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Database: UniProt
Entry: A0A0V1ME67_9BILA
LinkDB: A0A0V1ME67_9BILA
Original site: A0A0V1ME67_9BILA 
ID   A0A0V1ME67_9BILA        Unreviewed;      2047 AA.
AC   A0A0V1ME67;
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   Name=Ca-alpha1D {ECO:0000313|EMBL:KRZ69839.1};
GN   ORFNames=T10_13548 {ECO:0000313|EMBL:KRZ69839.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichocephalida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ69839.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ69839.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ69839.1};
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:KRZ69839.1}.
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DR   EMBL; JYDO01000127; KRZ69839.1; -; Genomic_DNA.
DR   Proteomes; UP000054843; 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   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR031688; CAC1F_C.
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; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 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:UP000054843};
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:UP000054843};
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    139    157       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    177    198       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    210    230       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    270    289       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    351    372       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    384    406       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    515    531       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    551    576       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    583    601       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    638    658       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    679    696       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    708    731       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    876    894       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    914    943       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1016   1035       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1126   1153       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1205   1222       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1229   1248       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1294   1314       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1380   1404       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1560   1594       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   2047 AA;  233633 MW;  CB361401AFBA6E49 CRC64;
     MGRSIFVGTV NPALSKSSVP LPIPEHLRAS LQLDHDHHAR SEANFNDDVN IGKELSGNEA
     AALLHGDEAR ASRADLWQQT LQAAVAAQTE SSTTTKKRQQ QRKMQRNVQQ ERPERSLLCL
     GLKNPIRKLF ISIVEWKPFE WLILCMICAN CIALAVYQPF PAHDSDRKNA VLEQVEYIFI
     VVFTIECVMK VIAYGFLFHP GAYLRNGWNL LDFLIVVIGL ISTALSTLNI HGFDVKALRA
     FRVLRPLRLV SGVPSLQVVL NSILRAMVPL FHIALLVLFV IIIYAIIGLE LFCGKLHKTC
     VDQWTGEHVP DPGPCGESHT SFHCDRSKNL VCTENHTWPG PNDGITNFDN FGLAMLTVFQ
     CISLEGWTDV MYWVNDSVGR EWPWIYFITL VILGSFFVLN LVLGVLSGEF SKEREKARAR
     GLFQKFREKQ QLEDDLKGYL DWITQAEDID LVNEEDEEQE AMDREEFGAD GEGGEEGGSK
     EEYQRQSWFS MKIKRLKKLN RRCRRSCRRI VKSQAFYWLV IVLVFLNTMV LTSEHYGQPE
     WLDHFQEIAN LFFVVLFTLE MFLKMYSLGF VNYFVALFNR FDCFVVIGSI LEFALTFAGL
     MKPLGVSVLR SARLLRIFKV TKYWNSLRNL VASLLNSLRS IASLLLLLFL FIVIFALLGM
     QVFGGKFNTI DPNMNKPRAN FDTFVQALLT VFQILTGEDW NAVMYNGIAA FGGVHSIGVI
     VCIYFIVLFI CGNYILLNVF LAIAVDNLAD AESLTAAEKE EEGKRVNEAD PDDAMVKVPA
     DEDAVSVEQF HESGEVKLPF NEPTDAEDEH LASGDEDQER EMENQSQFKP TARPHRQSEL
     NLPKKTKPIP DASSLFLFSS TNKVRIICNK VINHSYFTNS VLVCILVSSA MLAAEDPLQA
     SSFRNEVLNY FDYFFTTVFT IEISLKVLGV NVMMMVLVYG LILHKGSFCR NAFNLLDMLV
     VGVSLTSFGL KSGAISVVKI LRVLRVLRPL RAINRAKGLK HVVQCVIVAV KTIGNIMLVT
     FMLEFMFAII GVQIFKGAFF RCTDRARLTA EECKGTFIEF EGGDVTRPHV RSREWTNYDF
     NFDNVQNAMV ALFVVSTFEG WPDLLHVAMD SSDEGIGPQY NARVSVAIFF ITFIVVIAFF
     MMNIFVGFVI VTFQSEGERE YENCELDKNQ RKCIEFALTA KPQRRYIPKN RFQYKIWWFV
     TSQPFEYAIF IIIILNTLIL GMKNYFGDAW NVFDFIIVLG SFIDIIYGKP GSNIISINFF
     RLFRVMRLVK LLSRGEGIRT LLWTFMKSFQ ALPYVALLIV LLFFIYAVIG MQIFGKIALN
     SNTEIHRNNN FQTFPSAVLV LFRSATGEAW QLIMLSCANT PTAMCDPESD DRGQPCGNDF
     AYPFFISFFM LCSFLIINLF VAVIMDNFDY LTRDWSILGP HHLDEFVRLW SEYDPDAKGR
     IKHLDVVTLL RKISPPLGFG KLCPHRLACK RLVSMNMPLN SDGTVCFNST LFALVRTNLK
     IYTEERPFLF LKKSEKVESQ SLVSSNIEEA NEQLRAVIKR IWKRTPQRLL DEIVPPSGRD
     DEITVGKFYA TYLIQDYFRR FKKRKEVEQK ETNLQGNITM SLQAGLRTLH EIGPEIKRAI
     SGNLETDWSK EFEEPQHRRD HSLFGTLVHA LQAHYKPFIE GNLANPAYSN VNGDLKSQEG
     DDEVEQHQHQ EQEPQHQHQQ QPQPQQMMMM FKMNDLKSPP VKSDRDKISE FESDESVCNK
     PERRCNSFFS NIRRRVDSIV SPSIMLFDSD HDSSEHEMQE RVRFVPRGSK PTTGLSFEGS
     RWLPRKLSFR RAPIGAAVSN LQQGNNKRLQ FSNAIILDDS DPDSIMHPEN VVDLTESGDD
     SKSSVSPPLE LRDDAYYLDG IDYNTWRPAP MGQGVRLRRR GNNGRRKSRS MPLPHDQRNY
     ADVLVEKVLA DQGLGRYADP NLIRTTQLEI AEAYNMTEAQ MHSAARSLMQ RSPKYFEHMG
     GQRPADIKDF NQYSKTALLK PREMNNSEDV DISDDMNMFM SVAESWIKTG RVLMDSNVSL
     RSDRLSP
//
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