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Database: UniProt
Entry: A0A0V1PAA5_9BILA
LinkDB: A0A0V1PAA5_9BILA
Original site: A0A0V1PAA5_9BILA 
ID   A0A0V1PAA5_9BILA        Unreviewed;      1649 AA.
AC   A0A0V1PAA5;
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=T08_7959 {ECO:0000313|EMBL:KRZ93149.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichocephalida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ93149.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ93149.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ93149.1};
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:KRZ93149.1}.
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DR   EMBL; JYDM01000028; KRZ93149.1; -; Genomic_DNA.
DR   Proteomes; UP000054924; 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:UP000054924};
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:UP000054924};
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    642    670       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    791    809       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    829    850       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    862    888       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    908    938       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1033   1060       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1103   1129       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1141   1167       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1238   1260       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1336   1357       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1485   1519       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1649 AA;  188991 MW;  8A0106AB7F8AA918 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 SFPQSLLTIL TGEDWNSVMY AGIQSFGGAS SIGIVVCVYF IVLFVCGNYI
     LLNVFLAIAV DNLGDNDQSE PETALPHVNE ETLQEQDDEK MMIDNDNIEQ EEEEEEANFE
     IQLCNGETQP DGTKDETDDA TVLNGNNRKR GASLLAKDDS FGENCRKASL LHIPPYNSLL
     RIACAKLIRH AYFKNLVLLC ILVSSALLAA EDPLSRHSTL NDVLGFFDIF FTSVFTVEIV
     LKIITFGLVL HEESFCRNAF NLLDLLVVAV SLASFGLKSG AISVVKILRV LRVLRPLRAI
     NRAKGLKHVV QCVIVAVKTI GNILLVTFML QFMFAIVGVQ LFKGTFYRCT DSTKTNPQDC
     RGVFIHYDGG DRTKPVVEFR EWVNNDFNFD DIRNALISLF VVGTFEGWPD LLYVAIDSTE
     EDSGPVYNYR QAVAIFFIAY IVVIAFFMQN IFVGFVIITF QNEGEREYEN CELDKNQRKC
     IDFTLNVKPQ KRYVPSSQFR YKLWLFVTSS YFEYGILFII ILNTFVLAMR HHHPNPITEE
     VLDFLNFIFT SVFAAEVLLK LMAFTIVNYF ADAWNVFDFI VVLGSVIDIV CSKVGPGESV
     ISMNFFRLFR VMRLVKLLGR GEGMRTLVWT FLKSFQSLPY VVLLIVLLFF IYAVIGMQVF
     GKIAFDDDTQ IHRHNNFRTF YSALLVLFRC ATGEAWQNIM LDCSDRPTVL CEKAFLHEDE
     EASGATTCGT NFAYPYFISF FILSSCLIIN LFVAIIMDNF DYLTRDWSIL GPHHLEEFVR
     LWSEFDPDAR GRIKHLDVLI LLRKISPPLG FGDFCPHRIA CKKLISMNMS LFPDGTVGFH
     ATLLALVRTN SIEMANIRLR RVIRKVWKKT SESFLDEILP LTTGEDDVTV GKFYATYLIQ
     DYFLRFKRRR MLEARRMNQT PRHGIKVLMA GLREPIHDSA EPHRRYSGNL FADWMKDFEE
     PQHRRNHILF NGLTNDHQKQ QRVNNKNFSS AINYKEHFRK KKNVPSLQIN KTTHSTSTPN
     GHVPQSESDD PQPWRPYPHN ACVRLFDLH
//
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