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Database: UniProt
Entry: G3TJA9_LOXAF
LinkDB: G3TJA9_LOXAF
Original site: G3TJA9_LOXAF 
ID   G3TJA9_LOXAF            Unreviewed;      2004 AA.
AC   G3TJA9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   25-OCT-2017, entry version 45.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1C {ECO:0000313|Ensembl:ENSLAFP00000014806};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000014806};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000014806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000014806};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S.,
RA   Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000014806}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000014806};
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:ENSLAFP00000014806}.
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DR   STRING; 9785.ENSLAFP00000014806; -.
DR   Ensembl; ENSLAFT00000017657; ENSLAFP00000014806; ENSLAFG00000017643.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; G3TJA9; -.
DR   OMA; PTTKINM; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IEA:Ensembl.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0051393; F:alpha-actinin binding; IEA:Ensembl.
DR   GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IEA:Ensembl.
DR   GO; GO:0086056; F:voltage-gated calcium channel activity involved in AV node cell action potential; IEA:Ensembl.
DR   GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; IEA:Ensembl.
DR   GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0002520; P:immune system development; IEA:Ensembl.
DR   GO; GO:0098912; P:membrane depolarization during atrial cardiac muscle cell action potential; IEA:Ensembl.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
DR   GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IEA:Ensembl.
DR   InterPro; IPR031688; CAC1F_C.
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   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 2.
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:UP000007646};
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:UP000007646};
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     56       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    109    131       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    190    211       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    223    245       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    391    408       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    428    451       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    520    539       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    592    619       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    762    785       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    797    816       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    837    863       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    883    912       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1008   1035       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1086   1107       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1119   1139       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1225   1243       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1319   1342       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1476   1510       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      622    648       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2004 AA;  225944 MW;  F23611BF84E1F33E CRC64;
     ERVEYLFLII FTVEAFLKVI AYGLLFHPNA YLRNGWNLLD FIIVVVGLFS AILEQATKAD
     GANALGGKGA GFDVKALRAF RVLRPLRLVS GVPSLQVVLN SIIKAMVPLL HIALLVLFVI
     IIYAIIGLEL FMGKMHKTCY NQEGIADVPA EDDPSPCALE TGHGRQCQNG TVCKPGWDGP
     KHGITNFDNF AFAMLTVFQC ITMEGWTDVL YWVNDAVGRD WPWIYFVTLI IIGSFFVLNL
     VLGVLSGEFS KEREKAKARG DFQKLREKQQ LEEDLKGYLD WITQAEDIDP ENEDEGMDEE
     KPRNRGTPAG LLDKKKGKFA WFSHSTKTHV SMPTSETESV NTENVAGGDI EGENCGARLA
     HRISKSKFSR YWRRWNRFCR RKCRAAVKSN IFYWLVIFLV FLNTLTIASE HYNQPHWLTE
     VQDTANKALL ALFTAEMLLK MYSLGLQAYF VSLFNRFDCF IVCGGILETI LVETKIMSPL
     GISVLRCVRL LRIFKITRYW NSLSNLVASL LNSVRSIASL LLLLFLFIII FSLLGMQLFG
     GKFNFDEMQT RRSTFDNFPQ SLLTVFQILT GEDWNSVMYD GIMAYGGPSF PGMLVCIYFI
     ILFICGNYIL LNVFLAIAVD NLADAESLTS AQKEEEEEKE RKKLARTASP EKKQELVEKP
     AVEETKEEKI ELKSITADGE SPPTTKINMD DLQPNENEDK SPYPNPETTG EEEEEEPEMP
     VGPRPRPLSE LHLKEKAVPM PEASAFFIFS ANNRFRLQCH RIVNDTIFTN LILFFILLSS
     ISLAAEDPVQ HTSFRNHILY YFDIVFTTIF TIEIALKMTA YGAFLHKGSF CRNYFNILDL
     LVVSVSLISF GIQSSAINVV KILRVLRVLR PLRAINRAKG LKHVVQCVFV AIRTIGNIVI
     VTTLLQFMFA CIGVQLFKGK LYTCSDSSKQ TEAECKGNYI TYKDGEVDHP IIQPRSWENS
     KFDFDNVLAA MMALFTVSTF EGWPELLYRS IDSHTEDKGP IYNYRVEISI FFIIYIIIIA
     FFMMNIFVGF VIVTFQEQGE QEYKNCELDK NQRQCVEYAL KARPLRRYIP KNQHQYKVWY
     VVNSTYFEYL MFVLILLNTI CLAMQHYGQS CLFKIAMNIL NMLFTGLFTV EMILKLIAFK
     PKHYFCDAWN TFDALIVVGS IVDIAITEVN PAEHTQCSPS MNAEENSRIS ITFFRLFRVM
     RLVKLLSRGE GIRTLLWTFI KSFQALPYVA LLIVMLFFIY AVIGMQVFGK IALNDTTEIN
     RNNNFQTFPQ AVLLLFRCAT GEAWQDIMLA CMPGKKCAPE SEPSNSTEGE TPCGSSFAVF
     YFISFYMLCA FLIINLFVAV IMDNFDYLTR DWSILGPHHL DEFKRIWAEY DPEAKGRIKH
     LDVVTLLRRI QPPLGFGKLC PHRVACKRLV SMNMPLNSDG TVMFNATLFA LVRTALRIKT
     EGNLEQANEE LRAIIKKIWK RTSMKLLDQV VPPAGDDEVT VGKFYATFLI QEYFRKFKKR
     KEQGLVGKPS QRNTLSLQAG LRTLHDLGPE IRRAISGDLT AEEELDKAMK EAVSAASEDD
     IFRRAGGLFG NHVSYYQSDG RNAFPQTFTT QRPLHINKAG NSQGDTESPS HEKLVDSTFT
     PSSYSSTGSN ANINNNNTAL GRFPRPTGYP STVSTVEGHG PPLSPAIRVQ ESAWKLSSKR
     CHSRESQIAM VCQEEVSQDE TYEVKINEDA EYCSEPSLIS TEMLSYQDDE NRQLTPPEDK
     RDIRQSPKRG FLRSASLGRR ASFHLECLKR QKNQGGDISQ KTVLPLHLVH HQALAVAGLS
     PLLQRSHSPT MFPRPCATPP ATPGSRGWPP QPIPTLRLEG AESSEKLNSS FPSIHCSSWS
     EESPSCDGGG STIRRTRPVS LTVPSQAGAP GRQFHGSASS LVEAVLISEG LGQFAQDPKF
     IEVTTQELAD ACDMTIEEME NAADNILSGG AQQSPNGTLL PFVNCRDPGQ DRAGGEEDAT
     CGPALECRKS EEELQDSRVY VSSL
//
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