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Database: UniProt
Entry: A0A0V1A4Q1_9BILA
LinkDB: A0A0V1A4Q1_9BILA
Original site: A0A0V1A4Q1_9BILA 
ID   A0A0V1A4Q1_9BILA        Unreviewed;      1693 AA.
AC   A0A0V1A4Q1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   28-MAR-2018, entry version 14.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=T12_6365 {ECO:0000313|EMBL:KRY19839.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY19839.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY19839.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY19839.1};
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
CC       opposite 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:KRY19839.1}.
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DR   EMBL; JYDQ01000031; KRY19839.1; -; Genomic_DNA.
DR   Proteomes; UP000054783; 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   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.350; -; 4.
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   InterPro; IPR027359; Volt_channel_dom_sf.
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:UP000054783};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAAS:SAAS00085096, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00084820,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00084701,
KW   ECO:0000256|SAM:Phobius}; 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    827    845       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    865    886       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    898    924       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    944    974       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1069   1096       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1139   1165       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1177   1203       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1274   1296       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1372   1393       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1528   1562       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1693 AA;  194318 MW;  D3AD119BD01C597A 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 IEQEEEEEAN
     FEIQLCNGET QRENGQFEQL NNNNWSNCTR FSYLYYWSDG TKDETDDATV LNGNNRKRGA
     SLLAKDDSFG ENCRKASLLH IPPYNSLFIF SPQNKLRIAC AKLIRHAYFK NLVLLCILVS
     SALLAAEDPL SRHSTLNDVL GFFDIFFTSV FTVEIVLKII TFGLVLHEES FCRNAFNLLD
     LLVVAVSLAS FGLKSGAISV VKILRVLRVL RPLRAINRAK GLKHVVQCVI 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
     QKQQRANNKN FSSAINYKEH FRKKKNVPSL QINKTTHSTS TPNGHVPQSE SDDPQPWRPY
     PHNACVRLFD LDG
//
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