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Database: UniProt
Entry: F7BKP4_CALJA
LinkDB: F7BKP4_CALJA
Original site: F7BKP4_CALJA 
ID   F7BKP4_CALJA            Unreviewed;      2192 AA.
AC   F7BKP4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 2.
DT   20-JUN-2018, entry version 44.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1D {ECO:0000313|Ensembl:ENSCJAP00000051432};
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:ENSCJAP00000051432, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000051432, 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:ENSCJAP00000051432}
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; ENSCJAT00000061455; ENSCJAP00000051432; ENSCJAG00000007392.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   Proteomes; UP000008225; Unplaced.
DR   GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IEA:Ensembl.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR   GO; GO:0051393; F:alpha-actinin binding; IEA:Ensembl.
DR   GO; GO:0030506; F:ankyrin binding; IEA:Ensembl.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IEA:Ensembl.
DR   GO; GO:0086059; F:voltage-gated calcium channel activity involved SA node cell action potential; IEA:Ensembl.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0070509; P:calcium ion import; IEA:Ensembl.
DR   GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IEA:Ensembl.
DR   GO; GO:0051928; P:positive regulation of calcium ion transport; IEA:Ensembl.
DR   GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; IEA:Ensembl.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
DR   GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   Gene3D; 1.20.120.350; -; 3.
DR   InterPro; IPR031688; CAC1F_C.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005452; LVDCC_a1dsu.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037:SF139; PTHR10037:SF139; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 3.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01636; LVDCCALPHA1D.
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   2192 AA;  248908 MW;  5F8725D2E75D8B9F CRC64;
     MMMMMMMKKM QHQRQQQADH ANEANYARGT RLPLSGEGPT SQPNSSKQTV LSWQAAIDAA
     RQAKAAQTMS TSAPPPVGSL SQRKRQQYAK SKKQGNSSNS RPARALFCLS LNNPIRRACI
     SIVEWKPFDI FILLAIFANC VALAIYIPFP EDDSNSTNHN LEKVEYAFLI IFTVETFLKI
     IAYGLLLHPN AYVRNGWNLL DFVIVIVGLF SVILEQLTKE TEGGNHSSGK SGGFDVKALR
     AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFIGKMHKT
     CFFADSDIVA EEDPAPCAFS GNGRQCTANG TECRSGWVGP NGGITNFDNF AFAMLTVFQC
     ITMEGWTDVL YWVNDAIGWE WPWVYFVSLI ILGSFFVLNL VLGVLSGEFS KEREKAKARG
     DFQKLREKQQ LEEDLKGYLD WITQAEDIDP ENEEEGGEEG KRNTSMPTSE TESVNTENVS
     GEAETRGCCR SLCQAISKSK LSRRWRRWNR FNRRRCRAAV KSVTFYWLVI VLVFLNTLTI
     SSEHYNQPDW LTQIQDIANK VLLALFTCEM LVKMYSLGLQ AYFVSLFNRF DCFVVCGGIT
     ETILVELEIM SPLGISVFRC VRLLRIFKVT RHWTSLSNLV ASLLNSMKSI ASLLLLLFLF
     IIIFSLLGMQ LFGGKFNFDE TQTKRSTFDN FPQALLTVFQ ILTGEDWNAV MYDGIMAYGG
     PSSSGMIVCI YFIILFICGN YILLNVFLAI AVDNLADAES LNTAQKEEAE EKERKKIARK
     ESLENKKNNK PEVNQVANSD NKVTIDDYRE EDEDKDPYPP CDVPVGEEEE EEEEDEPEVP
     AGPRPRRISE LNMKEKIAPI PEGSAFFILS KTNPIRVGCH KLINHHIFTN LILVFIMLSS
     AALAAEDPIR SHSFRNTILG YFDYAFTAIF TVEILLKMTT FGAFLHKGAF CRNYFNLLDM
     LVVGVSLVSF GIQSSAISVV KILRVLRVLR PLRAINRAKG LKHVVQCVFV AIRTIGNIMI
     VTTLLQFMFA CIGVQLFKVE ALPLSRKPKW ISLRRSCIDL TACLLSTQGK FYRCTDEAKS
     NPEECRGLFI LYKDGDVDSP VVRERIWQNS DFNFDNVLSA MMALFTVSTF EGWPALLYKA
     IDSNGENVGP VYNHRVEISI FFIIYIIIVA FFMMNIFVGF VIVTFQEQGE KEYKNCELDK
     NQRQCVEYAL KARPLRRYIP KNPYQYKFWY VVNSSPFEYM MFVLIMLNTL CLAMQHYEQS
     KMFNDAMDIL NMVFTGVFTV EMVLKVIAFK PKHYFTDAWN TFDALIVVGS VVDIAITEVN
     PTESETVPVP TATPGNSEES NRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL
     PYVALLIAML FFIYAVIGMQ MFGKVAMKDN NQINRNNNFQ TFPQAVLLLF RCATGEAWQE
     IMLACLPGKL CDPESDYNPG EEYTCGSNFA IVYFISFYML CAFLIINLFV AVIMDNFDYL
     TRDWSILGPH HLDEFKRIWS EYDPEAKGRI KHLDVVTLLR RIQPPLGFGK LCPHRVACKR
     LVAMNMPLNS DGTVMFNATL FALVRTALKI KTEGNLEQAN EELRAVIKKI WKKTSMKLLD
     QVVPPAGDDE VTVGKFYATF LIQDYFRKFK KRKEQGLVGK YPAKNTTIAL QAGLRTLHDI
     GPEIRRAISC DLQDDEPEEA KREEEDDVFK RNGALLGNHV NHVNSDRRDS LQQTNTTHRP
     LHVQRPSIPP ASDTEKPLFP PAGNSVCHNH HNHNSIGKQV PTSTNANLNN ANMSKAAHGK
     RPSIGNLEHV SENGHHSSHK HDREPQRRSS VKRTRYYETY IRSDSGDEQL PTICREDPEV
     HGYFRDPRCL GEQEYFSSEE CYEDDSSPTW SRQNYGYYSR YPGRNMDFER PRGYHQPQGF
     LEDDDSPICY DSRRSPRRRL LPPTPASHRR SSFNFECLRR QSSQEEIPSS PTFFPHRTAL
     PLHLMQQQIM AVAGLDSSKA QKYSPSHSTR SWATPPATPP YRDWTPCYTP LIQVEQSEAL
     DQVNGSLPSL HRSSWYTDEP DISYRTFTPA SLTIPSSFRN KNSDKQRSAD SLVEAVLISE
     GLGRYARDPK FVSATKYEIA DACDLTIDEM ESAASTLLNG NVRPRANGDV GPLSHQQDYE
     LQDFGPGYSD EEPDLGRDEE DLADEMICIT TL
//
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