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Database: UniProt
Entry: A0A085MB00_9BILA
LinkDB: A0A085MB00_9BILA
Original site: A0A085MB00_9BILA 
ID   A0A085MB00_9BILA        Unreviewed;      1678 AA.
AC   A0A085MB00;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-SEP-2017, entry version 19.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=M513_04739 {ECO:0000313|EMBL:KFD54396.1}, M514_04739
GN   {ECO:0000313|EMBL:KFD61669.1};
OS   Trichuris suis (pig whipworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichocephalida; Trichuridae; Trichuris.
OX   NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD54396.1, ECO:0000313|Proteomes:UP000030764};
RN   [1] {ECO:0000313|EMBL:KFD54396.1, ECO:0000313|Proteomes:UP000030758, ECO:0000313|Proteomes:UP000030764}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD61669.1}, and DCEP-RM93M
RC   {ECO:0000313|EMBL:KFD54396.1};
RX   PubMed=24929829; DOI=10.1038/ng.3012;
RA   Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA   Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA   Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT   "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL   Nat. Genet. 46:701-706(2014).
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; KL363208; KFD54396.1; -; Genomic_DNA.
DR   EMBL; KL367615; KFD61669.1; -; Genomic_DNA.
DR   Proteomes; UP000030758; Unassembled WGS sequence.
DR   Proteomes; UP000030764; 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:UP000030758,
KW   ECO:0000313|Proteomes:UP000030764};
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:UP000030758};
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     86    104       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    124    145       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    157    178       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    214    234       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    330    352       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    459    480       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    492    515       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    585    607       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    663    688       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    800    819       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    831    853       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    873    896       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    917    945       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1003   1024       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1045   1068       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1111   1137       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1149   1175       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1181   1203       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1245   1268       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1341   1365       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1500   1534       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1678 AA;  192747 MW;  0B935070FA61BCD5 CRC64;
     MAENSLTTVV EQSPPLQAQS VSSSDRIVLE SDGQIETEDI TFPLKRAATK KADPYKKERP
     KRSLFCLTEK NRFRQLCIHI VEWKPFEWLI LTMICANCLA LAFYQPYPNF DSDTRNMILE
     QLEYAFVIIF TIESALKIIA HGFVLHPGAY LRNGWNVLDF VIVVVGNCST LFAFLNIPNV
     DVKALRAFRV LRPLRLVSGV PSLQIVLNSI LQAMVPLFHV ALLVLFVIII YAVMGLELFC
     GKLNRTCVDA NTGEPVDSEP VPCGFASSAR HCAVAENCTE TEHWSGPNQG ITNFDNIGFA
     MLTVFTCISQ EGWSDVMYWV NDAIGTEWPW LYFVSLVVLG SFFVLNLILG VLSGEFSKER
     EKARVRGLFR KRREKVQLEE ELRSYLNWIM QAEDILDVDQ DQEIYEMETT DENAVKVVEY
     TVEHWLSRCS RWCMSNMQKF RISNLKVRRY GRMLIKSQAF YWTVLVMVFL NTFVLTLEHY
     QQPEWLEDLQ DVVNICFITL FALEMMLKMY CLGFYTYFIS LFNRFDCFVV LCSIAEISLT
     HAKVIKPLGL SVLRAARLLR IFKITRYWNS LRNLVASLLN SLRSIVSLLL LLFLFIVIFA
     LLGMQIFGGR FKYDSHQPMP RSNFDTFAQS LLTVFQILTG EDWNSVMYIG IDSFGGATSP
     GIVVCLYFIV LFICGNYVLL NVFLAIAVDN LADTDSNGDE GNAKSEENDV GGEEEEEEQE
     NNDDDNAVLN NKQRCNGGDQ RGENASDKVA IIMPSPGKRR STMSQADPAS MLLPKHNSLF
     IFSSKNRFRI LSAKLIRHSY FKNLVLLCIL VSSALLAAED PLTKQSSLNE ILGFFDIFFT
     TVFTIEILLK IVVDGLLLHK GSFCRNAFNL LDLLVVCVSL ASFGLKKEAI SVVKILRVLR
     VLRPLRAINR AKGLKRVVQC VIVAVKTIGN ILLVTSMLQF MFAIIGVQLF KGTFFRCTDP
     VRSTPESCRG YFIEFQEGDM TKPIVKQREW VNNDFNFDNI KNALVSLFVV GTFEGWPQLL
     YVAIDSTAEG RGPIYNYRQT VAIFFISYIV VIAFFMQNIF VGFVIVTFQN EGEREYEHCE
     LDKNQRKCIE FTLTAKPQRR YVPKTRLRYK IWLFVTSSYF EYGILVIIIL NTVVLAMRHH
     QPNPVMEEVL DFLNFVFTSI FAAEVLLKLI AFTIVNYFAD AWNVFDFIVV LGSVIDIICS
     RLATRESLIS MNFFRLFRVM RLVKLLGRGE GIRTLVWTFL KSFQALPYVV LLIVLLFFIY
     AVIGMQVFGK IALNDETQIH RHNNFRTFYT SLLVLFRSAT GEAWQNIMLD CSDRPSVVCD
     RDFSFEEGEE KGSTGCGTDF AYPYFISFFL LSSCLIINLF VAIIMDNFDY LTRDWSILGP
     HHLEEFVRLW SEFDPDARGR IKHLDVLILL RKITPPLGFG DFCPHRIACK RLISMNMSLH
     PDGTVGFHAT LIALVRTNLN IYSEDPIELA NTKLRSFIRR VWKRTSPEFL DEILPLTTGE
     DDVTVGKFYA TFLIQDYFLR FKRRKLWEKK RKRDLSKQMK LLQAGLRDNL EAEKAPEPKR
     RWSGYLLADW KKDFEQPQHR RNHFLFNTFN EKPTTSRSSS FSSTEAMERL ELINGMLPQN
     RGKKKRAKKS RKRAAANGLL ANDLNMENEP WRPFPYNRCV ELHAGQDSVG TFFLTSYE
//
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