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Database: UniProt
Entry: A0A093I2D8_STRCA
LinkDB: A0A093I2D8_STRCA
Original site: A0A093I2D8_STRCA 
ID   A0A093I2D8_STRCA        Unreviewed;      2169 AA.
AC   A0A093I2D8;
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=N308_01959 {ECO:0000313|EMBL:KFV88106.1};
OS   Struthio camelus australis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV88106.1, ECO:0000313|Proteomes:UP000053584};
RN   [1] {ECO:0000313|EMBL:KFV88106.1, ECO:0000313|Proteomes:UP000053584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV88106.1};
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}.
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DR   EMBL; KL206989; KFV88106.1; -; Genomic_DNA.
DR   Proteomes; UP000053584; 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; IPR031688; CAC1F_C.
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   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037:SF139; PTHR10037:SF139; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 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:UP000053584};
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:UP000053584};
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    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   1001   1032       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1090   1111       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1131   1158       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1210   1230       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1242   1262       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1274   1295       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1360   1383       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1452   1475       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1609   1643       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      753    787       {ECO:0000256|SAM:Coils}.
FT   COILED     1570   1590       {ECO:0000256|SAM:Coils}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KFV88106.1}.
FT   NON_TER    2169   2169       {ECO:0000313|EMBL:KFV88106.1}.
SQ   SEQUENCE   2169 AA;  246844 MW;  1BCF107B49E87356 CRC64;
     EANYASSTRI PLPGDGPTIQ SNSSAPSKQT VLSWQAAIDA ARQAKAAQNM STTTTQPVGS
     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 ENPACCGSLC 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 SDQKKPKDNK VTIAEYGEGE DEDKDPYPPC DVPVGEDEED EEDEPEVPAG
     PRPRRISELN MKEKITPIPE GSAFFIFSST NPIRVGCHRL INHHIFTNLI LVFIMLSSVS
     LAAEDPIRSH SFRNNILGYA DYVFTSMFTF EIILKVTAFG AFLHKGSFCR NYFNLLDLLV
     VGVSLVSFGI QSSAISVVKI LRVLRVLRPL RAINRAKGLK HVVQCVFVAI RTIGNIMIVT
     TLLQFMFACI GVQLFKVNRL SKFTPHQERQ SSADFLVAWG IYIVYKDGDV DNPMVKERVW
     QNSDFNFDNV LSAMMALFTV STFEGWPALL YKAIDSNGEN VGPVYNYRVE ISIFFIIYII
     IIAFFMMNIF VGFVIVTFQE QGEQEYKNCE LDKNQRQCVE YALKARPLRR YIPKNPYQYK
     FWYVVNSTGF EYIMFVLIML NTLCLAMQHY GQSKLFNDAM DIMNMVFTGV FTVEMVLKLI
     AFKPKIFVRK KERWLGYFSD AWNTFDSLIV IGSIVDVVLS EADPKPTETV TTDESGNSED
     SARISITFFR LFRVMRLVKL LSRGEGIRTL LWTFIKSFQA LPYVALLIAM LFFIYAVIGM
     QVFGKVAMRD NNQINRNNNF QTFPQAVLLL FRCATGEAWQ EIMLACLPGK RCDPESDYNP
     GEEYTCGSNF AIIYFISFYM LCAFLIINLF VAVIMDNFDY LTRDWSILGP HHLDEFKRIW
     SEYDPEAKGR IKHLDVVTLL RRIQPPLGFG KLCPHRVACK RLVAMNMPLN SDGTVMFNAT
     LFALVRTALK IKTEGNLEQA NEELRAVIKK IWKKTSMKLL DQVVPPAGDD EVTVGKFYAT
     FLIQDYFRKF KKRKEQGLVG KYPAKNTTIA LQAGLRTLHD IGPEIRRAIS CDLQDDEPEE
     NNPEEEEDVY KRNGALFGNH INHISSDRRD SFQQINTTHR PLHVQRPSIP SASDTEKNIY
     PQAGNSVYHN HNSVGKHVPN STNANLNNAN MSKVVHGKHI NIGNHEHRSE NGYHSYSRAD
     HEKRRRPSSR RTRYYETYIR SDSGDGRRPA ICREEHEVQD YCNDDHYLGE QDYFSGEEYY
     EEDSMLSGSR HIYDYHCRYH CHDSDFERPK GYHHPHGFFE EDDSQICYDT KRSPRRRLLP
     PTPTPNRRSS FNFECLRRQS SQDDIPLSPS FQHRTALPLH LMQQQVMAVA GLDSSKAHRH
     SPSRSTRSWA TPPATPPIRD RTPYYTPLIQ VDRAESTEQM NGSLPSLHRS SWYTDDPDIS
     YRTFTPANLT VPNDFRHKHS DKQRSADSLV EAVLISEGLG RYAKDPKFVS ATKHEIADAC
     DMTIDEMESA ASNLLNGNIS NGTNGDMFPI LSRQDYELQD FGPGYSDEEP DTGRYEEDLA
     DEMICITSL
//
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