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Database: UniProt
Entry: H2UWU1_TAKRU
LinkDB: H2UWU1_TAKRU
Original site: H2UWU1_TAKRU 
ID   H2UWU1_TAKRU            Unreviewed;      1623 AA.
AC   H2UWU1;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   25-OCT-2017, entry version 40.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=LOC101064574 {ECO:0000313|Ensembl:ENSTRUP00000041419};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae;
OC   Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000041419, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000041419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A.,
RA   Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu
RT   facilitates insights into distinct features of genome evolution in
RT   teleosts and mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000041419}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
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 Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSTRUP00000041419}.
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DR   Ensembl; ENSTRUT00000041563; ENSTRUP00000041419; ENSTRUG00000016197.
DR   GeneTree; ENSGT00830000128247; -.
DR   OMA; PTTKINM; -.
DR   Proteomes; UP000005226; Unplaced.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005226};
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:UP000005226};
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      5     23       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     90    113       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    166    187       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    199    221       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    386    403       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    423    446       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    515    534       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    582    604       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    901    919       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    939    959       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1017   1046       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1140   1169       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1220   1238       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1250   1273       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1285   1303       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1347   1369       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1438   1462       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1596   1623       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      615    641       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1623 AA;  185570 MW;  A49F465AEBABCB61 CRC64;
     EYLFLIIFTV EAFLKVIAYG LLFHPNAYLR NGWNLLDFII VVVGPIGGKA AGFDVKALRA
     FRVLRPLRLV SGVPSLQVVL NSIIKAMVPL LHIALLVLFV IIIYAIIGLE LFMGKMHKTC
     YYKQPKEKPA PCAPEGAYGR HCKRNGTVCL MEWDGPNDGI TNFDNFAFAM LTVFQCITME
     GWTDVLYWVN DAVGYEWPWL YFVTLIIIGS FFVLNLVLGV LSGEFSKERE KAKARGDFQK
     LREKQQLEED LKGYLDWITQ AEDIDPENEE EGLDDDKPRN LRPASEGPIM ALYQAGKSEQ
     CDAPLPFSSA DGSSSRMMNG GSLFPLSVIS FTHVQEHSDG LMQYLEIGSP NPSSXLDVSS
     LLCSRYSRRW NRLFRRKCRA GVKSQVFYWL VIFLVFLNTL TIASEHHHQP QWLTDVQDIA
     NKVLLALFTG EMLLKMYSLG LQAYFVSLFN RFDSFVVCGG ILETILVETK IMSPLGISVL
     RCVRLLRIFK ITRYWNSLSN LVASLLNSVR SIASLLLLLF LFIIIFSLLG MQLFGGKFNF
     EETRRSTFDN FPQSLLTVFQ ILTGEDWNSV MYDGIMAYGG PAFPGMLVCI YFIILFICGN
     YILLNVFLAI AVDNLADAES LTSAQKEEEE EKERKKLARD ANATISKICL HGFHNFTVIL
     APRGLQRSIV INSNHKSLNV SLDTSCIDQR GESVKENNHY SAVPNWDWDS RHHRSLFSRL
     KCSYQLHTRC VIDDPCEKRK LKAESHSHAH LFQVGQPREA SQQRKTSLGG GEEGEDRVKV
     HHLRWRSTKT YGKTASQNNE RDHKRTDDLT DPHDDSEEKN PYPANDYIGK LIHTEVAFSL
     LSSGEDDEDE PEMPVGPRPR PLSDIQLKEK VVPMPEARAF FVFSHTNKFR ITCHKIVNHN
     IFTNLILFFI LLSSISLAAE DPVKNDSSRN QILGYADHVF TGLFTIEIIL KMTAYGAFLH
     KGSFCRNYFN ILDLVVVSVS LISSGIQSSA INVVKILRVL RVLRPLRAIN RAKGLKHVVQ
     CVFVAIRTIG NIVIVTTLLQ FMFACIGVQL FKGKFFLCTD SSKQTQAECR GSYIMYKDGD
     VGKPERAQRL WENSEFNFDN VLQGMMALFA VSTFEGWPGL LYRAIDSVAE DFGPIYNYRV
     IISIFFIIYI IIIAFFMMNI FVGFVIVTFQ EQGEQEYKNC ELDKNQRQCV EYALKARPLR
     RYIPKNPYQY KVWYVVNSTY FEYLMFTLIL LNTICLAMQH HGQTKSFNNA MNILNMLFTG
     LFTVEMILKL IAFKPRGYFS DPWNVFDFLI VIGSIIDVIL SEINVKNARI SITFFRLFRV
     MRLVKLLSRG EGIRTLLWTF IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIALRDNTQI
     NRNNNFQTFP QAVLLLFRCA TGEAWQEIML ACTLNRPCEK GSTNETNQST EDCGSQFAII
     YFVSFYMLCA FLIINLFVAV IMDNFDYLTR DWSILGPHHL DEFKRIWAEY DPEAKGRIKH
     LDVVTLLRRI QPPLGFGKLC PHRVACKRLV SMNMPLNSDG TVMFNATLFA LVRTALRIKT
     EGNLEQANEE LRAIVKKIWK RTSMKLLDQV VPPAGDDEVT VGKFYATFLI QEYFRKFKKR
     KEQ
//
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