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Database: UniProt
Entry: E2R486_CANLF
LinkDB: E2R486_CANLF
Original site: E2R486_CANLF 
ID   E2R486_CANLF            Unreviewed;      1873 AA.
AC   E2R486;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 2.
DT   28-MAR-2018, entry version 61.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1S {ECO:0000313|Ensembl:ENSCAFP00000016109,
GN   ECO:0000313|VGNC:VGNC:38640};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000016109, ECO:0000313|Proteomes:UP000002254};
RN   [1] {ECO:0000313|Ensembl:ENSCAFP00000016109, ECO:0000313|Proteomes:UP000002254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000016109,
RC   ECO:0000313|Proteomes:UP000002254};
RX   PubMed=16341006; DOI=10.1038/nature04338;
RG   Broad Sequencing Platform;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
RA   Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
RA   Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
RA   Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
RA   Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
RA   Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
RA   Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
RA   Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
RA   Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
RA   Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
RA   Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
RA   Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
RA   Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
RA   Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
RA   Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
RA   Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
RA   Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
RA   Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
RA   Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
RA   Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
RA   Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
RA   Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
RA   Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
RA   Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
RA   Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
RA   Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
RA   Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
RA   Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
RA   Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
RA   Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
RA   Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
RA   Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
RA   Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
RA   Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
RA   Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2] {ECO:0000313|Ensembl:ENSCAFP00000016109}
RP   IDENTIFICATION.
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000016109};
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   EMBL; AAEX03005027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_848685.3; XM_843592.5.
DR   STRING; 9615.ENSCAFP00000016109; -.
DR   PaxDb; E2R486; -.
DR   Ensembl; ENSCAFT00000017400; ENSCAFP00000016109; ENSCAFG00000010884.
DR   GeneID; 490244; -.
DR   CTD; 779; -.
DR   VGNC; VGNC:38640; CACNA1S.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; E2R486; -.
DR   OMA; ACSYGKL; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Reactome; R-CFA-5576892; Phase 0 - rapid depolarisation.
DR   Reactome; R-CFA-5576893; Phase 2 - plateau phase.
DR   Proteomes; UP000002254; Chromosome 7.
DR   Bgee; ENSCAFG00000010884; -.
DR   GO; GO:0031674; C:I band; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:Ensembl.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR   GO; GO:0006936; P:muscle contraction; IEA:Ensembl.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.350; -; 4.
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   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037:SF190; PTHR10037:SF190; 1.
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; PR01634; LVDCCALPHA1S.
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   Complete proteome {ECO:0000313|Proteomes:UP000002254};
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:UP000002254};
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}.
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    556    576       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    635    661       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    800    819       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    831    853       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    917    950       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1041   1068       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1119   1140       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1152   1172       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1184   1202       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1266   1284       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1358   1381       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1515   1548       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1873 AA;  212348 MW;  89F3BC787F32454A CRC64;
     MEPSSPQDEG LRKKQPKKPV PEILPRPPRA LFCLTLQNPL RKACINIVEW KPFETIILLT
     IFANCVALAV YLPMPEDDNN TLNLGLEKLE YFFLIVFSIE AAMKIIAYGF LFHQDAYLRS
     GWNVLDFIIV FLGVFTVILE QVNVIQSNTA PMSSKGAGLD VKALRAFRVL RPLRLVSGVP
     SLQVVLNSIF KAMLPLFHIA LLVLFMVIIY AIIGLELFKG KMHKTCYFIG TDIVATVENE
     KPSPCARTGS GRPCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIT MEGWTDVLYW
     VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF QKLREKQQLE
     EDLRGYMSWI TQGEVMDVED LREGKLSLDE GGSDTESLYE IEGLNKIIQF VRHWRQWNRI
     FRWKCHDVIK SRVFYWLVIL VVALNTLSIA SEHHNQPLWL THLQDVANRV LLALFTVEML
     MKMYGLGLRQ YFMSIFNRFD CFVVCSGLLE ILLVESGAMS PLGISVLRCI RLLRIFKITK
     YWTSLSNLVA SLLNSIRSIA SLLLLLFLFI IIFALLGMQL FGGRYDFEDT EVRRSNFDNF
     PQALISVFQV LTGEDWNSMM YSGIMAYGGP SYPGVLVCIY FIILFVCGNY ILLNVFLAIA
     VDNLAEAESL TSAQKAKAEE RKRRKMSKGL PDKSEEEKSV MAKKLEQKPK GEGIPTTAKL
     KIDEFESNVN EVKDPYPSAD FPGDDEEDEP EIPVSPRPRP LAELQLKEKA VPIPEASSFF
     IFSPTNKIRV LCHRIVNATW FTNFILLFIL LSSAALAAED PIRAESVRNQ ILGYFDIAFT
     SVFTVEIVLK MTTYGAFLHK GSFCRNYFNI LDLLVVAVSL ISMGLESSTI SVVKILRVLR
     VLRPLRAINR AKGLKHVVQC VFVAIRTIGN IVLVTTLLQF MFACIGVQLF KGKFFSCNDL
     SKMTEQECRG YYYVYKDGDP TQMELRPRQW IHSDFHFDNV LSAMMSLFTV STFEGWPQLL
     YQAIDSYKED MGPVYNNRVE MAIFFIIYII LIAFFMMNIF VGFVIVTFQE QGETEYKNCE
     LDKNQRQCVQ YALKARPLRC YIPKNPYQYQ VWYVVTSSYF EYLMFALIML NTICLGMQHY
     NQSEEMNHIS DILNVAFTII FTLEMVLKLM AFKARGYFGD PWNVFDFLIV IGSIIDVILS
     EIDTFLASSG GLYCLGGGCG NVDPDESARI SSAFFRLFRV MRLIKLLSRA EGVRTLLWTF
     IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIAMVDGTQI NRNNNFQTFP QAVLLLFRCA
     TGEAWQEILL ACSYGKLCDP ESDYAPGEEY TCGTNFAYYY FISFYMLCAF LIINLFVAVI
     MDNFDYLTRD WSILGPHHLD EFKAIWAEYD PEAKGRIKHL DVVTLLRRIQ PPLGFGKFCP
     HRVACKRLVG MNMPLNSDGT VTFNATLFAL VRTALKIKTE GNFEQANEEL RAIIKKIWKR
     TSMKLLDQVI PPIGDDEVTV GKFYATFLIQ EHFRKFMKRQ EEYYGYRPKK DTIQIQAGLR
     TIEEEAAPEI RRTISGDLTA EEELERAMVE AAMEEGIFRR TGGLFGQVDN FLERTNSLPP
     VMANQRPLQF AEIEMEELES PVFLEDFPQD PRTNPLARAN TNNANANVAH DNSDHSNSQV
     FSSIRYEREF PGEPEPPAAR GGALGQPRRV LGPHGRPCVE KLKGQRTQRE MPRPLASPAP
     CQCAGPERPL PEERSCPPPG SLPQGAPPSR RPTESGCRCP TPATARLVRE ALVRGGLDTL
     AADASFVMAT GQALADACRM EPEDVEVAAT ELLKKQESPE GRASALGRRS RGSSLGSLDL
     HLGSRETLVP PRQ
//
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