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Database: UniProt
Entry: M3Z2Z8_MUSPF
LinkDB: M3Z2Z8_MUSPF
Original site: M3Z2Z8_MUSPF 
ID   M3Z2Z8_MUSPF            Unreviewed;      1479 AA.
AC   M3Z2Z8;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   25-OCT-2017, entry version 34.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1C {ECO:0000313|Ensembl:ENSMPUP00000017960};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000017960, ECO:0000313|Proteomes:UP000000715};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000017960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ID#1420 {ECO:0000313|Ensembl:ENSMPUP00000017960};
RA   Di Palma F., Alfoldi J., Johnson J., Jaffe D., Berlin A., Gnerre S.,
RA   Grabherr M., Hall G., Lara M., MacCallum I., Mauceli E.,
RA   Przyblyski D., Ribeiro F., Russell P., Sharpe T., Turner-Maier J.,
RA   Walker B.J., Young S., Birren B., Lindblad-Toh K.;
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMPUP00000017960}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2013) 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:ENSMPUP00000017960}.
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DR   EMBL; AEYP01082047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01082048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01082049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01082050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01082051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01082052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01082053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01082054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 9669.ENSMPUP00000017960; -.
DR   Ensembl; ENSMPUT00000018222; ENSMPUP00000017960; ENSMPUG00000018071.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; M3Z2Z8; -.
DR   OMA; PTTKINM; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   Proteomes; UP000000715; Unassembled WGS sequence.
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; 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; 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   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01635; LVDCCALPHA1C.
PE   3: Inferred from homology;
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:UP000000715};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000715};
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      6     26       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     38     56       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    109    131       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    194    215       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    227    249       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    349    366       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    386    409       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    478    497       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    550    577       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    713    736       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    748    767       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    788    814       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    834    863       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    959    986       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1037   1054       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1066   1088       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1100   1117       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1184   1207       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1277   1301       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        3    260       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      348    585       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      717    993       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1036   1311       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1313   1383       GPHH. {ECO:0000259|Pfam:PF16905}.
FT   DOMAIN     1384   1434       Ca_chan_IQ. {ECO:0000259|Pfam:PF08763}.
FT   COILED      580    606       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1479 AA;  167930 MW;  E916CCD550E8EFC0 CRC64;
     ERVEYLFLII FTVEAFLKVI AYGLLFHPNA YLRNGWNLLD FIIVVVGLFS AILEQATKAD
     GANALGGKGA GFDVKALRAF RVLRPLRLVS GVPSLQVVLN SIIKAMVPLL HIALLVLFVI
     IIYAIIGLEL FMGKMHKTCY NQEGIAAPSV ATGAEDDPSP CALETGHGRQ CQNGTVCKPG
     WDGPKHGITN FDNFAFAMLT VFQCITMEGW TDVLYWVNDA VGRDWPWIYF VTLIIIGSFF
     VLNLVLGVLS GEFSKEREKA KARGDFQKLR EKQQLEEDLK GYLDWITQAE DIDPENEDEG
     ILSAREEGCD SVGFRKASVF NKINQMSRYW RRWNRFCRRK CRAAVKSNVF YWLVIFLVFL
     NTLTIASEHY NQPHWLTEVQ DTANKALLAL FTAEMLLKMY SLGLQAYFVS LFNRFDCFIV
     CGGILETILV ETKIMSPLGI SVLRCVRLLR IFKITRYWNS LSNLVASLLN SVRSIASLLL
     LLFLFIIIFS LLGMQLFGGK FNFDEMQTRR STFDNFPQSL LTVFQILTGE DWNSVMYDGI
     MAYGGPSFPG MLVCIYFIIL FICGNYILLN VFLAIAVDNL ADAESLTSAQ KEEEEEKERK
     KLARTASPEK KQEVVEKPAV EETKEEKTDG ESPPTTKINM DDLQPNENED KSPYPNPENT
     GEEDEEEPEM PVGPRPRPLS ELHLKEKAVP MPEASAFFIF SPNNRFRLQC HRIVNDTIFT
     NLILFFILLS SISLAAEDPV QHTSFRNHIL FYFDIVFTTI FTIEIALKMT AYGAFLHKGS
     FCRNYFNILD LLVVSVSLIS FGIQSSAINV VKILRVLRVL RPLRAINRAK GLKHVVQCVF
     VAIRTIGNIV IVTTLLQFMF ACIGVQLFKG KLYTCSDSSK QTEAECKGNY ITYKDGEVDH
     PIIQPRSWEN SKFDFDNVLA AMMALFTVST FEGWPELLYR SIDSHTEDKG PIYNYRVEIS
     IFFIIYIIII AFFMMNIFVG FVIVTFQEQG EQEYKNCELD KNQRQCVEYA LKARPLRRYI
     PKNQHQYKVW YVVNSTYFEY LMFVLILLNT ICLAMQHYGQ SCLFKIAMNI LNMLFTGLFT
     VEMILKLIAF KPKGYFSDPW NVFDFLIVIG SIIDVILSET NDMVSSSAGS LQAGGGSGEV
     NAEENSRISI TFFRLFRVMR LVKLLSRGEG IRTLLWTFIK SFQALPYVAL LIVMLFFIYA
     VIGMQVFGKI ALNDTTEINR NNNFQTFPQA VLLLFRCATG EAWQDIMLAC MPGKKCAPES
     EPGNSTEGET PCGSSFAVFY FISFYMLCAF LIINLFVAVI MDNFDYLTRD WSILGPHHLD
     EFKRIWAEYD PEAKGRIKHL DVVTLLRRIQ PPLGFGKLCP HRVACKRLVS MNMPLNSDGT
     VMFNATLFAL VRTALRIKTE GNLEQANEEL RAIIKKIWKR TSMKLLDQVV PPAGGKYSQD
     LHTHDSCLVP ESMRLMGSLL SPPHSASPVG PEGPIGWKG
//
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