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Database: UniProt
Entry: H2RVE1_TAKRU
LinkDB: H2RVE1_TAKRU
Original site: H2RVE1_TAKRU 
ID   H2RVE1_TAKRU            Unreviewed;      1495 AA.
AC   H2RVE1;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   25-OCT-2017, entry version 37.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=LOC101064508 {ECO:0000313|Ensembl:ENSTRUP00000004109};
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:ENSTRUP00000004109, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000004109}
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:ENSTRUP00000004109}
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: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00448}.
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:ENSTRUP00000004109}.
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DR   Ensembl; ENSTRUT00000004131; ENSTRUP00000004109; ENSTRUG00000001782.
DR   GeneTree; ENSGT00830000128247; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005450; VDCC_L_a1ssu.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF190; PTHR10037:SF190; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01634; LVDCCALPHA1S.
DR   PROSITE; PS50222; EF_HAND_2; 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: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     67     84       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    104    124       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    136    154       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    208    230       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    290    311       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    323    345       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    445    462       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    482    504       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    574    596       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    650    676       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    813    836       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    848    867       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    934    963       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1057   1086       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1129   1150       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1170   1190       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1281   1303       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1371   1395       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1411   1446       EF-hand. {ECO:0000259|PROSITE:PS50222}.
SQ   SEQUENCE   1495 AA;  170906 MW;  D0C4C1AE4B0B6DF9 CRC64;
     MVGNSSPPLS SYIMDEDTLK RKQKEKLKKL MATGGNPRPA RSLLFLTLRN PFRKACLSIV
     EWKPFEIIIL LAIFANCVAL AVYLPMPEED SNNTNSNLES LEYIFLIIFS VECFLKIVAY
     GFLFHADAYL RNCWNILDFV CVSVGLFTVA MDAINHISGV EASIGDKGGG FDMKALRAFR
     VLRPLRLVSG VPSLQVVMNS ILKSMLPLFH ITLLVFFMVT IYSIMGLELF KCKMHKTCYY
     IGTNIIATVE NEKPAPCAQA GNGRRCLING TECRIGWPGP NQGITHFDNL GFSMLTVYQC
     ITTQGWTDVL YWVNDAIGME WPWIYFTTLI LVGSFFVLNL ILGVLSGEFT KEREKAKSRG
     EFQKLRETQQ LDEDLKGYME WITQAEVLDN EQESHGLLTT ENRGMENGRV GKMDTIQLIM
     YYYKVARKWN RWLRRKCRVC VKSRLFYWWV IMLVFLNTLA IATEHHKQTQ RLTNWQDNAN
     KLLLTMFFLE MFMKMYALGL PSYFMSLFNR NFFHSFNLVI VRSIFFNNQM LINVLHLNLP
     RLCILCNETC IIYYRYWTSL SNLVASLLNS IRSIACLLLL LFLFIVIFSL LGMQVFGGKF
     NFTNQPKPRS TFDSFPQALI TVFQILTGED WNAVMYDGIM AHGGPCIPGI LVSIYFIILF
     VCGNFILLNV FLAIAVDNLA EAESLTLAQK EKAEERKRKK LLRANMPDKT PEEKANLAKK
     LAEQRAKGVE GIPTTAKLKV DEFEFNVNEI KDPFPPADFP GDDEEEDPDI PQSPRPRPMA
     DLQLKEESVP IPEATSFFIF GPRNKFRKLC HRIINATTFT NIILLFILLS SISLAAEDPI
     DPLSFRNQVL AYADIVFTSV FTAEIVLKMT TYGAILHKGS FCRNSFNILD LLVVSVSLLS
     MGMESSAISV VKILRVLRVL RPLRAINRAK GLKHVVQCVF VAVKTIGNIV LVTMLLDFMF
     ACIGVQLFKG KFYSCTDPDK MIEETCRGWY IKYQEGALHE MEVCKRKWTN ADLNFDNILN
     GMLALFTIST FEGWPKILYK AIDSNSEDEG PLYNNRVAIS IFFIIYLILI AFFMMNIFVG
     FVIVTFQEQG EQEYKNCELD KNQRQCVQYA LKARPLRCYI PKNPYQYQVW YIVTSCYFEY
     LMFLLIMLNT MCLGMQHCNQ SDHVTHLSDM LNVIFTVLFT VEMVLKLMAF KAKGYFGDPW
     NVFDFVIVIG SVVDVILSEI NAALASSGGL YCLQGCNSSE NLSVSVTFFR LFRVMRLVKL
     LNRSEGIRNL LWTFIKSLQA LPYVALLILM LFFIYAVVGM QIFGKIAVVD GTYINRNNNF
     QTFPQAVLLL FRCATGEAWH EVMLACMYGK KCDPKSDYLP GEEYTCGSNF AIIYFMSFYM
     LCAFLIINLF VAVIMDNFDY LTRDWSILGP QHLDEFKKIW AEYDPEATGR IKHLDVVTLL
     RRIPPPLGFG KFCPHRIACK RLVSMNMPLN SDGTVTFNAT LFALVRTALK IKTEG
//
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