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Database: UniProt
Entry: A0A093IW94_EURHL
LinkDB: A0A093IW94_EURHL
Original site: A0A093IW94_EURHL 
ID   A0A093IW94_EURHL        Unreviewed;      1042 AA.
AC   A0A093IW94;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   25-OCT-2017, entry version 15.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
DE   Flags: Fragment;
GN   ORFNames=N326_13425 {ECO:0000313|EMBL:KFW07000.1};
OS   Eurypyga helias (Sunbittern).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Eurypygidae; Eurypyga.
OX   NCBI_TaxID=54383 {ECO:0000313|EMBL:KFW07000.1, ECO:0000313|Proteomes:UP000054232};
RN   [1] {ECO:0000313|EMBL:KFW07000.1, ECO:0000313|Proteomes:UP000054232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N326 {ECO:0000313|EMBL:KFW07000.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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}.
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DR   EMBL; KK570315; KFW07000.1; -; Genomic_DNA.
DR   Proteomes; UP000054232; 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   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   Pfam; PF00520; Ion_trans; 3.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
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:UP000054232};
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:UP000054232};
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      6     25       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     37     53       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    109    131       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    191    212       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    224    246       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    392    409       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    429    452       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    521    540       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    593    618       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    708    726       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    746    766       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    824    853       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    951    976       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1019   1039       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        3    257       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      391    622       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      708    983       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   COILED      621    654       {ECO:0000256|SAM:Coils}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KFW07000.1}.
FT   NON_TER    1042   1042       {ECO:0000313|EMBL:KFW07000.1}.
SQ   SEQUENCE   1042 AA;  119073 MW;  29295F346DD2A158 CRC64;
     ERVEYLFLII FTVEAFLKVI AYGLLFHPNA YLRNGWNLLD FIIVVVGLFS AILEQATKAD
     GGNSIGGKGA GFDVKALRAF RVLRPLRLVS GVPSLQVVLN SIIKAMVPLL HIALLVLFVI
     IIYAIIGLEL FMGKMHKTCY HVQGGLIDTP AEDDPSPCAP QSAHGRQCQN GTECKAGWEG
     PKHGITNFDN FAFAMLTVFQ CITMEGWTDV LYWMQDAMGY ELPWVYFVSL VIFGSFFVLN
     LVLGVLSGEF SKEREKAKAR GDFQKLREKQ QLEEDLKGYL DWITQAEDID PENEDEGMDE
     EKPRNRSTPA GLPDKKKGKF AWFSHSTETH VSMPTSETES VNTDNVPGAD IEGENCGARL
     AHRISKSKFS RYWRRWNRFC RRKCRAAVKS NVFYWLVIFL VFLNTLTIAS EHYNQPDWLT
     EVQDTANKVL LALFTAEMLL KMYSLGLQAY FVSLFNRFDC FIVCGGILET ILVETKIMSP
     LGISVLRCVR LLRIFKITRY WNSLSNLVAS LLNSVRSIAS LLLLLFLFII IFSLLGMQLF
     GGKFNFDEMQ TRRSTFDNFP QSLLTVFQIL TGEDWNSVMY DGIMAYGGPS FPGMLVCIYF
     IILFICGNYI LLFLAIAVDN LADAESLTSA QKEEEEEKER KKLARGEFSN AEEDEEEPEM
     PVGPRPRPMS ELHLKEKAVP MPDASAFFIF SPNNRFRVHC HRIVNDNIFT NLILFFILLS
     SISLAAEDPV RHLSFRNQIL GNADYVFTSI FTLEIILKMT AYGAFLHKGS FCRNYFNILD
     LLVVSVSLIS FGIQSSAINV VKILRVLRVL RPLRAINRAK GLKHVVQCVF VAIRTIGNIV
     IVTTLLQFMF ACIGVQLFKG KLYSCTDSSK QTAAECRGYY ITYKDGEVNQ PMIQPRSWEN
     SKFDFDNVLT AMMALFTVST FEGWPELLYR SIDSHMEDVG PIYNHRVEIS IFFIIYIIII
     AFFMMNIFVG FVIVTFQEQG EQEYKNCELD KNQRQCVEYA LKARPLRRYI PKNQYQYKVW
     YVVNSTYFEY LMFVLKICLA MQ
//
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