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Database: UniProt
Entry: A0A140LFX5_DANRE
LinkDB: A0A140LFX5_DANRE
Original site: A0A140LFX5_DANRE 
ID   A0A140LFX5_DANRE        Unreviewed;      1969 AA.
AC   A0A140LFX5;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   20-DEC-2017, entry version 14.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
DE   Flags: Fragment;
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 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:ENSDARP00000142151}.
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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   STRING; 7955.ENSDARP00000084389; -.
DR   Ensembl; ENSDART00000173386; ENSDARP00000142151; ENSDARG00000102773.
DR   ZFIN; ZDB-GENE-030616-135; cacna1da.
DR   GeneTree; ENSGT00830000128247; -.
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; 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: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   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|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
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   TRANSMEM      6     25       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     37     56       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    119    142       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    197    218       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    230    252       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    394    412       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    432    455       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    524    544       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    598    623       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    717    735       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    747    770       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    834    867       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    917    938       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    959    985       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1039   1057       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1069   1089       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1164   1182       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1256   1279       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1413   1447       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      299    319       {ECO:0000256|SAM:Coils}.
FT   COILED     1374   1394       {ECO:0000256|SAM:Coils}.
FT   NON_TER       1      1       {ECO:0000313|Ensembl:ENSDARP00000142151}.
SQ   SEQUENCE   1969 AA;  225181 MW;  3CE00773B50CC8AC CRC64;
     ETVEYAFLII FTIETFLKII AYGLVMHQNA YVRNGWNMLD FVIVVIGLFS VVLEVLTKEG
     GEKEEVGENL SAHGHGGKPG GFDVKALRAF RVLRPLRLVS GVPSLQVVLN SIIKAMVPLL
     HIALLVLFVI IIYAIIGLEL FIGKMHASCY FQGTDILEDE PAPCAVNGHG RTCPINGTLC
     KEGWQGPNGG ITNFDNFMFA MLTVFQCITM EGWTDVLYWM NDAMGLELPW VYFVSLVIFG
     SFFVLNLVLG VLSGEFSKER EKAKARGDFQ KLREKQQLEE DLKGYLDWIT QAEDIDPENE
     EEEEESKRNR VTLASLMEKK KKGFGWFSQS SDTHASMPAS ETESMNTENE KGEDEKATCC
     GPTCQKISKS KFSRRWRRWN RLCRRNCRLA VKSVPFYWLV IILVFLNTLT ISSEHYNQPM
     WLTQVQDVAN KVLLAMFTCE MLVKMYSLGL QAYFVSLFNR FDCFVVCGGI TETILVEFEI
     MSPLGISVFR CVRLLRIFKV TRHWASLSNL VASLLNSMKS IASLLLLLFL FIIIFSLLGM
     QVFGGKFNFD ETQTKRSTFD NFPQALLTVF QILTGEDWNA VMYDGIMAYG GPSSSGMIVC
     IYFIILFICG NYILLNVFLA IAVDNLADAE SLNTDDTKKP DEIDEIEDEA KAGEEDEKDN
     AEEDEEEPDV PAGPRPKISE LVKKEKITPI PEGSAFFIFS NTNPVRVACH KLINHHIFTN
     LILVFIMLSS ASLAAEDPIR NFSARNIILG YFDYAFTAIF TVEIVLKMTT YGAFLHKGAF
     CRNYFNLLDL LVVGVSLVSF GIQSSAISVV KILRVLRVLR PLRAINRAKG LKHVVQCVFV
     AIRTIGNIMI VTTLLQFMFA CIGVQLFKGK FYRCNDEAKS SPEECKGTYI MYKEGDVNQP
     IIQKRHWHNS DFNFDNVLMA MMALFTVSTF EGWPALLYKA IDSNRENMGP IYNYRVEISI
     FFIIYIIIIA FFMMNIFVGF VIVTFQEQGE KEYKNCELDK NQRQCVEYAL KARPLRRYIP
     KNPYQYKFWY VVNSTGFEYI MFVLILLNTI CLAVQHYGQS ELFNYVMDIL NMVFTAVFTV
     EMVLKLIAFK PRHYFTDAWN TFDALIVVGS VVDIAITEVN NTEDSARISI TFFRLFRVMR
     LVKLLSRGEG IRTLLWTFIK SFQALPYVAL LIAMLFFIYA VIGMQVFGKI AMVDHTQINR
     NNNFQTFPQA VLLLFRCATG EAWQEIMLAC MPGKLCDPES DYNPGEEMTC GSSFAIIYFI
     TFYMLCAFLI INLFVAVIMD NFDYLTRDWS ILGPHHLDEF KRIWSEYDPE AKGRIKHLDV
     VTLLRRIQPP LGFGKLCPHR VACKRLVAMN MPLNSDGTVM FNATLFALVR TALKIKTEGN
     LEQANEELRA VIKKIWKRTS MKLLDQVVPP AGDDEVTVGK FYATFLIQDY FRKFKKRKEE
     GLVGVHPAQN NTAIALQAGL RTLHDIGPEI RRAISCDLQD DELVDFIPEE DEEIYRRNGG
     LFGNHINHIN GDPRRSSGHQ TNATQRPLQV QPPPHYVHME QPVGRLGRAN AMAQQNHHRH
     HHHHHHHHHH NNSYNKSPKS TNINLNNANV SSLPNGGHNR YYEHAPANGY PGSYYGEYDK
     PRTPHGQRRR YYETYIRSQG SDRRRPTIRR EEEYEEDRYS GEYYSGEEFY EDDSMLSGDR
     YPNSDQEYET PRGYHHPDSY YEDDEQPLYH DSHRSPKRRL LPPTPQGNRR PSFNFECLRR
     QSSQDDLPHQ RTALPLHLMQ HQVMAVAGLD SSRAHRLSPT RSTRSWASPP PTPASKDRTP
     YYTPLIRVDR PLRDSASSSH SSIRKSSWYT DDPEYQQRNF SPVHLQVPPE YRNQYLQKRG
     SATSLVEAVL ISEGLGRYAK DPKFVAATKH EIADACEMTI DEMESAASHL LNGGITPVVN
     GVNVFPILGH RDYELQDVSA SYSDEEPEPE PRPRYEEDLA DEMICITTL
//
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