GenomeNet

Database: UniProt
Entry: A0A091EXP9_CORBR
LinkDB: A0A091EXP9_CORBR
Original site: A0A091EXP9_CORBR 
ID   A0A091EXP9_CORBR        Unreviewed;      1635 AA.
AC   A0A091EXP9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   28-MAR-2018, entry version 22.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
DE   Flags: Fragment;
GN   ORFNames=N302_04689 {ECO:0000313|EMBL:KFO54430.1};
OS   Corvus brachyrhynchos (American crow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC   Corvus.
OX   NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO54430.1, ECO:0000313|Proteomes:UP000052976};
RN   [1] {ECO:0000313|EMBL:KFO54430.1, ECO:0000313|Proteomes:UP000052976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO54430.1};
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
CC       opposite 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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; KK718109; KFO54430.1; -; Genomic_DNA.
DR   Proteomes; UP000052976; 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   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.350; -; 4.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005451; VDCC_L_a1csu.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
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; PR01635; LVDCCALPHA1C.
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:UP000052976};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAAS:SAAS00085096, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052976};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00084820,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00084701,
KW   ECO:0000256|SAM:Phobius}; 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    383    400       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    420    443       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    512    531       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    574    596       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    739    757       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    777    797       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    855    884       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    980   1007       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1103   1123       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1138   1155       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1223   1246       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1316   1340       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1474   1508       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      625    645       {ECO:0000256|SAM:Coils}.
FT   COILED     1435   1455       {ECO:0000256|SAM:Coils}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KFO54430.1}.
FT   NON_TER    1635   1635       {ECO:0000313|EMBL:KFO54430.1}.
SQ   SEQUENCE   1635 AA;  185878 MW;  82440FD762688FB2 CRC64;
     ERVEYLFLII FTVEAFLKVI AYGLLFHPNA YLRNGWNLLD FIIVVVGLFS AILEQATKAD
     GGNSIGGKGA GFDVKALRAF RVLRPLRLVS GVPSLQVVLN SIIKAMVPLL HIALLVLFVI
     IIYAIIGLEL FMGKMHKTCY HVQGGLMDTP AEDDPSPCAP QSAHGRQCQN GTECKAGWEG
     PKHGITNFDN FAFAMLTVFQ CITMEGWTDV LYWVNDAIGR DWPWIYFVTL IIIGSFFVLN
     LVLGVLSGEF SKEREKAKAR GDFQKLREKQ QLEEDLKGYL DWITQAEDID PENEDEGMDE
     EKPRNRSPPA GLPDEKKGKF AWFSHSTESH VSMPTSETES VNTDNVPGAD MEGENCGARL
     ARYWRRWNRF CRRKCRAAVK SNVFYWLVIF LVFLNTLTIA SEHYNQPDWL TEVQDTANKV
     LLALFTAEML LKMYSLGLQA YFVSLFNRFD CFIVCGGILE TILVETKIMS PLGISVLRCV
     RLLRIFKITR YWNSLSNLVA SLLNSVRSIA SLLLLLFLFI IIFSLLGMQL FGGKFNFDEM
     QTRRSTFDNF PQSLLTVFQI LTGEDWNSVM YDGIMAYGGP SFPGMLVCIY FIILFICGNW
     KQLSTFVTLR FLSCKIARTA SPEKKQEMEK TAVEEETKEE KIELKSITAD GESPPATKIN
     VDDYQPNENE EKSPYPTTEA PAEEDEEEPE MPVGPRPRPM SELHLKEKAV PMPDASAFFI
     FSPNNRFRVH CHRIVNDNIF TNLILFFILL SSISLAAEDP VRHLSFRNQI LGNADYVFTS
     IFTLEIILKM TAYGAFLHKG SFCRNYFNIL DLLVVSVSLI SFGIQSSAIN VVKILRVLRV
     LRPLRAINRA KGLKHVVQCV FVAIRTIGNI VIVTTLLQFM FACIGVQLFK GKLYSCTDSS
     KQTEAECRGY YITYKDGEVS QPMIQPRSWE NSKFDFDNVL TAMMALFTVS TFEGWPELLY
     RSIDSHMEDV GPIYNHRVEI SIFFIIYIII IAFFMMNIFV GFVIVTFQEQ GEQEYKNCEL
     DKNQRQCVEY ALKARPLRRY IPKNQYQYKV WYVVNSTYFE YLSKLGGVLC IPDCWHVLPS
     HSCWDAIFQH YGQSCMFKEA MNILNMLFTG LFTVEMVLKL IAFKPKVGAL GGYFSDPWNV
     FDFLIVIGSI IDVILSETNV RPSFLSCCCN SCLCANGFQN AEENSRISIT FFRLFRVMRL
     VKLLSRGEGI RTLLWTFIKS FQALPYVALL IVMLFFIYAV IGMQVFGKIA LNDTTEINRN
     NNFQTFPQAV LLLFRCATGE AWQEIMLACL PDKKCDPESE PANSTEADHS CGRSFAVFYF
     ISFYMLCAFL IINLFVAVIM DNFDYLTRDW SILGPHHLDE FKRIWAEYDP EAKGRIKHLD
     VVTLLRRIQP PLGFGKLCPH RVACKRLVSM NMPLNSDGTV MFNATLFALV RTALRIKTEG
     NLEQANEELR AIIKKIWKRT SMKLLDQVVP PAGDDEVTVG KFYATFLIQE YFRKFKKRKE
     QGLVGKPSQR NALSLQAGLR TLHDIGPEIR RAISGDLTAE EELDKAMKEA VSAASEDDIF
     RRAGGLFGNH VSYYQSDGRS GFPQTFTTQR PLHINKSGNN HGDTESPSHE KLVDSTFTPS
     SYSSSGSNAN INNAN
//
DBGET integrated database retrieval system