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Database: UniProt
Entry: A0A0D9RN02_CHLSB
LinkDB: A0A0D9RN02_CHLSB
Original site: A0A0D9RN02_CHLSB 
ID   A0A0D9RN02_CHLSB        Unreviewed;      1873 AA.
AC   A0A0D9RN02;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   25-OCT-2017, entry version 17.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1S {ECO:0000313|Ensembl:ENSCSAP00000009991};
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:ENSCSAP00000009991, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000009991, 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:ENSCSAP00000009991}
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:ENSCSAP00000009991}.
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DR   EMBL; AQIB01112773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01112774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007987187.1; XM_007988996.1.
DR   Ensembl; ENSCSAT00000011932; ENSCSAP00000009991; ENSCSAG00000013846.
DR   GeneID; 103230339; -.
DR   CTD; 779; -.
DR   GeneTree; ENSGT00830000128247; -.
DR   OMA; ACSYGKL; -.
DR   Proteomes; UP000029965; Chromosome 25.
DR   GO; GO:0031674; C:I band; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0006936; P:muscle contraction; IEA:Ensembl.
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   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: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     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    562    581       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    634    661       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    795    817       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    837    858       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    870    896       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    916    946       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1042   1068       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1122   1140       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1152   1170       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1266   1284       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1357   1381       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1515   1548       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1873 AA;  212399 MW;  D862FC504D75DDD0 CRC64;
     MEPSSPQDEG LRKKQPKKPV PEILPRPPRA LFCLTLENPL RKACISIVEW KPFETIILLT
     IFANCVALAV YLPMPEDDNN SLNLGLEKLE YFFLIVFSIE AAMKIIAYGF LFHQDAYLRS
     GWNVLDFTIV FLGVFTVILE QVNVIQSNTA PLSSKGAGLD VKALRAFRVL RPLRLVSGVP
     SLQVVLNSIF KAMLPLFHIA LLVLFMVIIY AIIGLELFKG KMHKTCYFTG TDIMATVENE
     EPSPCARTGS GRRCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIT MEGWTDVLYW
     VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF QKLREKQQLD
     EDLRGYMSWI TQGEVMDVED FREGKLSLDE GGSDTESLYE IAGLNKIIQF IRHWRQWNRI
     FRWKCHDIVK SKVFYWLVIL IVALNTLSIA SEHHNQPLWL TRLQDIANRV LLSLFTVEML
     MKMYGLGLRQ YFMSIFNRFD CFVVCSGILE ILLVESGAMT PLGISVLRCI RLLRIFKITK
     YWTSLSNLVA SLLNSIRSIA SLLLLLFLFI VIFALLGMQL FGGRYDFEDT EVRRSNFDNF
     PQALISVFQV LTGEDWTSMM YNGIMAYGGP SYPGMLVCIY FIILFVCGNY ILLNVFLAIA
     VDNLAEAESL TSAQKAKAEE RKRRKMSKGL PDKSEEEKST MAKKLEQKPK GEGIPTTAKL
     KIDEFESNVN EVKDPYPSAD FPGDDEEDEP EIPLSPRPRP LAELQLKEKA VPIPEASSFF
     IFSPTNKIRV LCHRIVNATW FTNFILLFIL LSSAALAAED PIRADSMRNQ ILKHFDIGFT
     SVFTVEIVLK MTTYGAFLHK GSFCRNYFNM LDLLVVAVSL ISMGLESSAI SVVKILRVLR
     VLRPLRAINR AKGLKHVVQC MFVAISTIGN IVLVTTLLQF MFACIGVQLF KGKFFRCTDL
     SKMTEQECRG YYYVYKDGDP TQIELRRREW VHSDFHFDNV LSAMMSLFTV STFEGWPQLL
     YKAIDSNEED VGPIYNNRVE MAIFFIIYII LIAFFMMNIF VGFVIVTFQE QGETEYKNCE
     LDKNQRQCVQ YALKARPLRC YIPKNPYQYQ VWYVVTSSYF EYLMFALIML NTICLGMQHY
     NQSEQMNHIS DILNVAFTII FTLEMILKLM AFKARGYFGD PWNVFDFLIV IGSIIDVILS
     EIDTFLASSG GLYCLGGGCG NVDPDESARI SSAFFRLFRV MRLIKLLSRA EGVRTLLWTF
     IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIALVDGTQI NRNNNFQTFP QAVLLLFRCA
     TGEAWQEILL ACSYGKLCDP ESDYAPGEEY TCGTNFAYYY FISFYMLCAF LVINLFVAVI
     MDNFDYLTRD WSILGPHHLD EFKAIWAEYD PEAKGRIKHL DVVTLLRRIQ PPLGFGKFCP
     HRVACKRLVG MNMPLNSDGT VTFNATLFAL VRTALKIKTE GNFEQANEEL RAIIKKIWKR
     TSMKLLDQVI PPIGDDEVTV GKFYATFLIQ EHFRKFMKRQ EEYYGYRPKK DIVQIQAGLR
     TIEEEAAPEI RRTVSGDLAA EEELERAMVE AAMEEGIFRR TGGLFGQVDN FLERTNSLPP
     VMASQRPLQF TEIEMEELES PVFLEDFHQD PRTNPLARAN TNNANANVAY GNSNHSNSHV
     FSSVHYEREF PEETETSAIR GGALGQPCRA LGPHSKPCVE KLKGLMTRRA MPRGQAPPAP
     CQCPRVESPM PEDRRSSTPG SLHEETPHSR STGENTFRCS APATTLLIQE ALVRGGLGTL
     AADANFIMAT GQALADACQM EPEEVEVMAT ELLKGREAPE GMASSLGCLN LGSSLGSLDQ
     HQGSQETLIP PRL
//
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