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Database: UniProt
Entry: A0A087WQJ4_MOUSE
LinkDB: A0A087WQJ4_MOUSE
Original site: A0A087WQJ4_MOUSE 
ID   A0A087WQJ4_MOUSE        Unreviewed;      2156 AA.
AC   A0A087WQJ4;
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:ENSMUSP00000140220,
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:ENSMUSP00000140220, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000140220, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000140220,
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:ENSMUSP00000140220}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000140220};
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:ENSMUSP00000140220}.
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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; A0A087WQJ4; -.
DR   PaxDb; A0A087WQJ4; -.
DR   Ensembl; ENSMUST00000189520; ENSMUSP00000140220; ENSMUSG00000051331.
DR   MGI; MGI:103013; Cacna1c.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000051331; -.
DR   ExpressionAtlas; A0A087WQJ4; 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; 5.
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:A0A087WQJ4};
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   1376   1399       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1469   1493       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1627   1661       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      756    782       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2156 AA;  242083 MW;  68E8B7D8CE063098 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 SETNHYFCDA WNTFDALIVV
     GSIVDIAITE VHSAEENSRI SITFFRLFRV MRLVKLLSRG EGIRTLLWTF IKSFQALPYV
     ALLIVMLFFI YAVIGMQVFG KIALNDTTEI NRNNNFQTFP QAVLLLFRCA TGEAWQDIML
     ACMPGKKCAP ESEPSNSTEG ETPCGSSFAV FYFISFYMLC AFLIINLFVA VIMDNFDYLT
     RDWSILGPHH LDEFKRIWAE YDPEAKGRIK HLDVVTLLRR IQPPLGFGKL CPHRVACKRL
     VSMNMPLNSD GTVMFNATLF ALVRTALRIK TEGNLEQANE ELRAIIKKIW KRTSMKLLDQ
     VVPPAGDDEV TVGKFYATFL IQEYFRKFKK RKEQGLVGKP SQRNALSLQA GLRTLHDIGP
     EIRRAISGDL TAEEELDKAM KEAVSAASED DIFRRAGGLF GNHVTYYQSD SRGNFPQTFA
     TQRPLHINKT GNNQADTESP SHEKLVDSTF TPSSYSSTGS NANINNANNT ALGRFPHPAG
     YSSTVSTVEG HGPPLSPAVR VQEAAWKLSS KRCHSRESQG ATVNQEIFPD ETRSVRMSEE
     AEYCSEPSLL STDMFSYQED EHRQLTCPEE DKREIQPSPK RSFLRSASLG RRASFHLECL
     KRQKDQGGDI SQKTALPLHL VHHQALAVAG LSPLLQRSHS PTTFPRPCPT PPVTPGSRGR
     PLRPIPTLRL EGAESSEKLN SSFPSIHCSS WSEETTACSG SSSMARRARP VSLTVPSQAG
     APGRQFHGSA SSLVEAVLIS EGLGQFAQDP KFIEVTTQEL ADACDMTIEE MENAADNILS
     GGAQQSPNGT LLPFVNCRDP GQDRAVAPED ESCAYALGRG RSEEALADSR SYVSNL
//
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