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Database: UniProt
Entry: F1R1T3_DANRE
LinkDB: F1R1T3_DANRE
Original site: F1R1T3_DANRE 
ID   F1R1T3_DANRE            Unreviewed;      2168 AA.
AC   F1R1T3;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   25-OCT-2017, entry version 49.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=cacna1c {ECO:0000313|Ensembl:ENSDARP00000031067,
GN   ECO:0000313|ZFIN:ZDB-GENE-020129-1};
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:ENSDARP00000031067, ECO:0000313|Proteomes:UP000000437};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000031067}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000031067};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000031067, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000031067,
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:ENSDARP00000031067}.
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DR   EMBL; BX248410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX649380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PaxDb; F1R1T3; -.
DR   Ensembl; ENSDART00000028856; ENSDARP00000031067; ENSDARG00000008398.
DR   ZFIN; ZDB-GENE-020129-1; cacna1c.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
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 4.
DR   Bgee; ENSDARG00000008398; -.
DR   ExpressionAtlas; F1R1T3; baseline.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IC:ZFIN.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:ZFIN.
DR   GO; GO:0070509; P:calcium ion import; IMP:ZFIN.
DR   GO; GO:0006816; P:calcium ion transport; IMP:ZFIN.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:ZFIN.
DR   GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR   GO; GO:0003007; P:heart morphogenesis; IMP:ZFIN.
DR   GO; GO:0001822; P:kidney development; IMP:ZFIN.
DR   GO; GO:0003301; P:physiological cardiac muscle hypertrophy; IMP:ZFIN.
DR   GO; GO:0008016; P:regulation of heart contraction; 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; IPR005451; VDCC_L_a1csu.
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   PRINTS; PR01635; LVDCCALPHA1C.
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    138    155       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    175    194       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    206    222       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    278    300       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    362    383       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    395    417       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    538    555       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    575    598       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    667    686       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    737    764       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    908    930       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    950    971       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1029   1058       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1156   1181       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1232   1250       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1262   1285       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1379   1397       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1469   1493       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1627   1661       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      767    793       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2168 AA;  243243 MW;  A77AA30652C4179E CRC64;
     MVNESKNMYI PEDTLENHQG SNYSSPSLAP VPSLNEDEHV GGGGGVLGLA PEHIPTPGAP
     LSWQAAIDAA RQAKLMGTTG APISTASSTQ RKRQHYTKPK KQASTASTRP PRALLCLTLK
     NPIRRACINI VEWKPFEIII LMTIFANCVA LAVYIPFPED DSNATNSNLE RVEYLFLIIF
     TVEAFLKVIA YGLLCHPNAY LRNGWNLLDF IIVVVGLFSA ILEQATKGDG GTSMGGKAAG
     FDVKALRAFR VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH IALLVLFVII IYAIIGLELF
     MGKMHRTCFF YKDGHKGHIA EEKPAPCAPS SAHGRHCSPP NITQCMMGWE GPNDGITNFD
     NFAFAMLTVF QCITMEGWTD VLYWMQDAMG YELPWVYFVS LVIFGSFFVL NLVLGVLSGE
     FSKEREKAKA RGDFQKLREK QQLEEDLKGY LDWITQAEDI DPENDDEGLD DDKPRNLSMP
     ASENESVNTD NAPAGDMEGE TCCTRMANRI SKSKFSRYSR RWNRLCRRKC RAAVKSNVFY
     WLVIFLVFLN TLTIASEHHQ QPEWLTNVQD IANKVLLALF TGEMLLKMYS LGLQAYFVSL
     FNRFDSFVVC GGILETILVE TKIMSPLGIS VLRCVRLLRI FKITRYWNSL SNLVASLLNS
     VRSIASLLLL LFLFIIIFSL LGMQLFGGKF NFDETRRSTF DNFPQSLLTV FQILTGEDWN
     SVMYDGIMAY GGPSFPGMLV CIYFIILFIC GNYILLNVFL AIAVDNLADA ESLTSAQKEE
     EEEKERKKLA RTASPEKRQN SEKPPLEDEK KEEKIELKSI TSDGETPTAT KINIDEYTGE
     DNEEKNPYPV NDFPAGEDDE EEPEMPVGPR PRPLSDIQLK EKAVPMPQAK AFFIFSPSNK
     FRVLCHKIVN HNIFTNLILF FILLSSISLA AEDPVKNDSF RNQILGYADY VFTGIFTIEI
     ILKMTAYGAF LHKGSFCRNY FNILDLVVVS VSLISSGIQS SAINVVKILR VLRVLRPLRA
     INRAKGLKHV VQCVFVAIRT IGNIVIVTSL LQFMFACIGV QLFKGKFFYC TDTSKQTQAE
     CRGAYILYKD GNVGKPEKAQ RSWENSDFNF DDVLQGMMAL FAVSTFEGWP GLLYRAIDSH
     AEDVGPIYNY RVVISIFFII YIIIIAFFMM NIFVGFVIVT FQEQGEQEYK NCELDKNQRQ
     CVEYALKARP LRRYIPKNPY QYKVWYVVNS TYFEYLMFTL ILLNTICLAM QHHGQSQSFN
     KAMNILNMLF TGLFTVEMIL KLIAFKPRHY FVDAWNTFDA LIVVGSVVDI AITEVNPADP
     SSSPPSSVVR PMGLQNTEDN ARISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL
     PYVALLIVML FFIYAVIGMQ MFGKIALRDN SQINRNNNFQ TFPQAVLLLF RCATGEAWQE
     IMLACSPNRP CEKGSEINHS SEDCGSHFAI FYFVSFYMLC AFLIINLFVA VIMDNFDYLT
     RDWSILGPHH LDEFKRIWAE YDPEAKGRIK HLDVVTLLRR IQPPLGFGKL CPHRVACKRL
     VSMNMPLNSD GTVMFNATLF ALVRTALRIK TEGNLEQANE ELRAIVKKIW KRTSMKLLDQ
     VVPPAGDDEV TVGKFYATFL IQEYFRKFKK RKEQGLVAKI PPKTALSLQA GLRTLHDMGP
     EIRRAISGDL TVEEELERAM KETVCAASED DIFRRSGGLF GNHVNYYHQS DGHVSFPQSF
     TTQRPLHISK SGSPGEAESP SHQKLVDSTF TPSSYSSSGS NANINNANNT AIGHRYPKPT
     VSTVDGQTGP PLTTIPLPRP TWCFPNKSSD SSDSRLPIIR REEASTDETY DETFLDERDQ
     AMLSMDMLEF QDEESKQLAP MVEAEVGEER RPWQSPRRRA FLCPTALGRR SSFHLECLRK
     HNRPDVSQKT ALPLHLVHHQ ALAVAGLSPL LRRSHSPTLF TRLCSTPPAS PSGRSGGGPC
     YQPVPSLRLE GSGSYEKLNS SMPSVNCSSW YSDSNGNHSG RAQRPVSLTV PPVTRRDSIS
     LAHGSAGSLV EAVLISEGLG RYAHDPSFIQ VAKQEIAEAC DMTMEEMENA ADNILNANAP
     PNANGNLLPF IQCRDTGSQE SRCSLSLGLS PATGSDGALE AELEESEGAG QRNSPLMEDE
     DMECVTSL
//
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