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Database: UniProt
Entry: A0A0V1CV45_TRIBR
LinkDB: A0A0V1CV45_TRIBR
Original site: A0A0V1CV45_TRIBR 
ID   A0A0V1CV45_TRIBR        Unreviewed;      1681 AA.
AC   A0A0V1CV45;
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=T03_15840 {ECO:0000313|EMBL:KRY52908.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichocephalida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY52908.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY52908.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY52908.1};
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:KRY52908.1}.
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DR   EMBL; JYDI01000096; KRY52908.1; -; Genomic_DNA.
DR   Proteomes; UP000054653; 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:UP000054653};
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:UP000054653};
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    431    449       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    464    487       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    499    517       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    557    581       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    602    623       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    629    652       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    802    820       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    840    861       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    873    899       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    919    949       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1044   1071       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1114   1140       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1152   1178       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1249   1271       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1347   1368       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1503   1537       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1681 AA;  193172 MW;  30C063E2DD85FB66 CRC64;
     MSAENYTTPS DTTIVDSCLL SSTVAGTTPT ARSKRNNSSY 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 FETVENNDGR FSRLKCKKLQ MLPFYSSKLR
     RKGRKLIKSQ AFYWIVIVLV FLNTFVLTLE HHRQPLWLEE FQDYVNICFV ILFALEMLLK
     MFCLGFYNYF MSLFNRFDCF VVLCSIVEIS LTQARVIKPL GLSVLRSARL LRLFKVTRYW
     DSLRNLVASL LNSLRSIVSL LLLLFLFIVI FALLGMQIFG GKFKFDPFGS KPRSNFDSFP
     QSLLTVFQVG HFLIIPYLFL LWIQSFGGAS SIGIVVCVYF IVLFVCGNYI LLNVFLAIAV
     DNLGDNDQSE PETALPHVNE ETLQEQDDEK MMIDNDNIEQ EEEANFEIQL CNGETQRENG
     QFEQLNNNNW SNSDGTKDET DDATVLNGNN RKRGASLLAK DDSFGENCRK ASLLHIPPYN
     SLFIFSPQNK LRIACAKLIR HAYFKNLVLL CILVSSALLA AEDPLSRHST LNDVLGFFDI
     FFTSVFTVEI VLKIITFGLV LHEESFCRNA FNLLDLLVVA VSLASFGLKS GAISVVKILR
     VLRVLRPLRA INRAKGLKHV VQCVIVAVKT IGNILLVTFM LQFMFAIVGV QLFKGTFYRC
     TDSTKTNPQD CRGVFIHYDG GDRTKPVVEF REWVNNDFNF DDIRNALISL FVVGTFEGWP
     DLLYVAIDST EEDSGPVYNY RQAVAIFFIA YIVVIAFFMQ NIFVGFVIIT FQNEGEREYE
     NCELDKNQRK CIDFTLNVKP QKRYVPSSQF RYKLWLFVTS SYFEYGILFI IILNTFVLAM
     RHHHPNPITE EVLDFLNFIF TSVFAAEVLL KLMAFTIVNY FADAWNVFDF IVVLGSVIDI
     VCSKVGPGES VISMNFFRLF RVMRLVKLLG RGEGMRTLVW TFLKSFQSLP YVVLLIVLLF
     FIYAVIGMQV FGKIAFDDDT QIHRHNNFRT FYSALLVLFR CATGEAWQNI MLDCSDRPTV
     LCEKAFLHED EEASGATTCG TNFAYPYFIS FFILSSCLII NLFVAIIMDN FDYLTRDWSI
     LGPHHLEEFV RLWSEFDPDA RGRIKHLDVL ILLRKISPPL GFGDFCPHRI ACKKLISMNM
     SLFPDGTVGF HATLLALVRT SLNIFCDNSI EMANIRLRRV IRKVWKKTSE SFLDEILPLT
     TGEDDVTVGK FYATYLIQDY FLRFKRRRML EARRMNQTPR HGIKVLMAGL REPIHDSAEP
     HRRYSGNLFA DWMKDFEEPQ HRRNHILFNG LTNDHQKHQR VNNKNFSSAI NYKEHFRKKK
     NVPSLQINKT THSTSTPNGH VPQSESDDPQ PWRPYPHNAC VRLFDLVSRL NKYPYIYRYF
     I
//
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