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Entry: A0A091PTL8_HALAL
LinkDB: A0A091PTL8_HALAL
Original site: A0A091PTL8_HALAL 
ID   A0A091PTL8_HALAL        Unreviewed;      1551 AA.
AC   A0A091PTL8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   25-OCT-2017, entry version 17.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
DE   Flags: Fragment;
GN   ORFNames=N329_13231 {ECO:0000313|EMBL:KFQ11000.1};
OS   Haliaeetus albicilla (White-tailed sea-eagle).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Falconiformes; Accipitridae;
OC   Accipitrinae; Haliaeetus.
OX   NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ11000.1, ECO:0000313|Proteomes:UP000054379};
RN   [1] {ECO:0000313|EMBL:KFQ11000.1, ECO:0000313|Proteomes:UP000054379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ11000.1};
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; KK665431; KFQ11000.1; -; Genomic_DNA.
DR   Proteomes; UP000054379; 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; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
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; 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   PRINTS; PR01634; LVDCCALPHA1S.
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:UP000054379};
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:UP000054379};
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     22       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     42     62       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    139    160       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    258    280       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    402    419       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    439    456       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    528    550       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    604    630       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    764    783       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    795    817       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    837    860       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    881    914       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1005   1032       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1073   1092       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1118   1138       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1213   1231       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1305   1328       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1462   1495       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KFQ11000.1}.
FT   NON_TER    1551   1551       {ECO:0000313|EMBL:KFQ11000.1}.
SQ   SEQUENCE   1551 AA;  177582 MW;  5A2F6D302BC4BF15 CRC64;
     RPFEIIILLT IFANCVALAV YLPMPEDDTN VANSSLEKIE YAFLIFFAIE AMLKIIAYGF
     LFHTDAYLRN GWNVLDFSIV SLGLITMTLE QVNAKQGGTS GGKGGFDVKA LRAFRVLRPL
     RLVSGVPSLQ VVLNSIIKAM VPLLHIALLV LFMIIIYAIV GQELFKGKMH KTCYYLGTDV
     IATVASEKPA PCTSSGHGRH CTINGTECRS GWPGPNNGIT HFDNFGFAML TVYQCITMEG
     WTEVLYWVND AIGNEWPWIY FVSLILLGSF FVLNLVLGVL SGEFTKEREK AKSRGTFQKL
     REKQQLEEDL KGYMDWITHA EVMDSDRARG EGSSSAWSKT LSMRVGFLTL TILERQGRDS
     LPHVLPKGSS ESLGCRSLLS RRWRRWNRMF RRKCRDVVKS KFFYWLVILL VALNTLSIAS
     EHHFQPEWLT QVQDNANRVL LALFVAEMLL KMYALGLRQY FMSLFNRFDC FVVCAGILET
     ILVELGTLSP LGISVLRCIR LLRIFKITRY WTSLSNLVAS LLNSVRSIAS LLLLLFLFII
     VFALLGMQLF GGKFDFEDME VRRSTFDNFP QALISVFQIL TGEDWNSIMY DGIMAYGGPS
     FPGMLVCIYF IILFVCGNYI LLNVFLAIAV DNLAEAESLT LAQKAKAEER KRRKMSRVWP
     TCSIWQQYWH TQLHVLSVSP LFQLKVDEFE SNVNEIKDPY PSADFPGDDE EDEPEIPLSP
     RPRPLAELQL KEKAVPMPEA SSFFIFSPTN KFRMLCHRIV NATWFTNFIL LFILLSSISL
     AAEDPIRAES FRNQILGYFD IGFTSVFTVE IVLKMTAYGA FLHKGSFCRN SFNILDLLVV
     AVSLISMGIE SSAISVVKIL RVLRALRALR AINRAKGLKH VVQCVFVAIK TIGNIVVVTT
     LLQFMFACIG VQLFKGKFYR CTDPSKMTEK ECRGYFINYV DGDPTQIELQ ERVWLHSNFH
     FDNVFSAMMS LFTVSTFEGW PELLYMAIDT NAEDTGPVYN YRVEIAMFFI IYIILIAFFM
     MNIFVGFVIV TFQEQGESEY KNCELDKNQR QCVQYALKAR PLRRYIPKNP YQYQIWYVVT
     SSYFEYLIVW TYRGLTWLLL PSPQHYNQSA EMNHISDILN VAFTILFTLE MILKLMAFKA
     KGYFGDPWNV FDFLIVIGSI IDVILSEIDD SDDNSRVSIT FFRLFRVMRL VKLLSRGEGV
     RTLLWTFIKS FQALPYVALL IVMLFFIYAV IGMQMFGKIA MVDGTQINRN NNFQTFPQAV
     LLLFRCATGE AWQEILLDCS YGKLCDPESD FAEGEEYTCG TGFAYFYFIS FYMLCAFLII
     NLFVAVIMDN FDYLTRDWSI LGPHHLDEFK RIWAEYDPEA KGRIKHLDVV TLLRRIQPPL
     GFGKFCPHRV ACKRLVCMNM PLNSDGTVTF NATLFALVRT ALKIKTEGNF EQANEELRAI
     IKKIWKRTSM KLLDQVIPPI GDDEVTVGKF YATFLIQEHF RKFMKRQEEY YGYRPKKNPV
     EIQAGLRSIE EEAAPEIHRA ISGDLTAEEE LERAMVEAAM EEGIYRVSAA L
//
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