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Database: UniProt
Entry: G3WVG8_SARHA
LinkDB: G3WVG8_SARHA
Original site: G3WVG8_SARHA 
ID   G3WVG8_SARHA            Unreviewed;      1211 AA.
AC   G3WVG8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   25-OCT-2017, entry version 40.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000019423};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000019423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E.,
RA   Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q.,
RA   Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A.,
RA   Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S.,
RA   Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y.,
RA   Kreiss A., Woods G.M., Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered
RT   marsupial Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000019423}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2011) to UniProtKB.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSSHAP00000019423}.
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DR   EMBL; AEFK01087093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEFK01087094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEFK01087095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEFK01087096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEFK01087097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 9305.ENSSHAP00000019423; -.
DR   Ensembl; ENSSHAT00000019580; ENSSHAP00000019423; ENSSHAG00000016495.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; G3WVG8; -.
DR   OMA; HNITDEI; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Proteomes; UP000007648; 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; IPR005452; LVDCC_a1dsu.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF139; PTHR10037:SF139; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01636; LVDCCALPHA1D.
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:UP000007648};
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:UP000007648};
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     26       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     38     57       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    110    133       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    189    210       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    222    244       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    362    380       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    400    423       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    492    511       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    564    591       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    725    743       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    755    774       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    795    821       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    841    871       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    968    993       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1047   1065       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1077   1097       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1189   1207       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        3    255       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      363    598       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      723   1000       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1043   1211       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   COILED      594    628       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1211 AA;  137700 MW;  2063B8FC02FA5595 CRC64;
     EKVEYAFLII FTVETFLKII AYGLLLHPNA YVRNGWNLLD FVIVIVGLFS VILEQLTKET
     EGGNHSSGKS GGFDVKALRA FRVLRPLRLV SGVPSLQVVL NSIIKAMVPL LHIALLVLFV
     IIIYAIIGLE LFIGKMHKSC FFTDTDILAE DDPAPCAFSG NGRQCTANGT ECRSGWVGPN
     GGITNFDNFA FAMLTVFQCI TMEGWTDVLY WMNDAMGFEL PWVYFVSLVI FGSFFVLNLV
     LGVLSGEFSK EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEDEGGEENK
     RSTSMPTSET ESVNTENISG EGETQGCCGR LCQAISKSKL SRRWRRWNRF SRRRCRAAVK
     SVSFYWLVIV LVFLNTLTIS SEHYNQPDWL TQIQDIANKV LLAMFTCEML VKMYSLGLQA
     YFVSLFNRFD CFVVCGGITE TILVELEIMS PLGISVFRCV RLLRIFKVTR HWTSLSNLVA
     SLLNSMKSIA SLLLLLFLFI IIFSLLGMQL FGGKFNFDET QTKRSTFDNF PQALLTVFQI
     LTGEDWNAVM YDGIMAYGGP SSSGMIVCIY FIILFICGNY ILLNVFLAIA VDNLADAESL
     NTAQKEEAEE KERKKTARKE SLENKRNDKP EVNPMANSDH KVIIDDYRGE DEDKDPYPPC
     DVPVGEEEEE EEDEPEVPAG PRPRRISELN MKEKIIPIPE GSAFFIFSKT NPIRVGCHRL
     INHHIFTNLI LVFIMLSSAS LAAEDPIRSH SFRNIILGYF DYAFTAIFTV EILLKMTTFG
     AFLHKGAFCR NYFNLLDMLV VGVSLVSFGI QSSAISVVKI LRVLRVLRPL RAINRAKGLK
     HVVQCVFVAI RTIGNIMIVT TLLQFMFACI GVQLFKGKFY RCTDEAKSNP EECRGLFILY
     KDGDVNSPMV RERVWQNSDF NFDNVLSAMM ALFTVSTFEG WPALLYKAID SNGENVGPIY
     NYRVEISIFF IIYIIIVAFF MMNIFVGFVI VTFQEQGEKE YKNCELDKNQ RQCVEYALKA
     RPLRRYIPKN PYQYKFWYVV NSSPFEYMMF VLIMLNTLCL AMQHYEQSKI FNDAMDILNM
     VFTGVFTVEM VLKVIAFKPK HYFTDAWNTF DALIVVGSVV DIAITEVNPT DNESSPVPVP
     TAAPGNSEES NRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIAML
     FFIYAVIGMQ V
//
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