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Database: UniProt
Entry: C7TQ59_MOUSE
LinkDB: C7TQ59_MOUSE
Original site: C7TQ59_MOUSE 
ID   C7TQ59_MOUSE            Unreviewed;      2169 AA.
AC   C7TQ59;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-SEP-2017, entry version 69.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=Cacna1c {ECO:0000313|EMBL:CAS06714.1,
GN   ECO:0000313|Ensembl:ENSMUSP00000140961, ECO:0000313|MGI:MGI:103013};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:CAS06714.1};
RN   [1] {ECO:0000313|EMBL:CAS06714.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6N {ECO:0000313|EMBL:CAS06714.1};
RC   TISSUE=Heart {ECO:0000313|EMBL:CAS06714.1};
RA   Link S.A.M.;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAS06714.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6N {ECO:0000313|EMBL:CAS06714.1};
RC   TISSUE=Heart {ECO:0000313|EMBL:CAS06714.1};
RA   Link S., Meissner M., Held B., Beck A., Weissgerber P., Freichel M.,
RA   Flockerzi V.;
RT   "Diversity and developmental expression of L-type calcium channel ?2
RT   proteins and their influence on calcium current in murine heart.";
RL   J. Biol. Chem. 0:0-0(2009).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000140961, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000140961,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4] {ECO:0000213|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [5] {ECO:0000313|Ensembl:ENSMUSP00000140961}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000140961};
RG   Ensembl;
RL   Submitted (SEP-2014) 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}.
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DR   EMBL; AC036121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC115816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC126453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC127328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC163353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FM872411; CAS06714.1; -; mRNA.
DR   RefSeq; NP_001242928.1; NM_001255999.2.
DR   UniGene; Mm.41628; -.
DR   UniGene; Mm.436656; -.
DR   Ensembl; ENSMUST00000187474; ENSMUSP00000140961; ENSMUSG00000051331.
DR   GeneID; 12288; -.
DR   UCSC; uc012erh.3; mouse.
DR   CTD; 775; -.
DR   MGI; MGI:103013; Cacna1c.
DR   GeneTree; ENSGT00830000128247; -.
DR   ChiTaRS; Cacna1c; mouse.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000051331; -.
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; 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; 1.
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   1: Evidence at protein level;
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:UP000000589};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Proteomics identification {ECO:0000213|MaxQB:C7TQ59};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
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    158    175       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    195    215       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    227    245       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    298    320       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    379    400       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    412    434       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    555    573       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    681    703       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    757    783       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    931    950       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    962    984       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1004   1027       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1048   1081       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1173   1199       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1250   1267       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1279   1301       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1389   1412       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1482   1506       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1640   1674       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      786    812       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2169 AA;  243507 MW;  DD71D35A97F120BA CRC64;
     MIRAFVQPST PPYQPLSSHS SEETERKFKG KVVHEAQLNC FYISPGGSNY GSPRPAHANM
     NANAAAGLAP EHIPTPGAAL SWQAAIDAAR QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK
     KQGGTTATRP PRALLCLTLK NPIRRACISI VEWKPFEIII LLTIFANCVA LAIYIPFPED
     DSNATNSNLE RVEYLFLIIF TVEAFLKVIA YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA
     ILEQATKADG ANALGGKGAG FDVKALRAFR VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH
     IALLVLFVII IYAIIGLELF MGKMHKTCYN QEGIIDVPAE EDPSPCALET GHGRQCQNGT
     VCKPGWDGPK HGITNFDNFA FAMLTVFQCI TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI
     FGSFFVLNLV LGVLSGEFSK EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE
     NEDEGMDEDK PRNMSMPTSE TESVNTENVA GGDIEGENCG ARLAHRISKS KFSRYWRRWN
     RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT IASEHYNQPH WLTEVQDTAN KALLALFTAE
     MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI LETILVETKI MSPLGISVLR CVRLLRIFKI
     TRYWNSLSNL VASLLNSVRS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD
     NFPQSLLTVF QILTGEDWNS VMYDGIMAYG GPSFPGMLVC IYFIILFICG NYILLNVFLA
     IAVDNLADAE SLTSAQKEEE EEKERKKLAR TASPEKKQEV MEKPAVEESK EEKIELKSIT
     ADGESPPTTK INMDDLQPSE NEDKSPHSNP DTAGEEDEEE PEMPVGPRPR PLSELHLKEK
     AVPMPEASAF FIFSPNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE DPVQHTSFRN
     HILFYFDIVF TTIFTIEIAL KMTAYGAFLH KGSFCRNYFN ILDLLVVSVS LISFGIQSSA
     INVVKILRVL RVLRPLRAIN RAKGLKHVVQ CVFVAIRTIG NIVIVTTLLQ FMFACIGVQL
     FKGKLYTCSD SSKQTEAECK GNYITYKDGE VDHPIIQPRS WENSKFDFDN VLAAMMALFT
     VSTFEGWPEL LYRSIDSHTE DKGPIYNYRV EISIFFIIYI IIIAFFMMNI FVGFVIVTFQ
     EQGEQEYKNC ELDKNQRQCV EYALKARPLR RYIPKNQHQY KVWYVVNSTY FEYLMFVLIL
     LNTICLAMQH YGQSCLFKIA MNILNMLFTG LFTVEMILKL IAFKPKGYFS DPWNVFDFLI
     VIGSIIDVIL SETNPAEHTQ CSPSMSAEEN SRISITFFRL FRVMRLVKLL SRGEGIRTLL
     WTFIKSFQAL PYVALLIVML FFIYAVIGMQ VFGKIALNDT TEINRNNNFQ TFPQAVLLLF
     RCATGEAWQD IMLACMPGKK CAPESEPSNS TEGETPCGSS FAVFYFISFY MLCAFLIINL
     FVAVIMDNFD YLTRDWSILG PHHLDEFKRI WAEYDPEAKG RIKHLDVVTL LRRIQPPLGF
     GKLCPHRVAC KRLVSMNMPL NSDGTVMFNA TLFALVRTAL RIKTEGNLEQ ANEELRAIIK
     KIWKRTSMKL LDQVVPPAGD DEVTVGKFYA TFLIQEYFRK FKKRKEQGLV GKPSQRNALS
     LQAGLRTLHD IGPEIRRAIS GDLTAEEELD KAMKEAVSAA SEDDIFRRAG GLFGNHVTYY
     QSDSRGNFPQ TFATQRPLHI NKTGNNQADT ESPSHEKLVD STFTPSSYSS TGSNANINNA
     NNTALGRFPH PAGYSSTVST VEGHGPPLSP AVRVQEAAWK LSSKRCHSRE SQGATVNQEI
     FPDETRSVRM SEEAEYCSEP SLLSTDMFSY QEDEHRQLTC PEEDKREIQP SPKRSFLRSA
     SLGRRASFHL ECLKRQKDQG GDISQKTALP LHLVHHQALA VAGLSPLLQR SHSPTTFPRP
     CPTPPVTPGS RGRPLRPIPT LRLEGAESSE KLNSSFPSIH CSSWSEETTA CSGSSSMARR
     ARPVSLTVPS QAGAPGRQFH GSASSLVEAV LISEGLGQFA QDPKFIEVTT QELADACDMT
     IEEMENAADN ILSGGAQQSP NGTLLPFVNC RDPGQDRAVA PEDESCAYAL GRGRSEEALA
     DSRSYVSNL
//
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