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Database: UniProt
Entry: F1R736_DANRE
LinkDB: F1R736_DANRE
Original site: F1R736_DANRE 
ID   F1R736_DANRE            Unreviewed;      1859 AA.
AC   F1R736;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 3.
DT   20-JUN-2018, entry version 53.
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
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; AL831748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX072561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSDART00000011078; ENSDARP00000022597; ENSDARG00000112226.
DR   ZFIN; ZDB-GENE-091204-7; cacna1fa.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
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; Unplaced.
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:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0050808; P:synapse organization; IMP: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; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
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|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}.
SQ   SEQUENCE   1859 AA;  210345 MW;  6F5A3F9D42EC7D08 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 FYIGTDNYAD DDPLPCAFAG HGRQCYVNGS ECRGKWEGPN
     GGITNFDNFF FAMLTVFQCI TMEGWTDVLY WMNDAIGFEL PWVYFVSLVI FGSFFVLNLV
     LGVLSGEFSK EREKAKARGD FQKLREKQQM EEDLCGYMDW ITQAEDIDEF DEDGNRRVTL
     RDLADKKRGK FGWFSHSNET HGTANQNEPH 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 PLYFFLSIFP LEEGKIQLNV
     ADFAPPKEKI LPIPEGSAFF CLSKTNPIRV GCHTLIHHHI FTNLILVFII LSSISLAAED
     PIRAHSFRNN VLGYADYAFT SIFTVEILLK VLRQKNIFAV SIFSSDLFFS ISLSSSAISV
     VKILRVLRVL RPLRAINRAK GLKHVVQCVF VAIRTIGNIM IVTTLLQFMF ACIGVQLFKG
     KFYRCTDEAK NTPEQCKGTF VVYKDGDVSH PMVRERIWLN SDFNFDNVLM GMMALFTVST
     FEGWPALLYK AIDANGENHG PIYNYRVEIS IFFIVYIIII AFFMMNIFVG FVIITFREQG
     EAEFKNCELD KNQRQCVEYA LKAQPLKLYI PKNPVQYKFW SIINSTGFEY VMFVLILLNT
     VTLAVQHYDQ SKFFSQVMDI LNMVFTGLFT VEMIIKLMAL RLRHYFVDAW NSFDALIVVG
     SVVDIVVTEF SSSEDSSRVS ITFFRLFRVM RLVKLLSKGE GIRTLLWTFV KSLQALPYVA
     LLIAMIFFIY AVIGMQTFGK IAMQDHTQIN RNNNFQTFPQ AVLLLFRCAT GEAWQEIMLA
     SLPGKRCDAE SDFEPGEEFS CGSNIAIVYF ISFFMLCAFL IINLFVAVIM DNFDYLTRDW
     SILGPHHLDE FKRIWSEYDP EAKGRIKHLD VVALLRRIQP PLGFGKLCPH RVACKRLVAM
     NMPLNADGTV TFNATLFALV RTALKIKTDG NPDQENEELR IIIKKIWKRT KPKVLDEVIP
     PPAEEEVTVG KFYATFLIQD YFRKFRKRKE KVGLEEEGNG NPTALQAGLR TLQELGPEMR
     LAMNEDLEEE EEGLDEEQEE DDAHYKVPIT SGFCYVKNPD DKGFKAYDEN TISILKMFSI
     RHGYPEDSTI FQGHRDMYDG HSMRHPVYGN HYGNSYGDGR RTARRRLLPA TPTGRKASFN
     IQCLRRQGSS DDLPIPGTYH QNSPPCRAPS WANTGPRRGR LLYAPLILVE EEGAAGAGGV
     GWYSGPSPYR AYTTLRVPTQ LSPHYSEKRG SADSLVEAVL ISEGLGLYAK DPKFVAFAKR
     EIADACHMTI DEMESAASSE KSQKFMNHTD TGLVYSDEEP IKSHEEEELA DEMTCVTSF
//
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