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Database: UniProt
Entry: A0A087WR02_MOUSE
LinkDB: A0A087WR02_MOUSE
Original site: A0A087WR02_MOUSE 
ID   A0A087WR02_MOUSE        Unreviewed;      2139 AA.
AC   A0A087WR02;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-SEP-2017, entry version 23.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=Cacna1c {ECO:0000313|Ensembl:ENSMUSP00000140415,
GN   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|Ensembl:ENSMUSP00000140415, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000140415, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000140415,
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   [2] {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   [3] {ECO:0000313|Ensembl:ENSMUSP00000140415}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000140415};
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}.
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:ENSMUSP00000140415}.
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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   SMR; A0A087WR02; -.
DR   Ensembl; ENSMUST00000188078; ENSMUSP00000140415; ENSMUSG00000051331.
DR   MGI; MGI:103013; Cacna1c.
DR   GeneTree; ENSGT00830000128247; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000051331; -.
DR   ExpressionAtlas; A0A087WR02; baseline and differential.
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:A0A087WR02};
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    128    145       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    165    185       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    197    215       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    268    290       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    349    370       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    382    404       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    525    542       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    562    585       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    654    673       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    726    753       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    896    918       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    938    959       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1017   1046       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1142   1169       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1220   1237       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1249   1271       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1283   1300       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1359   1382       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1452   1476       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1610   1644       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      756    782       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2139 AA;  240120 MW;  4BAFEB3E7FBCA2A0 CRC64;
     MVNENTRMYV PEENHQGSNY 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 WVNDAVGRDW PWIYFVTLII IGSFFVLNLV 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 HILGNADYVF TSIFTLEIIL 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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