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Database: UniProt
Entry: A0A0V0V216_9BILA
LinkDB: A0A0V0V216_9BILA
Original site: A0A0V0V216_9BILA 
ID   A0A0V0V216_9BILA        Unreviewed;      1703 AA.
AC   A0A0V0V216;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=T09_12799 {ECO:0000313|EMBL:KRX57538.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichocephalida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX57538.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX57538.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX57538.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KRX57538.1}.
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DR   EMBL; JYDN01000100; KRX57538.1; -; Genomic_DNA.
DR   Proteomes; UP000054681; Unassembled WGS sequence.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
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; 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   Complete proteome {ECO:0000313|Proteomes:UP000054681};
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:UP000054681};
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     71     89       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    109    129       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    141    160       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    202    221       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    450    468       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    483    506       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    576    598       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    651    679       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    824    842       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    862    883       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    895    921       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    941    971       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1066   1093       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1136   1162       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1174   1200       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1271   1293       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1369   1390       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1525   1559       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1703 AA;  195456 MW;  19DCEEFDA0D77CB7 CRC64;
     MSAENYTTPS DTTIVDSCLL SSTVAGTTPT TRSKRNNSSY TIERPKRSLF CLDQKNRFRL
     LCIHIVEWKP FEWLILTMIC ANCLALAIYQ PYSGLDSDFR NTILEMLEYV FIFVFTIECL
     LKIVAYGFVM HPGAYLRNAW NILDFVIIVV GNCSTALSWA NLPNVDVKAL RAFRVLRPLR
     LVSGVPSLQI VLNSVLQAMV PLFHVALLVL FVIIIYAIMG LELFCGKLSR TCVHPDTGSI
     VVIGLPLQGG SSSPCGFGHS ARHCSINANC SETKYWPGPN HGITNFDNIG FAMLTVFTCV
     SQEGWTDVMY WVNDAVGNEW PWIYFVSLVV LGSFFVLNLV LGVLSGEFSK EREKARVRGI
     FKKRREKIRF EEELRSYLDW ILQAEDIWDA VGDEATFETV ENNDAKYTSG SRLDWLLGRF
     SRLKCKKLQM LPFYSSKLRR KGRKLIKSQA FYWIVIVLVF LNTFVLTLEH HRQPLWLEEF
     QDYVNICFVI LFALEMLLKM FCLGFYNYFM SLFNRFDCFV VLCSIVEISL TQARVIKPLG
     LSVLRSARLL RLFKVTRYWD SLRNLVASLL NSLRSIVSLL LLLFLFIVIF ALLGMQIFGG
     KFKFDPFGSK PRSNFDSFPQ SLLTVFQILT GEDWNSVMYA GIQSFGGASS IGIVVCVYFI
     VLFVCGNYIL LNVFLAIAVD NLGDNDQSEP ETALPHVNEE TLREQDDEKM IIDNDNIEQE
     EEEEEANFEI QLCNGETQRE NGQFEQLNNN NWSNSDGTKD ETDDATVLNG NNRKTGASLL
     AKDDSFGENC RKASLLHIPP YNSLFIFSPQ NKLRIACAKL IRHAYFKNLV LLCILVSSAL
     LAAEDPLSRH STLNDVLGFF DIFFTSVFTV EIVLKIITFG LVLHEESFCR NAFNLLDLLV
     VAVSLASFGL KSGAISVVKI LRVLRVLRPL RAINRAKGLK HVVQCVIVAV KTIGNILLVT
     FMLQFMFAIV GVQLFKGTFY RCTDSTKTNP QDCRGVFIHY DGGDRTKPVV EFREWVNNDF
     NFDDIRNALI SLFVVGTFEG WPDLLYVAID STEEDSGPVY NYRQAVAIFF IAYIVVIAFF
     MQNIFVGFVI ITFQNEGERE YENCELDKNQ RKCIDFTLNV KPQKRYVPSS QFRYKLWLFV
     TSSYFEYGIL FIIILNTFVL AMRHHHPNPI TEEVLDFLNF IFTSVFAAEV LLKLMAFTIV
     NYFADAWNVF DFIVVLGSVI DIVCSKVGPG ESVISMNFFR LFRVMRLVKL LGRGEGMRTL
     VWTFLKSFQS LPYVVLLIVL LFFIYAVIGM QVFGKIAFDD DTQIHRHNNF RTFYSALLVL
     FRCATGEAWQ NIMLDCSDRP TVLCEKAFLH EDEEASGATT CGTNFAYPYF ISFFILSSCL
     IINLFVAIIM DNFDYLTRDW SILGPHHLEE FVRLWSEFDP DARGRIKHLD VLILLRKISP
     PLGFGDFCPH RIACKKLISM NMSLFPDGTV GFHATLLALV RTNLNIFCDN SIEMANIRLR
     RVIRKVWKKT SESFLDEILP LTTGEDDVTV GKFYATYLIQ DYFLRFKRRR MLEARRMNQT
     PRHGIKVLMA GLREPIHDSA EPHRRYSGNL FADWMKDFEE PQHRRNHILF NGLTNDHQKH
     QRVNNKNFSS AINYKEHFRK KKNVPSLQIN KTTHSTSTPN GHVPQSESDD PQPWRPYPHN
     ACVRLFDLVS RLNKYPYIYR YFI
//
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