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Database: UniProt
Entry: H0XGF3_OTOGA
LinkDB: H0XGF3_OTOGA
Original site: H0XGF3_OTOGA 
ID   H0XGF3_OTOGA            Unreviewed;      1783 AA.
AC   H0XGF3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   25-OCT-2017, entry version 42.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1D {ECO:0000313|Ensembl:ENSOGAP00000015157};
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirrhini;
OC   Lorisiformes; Galagidae; Otolemur.
OX   NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000015157, ECO:0000313|Proteomes:UP000005225};
RN   [1] {ECO:0000313|Ensembl:ENSOGAP00000015157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSOGAP00000015157}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2012) 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:ENSOGAP00000015157}.
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DR   EMBL; AAQR03061872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03061873; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03061874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03061875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03061876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03061877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 30611.ENSOGAP00000015157; -.
DR   Ensembl; ENSOGAT00000016932; ENSOGAP00000015157; ENSOGAG00000016920.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; H0XGF3; -.
DR   OMA; LIQVERP; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
DR   GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IEA:Ensembl.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR   GO; GO:0051393; F:alpha-actinin binding; IEA:Ensembl.
DR   GO; GO:0030506; F:ankyrin binding; IEA:Ensembl.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IEA:Ensembl.
DR   GO; GO:0086059; F:voltage-gated calcium channel activity involved SA node cell action potential; IEA:Ensembl.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0070509; P:calcium ion import; IEA:Ensembl.
DR   GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IEA:Ensembl.
DR   GO; GO:0051928; P:positive regulation of calcium ion transport; IEA:Ensembl.
DR   GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; IEA:Ensembl.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
DR   GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
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   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; 3.
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:UP000005225};
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:UP000005225};
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    144    162       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    182    205       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    274    293       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    346    373       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    507    525       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    545    565       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    577    603       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    623    653       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    750    775       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    829    847       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    859    879       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    969    987       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1063   1086       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1220   1254       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      376    407       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1783 AA;  203617 MW;  EDD40D4749333AFA CRC64;
     LVLFASPREF SKEREKAKAR GDFQKLREKQ QLEEDLKGYL DWITQAEDID PENEEEGGEE
     SKRNTSMPTS ETESVNTENV SGEGETQGCC ASLWCWWRRR DAAKTGPSGC RRWGQAISKS
     KLSRRWRRWN RFNRRRCRAA VKSVTFYWLV IVLVFLNTLT ISSEHYNQPD WLTQIQDIAN
     KVLLALFTCE MLVKMYSLGL QAYFVSLFNR FDCFVVCGGI TETILVELEI MSPLGISVFR
     CVRLLRIFKV TRHWTSLSNL VASLLNSMKS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD
     ETQTKRSTFD NFPQALLTVF QILTGEDWNA VMYDGIMAYG GPSSSGMIVC IYFIILFICG
     NYILLNVFLA IAVDNLADAE SLNTAQKEEA EEKERKKIAR KESLENKKNK PEVNQIANSD
     NKVTIDDYQE EEEDKDPYPP CDVPVGEEEE EEEEDEPEVP AGPRPRRISE LNMKEKITPI
     PEGSAFFILS KTNPIRVGCH KLINHHIFTN LILVFIMLSS AALAAEDPIR SHSFRNTILG
     YFDYAFTAIF TVEILLKMTT FGAFLHKGAF CRNYFNLLDM LVVGVSLVSF GIQSSAISVV
     KILRVLRVLR PLRAINRAKG LKHVVQCVFV AIRTIGNIMI VTTLLQFMFA CIGVQLFKGK
     FYRCTDEAKS NPEDCKGLFI LYKDGDVDSP VVRERIWQNS DFNFDNVLSA MMALFTVSTF
     EGWPALLYKA IDSNGENVGP VYNYRVEISI FFIIYIIIVA FFMMNIFVGF VIVTFQEQGE
     KEYKNCELDK NQRQCVEYAL KARPLRRYIP KNPYQYKFWY VVNSSPFEYM MFVLIMLNTL
     CLAMQHYEQS KMFNDAMDIL NMVFTGVFTV EMVLKVIAFK PKHYFTDAWN TFDALIVVGS
     VVDIAITEVN PTESENVPVP TTTPGNSEES NRISITFFRL FRVMRLVKLL SRGEGIRTLL
     WTFIKSFQAL PYVALLIAML FFIYAVIGMQ MFGKVAMRDN NQINRNNNFQ TFPQAVLLLF
     RKRCATGEAW QEIMLACLPG KLCDPESDYN PGEEYTCGSN FAIVYFISFY MLCAFLIINL
     FVAVIMDNFD YLTRDWSILG PHHLDEFKRI WSEYDPEAKG RIKHLDVVTL LRRIQPPLGF
     GKLCPHRVAC KRLVAMNMPL NSDGTVMFNA TLFALVRTAL KIKTEGNLEQ ANEELRAVIK
     KIWKKTSMKL LDQVVPPAGD DEVTVGKFYA TFLIQDYFRK FKKRKEQGLV GKYPAKNTTI
     ALQAGLRTLH DIGPEIRRAI SCDLQDDEPE ETKREEEEDV FKRNGALLGN HVNHVNSDRR
     DSLQQTNTTH RPLHVQRPSI PPASDTEKPL FPPAGNSVCH NHHNHNSIGK HVPTSTNANL
     NNANMSKAAH GKRPSTGNLE HVSENGHHSS HKHDREPQRR SSIKRTRYYE TYIRSDSGDE
     QLPTICREDP EIHGYFRDPR CLGEQEYFSS EECYEDDSSP PASRQTYGYY SRYLGSNSDF
     ERPRGYHHPQ GFLEDDDSPV CYDSRRSPRR RLLPPTPTSH RRSSFNFECL RRQSSQEEVP
     PSPIFPHRTA LPLHLMQQQI MAVAGLDSSK AQKYSPSHST RSWATPPATP PYQDWAPCYT
     PLIQVERSES LDQVNGSLPS LHRSSWYTDE PDISYRTFTP ASLTVPSSFR NKNSDKQRSA
     DSLVEAVLIS EGLGRYARDP KFVSATKHEI ADACDLTIDE MESAASTLLN GNVHPRANGD
     VGPTSHRQDY ELQDFGPGYS DDEPDPGRDE EDLADEMICI TTL
//
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