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Database: UniProt
Entry: I3MNK9_ICTTR
LinkDB: I3MNK9_ICTTR
Original site: I3MNK9_ICTTR 
ID   I3MNK9_ICTTR            Unreviewed;      2009 AA.
AC   I3MNK9;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-SEP-2017, entry version 37.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1C {ECO:0000313|Ensembl:ENSSTOP00000013255};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel)
OS   (Spermophilus tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha;
OC   Sciuridae; Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000013255, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Ensembl:ENSSTOP00000013255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000013255}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAY-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:ENSSTOP00000013255}.
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DR   EMBL; AGTP01074475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01074476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 43179.ENSSTOP00000013255; -.
DR   Ensembl; ENSSTOT00000014797; ENSSTOP00000013255; ENSSTOG00000014780.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; I3MNK9; -.
DR   OMA; PTTKINM; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Proteomes; UP000005215; 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 of dendrite; 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   PANTHER; PTHR10037:SF240; PTHR10037:SF240; 1.
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:UP000005215};
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:UP000005215};
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    193    214       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    226    248       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    394    411       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    431    454       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    523    542       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    595    622       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    765    788       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    800    819       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    840    866       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    886    915       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1011   1038       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1089   1106       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1118   1140       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1228   1251       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1321   1345       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1479   1513       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      625    651       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2009 AA;  226341 MW;  3C64E4E95D34817E CRC64;
     ERVEYLFLII FTVEAFLKVI AYGLLFHPNA YLRNGWNLLD FIIVVVGLFS AILEQATKAD
     GANALGGKGA GFDVKALRAF RVLRPLRLVS GVPSLQVVLN SIIKAMVPLL HIALLVLFVI
     IIYAIIGLEL FMGKMHKTCY NQEGIADLGD VPAEEDPSPC ALETGHGRQC QNGTVCKPGW
     DGPKHGITNF DNFAFAMLTV FQCITMEGWT DVLYWMQDAM GYELPWVYFV SLVIFGSFFV
     LNLVLGVLSG EFSKEREKAK ARGDFQKLRE KQQLEEDLKG YLDWITQAED IDPENEDEGM
     DEEKPRNRGT PAGLLDQKKG KFAWFSHSTE THVSMPTSET ESVNTENVAG GDIEGENCGA
     RLAHRISKSK FSRYWRRWNR FCRRKCRAAV KSNVFYWLVI FLVFLNTLTI ASEHYNQPHW
     LTEVQDTANK ALLALFTAEM LLKMYSLGLQ AYFVSLFNRF DCFIVCGGIL ETILVETKIM
     SPLGISVLRC VRLLRIFKIT RYWNSLSNLV ASLLNSVRSI ASLLLLLFLF IIIFSLLGMQ
     LFGGKFNFDE MQTRRSTFDN FPQSLLTVFQ ILTGEDWNSV MYDGIMAYGG PSFPGMLVCI
     YFIILFICGN YILLNVFLAI AVDNLADAES LTSAQKEEEE EKERKKLART ASPEKKQEVV
     EKPAVEETKE EKIELKSITA DGESPPTTKI NMDDLQPNEN EDKSSYPNPE AAGEEDEEEP
     EMPVGPRPRP LSELHLKEKA VPMPEASAFF IFSPNNRFRL QCHRIVNHTI FTNLILFFIL
     LSSISLAAED PVQHTSFRNH ILFYFDIVFT TIFTIEIALK MTAYGAFLHK GSFCRNYFNI
     LDLLVVSVSL ISFGIQSSAI NVVKILRVLR VLRPLRAINR AKGLKHVVQC VFVAIRTIGN
     IVIVTTLLQF MFACIGVQLF KGKLYTCSDS SKQTEAECKG NYITYKDGEV DHPIIQPRSW
     ENSKFDFDNV LAAMMALFTV STFEGWPELL YRSIDSHTED KGPIYNYRVE ISIFFIIYII
     IIAFFMMNIF VGFVIVTFQE QGEQEYKNCE LDKNQRQCVE YALKARPLRR YIPKNQHQYK
     VWYVVNSTYF EYLMFVLILL NTICLAMQHY GQSCLFKIAM NILNMLFTGL FTVEMILKLI
     AFKPKGYFSD PWNVFDFLIV IGSIIDVILS ETNPAEHTQC SPSMNAEENS RISITFFRLF
     RVMRLVKLLS RGEGIRTLLW TFIKSFQALP YVALLIVMLF FIYAVIGMQV FGKIALNDTT
     EINRNNNFQT FPQAVLLLFR CATGEAWQDI MLACMPGKKC APESEPSNST EGETPCGSSF
     AVFYFISFYM LCAFLIINLF VAVIMDNFDY LTRDWSILGP HHLDEFKRIW AEYDPEAKGR
     IKHLDVVTLL RRIQPPLGFG KLCPHRVACK RLVSMNMPLN SDGTVMFNAT LFALVRTALR
     IKTEGNLEQA NEELRAIIKK IWKRTSMKLL DQVVPPAGDD EVTVGKFYAT FLIQEYFRKF
     KKRKEQGLVG KPSQRNALSL QAGLRTLHDI GPEIRRAISG DLTAEEELDK AMKEAVSAAS
     EDDIFRRAGG LLVNHVNYYQ SDSRGAFPQT FTTQRPLHIN KAGNNQGDTE SPSHEKLVDS
     TFTPSSYSST GSNANINNAN NTALGRFPRP SGYPSTVSTV EGHGPPLSPA IRVQEAAWKL
     NSRRCSSRDS QLAMVCQEDG SREETYDVKM SEEAEYCSEP SLLSTEMLSY QDDENRQLTP
     PEEDKRDIRQ SPKRGFLRSA SLGRRASFHL ECLKRQKNQG GDISQKTVLP LHLVHHQALA
     VAGLSPLLQR SHSPTTFPRP CATPPATPGT RAWPPQPIPT LRLEGAESIE KLNSSFPSIH
     CSSWSEETAS CSGGSNTIRR ARPVSLTVPT QAAAPGRQFH GSASSLVEAV LISEGLGQFA
     QDPKFIEVTT QELADACDMT IEEMENAADS ILSGGAQQSP NGTLLPFVNC RDPGQDRAGG
     EEDGSCARAL GRGRSEEELQ DSRVYVSSL
//
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