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Database: UniProt
Entry: F1R736_DANRE
LinkDB: F1R736_DANRE
Original site: F1R736_DANRE 
ID   F1R736_DANRE            Unreviewed;      2004 AA.
AC   F1R736;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   27-SEP-2017, entry version 49.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=cacna1fa {ECO:0000313|Ensembl:ENSDARP00000022597,
GN   ECO:0000313|ZFIN:ZDB-GENE-091204-7};
GN   Synonyms=si:ch73-289n4.1 {ECO:0000313|ZFIN:ZDB-GENE-091204-7};
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:ENSDARP00000022597, ECO:0000313|Proteomes:UP000000437};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000022597}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000022597};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000022597, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000022597,
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).
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:ENSDARP00000022597}.
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DR   EMBL; CABZ01031006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU571250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU861668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FO082780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PaxDb; F1R736; -.
DR   Ensembl; ENSDART00000011078; ENSDARP00000022597; ENSDARG00000010933.
DR   ZFIN; ZDB-GENE-091204-7; cacna1fa.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; F1R736; -.
DR   OMA; LALVEWK; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Reactome; R-DRE-5576892; Phase 0 - rapid depolarisation.
DR   Reactome; R-DRE-5576893; Phase 2 - plateau phase.
DR   Proteomes; UP000000437; Chromosome 8.
DR   Bgee; ENSDARG00000010933; -.
DR   ExpressionAtlas; F1R736; baseline.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR   GO; GO:0050808; P:synapse organization; IMP:ZFIN.
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   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     45     64       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     84    103       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    115    132       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    190    213       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    269    290       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    302    324       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    468    486       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    506    528       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    598    618       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    675    697       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    797    814       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    834    855       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    867    893       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    913    943       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1038   1065       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1117   1137       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1149   1168       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1246   1264       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1338   1361       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1495   1529       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      709    740       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2004 AA;  225622 MW;  F29523E23D90631C CRC64;
     QKRAGGAKKH TQANKSALRA PRALCCLTLS NPIRMAALAL VEWKPFDIFI LLAIFANCVA
     LGVSKPFPED DSNATNHNLE QVEYVFLVIF TIETFTKILA YGLVMHPSAY IRSGWNLLDF
     IIVIVGLFSV IAEMGGDGQK ADSHHAAGKP GGLDVKALRA FRVLRPLRLV SGVPSLQIVL
     NSIMKAMVPL LHIGLLVMFV IIIYAIIGLE LFIGRMHKTC FYVGTELMVE DDPTPCAFAG
     HGRVCIGNNT DCRGGWEGPN GGITNFDNIF FAMLTVFQCI TMEGWTDVLY WMNDSIGFEL
     PWVYFVSLVI FGSFFVLNLV LGVLSGEFSK EREKAVCRGE LQKAQEKQQM EEDMIGYMDW
     LIEAEDMDED GNKQSHGFNS FIVLTTGAVV AKKKMMKKYG WYKHSEDGGT EHIFIKSDSD
     SEFEAFLDDD NGCCASIMAR LMAISFCEQL YHLNVVMRKN CRVAVKSTNF YWLVLLLVFL
     NTAASASEHY GQPKWLTDIQ ERANKILLAL FTLEMLMKIY SFGFQIYFMA LFNRFDCFVV
     CGGILETVLV EMEVIPPIGI SVLRCVRLLR IFKVTRHWAA LSDLVGSLLN SMKAICSLLL
     LLFLFLIIFA LLGMQLFGGK FNFDETQMKR STFDSFPSAL LTCFQILTGE DWNSVMYDGI
     MAYGGPVFPN MIVCIYFVIL FVCGNYILLN VFLAIAVDNL AGDGGKKKKE EKKEEEEEWE
     DEDEREEDDA GNEMDDWEEN EELRAIEGLE GIGTPMKVES FQPKEKIVPI PDGSSFFVLG
     KKNCLRVACH NLIHHHYFTN FILIFIILSS FSLAAEDPIK THSVRNVMLG YADYVFTTVF
     TIEIMLKMTV YGAFLHQGSF CRNAFNLLDL LVVSVSLTSF FLNSSAISVV KILRVLRVLR
     PLRAINRAKG LKSVIQCVFV AIRTIGNILI VTTLLQFMFA CIGVQLFKGR FYRCTDEAKH
     TPEECKGTFV VFKDGDMNHP MVRERVWENS EFNFDNVLMG MLALFTVSTF EGWPQLLYKA
     IDANAENRGP IYNYRVEISI FFIIYIIIIA FFMMNIFVGF VIITFREQGE AEFKNCELNK
     NQRQCVYYAL KAQPIKIYIP KNPSQLKFWK IINSSQFEYI MFVLILLNTL TLAVQHYEQS
     KLFNSVMDIL NMIFTTLFTV EMIIKLMALR PYHYFIDAWN SFDALIVVGS LVDIMIAEFK
     QGKEGESAKV SITFFRLFRV MRLVKLLSKG EGIRTLLWTF VKSLQALPYV GLLIAMIFFI
     YGVIGMQIFG KIAIDDDTEL NRNNNFQTFF MAVLLLFRCA TGEQWQQIML AALPGHRCDP
     ESDFEAGEEF TCGSNLAYLY FISFFALCAF LIINLFIAVI MDNFEYLTRD WTVLGTHHLD
     EFKRVWSDYD PEATGRIKHL DVVTMLRRIQ PPLGFGKLCP HRVACRRLVA MNVPLYPDGT
     VSFNATLFAL VRTSLKIKTD GPIDQQNEEL RAIIKKIWKR TKPKLLDEVI PPPSGNEVTA
     GKFYASFLIQ DYFKKFRKRK EKERKKKGKD KSASLQAGLR TLQDLAPEMR LAMAMEDEEA
     LEGEMMEDLQ SDSVFSDVPP TPTMSTPRST PMPPHLDQTT VNIELPPRIR NGSLMLDNHF
     KIFHNILYFK FFVSCNTIHQ SKQEPLRNDS TGVCVYPPSP SPDVAMQNGQ VTEGDVVPGG
     HGGATMGGVM TTECVAPVQP INLNGNGYQG NIQDAGNYNG SFPGNGYNGN GTNGTDYPGN
     RCSSNGYSTN GYNGNGYNSN GFNGNGYNNN EYSGNGFAAR RRMLPPTPLG FMLGRKPNFN
     IQCLRRQGSN EDLPVPGTYH QNSPPCRARA QITQTHNSFD SRRSSISSGI SSASWANNQA
     RRGRLLYAPL ILVNEAMWSD TNGSTTLPAS ARPGWLGSAM AGVPQQPRAY TTLRVPSQNS
     PGYIERGSAD SLVESILISE GLGLYAKDRK FVDFAKREIA DACQMTVDEM ENAATDLLCR
     GRAGQPTGRF DEDLSDEMNC VISY
//
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