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Database: UniProt
Entry: A0A151WY92_9HYME
LinkDB: A0A151WY92_9HYME
Original site: A0A151WY92_9HYME 
ID   A0A151WY92_9HYME        Unreviewed;      2282 AA.
AC   A0A151WY92;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-SEP-2017, entry version 8.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=ALC60_08171 {ECO:0000313|EMBL:KYQ52756.1};
OS   Trachymyrmex zeteki.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
OC   Vespoidea; Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ52756.1, ECO:0000313|Proteomes:UP000075809};
RN   [1] {ECO:0000313|EMBL:KYQ52756.1, ECO:0000313|Proteomes:UP000075809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ52756.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYQ52756.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex zeteki WGS genome.";
RL   Submitted (SEP-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; KQ982656; KYQ52756.1; -; Genomic_DNA.
DR   Proteomes; UP000075809; 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   Complete proteome {ECO:0000313|Proteomes:UP000075809};
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:UP000075809};
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    113    132       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    152    173       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    185    204       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    242    264       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    320    341       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    353    375       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    484    505       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    517    535       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    599    632       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    676    698       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    971    989       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1001   1024       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1044   1067       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1088   1116       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1128   1152       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1252   1275       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1359   1379       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1391   1421       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1442   1470       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1543   1567       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1702   1736       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   2282 AA;  257405 MW;  1DE553CA7B5E3985 CRC64;
     MSAGGDGGSV LGPPARLPGA QPIAATPYIA IPPNAGQQLN VGGAMDATQL ANMQPPPSQT
     GPGAASAVSK SAQKKPVRRG AKPPPDRPVR ALFCLTLTNP VRKLCIKVVE WKAFEYLILM
     TIFANCVALA VYTPYPCSDS NLTNQYLEKI EYVFLVIFTV ECVMKIIAYG FVAHPGAYLR
     NGWNLLDFTI VVIGMVSTVL TILMKEGFDV KALRAFRVLR PLRLVSGLQV VLNSILRAMV
     PLLHIALLVL FVIIIYAIIG LELFSGKMHK TCRHNITDEI MDDPVPCGSG GFQCYQTGAY
     YCSKQFWEGP NYGITNFDNF GLSMLTVFQC ITLEGWTDVL YNIEDAMGSS WQWIYFISMV
     ILGAFFVMNL ILGVLSGEFS KEREKAKARG DFHKLREKQQ IEDDLRGYLD WITQAEDIEP
     ETDEPKMLQD GKTKQQNEIE STDQLEGDEE GIQQESIYKK KKRDLERVNR RMRRACRKAV
     KSQVFYWLII VLVFLNTGVL ATEHYDQPEW LDHFQEITNM FFIVLFSMEM ILKMYSLGFQ
     GYFVSLFNRF DCFVVIGSIT EMILTNTRVM PPLGVSVLRC VRLLRVFKVT KYWRSLSNLV
     ASLLNSIQSI ASLLLLLFLF IVIFALLGMQ VFGGKFNFSD MEEKTRHNFD SFWQSLLTVF
     QILTGEDWNA VMYVGILAYG GVASIGVLAC VYFIILFICD SNADILLNVF LAIAVDNLAD
     AESLTAIEKE AEEEVKYFSY TTSFSLNDTL FDPSIKLMKK YNYTVSRKTL TQKNMQAINS
     STRHRLFVRI VGSCRARSNK SEGFLRRMCS CCNSRSYAKQ RNFTCKEKNK SRSGSPARDE
     VSGEAGDDGG EGTGGEDEGA GTDLEHDPNE TMEDYEAALD TETSEKSEDM NTHKVRLNVE
     SDEEVEEEEE EEDEPEEMQD EEPEVTARPR RMSEYNTTTK KEPIPAGSAF FIFSSTNRFR
     VFCHWFCNHS YFSNVILICI MISSAMLAAE DPLRTTSDRN LILNYFDYFF TAVFTIEICL
     KMISYGFIIH EGAFCRSAFN LLDLLVVCAS LVSMTVKAGA FSFIKVLRVL RVLRPLRAIN
     RAKGLKHVVQ CVIVAVKTIG NIVLVTSLLQ FVFAVIGVQL FKYVVKCVIV AIKTIGNIML
     VTYLLQFMFA VIGVQLFKGK FFYCTDASKM TEDECQGTYL EFENSNINRP IVKYREWQQH
     RFHFDNVAKA MLTLFTVSTF EGWPSLLEWS IDSNQEKHGP IHNFRPIVAA YYIIYIIIIA
     FFMVNIFVGF VIVTFQNEGE QEYKNCELDK NQRNCIEFAL KAKPVRRYIP KHRIQYKVWW
     FVTSQPFEYT IFTLIMINTV TLAMKFYRQP QIYTDVLDVL NMIFTAVFAL EFVFKLAAFR
     FKNYFGDAWN VFDFVIVLGS FIDIVYSEVN PGATIISINF FRLFRVMRLV KLLSRGEGIR
     TLLWTFIKSF QALPYVALLI IMLFFIYAVI GMQVFGKIAI DDDTAINRNN NFQSFPQAVL
     VLFRSATGEA WQEIMMDCSS QDSVKCDSNS DELDKNSCGS DIAFPYFISF YVLCSFLIIN
     LFVAVIMDNF DYLTRDWSIL GPHHLDEFIR LWSEYDPDAK GRIKHLDVVT LLRKISPPLG
     FGKLCPHRVA CKRLVSMNMP LNSDGTVLFN ATLFAVVRTS LRIKTEGNID DANAELRAVI
     KKIWKRTSPK LLDQVVPPPG VDDEVTVGKF YATFLIQDYF RRFKKRKEQE MKDGDRDCHN
     TVTLQAGLRT LHEAGPELKR AISGNLEELL DDNPEPMHRR NHSLFGSVWS SMRKGHHFHR
     TKSLKVNSTA AKARNASPTN SIDFLPYASL RRTAVTDVTR QIAQQIVPNI AGGLSDGAMN
     QIGSDLRLAV EENIPLRPLA VFGNPAQQTS YKVVDGSSSG NYLHPNSEYE RPLRFSFLPS
     PSYPACAYAR SCSLQDGIER QLTPPTPPPR RNAPSSSTGT PTMDINESQS PIAVLAKESL
     TSCDLTFQSI NLLTICFPLI NVPVSSHVAI DDCDDEDTST GSGSSDSGKW NPHSEGGVAR
     GTTGKPHVTV LGGRSSKRRA KARRDSAGAA SSSGPGSRTV ANGLKMAQNQ AIAVAGFLAD
     VDSRQWRVCA SCLSHRASSY HGRVSWARES NGSVGAERLS HSMPGSPADR KPNFEVIGSA
     ESLVGRVLVE QGLGKFCDPD FVRYTSREMQ EALDMTREEM DQAAHQLLLQ ERRGQPLTYQ
     LQQGAEQQQL QPWSTQQQTT TGIGYQPLQE QPPSQPVYRQ LHSSSYRRNS NRQQQQQRQS
     PS
//
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