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Database: UniProt
Entry: A0A0V0U6Q6_9BILA
LinkDB: A0A0V0U6Q6_9BILA
Original site: A0A0V0U6Q6_9BILA 
ID   A0A0V0U6Q6_9BILA        Unreviewed;      1716 AA.
AC   A0A0V0U6Q6;
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=T05_8431 {ECO:0000313|EMBL:KRX46895.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichocephalida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX46895.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX46895.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX46895.1};
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:KRX46895.1}.
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DR   EMBL; JYDJ01000050; KRX46895.1; -; Genomic_DNA.
DR   Proteomes; UP000055048; 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:UP000055048};
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:UP000055048};
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    159       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    203    221       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    316    338       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    444    462       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    477    500       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    570    592       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    645    673       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    819    837       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    857    878       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    969    988       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1079   1106       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1149   1175       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1187   1213       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1284   1306       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1382   1403       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1538   1572       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1716 AA;  197267 MW;  58C62DAB60EA6D10 CRC64;
     MSAENYTTPS DTTIVDSCLL SSTVAGTTPT TRSKRNNSSY TIERPKRSLF CLDQKNRFRL
     LCIHIVEWKP FEWLILTMIC ANCLALAIYQ PYSGLDSDFR NTILEMLEYV FIFVFTIECL
     LKIVAYGFVM HPGAYLRNAW NILDFVIIVV GNCSTALSWA NLPNVDVKAL RAFRVLRPLR
     LVSGVPSLQI VLNSVLQAMV PLFHVALLVL FVIIIYAIMG LELFCGKLSR TCVHPDTGLP
     LQGGSSSPCG FGHSARHCSI NANCSETKYW PGPNHGITNF DNIGFAMLTV FTCVSQEGWT
     DVMYWVNDAV GNEWPWIYFV SLVVLGSFFV LNLVLGVLSG EFSKEREKAR VRGIFKKRRE
     KIRFEEELRS YLDWILQAED IWDAVGDEAT FETVENNDAK YTSGSRLDWL LGRFSRLKCK
     KLQMLPFYSS KLRRKGRKLI KSQAFYWIVI VLVFLNTFVL TLEHHRQPLW LEEFQDYVNI
     CFVILFALEM LLKMFCLGFY NYFMSLFNRF DCFVVLCSIV EISLTQARVI KPLGLSVLRS
     ARLLRLFKVT RYWDSLRNLV ASLLNSLRSI VSLLLLLFLF IVIFALLGMQ IFGGKFKFDP
     FGSKPRSNFD SFPQSLLTVF QILTGEDWNS VMYAGIQSFG GASSIGIVVC VYFIVLFVCG
     NYILLNVFLA IAVDNLGDND QSEPETALPH VNEETLQEQD DEKMMIDNDN IEQQEEEEEE
     ANFEIQLCNG ETQRENGQFE QLNNNNWSNS DGTKDETDDA TVLNGNNRKR GASLLAKDDS
     FGENCRKASL LHIPPYNSLF IFSPQNKLRI ACAKLIRHAY FKNLVLLCIL VSSALLAAED
     PLSRHSTLND VLGFFDIFFT SVFTVEIVLK IITFGLVLHE ESFCRNAFNL LDLLVVAVSL
     ASFGLKSGAI SVVKILRVLR VLRPLRAINR AKGLKVIFFL IMKNVVIQQH FFKHVVQCVI
     VAVKTIGNIL LVTFMLQFMF AIVGVQLFKG TFYRCTDSTK TNPQDCRGVF IHYDGGDRTK
     PVVEFREWVN NDFNFDDIRN ALISLFVVGT FEGWPDLLYV AIDSTEEDSG PVYNYRQAVA
     IFFIAYIVVI AFFMQNIFVG FVIITFQNEG EREYENCELD KNQRKCIDFT LNVKPQKRYV
     PSSQFRYKLW LFVTSSYFEY GILFIIILNT FVLAMRHHHP NPITEEVLDF LNFIFTSVFA
     AEVLLKLMAF TIVNYFADAW NVFDFIVVLG SVIDIVCSKV GPGESVISMN FFRLFRVMRL
     VKLLGRGEGM RTLVWTFLKS FQSLPYVVLL IVLLFFIYAV IGMQVFGKIA FDDDTQIHRH
     NNFRTFYSAL LVLFRCATGE AWQNIMLDCS DRPTVLCEKA FLHEDEEASG ATTCGTNFAY
     PYFISFFILS SCLIINLFVA IIMDNFDYLT RDWSILGPHH LEEFVRLWSE FDPDARGRIK
     HLDVLILLRK ISPPLGFGDF CPHRIACKKL ISMNMSLFPD GTVGFHATLL ALVRTSLNIF
     CDNSIEMANI RLRRVIRKVW KKTSESFLDE ILPLTTGEDD VTVGKFYATY LIQDYFLRFK
     RRRMLEARRM NQTPRHGIKV LMAGLREPIH DSAEPHRRYS GNLFADWMKD FEEPQHRRNH
     ILFNGLTNDH QKHQRVNNKN FSSAINYKEH FRKKKNVPSL QINKTTHSTS TPNGHVPQSE
     SDDPQPWRPY PHNACVRLFD LVSRLNKYPY IYRYFI
//
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