ID I3MNK9_ICTTR Unreviewed; 2193 AA.
AC I3MNK9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 28-MAR-2018, entry version 43.
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
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}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AGTP01074468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01074469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01074470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01074471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01074472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01074473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01074474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
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 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; 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:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IEA:Ensembl.
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; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR005451; VDCC_L_a1csu.
DR InterPro; IPR005446; VDCC_L_a1su.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
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|SAAS:SAAS00085096, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
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 156 173 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 193 213 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 225 243 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 296 318 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 377 398 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 410 432 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 578 595 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 615 638 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 707 726 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 779 806 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 949 972 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 984 1003 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1024 1050 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1070 1099 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1195 1222 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1273 1290 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1302 1324 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1412 1435 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1505 1529 Helical. {ECO:0000256|SAM:Phobius}.
FT DOMAIN 1663 1697 Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT COILED 809 835 {ECO:0000256|SAM:Coils}.
FT COILED 1624 1644 {ECO:0000256|SAM:Coils}.
SQ SEQUENCE 2193 AA; 246107 MW; 4ED0CDDD2C37E646 CRC64;
MLRAFVQPST PAYQPLSSHL SAETEVKFKG TLVHEAQLNC FYISPGGSNY GSPRSANMNA
NAAAGLAPEH IPTPGAALSW QAAIDAARQA KLMGSAGNAT ISTVSSTQRK RQQYGKPKKQ
SGTTATRPPR ALLCLTLKNP IRRACISIVE WKPFEIIILL TIFANCVALA IYIPFPEDDS
NATNSNLERV EYLFLIIFTV EAFLKVIAYG LLFHPNAYLR NGWNLLDFII VVVGLFSAIL
EQATKADGAN ALGGKGAGFD VKALRAFRVL RPLRLVSGVP SLQVVLNSII KAMVPLLHIA
LLVLFVIIIY AIIGLELFMG KMHKTCYNQE GIADVPAEED PSPCALETGH GRQCQNGTVC
KPGWDGPKHG ITNFDNFAFA MLTVFQCITM EGWTDVLYWM QDAMGYELPW VYFVSLVIFG
SFFVLNLVLG VLSGEFSKER EKAKARGDFQ KLREKQQLEE DLKGYLDWIT QAEDIDPENE
DEGMDEEKPR NRGTPAGLLD QKKGKFAWFS HSTETHVSMP TSETESVNTE NVAGGDIEGE
NCGARLAHRI SKSKFSRYWR RWNRFCRRKC RAAVKSNVFY WLVIFLVFLN TLTIASEHYN
QPHWLTEVQD TANKALLALF TAEMLLKMYS LGLQAYFVSL FNRFDCFIVC GGILETILVE
TKIMSPLGIS VLRCVRLLRI FKITRYWNSL SNLVASLLNS VRSIASLLLL LFLFIIIFSL
LGMQLFGGKF NFDEMQTRRS TFDNFPQSLL TVFQILTGED WNSVMYDGIM AYGGPSFPGM
LVCIYFIILF ICGNYILLNV FLAIAVDNLA DAESLTSAQK EEEEEKERKK LARTASPEKK
QEVVEKPAVE ETKEEKIELK SITADGESPP TTKINMDDLQ PNENEDKSSY PNPEAAGEED
EEEPEMPVGP RPRPLSELHL KEKAVPMPEA SAFFIFSPNN RFRLQCHRIV NHTIFTNLIL
FFILLSSISL AAEDPVQHTS FRNHILFYFD IVFTTIFTIE IALKMTAYGA FLHKGSFCRN
YFNILDLLVV SVSLISFGIQ SSAINVVKIL RVLRVLRPLR AINRAKGLKH VVQCVFVAIR
TIGNIVIVTT LLQFMFACIG VQLFKGKLYT CSDSSKQTEA ECKGNYITYK DGEVDHPIIQ
PRSWENSKFD FDNVLAAMMA LFTVSTFEGW PELLYRSIDS HTEDKGPIYN YRVEISIFFI
IYIIIIAFFM MNIFVGFVIV TFQEQGEQEY KNCELDKNQR QCVEYALKAR PLRRYIPKNQ
HQYKVWYVVN STYFEYLMFV LILLNTICLA MQHYGQSCLF KIAMNILNML FTGLFTVEMI
LKLIAFKPKG YFSDPWNVFD FLIVIGSIID VILSETNPAE HTQCSPSMNA EENSRISITF
FRLFRVMRLV KLLSRGEGIR TLLWTFIKSF QALPYVALLI VMLFFIYAVI GMQVFGKIAL
NDTTEINRNN NFQTFPQAVL LLFRCATGEA WQDIMLACMP GKKCAPESEP SNSTEGETPC
GSSFAVFYFI SFYMLCAFLI INLFVAVIMD NFDYLTRDWS ILGPHHLDEF KRIWAEYDPE
AKGRIKHLDV VTLLRRIQPP LGFGKLCPHR VACKRLVSMN MPLNSDGTVM FNATLFALVR
TALRIKTEGN LEQANEELRA IIKKIWKRTS MKLLDQVVPP AGDDEVTVGK FYATFLIQEY
FRKFKKRKEQ GLVGKPSQRN ALSLQAGLRT LHDIGPEIRR AISGDLTAEE ELDKAMKEAV
SAASEDDIFR RAGGLLVNHV NYYQSDSRGA FPQTFTTQRP LHINKAGNNQ GDTESPSHEK
LVDSTFTPSS YSSTGSNANI NNANNTALGR FPRPSGYPST VSTVEGHGPP LSPAIRVQEA
AWKLNSRRCS SRDSQLAMVC QEDGSREETY DVKMSEEAEY CSEPSLLSTE MLSYQDDENR
QLTPPEEDKR DIRQSPKRGF LRSASLGRRA SFHLECLKRQ KNQGGDISQK TVLPLHLVHH
QALAVAGLSP LLQRSHSPTT FPRPCATPPA TPGTRAWPPQ PIPTLRLEGA ESIEKLNSSF
PSIHCSSWSE ETASCSGGSN TIRRARPVSL TVPTQAAAPG RQFHGSASSL VEAVLISEGL
GQFAQDPKFI EVTTQELADA CDMTIEEMEN AADSILSGGA QQSPNGTLLP FVNCRDPGQD
RAGGEEDGSC ARALGRGRSE EELQDSRVYV SSL
//
