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Database: UniProt
Entry: E7F278_DANRE
LinkDB: E7F278_DANRE
Original site: E7F278_DANRE 
ID   E7F278_DANRE            Unreviewed;      2346 AA.
AC   E7F278;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   25-OCT-2017, entry version 62.
DE   RecName: Full=Voltage-dependent N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=cacna1bb {ECO:0000313|Ensembl:ENSDARP00000084400,
GN   ECO:0000313|ZFIN:ZDB-GENE-090514-4};
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:ENSDARP00000084400, ECO:0000313|Proteomes:UP000000437};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000084400}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000084400};
RG   Ensembl;
RL   Submitted (APR-2011) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000084400, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000084400,
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-1B
CC       gives rise to N-type calcium currents. N-type calcium channels
CC       belong to the 'high-voltage activated' (HVA) group and are blocked
CC       by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin-
CC       IIIA (omega-Aga-IIIA). They are however insensitive to
CC       dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA).
CC       Calcium channels containing alpha-1B subunit may play a role in
CC       directed migration of immature neurons.
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:ENSDARP00000084400}.
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DR   EMBL; CR392036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU972453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FP015973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PaxDb; E7F278; -.
DR   Ensembl; ENSDART00000089967; ENSDARP00000084400; ENSDARG00000079295.
DR   ZFIN; ZDB-GENE-090514-4; cacna1bb.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; E7F278; -.
DR   OMA; FREDNLI; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Reactome; R-DRE-112308; Presynaptic depolarization and calcium channel opening.
DR   Proteomes; UP000000437; Chromosome 21.
DR   Bgee; ENSDARG00000079295; -.
DR   ExpressionAtlas; E7F278; 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   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005447; VDCC_N_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF161; PTHR10037:SF161; 2.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01631; NVDCCALPHA1.
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     89    106       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    126    146       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    158    176       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    213    235       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    289    310       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    322    344       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    476    495       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    501    519       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    601    623       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    679    701       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1109   1127       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1147   1167       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1240   1262       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1310   1331       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1352   1379       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1433   1453       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1465   1488       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1558   1580       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1646   1670       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1820   1854       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      697    724       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2346 AA;  265110 MW;  98308FDC93250D77 CRC64;
     MARFGDDLPT RYGGPAGAGR GGARAGGPSG GQRMYKQSMA QRARTMALYN PKQTKQNCFT
     VNRSLFIFSE DNVIRKYAKR ITEWPPFEYL ILTTIIANCI VLALEQHLPA LDKTPMSERL
     DDTEPYFIGI FCFEAGIKII ALGFVFHKDS YLRNGWNIMD FVVVVTGILT TVGSQFDLRT
     LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAIVMFAII GVEFYMGKFH
     FTCFKVDTGE KAVDYPCGAE PPSRSCPVGT NCTEYWKGPN FGITNFDNIL FAILTVFQCI
     TMEGWTDVLY HTNDAAGNTW NWLYFIPLII IGSFFMLNLV LGVLSGEFAK ERERVEKRQE
     FLKLRRQQQI ERELTGYLEW ICKAEEVLLA EEDQNAEEKS PLDVLKRTKS RKGRNDLISA
     EEGDEHFTDI SSVAPPGSPF ARASLKSSKN DSSSYFRRKE KRIRFFIRRM VKAQSFYWIV
     LCLVGLNTMC VAIVHYDQPE WLTKALYLAE FVFLGLFLTE MTLKMYGLGP RNYFHSSFNC
     FDFGVIVGSI FEVIWAAIQP GASFGISVLR ALRLLRIFKV TKYWNSLRNL VVSLLNSMKS
     IISLLFLLFL FIVVFALLGM QLFGGQFNFE DETPTTNFDS FPAAIMTVFQ ILTGEDWNAV
     MYHGIESQGG VRGGMFSSVY FIVLTLFGNY TLLNVFLAIA VDNLANAQEL TKDEEQQEEA
     AKKSLALQKA MEVKEVSPMS AANISIAAFV KQNRDAISRR SSVCSVHSPK EQQRSLQKLS
     IWEQRTNQLR RHNLRSSSEA LYNELEPEER LRVSSALHLR PDMKTHHDRP LVVEHRDSVD
     NLRSDKDGDT SEGQPASNHQ RKYHKCRGEN GDTGEGRLHR HHSQNRENQG GLERSNSQDG
     GQRNHHRSSG SPEEGIGIEE REHRHHHSRR PREVNGNGNG VIGNGGRGER IRGHREGEGG
     NGERRRHRPR VKAQSTLDGD ECRENGGKLY SGTQKYRSRP TETDSLTTSP LQSPSEEKPE
     DKDNLKNSTR VGPSGVNIPV TITAPPGETT VIPMNNIDGD SLLLNEEKKD LDELNQNAPK
     HILPYSSMFV FGPTNPVRRL CHYVVNLRYF EMCILTVITM SSIALAAEDP VQAHAPRNDV
     LKYLDYVFTG VFTFEMVIKM IDLGLLLHPG SYFRDLWNIL DFIVVSGALV AFACSGTKGK
     DINTIKSLRV LRVLRPLKTI KRLPKLKAVF DCVVNSLKNV LNILIVYILF MFIFAVIAVQ
     LFKGKFFHCT DESKALEKDC RGQFLEYGSD GVAMTQPREW KKYDFHYDNV LWAFLTLFTV
     STGFSFALFV LKHSVDATYE DQGPSPGYRM ETSIFYVVYF IVFPFFFVNI FVALIIITFQ
     EQGDKAMSEC SLEKNERACI DFAINAKPLT RYMPQDKNSY QYKMWKFVVS TPFEYSILTM
     IAINTVVLMM KFHGAPKPYE DMLKWLNIIF TALFTLECVL KVIAFGPLNY LKEAWNIFDF
     VTVLGSITDI LVTEIKKDKR INLSFLRLFR AARLIKLLRQ GYTIRILLWT FVQSFKALPY
     VCLLIAMLFF IYAIIGMQVF GNIALNNEDS AINIHNNFRT FFQALMLLFR SATGEAWHEI
     MLACLSERYC DIESGYSGKE CGSDFAYFYF VSFIFLCSFL MLNLFVAVIM DNFEYLTRDA
     SILGPHHLDE FIRVWAEYDP AACGRMSYLD MYEMLRHMSP PLGLGKKCPP RIAYKRLVRM
     NMPIAEDNTV HFTSTLMALI RTALEIKLAS GVLAQRICDA ELRKEINKIW PSLSSKTVDL
     LVTPHKLCFF FFFFCGFLVN NELTVGKVYA ALMIFDYYKQ NRAKRLQQQQ AAPGTQSKVG
     VLFRPMLPLT HLHDQEPLVP KGPPPSHLDI TPQSDATPTS FHLTNGDAVQ SQSSAMKKSP
     SGGPSQEVTQ ETNRRPIQRG QSEDVPNTYR SQELVEMTDM ENDSDVGGYH VLEGHGRAAS
     MPRLNAGFQR SHLRHTAGAY LAPIADVSPM RRSTSSLTPQ RGAREVNLSE YDLERPRMSP
     SQTFAQDRER ERVHHHHHHH HHRCQRRRDK KHKSLDRAIS EEQPPPAVFC TTADPNTEST
     PRERARERDR GRSHERKHHS SSAAERKQRY YSCDRYGSHE HGHSLSAGPS RSTSPGEPHD
     RLKQGINAAK GSSVGHTSGT STPCRGRRQL PQTPLTPRPA VAYKTANSSP VQLNTAQSTG
     PCPARLSRGL SEHDTLLSGS IHRQSPVPVT RIGSDPSLGP LQQDSHLSEA EDFHDALSTY
     GTGRSPRTTA IIAHTSSGAT ATSTLLSRSQ SGVPNGYHYS LGVNAAPGLS GRASGSYQET
     ERDDWC
//
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