5_DANRE
LinkDB: A0A140LFX5_DANRE
Original site: A0A140LFX5_DANRE 
ID   A0A140LFX5_DANRE        Unreviewed;      1869 AA.
AC   A0A140LFX5;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 2.
DT   18-JUL-2018, entry version 19.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=cacna1da {ECO:0000313|Ensembl:ENSDARP00000142151,
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:ENSDARP00000142151};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000142151, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000142151,
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:ENSDARP00000142151}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000142151};
RG   Ensembl;
RL   Submitted (MAR-2016) 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
CC       opposite 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}.
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DR   EMBL; BX072561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7955.ENSDARP00000084389; -.
DR   PaxDb; A0A140LFX5; -.
DR   Ensembl; ENSDART00000173386; ENSDARP00000142151; ENSDARG00000113558.
DR   ZFIN; ZDB-GENE-030616-135; cacna1da.
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; Unplaced.
DR   ExpressionAtlas; A0A140LFX5; 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:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0050808; P:synapse organization; IGI:ZFIN.
DR   Gene3D; 1.20.120.350; -; 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; IPR030157; VDCC_L_a1F.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037:SF184; PTHR10037:SF184; 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.
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   Coiled coil {ECO:0000256|SAM:Coils};
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|SAAS:SAAS00085096, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00084820,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00084701,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM     85    104       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    124    144       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    156    175       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    230    253       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    309    330       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    342    364       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    489    507       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    527    551       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    619    638       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    688    710       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    820    838       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    890    916       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    936    966       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1020   1041       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1061   1088       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1140   1160       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1172   1192       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1267   1285       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1359   1382       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1516   1550       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED     1572   1592       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1869 AA;  211551 MW;  B19F8D64DB0018B7 CRC64;
     SNEEEEGGGE AEEEEEEGGE GGGGGDEETL MSTTSSTATQ KKKSQHVKKQ VQGSNQVQRA
     PRALYCLKLN NPIRRAALHL VEWKPFDIFI LLAIFANCVA LGVSKPFPED DSNATNHDLE
     QVEYVFLIIF TIETFLKILA YGLVMHPSSY IRNGWNLLDF VIVIVGLFSV VLETVTHKSG
     ETTSHTPGKP GGLDVKALRA FRVLRPLRLV SGVPSLQIVL NSIMKAMVPL LHISLLVLFV
     IIIYAIIGLE LFIGRMHRTC FFIGTDNYAD DDPLPCAFAG HGRQCYVNGS ECRGKWEGPN
     GGITNFDNFF FAMLTVFQCI TMEGWTDVLY WMNDAIGFEL PWVYFVSLVI FGSFFVLNLV
     LGVLSGEFSK EREKAKARGD FQKLREKQQM EEDLCGYMDW ITQAEDIDEF DEDGNRRVTL
     RDLADKKRGK FGWFSHSNET HGTANKNEPH DPFTPSTALY IDPLNIVCRA LRRWNRCIRR
     NCRTAVKSVT FYWLVLILVF LNTALSASEH YNQPEWLTDV QDIANKVLLS LFTVEMLLKM
     YSLGLQVYFV AFFNRFDCFV VCGGILETVL VEMEIMPPLG ISVLRCVRLL RIFKVTRHWT
     ALSNLVASLL NSMKSIASLL LLLFLFLIIF ALLGMQLFGG KFNFDETQTK RSTFDSFPQA
     LLTCFQILTG EDWNVVMYDG IMAYGGPVFP GMIVCLYFVI LFICGNYILL NVFLAIAVDN
     LAGGDGDNKK NDPSGVSRGL GCQLKGTVLI ELDCDLINSI SLYFFLSIFP LEEGKIQLNV
     ADFAPPKEKI LPIPEGSAFF CLSKTNPIRV GCHTLIHHHI FTNLILVFII LSSISLAAED
     PIRAHSFRNN VLGYADYAFT SIFTVEILLK MTVHGAFLHE GSFCRNWFNL LDLLVVSVSL
     VSFFLHSSAI SVVKILRVLR VLRPLRAINR AKGLKHVVQC VFVAIRTIGN IMIVTTLLQF
     MFACIGVQLF KGKFYRCTDE AKNTPEQCKG TFVVYKDGDV SHPMVRERIW LNSDFNFDNV
     LMGMMALFTV STFEGWPALL YKAIDANGEN HGPIYNYRVE ISIFFIVYII IIAFFMMNIF
     VGFVIITFRE QGEAEFKNCE LDKNQRQCVE YALKAQPLKL YIPKNPVQYK FWSIINSTGF
     EYVMFVLILL NTVTLAVQHY DQSKFFSQVM DILNMVFTGL FTVEMIIKLM ALRLRHYFVD
     AWNSFDALIV VGSVVDIVVT EFSSSEDSSR VSITFFRLFR VMRLVKLLSK GEGIRTLLWT
     FVKSLQALPY VALLIAMIFF IYAVIGMQTF GKIAMQDHTQ INRNNNFQTF PQAVLLLFRC
     ATGEAWQEIM LASLPGKRCD AESDFEPGEE FSCGSNIAIV YFISFFMLCA FLIINLFVAV
     IMDNFDYLTR DWSILGPHHL DEFKRIWSEY DPEAKGRIKH LDVVALLRRI QPPLGFGKLC
     PHRVACKRLV AMNMPLNADG TVTFNATLFA LVRTALKIKT DGNPDQENEE LRIIIKKIWK
     RTKPKVLDEV IPPPAEEEVT VGKFYATFLI QDYFRKFRKR KEKVGLEEEG NGNPTALQAG
     LRTLQELGPE MRLAMNEDLE EEEEGLDEEQ EEDDAHYKVP ITSGFCYKPD DKGFKAYDEN
     TISILKMFSI RHGYPEDSTI FQGHRDMYDG HSMRHPVYGN HYGNSYGDGR RTARRRLLPA
     TPTGRKASFN IQCLRRQGSS DDLPIPGTYH QNSPPCRAPS WANTGPRRGR LLYAPLILVE
     EEGAAGAGGV GWYSGPSPYR AYTTLRVPTQ LSPHYSEKRG SADSLVEAVL ISEGLGLYAK
     DPKFVAFAKR EIADACHMTI DEMESAASSE KSQKFMNHTD TGLVYSDEEP IRSHEEEELA
     DEMTCVTSF
//
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