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Database: UniProt
Entry: E9QPX8_MOUSE
LinkDB: E9QPX8_MOUSE
Original site: E9QPX8_MOUSE 
ID   E9QPX8_MOUSE            Unreviewed;      1831 AA.
AC   E9QPX8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-SEP-2017, entry version 57.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=Cacna1s {ECO:0000313|Ensembl:ENSMUSP00000107699,
GN   ECO:0000313|MGI:MGI:88294};
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:ENSMUSP00000107699, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000107699, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000107699,
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:ENSMUSP00000107699}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000107699};
RG   Ensembl;
RL   Submitted (MAY-2011) 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:ENSMUSP00000107699}.
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DR   EMBL; AC124375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_055008.2; NM_014193.2.
DR   UniGene; Mm.4418; -.
DR   ProteinModelPortal; E9QPX8; -.
DR   MaxQB; E9QPX8; -.
DR   PaxDb; E9QPX8; -.
DR   Ensembl; ENSMUST00000112068; ENSMUSP00000107699; ENSMUSG00000026407.
DR   GeneID; 12292; -.
DR   KEGG; mmu:12292; -.
DR   UCSC; uc007cug.1; mouse.
DR   CTD; 779; -.
DR   MGI; MGI:88294; Cacna1s.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   KO; K04857; -.
DR   TreeFam; TF312805; -.
DR   Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR   Reactome; R-MMU-5576893; Phase 2 - plateau phase.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000026407; -.
DR   ExpressionAtlas; E9QPX8; baseline and differential.
DR   Genevisible; E9QPX8; MM.
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; IPR005450; VDCC_L_a1ssu.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF238; PTHR10037:SF238; 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; PR01634; LVDCCALPHA1S.
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   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:E9QPX8};
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     55     72       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     92    112       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    124    145       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    196    218       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    278    299       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    311    333       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    433    450       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    470    488       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    562    581       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    634    661       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    795    817       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    837    858       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    870    896       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    916    945       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1042   1068       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1122   1140       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1152   1172       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1247   1265       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1338   1362       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1496   1529       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1831 AA;  208434 MW;  C6DCF30D69E10B6C CRC64;
     MEPPSPQDEG LRKKQPKKPV PEILPRPPRA LFCLTLQNPL RKACISIVEW KPFETIILLT
     IFANCVALAV YLPMPEDDNN TLNLGLEKLE YFFLIVFSIE AAMKIIAYGF LFHQDAYLRS
     GWNVLDFIIV FLGVFTVILE QVNIIQTNTA PMSSKGAGLD VKALRAFRVL RPLRLVSGVP
     SLQVVLNSIF KAMLPLFHIA LLVLFMVIIY AIIGLELFKG KMHKTCYFIG TDIVATVENE
     KPSPCARTGS GRPCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIS MEGWTDVLYW
     VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF QKLREKQQLE
     EDLRGYMSWI TQGEVMDVDD LREGKLSLDE GGSDTESLYE IEGLNKIIQF IRHWRQWNRV
     FRWKCHDLVK SKVFYWLVIL IVALNTLSIA SEHHNQPLWL THLQDVANRV LLTLFTIEML
     MKMYGLGLRQ YFMSIFNRFD CFVVCSGILE ILLVESGAMS PLGISVLRCI RLLRLFKITK
     YWTSLSNLVA SLLNSIRSIA SLLLLLFLFI IIFALLGMQL FGGRYDFEDT EVRRSNFDNF
     PQALISVFQV LTGEDWNSVM YNGIMAYGGP TYPGVLVCIY FIILFVCGNY ILLNVFLAIA
     VDNLAEAESL TSAQKAKAEE RKRRKMSKGL PDKSEEERAT VTKKLEQKSK GEGIPTTAKL
     KIDEFESNVN EVKDPYPSAD FPGDDEEDEP EIPVSPRPRP LAELQLKEKA VPIPEASSFF
     IFSPTNKIRV LCHRIVNATW FTNFILLFIL LSSAALAAED PIRADSMRNQ ILEYFDYVFT
     AVFTVEIVLK MTTYGAFLHK GSFCRNYFNI LDLLVVAVSL ISMGLESSAI SVVKILRVLR
     VLRPLRAINR AKGLKHVVQC VFVAIRTIGN IVLVTTLLQF MFACIGVQLF KGKFYSCNDL
     SKMTEEECRG YYYIYKDGDP TQIELRPRQW IHNDFHFDNV LSAMMSLFTV STFEGWPQLL
     YKAIDSNEED TGPVYNNRVE MAIFFIIYII LIAFFMMNIF VGFVIVTFQE QGETEYKNCE
     LDKNQRQCVQ YALKARPLRC YIPKNPYQYQ VWYVVTSSYF EYLMFALIML NTICLGMQHY
     NQSEQMNHIS DILNVAFTII FTLEMVLKLI AFKPRGYFGD PWNVFDFLIV IGSIIDVILS
     EIDDPDESAR ISSAFFRLFR VMRLVKLLNR AEGVRTLLWT FIKSFQALPY VALLIVMLFF
     IYAVIGMQMF GKIAMVDGTQ INRNNNFQTF PQAVLLLFRC ATGEAWQEIL LACSYGKLCD
     PESDYAPGEE HTCGTNFAYY YFISFYMLCA FLIINLFVAV IMDNFDYLTR DWSILGPHHL
     DEFKAIWAEY DPEAKGRIKH LDVVTLLRRI QPPLGFGKFC PHRVACKRLV GMNMPLNSDG
     TVTFNATLFA LVRTALKIKT EGNFEQANEE LRAIIKKIWK RTSMKLLDQV IPPIGDDEVT
     VGKFYATFLI QEHFRKFMKR QEEYYGYRPK KDTVQIQAGL RTIEEEAAPE IHRAISGDLT
     AEEELERAMV EAAMEEGIFR RTGGLFGQVD NFLERTNSLP PVMANQRPLQ FAEIEMEELE
     SPVFLEDFPQ NPGTHPLARA NTNNANANVA YGNSSHRNNP VFSSICYERE FLGEADMPVT
     REGPLSQPCR ASGPHSRSHV DKLKRPMTQR GMPEGQVPPS PCQLSQAEHP VQKEGKGPTS
     RFLETPNSRN FEEHVPRNSA HRCTAPATAM LIQEALVRGG LDSLAADANF VMATGQALAD
     ACQMEPEEVE VAATELLKQE SPEGGAVPWE P
//
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