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Database: UniProt
Entry: A0A0D9RKP5_CHLSB
LinkDB: A0A0D9RKP5_CHLSB
Original site: A0A0D9RKP5_CHLSB 
ID   A0A0D9RKP5_CHLSB        Unreviewed;      2036 AA.
AC   A0A0D9RKP5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-SEP-2017, entry version 17.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1D {ECO:0000313|Ensembl:ENSCSAP00000009184};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000009184, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000009184, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000009184}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (APR-2015) 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:ENSCSAP00000009184}.
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DR   EMBL; AQIB01131992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01131993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSCSAT00000011102; ENSCSAP00000009184; ENSCSAG00000013020.
DR   GeneTree; ENSGT00830000128247; -.
DR   OMA; AVKRSSW; -.
DR   Proteomes; UP000029965; Chromosome 22.
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   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   PANTHER; PTHR10037:SF239; PTHR10037:SF239; 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; 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:UP000029965};
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:UP000029965};
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     12     32       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     44     61       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    118    141       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    197    218       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    230    252       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    370    388       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    408    431       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    500    519       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    572    599       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    734    752       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    772    792       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    804    830       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    850    880       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    977   1002       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1056   1074       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1086   1106       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1224   1242       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1316   1339       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1473   1507       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      602    633       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2036 AA;  231364 MW;  320E7F74B99E55B9 CRC64;
     MFLCFSSQEK VEYAFLIIFT VETFLKIIAY GLLLHPNAYV RNGWNLLDFV IVIVGLFSVI
     LEQLTKETEG GNHSSGKSGG FDVKALRAFR VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH
     IALLVLFVII IYAIIGLELF IGKMHKTCFF ADSDIVAEED PAPCAFSGNG RQCTANGTEC
     RSGWVGPNGG ITNFDNFAFA MLTVFQCITM EGWTDVLYWM NDAMGFELPW VYFVSLVIFG
     SFFVLNLVLG VLSGEFSKER EKAKARGDFQ KLREKQQLEE DLKGYLDWIT QAEDIDPENE
     EEGGEEGKRN TSMPTSETES VNTENVSGEG ETRGCCGSLC QAISKSKLSR RWRRWNRFNR
     RRCRAAVKSV TFYWLVIVLV FLNTLTISSE HYNQPDWLTQ IQDIANKVLL ALFTCEMLVK
     MYSLGLQAYF VSLFNRFDCF VVCGGITETI LVELEIMSPL GISVFRCVRL LRIFKVTRHW
     TSLSNLVASL LNSMKSIASL LLLLFLFIII FSLLGMQLFG GKFNFDETQT KRSTFDNFPQ
     ALLTVFQILT GEDWNAVMYD GIMAYGGPSS SGMIVCIYFI ILFICGNYIL LNVFLAIAVD
     NLADAESLNT AQKEEAEEKE RKKIARKESL ENKKNNKPEV NQIANSDNKV TIDDYREEDE
     DKDPYPPCDV PVGEEEEEEE EDEPEVPAGP RPRRISELNM KEKIAPIPEG SAFFILSKTN
     PIRVGCHKLI NHHIFTNLIL VFIMLSSAAL AAEDPIRSHS FRNTILGYFD YAFTAIFTVE
     ILLKMTTFGA FLHKGAFCRN YFNLLDMLVV GVSLVSFGIQ SSAISVVKIL RVLRVLRPLR
     AINRAKGLKH VVQCVFVAIR TIGNIMIVTT LLQFMFACIG VQLFKGKFYR CTDEAKSNPE
     ECRGLFILYK DGDVDSPVVR ERIWQNSDFN FDNVLSAMMA LFTVSTFEGW PALLYKAIDS
     NGENIGPIYN HRVEISIFFI IYIIIVAFFM MNIFVGFVIV TFQEQGEKEY KNCELDKNQR
     QCVEYALKAR PLRRYIPKNP YQYKFWYVVN SSPFEYMMFV LIMLNTLCLA MQHYEQSKMF
     NDAMDILNMV FTGVFTVEMV LKVIAFKPKG YFSDAWNTFD SLIVIGSIID VALSEADHYF
     TDAWNTFDAL IVVGSVVDIA ITEVNPTESE NVPVPTATPG NSEESNRISI TFFRLFRVMR
     LVKLLSRGEG IRTLLWTFIK SFQALPYVAL LIAMLFFIYA VIGMQMFGKV AMRDNNQINR
     NNNFQTFPQA VLLLFRCATG EAWQEIMLAC LPGKLCDPES DYNPGEEYTC GSNFAIVYFI
     SFYMLCAFLI INLFVAVIMD NFDYLTRDWS ILGPHHLDEF KRIWSEYDPE AKGRIKHLDV
     VTLLRRIQPP LGFGKLCPHR VACKRLVAMN MPLNSDGTVM FNATLFALVR TALKIKTEGN
     LEQANEELRA VIKKIWKKTS MKLLDQVVPP AGDDEVTVGK FYATFLIQDY FRKFKKRKEQ
     GLVGKYPAKN TTIALQAGLR TLHDIGPEIR RAISCDLQDD EPEEAKREEE DDVFKRNGAL
     LGNHVNHVNS DRRDSLQQTN TTHRPLHVQR PSIPPASDTE KPLFPPAGNS VCHNHHNHNS
     IGKQVPTSTN ANLNNANMSK AAHGKRPSIG NLEHVSENGH HSSHKHDREP QRRSSVKRTR
     YYETYIRSDS GDEQLPTICR EDPEIHGYFR DPRCFGEQEY FSSEECYEDD SSPTWSRQNY
     GYYSRYPGRN VDFERPRGYH HPQGFLEDDD SPICYDSRRS PRRRLLPPTP ASHRRSSFNF
     ECLRRQSSQE EVPSSPTFPH RTALPLHLMQ QQIMAVAGLD SSKAQKYSPS HSTRSWVTPP
     ATPPYRDWTP CYTPLIQVEQ SEALDQMNGS LPSLHRSSWY TDEPNISYRT FTPASLTVPS
     SFRNKNSDKQ RSADSLVEAV LISEGLGRYA RDPKFVSATK HEIADACDLT IDEMESAAST
     LLNGNVCPRA NGDVGPLSHR QDYELQDFGP GYSDEEPDPG RDEEDLADEM ICITTL
//
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