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Database: UniProt
Entry: A0A0V1ME06_9BILA
LinkDB: A0A0V1ME06_9BILA
Original site: A0A0V1ME06_9BILA 
ID   A0A0V1ME06_9BILA        Unreviewed;      2057 AA.
AC   A0A0V1ME06;
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:KRZ69843.1};
GN   ORFNames=T10_13548 {ECO:0000313|EMBL:KRZ69843.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichocephalida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ69843.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ69843.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ69843.1};
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:KRZ69843.1}.
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DR   EMBL; JYDO01000127; KRZ69843.1; -; 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    875    893       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    913    934       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1007   1026       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1117   1144       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1198   1216       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1228   1250       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1256   1275       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1319   1337       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1408   1433       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1570   1604       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   2057 AA;  234754 MW;  C03B9A5193CC3390 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 IEISLKVLVY GLILHKGSFC RNAFNLLDML VVGVSLTSFG
     LKSGAISVVK ILRVLRVLRP LRAINRAKGL KHVVQCVIVA VKTIGNIMLV TFMLEFMFAI
     IGVQIFKGAF FRCTDRARLT AEECKGTFIE FEGGDVTRPH VRSREWTNYD FNFDNVQNAM
     VALFVVSTFE GWPDLLHVAM DSSDEGIGPQ YNARVSVAIF FITFIVVIAF FMMNIFVGFV
     IVTFQSEGER EYENCELDKN QRKCIEFALT AKPQRRYIPK NRFQYKIWWF VTSQPFEYAI
     FIIIILNTLI LGMKHYKSSA AFDEALDVLN LFFTTVFALE FICKLFALTF KNYFGDAWNV
     FDFIIVLGSF IDIIYGKPGS NIISINFFRL FRVMRLVKLL SRGEGIRTLL WTFMKSFQAL
     PYVALLIVLL FFIYAVIGMQ IFGKIALNSN TEIHRNNNFQ TFPSAVLVLF RSATGEAWQL
     IMLSCANTPT AMCDPESDDR GQPCGNDFAY PFFISFFMLC SFLIINLFVA VIMDNFDYLT
     RDWSILGPHH LDEFVRLWSE YDPDAKGRIK HLDVVTLLRK ISPPLGFGKL CPHRLACKRL
     VSMNMPLNSD GTVCFNSTLF ALVRTNLKIY TEVSSNIEEA 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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