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Database: UniProt
Entry: A0A091LKQ2_CATAU
LinkDB: A0A091LKQ2_CATAU
Original site: A0A091LKQ2_CATAU 
ID   A0A091LKQ2_CATAU        Unreviewed;      1641 AA.
AC   A0A091LKQ2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   25-OCT-2017, entry version 18.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
DE   Flags: Fragment;
GN   ORFNames=N323_04195 {ECO:0000313|EMBL:KFP56267.1};
OS   Cathartes aura (Turkey vulture) (Vultur aura).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Ciconiiformes; Cathartidae;
OC   Cathartes.
OX   NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP56267.1, ECO:0000313|Proteomes:UP000053745};
RN   [1] {ECO:0000313|EMBL:KFP56267.1, ECO:0000313|Proteomes:UP000053745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP56267.1};
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; KL325792; KFP56267.1; -; Genomic_DNA.
DR   Proteomes; UP000053745; 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; IPR005452; LVDCC_a1dsu.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF139; PTHR10037:SF139; 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; PR01636; LVDCCALPHA1D.
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:UP000053745};
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:UP000053745};
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    111    128       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    148    168       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    180    198       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    252    275       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    331    352       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    364    386       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    521    539       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    559    582       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    651    670       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    723    750       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    885    903       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    923    943       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    955    981       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1016   1035       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1079   1100       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1120   1147       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1199   1219       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1231   1250       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1349   1372       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1440   1464       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1598   1632       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      753    787       {ECO:0000256|SAM:Coils}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KFP56267.1}.
FT   NON_TER    1641   1641       {ECO:0000313|EMBL:KFP56267.1}.
SQ   SEQUENCE   1641 AA;  186137 MW;  58C4D4BA95D6E072 CRC64;
     EANYASSTRI PLPGDGPAIQ SNSSAPSKQT VLSWQAAIDA ARQAKAAQNM STTTAQPVGS
     LSQRKRQQYA KSKKQGNTSN SRPPRALFCL SLNNPIRRAC ISLVEWKPFD IFILLSIFAN
     CVALAVYIPF PEDDSNSTNH NLEKVEYAFL IIFTVETFLK IIAYGLLLHP NAYVRNGWNL
     LDFVIVVVGL FSVILEQLTK ETEGGSHSGG KPGGFDVKAL RAFRVLRPLR LVSGVPSLQV
     VLNSIIKAMV PLLHIALLVL FVIIIYAIIG LELFIGKMHK SCFLIDSDIL VEEDPAPCAF
     SGNGRQCVMN GTECKGGWVG PNGGITNFDN FAFAMLTVFQ CITMEGWTDV LYWVNDAIGC
     EWPWIYFVSL IILGSFFVLN LVLGVLSGEF SKEREKAKAR GDFQKLREKQ QLEEDLKGYL
     DWITQAEDID PENDEEVDEE GKRNRVTLAD LMEEKKKSRF SCFGRSSNKH ASMPTSETES
     VNTENVSGEG ENAACCGSLC RRWRRWNRFN RRKCRAAVKS VTFYWLVIVL VFLNTLTISS
     EHYNQPDWLT QIQDIANKVL LALFTCEMLV KMYSLGLQAY FVSLFNRFDC FVVCGGIVET
     ILVELEIMSP LGISVFRCVR LLRIFKVTRH WASLSNLVAS LLNSMKSIAS LLLLLFLFII
     IFSLLGMQLF GGKFNFDETQ TKRSTFDNFP QALLTVFQIL TGEDWNAVMY DGIMAYGGPS
     SSGMIVCIYF IILFICGNYI LLNVFLAIAV DNLADAESLN TAQKEEAEEK ERKKNARKES
     LENKKSEKSE GDQKKPKDSK VTIAEYGEGE DEDKDPYPPC DVPVGEDEED EEDEPEVPAG
     PRPRRISELN MKEKITPIPE GSAFFIFSST NPIRVGCHRL INHHIFTNLI LVFIMLSSVS
     LAAEDPIRSH SFRNNILGYA DYVFTSMFTF EIILKVTAFG AFLHKGSFCR NYFNLLDLLV
     VGVSLVSFGI QSSAISVVKI LRVLRVLRPL RAINRAKGLK HVVQCVFVAI RTIGNIMIVT
     TLLQFMFACI GVQLFKVSRH SQNLHCIKGI YIVYKDGDVD NPMVKERVWQ NSDFNFDNVL
     SAMMALFTVS TFEGWPALLY KAIDSNGENV GPVYNYRVEI SIFFIIYIII IAFFMMNIFV
     GFVIVTFQEQ GEQEYKNCEL DKNQRQCVEY ALKARPLRRY IPKNPYQYKF WYVVNSTGFE
     YIMFVLIMLN TLCLAMQHYG QSKLFNDAMD IMNMVFTGVF TVEMVLKLIA FKPKIFVRKK
     ERWLHYFTDA WNTFDALIVV GSVVDIAITE VNPKPTETVT TDESGNSEDS ARISITFFRL
     FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIAML FFIYAVIGMQ VFGKVAMRDN
     NQINRNNNFQ TFPQAVLLLF RCATGEAWQE IMLACLPGKR CDPESDYNPG EEYTCGSNFA
     IIYFISFYML CAFLIINLFV AVIMDNFDYL TRDWSILGPH HLDEFKRIWS EYDPEAKGRI
     KHLDVVTLLR RIQPPLGFGK LCPHRVACKR LVAMNMPLNS DGTVMFNATL FALVRTALKI
     KTEGNLEQAN EELRAVIKKI WKKTSMKLLD QVVPPAGDDE VTVGKFYATF LIQDYFRKFK
     KRKEQGLVGK YPAKNTTIAL Q
//
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