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Database: UniProt
Entry: F6ZY03_CALJA
LinkDB: F6ZY03_CALJA
Original site: F6ZY03_CALJA 
ID   F6ZY03_CALJA            Unreviewed;      2031 AA.
AC   F6ZY03;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 2.
DT   20-JUN-2018, entry version 42.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1C {ECO:0000313|Ensembl:ENSCJAP00000001544};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000001544, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000001544, ECO:0000313|Proteomes:UP000008225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000001544}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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
CC       opposite 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}.
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DR   Ensembl; ENSCJAT00000001640; ENSCJAP00000001544; ENSCJAG00000000732.
DR   GeneTree; ENSGT00830000128247; -.
DR   Proteomes; UP000008225; Unplaced.
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   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.350; -; 4.
DR   InterPro; IPR031688; CAC1F_C.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 2.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   SMART; SM01062; Ca_chan_IQ; 1.
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:UP000008225};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAAS:SAAS00085096, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00084820,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00084701,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
SQ   SEQUENCE   2031 AA;  228080 MW;  17761E79E6126AF1 CRC64;
     CSCVFPLSFG GTQPVPSPRP SPLSSGLVPE EFWHNFPGER VEYLFLIIFT VEAFLKVIAY
     GLLFHPNAYL RNGWNLLDFI IVVVGLFSAI LEQATKADGA NALGGKGAGF DVKALRAFRV
     LRPLRLVSGV PSLQVVLNSI IKAMVPLLHI ALLVLFVIII YAIIGLELFM GKMHKTCYNQ
     EGIADVPAED DPSPCALETG HGRQCQNGTV CRPGWDGPKH GITNFDNFAF AMLTVFQCIT
     MEGWTDVLYW MQDAMGYELP WVYFVSLVIF GSFFVLNLVL GVLSGEFSKE REKAKARGDF
     QKLREKQQLE EDLKGYLDWI TQAEDIDPEN EDEGMDEEKP RNMSMPTSET ESVNTENVAG
     GDIEGENCGA RLAHRISKSK FSRYWRRWNR FCRRKCRAAV KSNVFYWLVI FLVFLNTLTI
     ASEHYNQPHW LTEVQDTANK ALLALFTAEM LLKMYSLGLQ AYFVSLFNRF DCFVVCGGIL
     ETILVETKIM SPLGISVLRC VRLLRIFKIT RYWNSLSNLV ASLLNSVRSI ASLLLLLFLF
     IIIFSLLGMQ LFGGKFNFDE MQTRRSTFDN FPQSLLTVFQ ILTGEDWNSV MYDGIMAYGG
     PSFPGMLVCI YFIILFICGN YILLNVFLAI AVDNLADAES LTSAQKEEEE EKERKKLART
     LGLGLPKLDL SPNPNPYPNP ETTGEDDEEE PEMPVGPRPR PLSELHLKEK AVPMPEASAF
     FIFSSNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE DPVQHTSFRN HILFYFDIVF
     TTIFTIEIAL 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
     SETNPAEHTQ CSPSMNAEEN SRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL
     PYVALLIVML FFIYAVIGMQ VFGKIALNDT TEINRNNNFQ TFPQAVLLLF RCATGEAWQD
     IMLACMPGKK CAPESEPSNS TEGETPCGSS FAVFYFISFY MLCAFLIINL FVAVIMDNFD
     YLTRDWSILG PHHLDEFKRI WAEYDPEAKG RIKHLDVVTL LRRIQPPLGF GKLCPHRVAC
     KRLVSMNMPL NSDGTVMFNA TLFALVRTAL RIKTEGNLEQ ANEELRAIIK KIWKRTSMKL
     LDQVVPPAGD DEVTVGKFYA TFLIQEYFRK FKKRKEQGLV GKPSQRNALS LQAGLRTLHD
     IGPEIRRAIS GDLTAEEELD KAMKEAVSAA SEDDIFRRAG GLFGNHVSYY QSDGRSAFPQ
     TFTTQRPLHI NKAGSSQGDT ESPSHEKLVD STFTPSSYSS TGSNANINNA NNTALGRLPR
     PTGHPSTVST VEGHGPPLSP AIRVQEVAWK LSSQRMHCSD MLGWWDFPPT LGPCRAPPCQ
     HQQLQRSLVG LREVPIGQWL PAGGTAPQCH SRESQTAVVG QEETSQDETY EVKMNDDTEA
     CSEPSLLSTE MLSYQDDENR QLTLPEEDKR DIRQSPKRGF LRTASLGRRA SFHLECLKRQ
     KDRAGDISQK TVLPLHLVHH QALAVAGLSP LLQRSHSPAS FPRPFATPPA TPGSRGWPPQ
     PIPTLRLEGA ESIEKLNSSF PSIHCGSWAE TTPCGGGSNA ARRARPVSLT VPSQAGAPGR
     QFHGSASSLV EAVLISEGLG QFAQDPKFIE VTTQELADAC DMTIEEMESA ADNILSGGAP
     QSPNGALLPF VNCRDAGQDL AGGEEDAGCV LARGRLSEEE LQDSRVYVSS L
//
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