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Database: UniProt
Entry: A0A087VZJ5_ECHMU
LinkDB: A0A087VZJ5_ECHMU
Original site: A0A087VZJ5_ECHMU 
ID   A0A087VZJ5_ECHMU        Unreviewed;      1635 AA.
AC   A0A087VZJ5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-SEP-2017, entry version 18.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=EmuJ_000140800 {ECO:0000313|EMBL:CDI97618.1};
OS   Echinococcus multilocularis (Fox tapeworm).
OC   Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda;
OC   Cyclophyllidea; Taeniidae; Echinococcus.
OX   NCBI_TaxID=6211 {ECO:0000313|EMBL:CDI97618.1, ECO:0000313|Proteomes:UP000017246};
RN   [1] {ECO:0000313|EMBL:CDI97618.1, ECO:0000313|Proteomes:UP000017246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Java {ECO:0000313|Proteomes:UP000017246};
RX   PubMed=23485966; DOI=10.1038/nature12031;
RA   Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A.,
RA   Sanchez-Flores A., Brooks K.L., Tracey A., Bobes R.J., Fragoso G.,
RA   Sciutto E., Aslett M., Beasley H., Bennett H.M., Cai J., Camicia F.,
RA   Clark R., Cucher M., De Silva N., Day T.A., Deplazes P., Estrada K.,
RA   Fernandez C., Holland P.W., Hou J., Hu S., Huckvale T., Hung S.S.,
RA   Kamenetzky L., Keane J.A., Kiss F., Koziol U., Lambert O., Liu K.,
RA   Luo X., Luo Y., Macchiaroli N., Nichol S., Paps J., Parkinson J.,
RA   Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M., Salinas G.,
RA   Wasmuth J.D., Zamanian M., Zheng Y., Taenia solium Genome Consortium,
RA   Cai X., Olson P.D., Laclette J.P., Brehm K., Berriman M.;
RT   "The genomes of four tapeworm species reveal adaptations to
RT   parasitism.";
RL   Nature 496:57-63(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-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; LN902844; CDI97618.1; -; Genomic_DNA.
DR   GeneDB; EmuJ_000140800.1:pep; -.
DR   Proteomes; UP000017246; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000017246};
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:UP000017246};
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     16     36       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    106    128       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    198    225       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    231    253       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    333    359       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    405    427       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    439    458       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    470    488       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    500    519       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    572    600       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    712    734       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    755    777       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    823    842       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    931    958       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    999   1023       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1043   1062       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1074   1094       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1139   1159       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1233   1257       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1397   1431       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED     1594   1617       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1635 AA;  186293 MW;  282A1AE6895876E6 CRC64;
     MGDYNATNVA LEKTELVFLI IFTTEAVLKI IAYGFVLHPD AYLRNFWNVL DFSIVVIGLG
     SKCLENTKLD VKSLRAFRVL RPLRLVSGLP SLQVVLNSIV TAMVPLFHIF LLVIFLIIIY
     AIIGLELFQS KLHATCYLVQ ENTTYTMMDN PRPCSNSSYS MAFNCSEIGP NYVCRDLPPE
     LGERYVGPED GLVNFDNFLY AMLTVFTCVT MEGWTTFGAY IAAAVGHWWP WIYFVSLILL
     GSFFVMNLVL GVLSGEFTKE KDKTDRKELF RKERQQRREQ QDYENYKEWI EIAGLMDGKS
     VEDQEAANEP TAKSQCCEGM RRLKKFRKRL RRVITAFVKS RQFFALILTF VFLNTIVLVT
     EHHNQPLWLN QFQSKSICTY RLIRTSFPQN RGFQSYICIL SHEDFANVLF VSLFTLEMII
     KMCAYGIQDY FATLFNRYDF FVVVVSILEI ILTYIGVIDP MGLSVLRCAR LLRIFKITHY
     WAGLRGLVNR LLKSIKSVAG LLLLLFLFIL ICSLLGMQWF GGTFNFPNTD KPRSHFDGIA
     QSMITVFQML TGEDWNAVMY NGMRAYKADG PLFAFVVIYF VIVFVVGNYI LLNVFLAIAV
     DNLSDEDEDD EEGGMDDDND VDDHPGSSAA AKKAAEAAVN AKGPLDAYME MNYEEVFAEE
     EEPDDGNLAS KLEQMEINMA NPQTIPPYSA FFIFDPTNKF RIFCHNIVSS PIFTNLVLAC
     ILISSALLCA EDPLNTYSLT NRMIAHGFIM HEGAFLRSMF NLLDLIVVFV ALISFMLENE
     AISAVKILRV LRVLRPLRAI NRAKGLKNVV QCVVTALKSI GNIMLVTVLI EFVFAVIGVQ
     LFKGKYVSCN DPSKLTEQDC KGFFIEYEHG RPADVVERVW THSELNFDNV ANAMLTLFVV
     LTFEGWPPIL YAGIDSNEED MGPLQDHRKY IALYFIIYLI VASFFMVNIF VGFVIVTFQR
     EGEREYKNCE LNKNQRKCIE YALKARPRRR YIPKGHLQYK IWSMVVSRKM EITIFTFIFL
     NTVTLACKHD KMDPTFSSVL DNFNYFFTAV FTVEFILKLS AFSFRHYFGD PWNVIDFIIV
     LGSYIDIIVS KASSETTLKF NINFFRLFRV MRLVKLLSKE ESIRKLLWTF IKSLQALPYV
     ALLIAMLFFI YAVIGMQLFG KISLHQPGLA LGEDGVIHRS NNFRNFFFAL LVLFRSATGE
     SWQEIMLACT PGRKCAVDSE DGSEGMNCGS NLAYPYFITF YLFCSFVIIN LFVAVIMDNF
     DYLTRDWSIL GPHHLDEFVT RWAEYDPEAK GRVRHLDVVT MLGKISPPLG FGSMCPHTRA
     CHKLVQMNMP LQSDGTVFFN ATLFALVRRN LRIKVPEDDE KEKSLDQLNE ELRIVIKKIW
     KRTSPKLLDQ ILPPKELDVV TVGKFYATFL IQNWFREWQK RKMIQKDTRY IPQILAGDRS
     MPHQPTIVGF PRRCSSDLTG DDIQRRKGEK RDVIPGGGIL GRTLTDWTRK RGKKHISSGH
     RDITEDVSEL RKRQLQAGGI VGGAGASVGG GGPNGLPQPG GQMPAIQVTA AHPAVIAVAT
     LGDKKIKTTI PAPSAEEKGG GGIMGLIRRG SSYLRRKEAE EQQQRQEEER KEDLEIARSM
     FAAARRESYY AHRAD
//
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