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Database: UniProt
Entry: A0A0R3RMG4_9BILA
LinkDB: A0A0R3RMG4_9BILA
Original site: A0A0R3RMG4_9BILA 
ID   A0A0R3RMG4_9BILA        Unreviewed;       471 AA.
AC   A0A0R3RMG4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-SEP-2017, entry version 9.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida;
OC   Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000267401-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000267401-mRNA-1}
RP   NUCLEOTIDE SEQUENCE.
RG   Helminth Genomes Consortium;
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:EEL_0000267401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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}.
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DR   WBParaSite; EEL_0000267401-mRNA-1; EEL_0000267401-mRNA-1; EEL_0000267401.
DR   Proteomes; UP000050640; Genome Assembly.
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; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   Pfam; PF00520; Ion_trans; 3.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
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:UP000050640};
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:UP000050640};
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     12     33       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    160    178       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    190    211       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    223    243       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    343    365       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        7     43       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      159    267       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      284    372       Ion_trans. {ECO:0000259|Pfam:PF00520}.
SQ   SEQUENCE   471 AA;  54652 MW;  B43A5009352D54CC CRC64;
     VNDAVGREWP WIYFVTLVIL GSFFVLNLVL GVLSGEFSKE REKARARGLF QKFREKQQLE
     EDLKGYLDWI NQAEDIEPVN DDEQEDEQQF NGMNFKAFKY WYKALFSYTM RKSDGEELDE
     EADEKTDDAR PSWWKKRLRR MQKLNRRCRR GCRRLVKSQT FYWLVIILVL LNTLVLTTEH
     YKQEPWLDHF QTVANLFFVI LFSMEMILKM YSLGLTTYTT SQFNRFDCFV VISSIVEFVL
     VYFDLMKPLG VSVLRSARLL RIFKVTNNMV HATPDSPVPK LHVFGGKFNF NPMNPKPRAN
     FDTFIQALLT VFQILTGEDW NTVMYNGIAS FGGVGSWGVL VSVYFIVLFI CGNYILLNVF
     LAIAVDNLAD ADSLTNAEKE EEQAGMLLSF ASVAEVEEEV AEDDYEDEKY DENGNEETRD
     DSRIVMEEEE EGGEIITARP RRMSELVTAK QQKPIPKASS LFILSHTNPF R
//
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