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Database: UniProt
Entry: H3BDR8_LATCH
LinkDB: H3BDR8_LATCH
Original site: H3BDR8_LATCH 
ID   H3BDR8_LATCH            Unreviewed;      1783 AA.
AC   H3BDR8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   25-OCT-2017, entry version 37.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1S {ECO:0000313|Ensembl:ENSLACP00000020039};
OS   Latimeria chalumnae (West Indian ocean coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000020039, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Ensembl:ENSLACP00000020039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000020039};
RX   PubMed=9215903;
RA   Zardoya R., Meyer A.;
RT   "The complete DNA sequence of the mitochondrial genome of a 'living
RT   fossil,' the coelacanth (Latimeria chalumnae).";
RL   Genetics 146:995-1010(1997).
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000020039}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2012) 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:ENSLACP00000020039}.
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DR   EMBL; AFYH01013996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01013997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSLACT00000020177; ENSLACP00000020039; ENSLACG00000017615.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
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   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:UP000008672};
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:UP000008672};
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     60     77       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     97    117       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    129    147       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    201    223       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    283    304       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    316    338       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    439    456       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    476    494       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    568    587       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    645    667       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    802    824       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    844    865       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    877    903       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    923    952       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1048   1075       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1126   1147       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1159   1177       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1257   1277       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1345   1369       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1503   1536       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1783 AA;  203840 MW;  28749D6DC1373C51 CRC64;
     MEPNAVPDTN SLQRKKQKEK AKKQMNAGSP RPARALFCLN LQNPIRKACI SIVEWKPFEI
     IILLTIFANC IALAVFLPMP EDDTNNTNSS LEKVEYIFLI IFTIEATLKI IAYGFLFHPD
     AYLRNGWNIL DFIIVFVGLC TVALEQISRI QGGTAPVGGK GAGFDVKALR AFRVLRPLRL
     VSGVPSLQVV LNSIIKAMVP LLHIALLVLF MIIIYAIIGL ELFMGKMHKT CYYVGSDVVA
     TVENEKAAPC ASAGHGRHCT LNMTECRTGW PGPNNGITHF DNFGFAMLTV YQCITMEGWT
     DVLYWVNDAI GNEWPWIYFV SLILLGSFFV LNLVLGVLSG EFTKEREKAK SRGAFQKLRE
     RQQLEEDLKG YLDWITHAEV MDPDQERGEG ILQSDENGSE TDSLYEIEGM NKCILFFRRW
     RRWNRLFRRK CRAVVKSKFF YWLVILLVFL NTLTIASEHH NQSDWLTSVQ DTANKVLLAL
     FTAEMLLKMY ALGFQPYFMS LFNRFDCFVV CGGILETILV EANIMSPLGI SVLRCIRLLR
     IFKITRYWTS LSNLVASLLN SVRSIASLLL LLFLFMIIFS LLGMQVFGGK YNFDDLEVRR
     STFDNFPQAL ISVFQILTGE DWNSVMYNGI IAYGGPSFPG VLVCIYFIIL FVCGNYILLN
     VFLAIAVDNL ADAESLTSAQ KAKAEEKKRR KMARSSHPEK SEEEKQLLLK KLEQKAKGEG
     IPTTAKLKID EFESNVNEIK DPYPSADFPG DDEEEEPEIP LSPRPRPLAE LQLKEKAVPM
     PEASAFFIFS PTNKIRVLCH RIVNATTFTN FILLFILLSS ISLAAEDPIR PDSFRNQILN
     YFDIVFTVIF TTEIVLKMTA YGAFLHKGSF CRNYFNILDL LVVSVSLISF GIQSSAISVV
     KILRVLRVLR PLRAINRAKG LKHVVQCVFV AIKTIGNIVI VTTLLQFMFA CIGVQLFKGK
     FYSCTDVSKM TEEECKGYYV MYKEGDVHQL ELRERKWVNS DFNFDSVLSA MMALFTVSTF
     EGWPQLLYKA IDSHAENMGP IYNYRIEIAI FFIIYIILIA FFMMNIFVGF VIVTFQEQGE
     QEYKNCELDK NQRQCVQYAL KARPLRRYIP KNPYQYQIWY VVTSSYFEYL MFALILLNTI
     CLGMQHYGQS DEISYLSDML NVVFTGLFTL EMVLKLLAFK VKGYFSDPWN VFDFLIVIGS
     IIDVVLSEID DSEDTSRISI TFFRLFRVMR LVKLLSRGEG VRTLLWTFIK SFQALPYVAL
     LIVMLFFIYA VIGMQVFGKV AMVDGTQINR NNNFQTFPQA VLLLFRCATG EAWQEILLGC
     SYGKLCDPES DYNPGEEYTC GSSFAYFYFI SFYMLCAFLI INLFVAVIMD NFDYLTRDWS
     ILGPHHLDEF KRIWAEYDPE AKGRIKHLDV VTLLRRIQPP LGFGKFCPHR VACKRLVSMN
     MPLNSDGTVT FNATLFALVR TALKVKTEGN FEQSNEELRA IIKKIWKRTS MKLLDQVIPP
     IGDDEVTVGK FYATFLIQDH FRKFMKRQEE YYGYRPKKSA VEIQAGLRSI EEEAAPEIHR
     TISGDLTAEE ELERAMEEEI YRRSGGLFGN HVDHFPMETS SPLQPHVTSQ RPLQFSESRG
     EDLESPVFLP NEVEFFPSGS SANVNNANNN AIARMYLEDE LNKEIPQACD STERGLSIKR
     RSRPLSMPER KLSFHLDHLK RRLTQQTDDT TIEMTELRGF AQQEPEVIVD PGSEQDGRVS
     QSSDPERLRA SGQHQQRETV LRTPATDKLI QKVGNNREKQ SLR
//
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