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Database: UniProt
Entry: F7C376_MOUSE
LinkDB: F7C376_MOUSE
Original site: F7C376_MOUSE 
ID   F7C376_MOUSE            Unreviewed;      2222 AA.
AC   F7C376;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 2.
DT   27-SEP-2017, entry version 45.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=Cacna1c {ECO:0000313|Ensembl:ENSMUSP00000108413,
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:ENSMUSP00000108413, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000108413, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000108413,
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:ENSMUSP00000108413}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000108413};
RG   Ensembl;
RL   Submitted (FEB-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:ENSMUSP00000108413}.
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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_001242931.1; NM_001256002.2.
DR   UniGene; Mm.41628; -.
DR   UniGene; Mm.436656; -.
DR   ProteinModelPortal; F7C376; -.
DR   STRING; 10090.ENSMUSP00000108413; -.
DR   MaxQB; F7C376; -.
DR   PaxDb; F7C376; -.
DR   Ensembl; ENSMUST00000112793; ENSMUSP00000108413; ENSMUSG00000051331.
DR   GeneID; 12288; -.
DR   UCSC; uc012erj.3; mouse.
DR   CTD; 775; -.
DR   MGI; MGI:103013; Cacna1c.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   OMA; PTTKINM; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   ChiTaRS; Cacna1c; mouse.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000051331; -.
DR   ExpressionAtlas; F7C376; baseline and differential.
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; 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:F7C376};
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    567       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    587    610       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    679    698       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    751    778       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    921    943       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    963    984       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    996   1022       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1042   1071       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1167   1194       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1245   1266       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1272   1293       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1442   1465       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1535   1559       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1693   1727       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      781    807       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2222 AA;  248894 MW;  A2EF8A07BFDEA80E 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 TSFRNHILGN
     ADYVFTSIFT LEIILKMTAY 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 KHYFCDAWNT FDALIVVGSI
     VDIAITEVHP AEHTQCSPSM VRTTLQTTFP ASVAPPLATH VLSTLISRAL GTQPSSHCMW
     PPCPLCALTA CAHVSCARSA 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 RAGGLFGNHV TYYQSDSRGN
     FPQTFATQRP LHINKTGNNQ ADTESPSHEK LVDSTFTPSS YSSTGSNANI NNANNTALGR
     FPHPAGYSST VSTVEGHGPP LSPAVRVQEA AWKLSSKRCH SRESQGATVN QEIFPDETRS
     VRMSEEAEYC SEPSLLSTDM FSYQEDEHRQ LTCPEEDKRE IQPSPKRSFL RSASLGRRAS
     FHLECLKRQK DQGGDISQKT ALPLHLVHHQ ALAVAGLSPL LQRSHSPTTF PRPCPTPPVT
     PGSRGRPLRP IPTLRLEGAE SSEKLNSSFP SIHCSSWSEE TTACSGSSSM ARRARPVSLT
     VPSQAGAPGR QFHGSASSLV EAVLISEGLG QFAQDPKFIE VTTQELADAC DMTIEEMENA
     ADNILSGGAQ QSPNGTLLPF VNCRDPGQDR AVAPEDESCA YALGRGRSEE ALADSRSYVS
     NL
//
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