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Database: UniProt
Entry: A0A087WS40_MOUSE
LinkDB: A0A087WS40_MOUSE
Original site: A0A087WS40_MOUSE 
ID   A0A087WS40_MOUSE        Unreviewed;      2153 AA.
AC   A0A087WS40;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-SEP-2017, entry version 25.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=Cacna1c {ECO:0000313|Ensembl:ENSMUSP00000140886,
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:ENSMUSP00000140886, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000140886, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000140886,
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:ENSMUSP00000140886}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000140886};
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:ENSMUSP00000140886}.
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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   RefSeq; NP_001242929.1; NM_001256000.2.
DR   UniGene; Mm.41628; -.
DR   UniGene; Mm.436656; -.
DR   SMR; A0A087WS40; -.
DR   Ensembl; ENSMUST00000188106; ENSMUSP00000140886; ENSMUSG00000051331.
DR   GeneID; 12288; -.
DR   UCSC; uc012erk.3; mouse.
DR   CTD; 775; -.
DR   MGI; MGI:103013; Cacna1c.
DR   GeneTree; ENSGT00830000128247; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000051331; -.
DR   ExpressionAtlas; A0A087WS40; 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:A0A087WS40};
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    550    568       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    676    698       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    752    778       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    926    945       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    957    979       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    999   1022       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1043   1076       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1168   1194       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1245   1262       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1274   1296       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1374   1391       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1467   1490       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1624   1658       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      781    807       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2153 AA;  241832 MW;  B82754F7A922FEB3 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 PRNRGAPAGL HDQKKGKFAW
     FSHSTETHVS MPTSETESVN TENVAGGDIE GENCGARLAH RISKSKFSRY WRRWNRFCRR
     KCRAAVKSNV FYWLVIFLVF LNTLTIASEH YNQPHWLTEV QDTANKALLA LFTAEMLLKM
     YSLGLQAYFV SLFNRFDCFI VCGGILETIL VETKIMSPLG ISVLRCVRLL RIFKITRYWN
     SLSNLVASLL NSVRSIASLL LLLFLFIIIF SLLGMQLFGG KFNFDEMQTR RSTFDNFPQS
     LLTVFQILTG EDWNSVMYDG IMAYGGPSFP GMLVCIYFII LFICGNYILL NVFLAIAVDN
     LADAESLTSA QKEEEEEKER KKLARTASPE KKQEVMEKPA VEESKEEKIE LKSITADGES
     PPTTKINMDD LQPSENEDKS PHSNPDTAGE EDEEEPEMPV GPRPRPLSEL HLKEKAVPMP
     EASAFFIFSP NNRFRLQCHR IVNDTIFTNL ILFFILLSSI SLAAEDPVQH TSFRNHILFY
     FDIVFTTIFT IEIALKMTAY GAFLHKGSFC RNYFNILDLL VVSVSLISFG IQSSAINVVK
     ILRVLRVLRP LRAINRAKGL KHVVQCVFVA IRTIGNIVIV TTLLQFMFAC IGVQLFKGKL
     YTCSDSSKQT EAECKGNYIT YKDGEVDHPI IQPRSWENSK FDFDNVLAAM MALFTVSTFE
     GWPELLYRSI DSHTEDKGPI YNYRVEISIF FIIYIIIIAF FMMNIFVGFV IVTFQEQGEQ
     EYKNCELDKN QRQCVEYALK ARPLRRYIPK NQHQYKVWYV VNSTYFEYLM FVLILLNTIC
     LAMQHYGQSC LFKIAMNILN MLFTGLFTVE MILKLIAFKP KGYFSDPWNV FDFLIVIGSI
     IDVILSETNS AEENSRISIT FFRLFRVMRL VKLLSRGEGI RTLLWTFIKS FQALPYVALL
     IVMLFFIYAV IGMQVFGKIA LNDTTEINRN NNFQTFPQAV LLLFRCATGE AWQDIMLACM
     PGKKCAPESE PSNSTEGETP CGSSFAVFYF ISFYMLCAFL IINLFVAVIM DNFDYLTRDW
     SILGPHHLDE FKRIWAEYDP EAKGRIKHLD VVTLLRRIQP PLGFGKLCPH RVACKRLVSM
     NMPLNSDGTV MFNATLFALV RTALRIKTEG NLEQANEELR AIIKKIWKRT SMKLLDQVVP
     PAGDDEVTVG KFYATFLIQE YFRKFKKRKE QGLVGKPSQR NALSLQAGLR TLHDIGPEIR
     RAISGDLTAE EELDKAMKEA VSAASEDDIF RRAGGLFGNH VTYYQSDSRG NFPQTFATQR
     PLHINKTGNN QADTESPSHE KLVDSTFTPS SYSSTGSNAN INNANNTALG RFPHPAGYSS
     TVSTVEGHGP PLSPAVRVQE AAWKLSSKRC HSRESQGATV NQEIFPDETR SVRMSEEAEY
     CSEPSLLSTD MFSYQEDEHR QLTCPEEDKR EIQPSPKRSF LRSASLGRRA SFHLECLKRQ
     KDQGGDISQK TALPLHLVHH QALAVAGLSP LLQRSHSPTT FPRPCPTPPV TPGSRGRPLR
     PIPTLRLEGA ESSEKLNSSF PSIHCSSWSE ETTACSGSSS MARRARPVSL TVPSQAGAPG
     RQFHGSASSL VEAVLISEGL GQFAQDPKFI EVTTQELADA CDMTIEEMEN AADNILSGGA
     QQSPNGTLLP FVNCRDPGQD RAVAPEDESC AYALGRGRSE EALADSRSYV SNL
//
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