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Database: UniProt
Entry: A0A0L7QL51_9HYME
LinkDB: A0A0L7QL51_9HYME
Original site: A0A0L7QL51_9HYME 
ID   A0A0L7QL51_9HYME        Unreviewed;      2238 AA.
AC   A0A0L7QL51;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-SEP-2017, entry version 14.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=WH47_11505 {ECO:0000313|EMBL:KOC59319.1};
OS   Habropoda laboriosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
OC   Apoidea; Apidae; Habropoda.
OX   NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC59319.1, ECO:0000313|Proteomes:UP000053825};
RN   [1] {ECO:0000313|EMBL:KOC59319.1, ECO:0000313|Proteomes:UP000053825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0110345459 {ECO:0000313|EMBL:KOC59319.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Habropoda laboriosa.";
RL   Submitted (JUL-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}.
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DR   EMBL; KQ414934; KOC59319.1; -; Genomic_DNA.
DR   Proteomes; UP000053825; 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; 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   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 5.
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:UP000053825};
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:UP000053825};
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    106    124       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    144    165       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    177    196       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    237    259       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    316    337       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    349    371       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    479    497       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    509    527       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    608    627       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    687    715       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    952    971       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    983   1006       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1081   1106       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1118   1142       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1242   1265       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1319   1337       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1349   1369       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1381   1411       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1432   1460       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1535   1559       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1694   1728       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED     2204   2234       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2238 AA;  250401 MW;  2ED80B071FBB442F CRC64;
     MSAGGDGGSG LGPPELPGAQ PTAATPPILG QHQNHQTAQD GQPAGAQSQT GQALGAGAGA
     AKSTAKRPAR RGGKAPPDRP VRALFCLPLK NPVRKMCIDV VEWKPFEWLI LMTIFANCVA
     LAVYTPYPFG DSNLTNQYLE KIEYIFLVIF TVECVMKIIA YGFVAHPGAY LRNGWNILDF
     SIVVIGMVSI VLTTLMKEGF DVKALRAFRV LRPLRLVSGV PSLQVVLNSI LRAMIPLLHI
     ALLVLFVIII YAIIGLELFS GKMHKTCRHN VTDAIMDEPV PCGPGGYQCD NVGPEYYCSK
     QFWEGPNWGI TNFDNFGLAM LTVFQCVTLE GWTDVLYSIE DAMGSSWQWI YFISMVILGA
     FFVMNLILGV LSGEFSKERE KAKARGDFHK LREKQQIEDD LRGYLDWITQ AEDIEPEADE
     PKMQDGKTKQ QSEMESTDQL EGDEEGVQQE SAWRRKKRDF NRVNRRMRRA CRKAVKSQVF
     YWLIIVLVFL NTGVLATEHY NQPHWLDDFQ EITNMFFIAL FSMEMMLKMY SLGFQGYFVS
     LFNRFDCFVV IGSITEMILT NTHVMPPLGV SVLRCVRLLR VFKVTKYWRS LSNLVASLLN
     SIQSIASLLL LLFLFIVIFA LLGMQVFGGK FNFSELQDKP RHNFDSFWQS LLTVFQASFS
     ASRILTGEDW NAVMYDGIRA YGGVSSFGML ACFYFIILFI CGNYILLNVF LAIAVDNLAD
     AESLTAIEKE AEEEARFPSL VITDAEAVAA ANLDAQSRGN LGKSLSRREI FFGGKVMSIV
     LPLTFNRTRL LVVSSGFKPS RRVREAEKNK SHSASPARDE VSGDEQGDGG EGTGPEDEGG
     GTYLEHDPNE TMEDYEAAVD TETSEKSEDI NTHAKVRLNV ESDEEVEEEE EVEQNEMHGD
     GTDQGVSARP RRMSEFNMAT KTQPIPAGSA FFIFAQNNRV RVFCHWLCNH SYFGNVILVC
     IMISSAMLAA EDPLRASSHR NHILLNFDYL FTTVFTIEIC LKMISYGFII HDGAFCRSAF
     NLLDLLVVCS SLISMSFRET SRCCSFSSGA FSVVKVLRVL RVLRPLRAIN RAKGLKHVVQ
     CVIVAVKTIG NIVLVTSLLQ FVFAVIGVQL FKYVVKCVIV AIKTIGNIML VTYLLQFMFA
     VIGVQLFKGK FFLCTDASKM TKDECQGTYL EFENGNINKP VMKERNWYQN RFHFDDVAKA
     MLTLFTVSTF EGWPTLLDVS IDSNKEDHGP IHNFRPIVAA YYIIYIIIIA FFMVNIFVGF
     VIVTFQNEGE QEYKNCELDK NQRNCIEFAL KAKPVRRYIP KHRIQYKVWW FVTSQPFEYT
     IFTLIMINTV TLAMKFYRQP EIYTEALDVL NMIFTAVFAL EFIFKLAAFR FKNYFGDAWN
     VFDFIIVLGS FIDIVYSEVN PGSTIISINF FRLFRVMRLV KLLSRGEGIR TLLWTFIKSF
     QALPYVALLI IMLFFIYAVI GMQVFGKIAI DDDTSIDRNN NFQSFPQAVL VLFRSATGEA
     WQEIMMDCSA QPGKVKCDPN SDEVNNPSGC GSDIAFPYFI SFYVLCSFLI INLFVAVIMD
     NFDYLTRDWS ILGPHHLDEF IRLWSEYDPD AKGRIKHLDV VTLLRKISPP LGFGKLCPHR
     VACKRLVSMN MPLNSDGTVL FNATLFAVVR TSLRIKTEGN IDDANAELRA VIKKIWKRTS
     PKLLDQVVPP PGGDDEVTVG KFYATFLIQD YFRRFKKRKE QEMKDGDKEC HNTVTLQAGL
     RTLHEAGPEL KRAISGNLEE LADDNPEPMH RRNHSLFGSV WSSMRKGHHN FNRARSLKVN
     STTKASPTNS IDFLPYSSLQ RGGGHDASNQ ITARSHQVVP NVAGGLSDSA MNQMGIDPKL
     TGIEESIPLR PLAVFGNPVQ QQPYHHLPYK VVDGPGSGNY LHPNSEYAID REDGDSSATS
     DYSECGASGG SGGSGVSGGS SGWSNSEKVV VGGRRGGSLR QELASSRCRA RGRLVGKSAP
     SSFRKRETGG SGGGGGGQSS SSTTSASTGF ARTVANGLKL AQTQAIAVAG FLADVDTRHA
     RVCASCLSHR ASYHGRVSWA GESNGSIGAE RLSHSLPGSP ADRKANFEVI GSAESLVGRV
     LVEQGLGKYC DPDFVRYTSR EMQEALDMTR EEMDRAAHQL LLQERRGQPL TYQLQQAADQ
     QWTPSYQQSQ QPTGIGYQPL QEQQPYRSYY HGGGGQAAPA TSDLTTQQQQ QQQQQQQQQQ
     QQQQQQQQQQ QQQQPPPS
//
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