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Database: UniProt
Entry: E3M7B8_CAERE
LinkDB: E3M7B8_CAERE
Original site: E3M7B8_CAERE 
ID   E3M7B8_CAERE            Unreviewed;      1879 AA.
AC   E3M7B8;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-SEP-2017, entry version 36.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=Cre-egl-19 {ECO:0000313|EMBL:EFO93645.1};
GN   ORFNames=CRE_12698 {ECO:0000313|EMBL:EFO93645.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; DS268427; EFO93645.1; -; Genomic_DNA.
DR   RefSeq; XP_003107746.1; XM_003107698.1.
DR   STRING; 31234.CRE12698; -.
DR   EnsemblMetazoa; CRE12698; CRE12698; WBGene00068721.
DR   GeneID; 9828458; -.
DR   CTD; 9828458; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   InParanoid; E3M7B8; -.
DR   OMA; PTTKINM; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   Proteomes; UP000008281; 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:EnsemblMetazoa.
DR   GO; GO:0035545; P:determination of left/right asymmetry in nervous system; IEA:EnsemblMetazoa.
DR   GO; GO:0040017; P:positive regulation of locomotion; IEA:EnsemblMetazoa.
DR   GO; GO:0045989; P:positive regulation of striated muscle contraction; IEA:EnsemblMetazoa.
DR   GO; GO:0043051; P:regulation of pharyngeal pumping; IEA:EnsemblMetazoa.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
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   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:UP000008281};
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:UP000008281};
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     92    110       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    130    151       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    163    179       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    224    242       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    345    367       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    474    492       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    504    525       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    597    617       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    674    695       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    801    819       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    839    859       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    917    946       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1042   1069       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1120   1138       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1150   1171       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1183   1200       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1247   1270       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1343   1367       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1502   1536       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1879 AA;  213311 MW;  F58F4383387F49AF CRC64;
     MIFTVLASMM SSGEDEEQAA TDEQERSDLW QQTLQAAVAA SSSQDATKKR PAQRKPLRQT
     NVVERSERSL LCLSLNNPIR KLCISIVEWK PFEFLILFMI CANCIALAIY QPYPAQDSDY
     KNTALETIEY VFIVVFTIEC VLKIVAMGFL FHPSAYLRNA WNILDFIIVV IGLVSTILSK
     MSIQGFDVKA LRAFRVLRPL RLVSGVPSLQ VVLNAILRAM IPLLHIALLV LFVILIYAII
     GLELFCGKLH STCIDPATGQ LAQKDPTPCG TDGSAFKCRP SDSLTNMGVR WECSSNTTWP
     GPNNGITNFD NFGLAMLTVF QCVSLEGWTD VMYWVNDAVG REWPWIYFVT LVILGSFFVL
     NLVLGVLSGE FSKEREKARA RGLFQKFREK QQLEEDLKGY LDWITQAEDI EPVNEDEQED
     EPVTQAVVGE EADEEGEERV EDVRPSKWAA RMKRLEKLNR RCRRACRRLV KSQTFYWLVI
     LLVLLNTLVL TSEHYGQSEW LDHFQTMANL FFVILFSMEM LLKMYSLGFT TYTTSQFNRF
     DCFVVISSIL EFVLVYFDLM KPLGVSVLRS ARLLRIFKVT KYWTSLRNLV SSLLNSLRSI
     ISLLLLLFLF IVIFALLGMQ VFGGKFNFNP QQPKPRANFD TFVQALLTVF QILTGEDWNT
     VMYHGIESFG GVGTLGVIVC IYYIVLFICG NYILLNVFLA IAVDNLADAD SLTNAEKEEE
     QQEIEGEDEE FDEGEEEGDE HGAEEPEGEE ETARPRRMSE VPAASTVKPI PKASSLFILS
     HTNSFRYAFY VFCNMVVNHS YFTNAVLFCI LVSSAMLAAE DPLQANSTRN MVLNYFDYFF
     TSVFTVEITL KVIVFGLVFH KGSFCRNAFN LLDILVVAVS LTSFVLRTDA MSVVKILRVL
     RVLRPLRAIN RAKGLKHVVQ CVIVAVKTIG NIMLVTFMLQ FMFAIIGVQL FKGTFFLCND
     LSKMTEAECR GEYIHYEDGD PTKPVSKKRV WSNNDFNFDN VGDAMVSLFV VSTFEGWPQL
     LYVAIDSNEE DKGPVHNSRQ AVALFFIAFI IVIAFFMMNI FVGFVIVTFQ NEGEREYENC
     ELDKNQRKCI EFALKAKPHR RYIPRNRLQY RVWWFVTSRA FEYVIFLIIV MNTVSLACKH
     YPSSRNFEDF LDVFNLIFTG VFAFEAVLKI VALNPKNYIS DRWNVFDLLV VVGSFIDITY
     GKLNPGGTNL ISINFFRLFR VMRLVKLLSR GEGIRTLLWT FMKSFQALPY VALLIVLLFF
     IYAVIGMQFF GKVALDDSTS VHRNNNFHSF PAAILVLFRS ATGEAWQDIM LSCSDREDVR
     CDPLSDDYSK GGFNESRCGN NFAYPYFISF FMLCSFLVIN LFVAVIMDNF DYLTRDWSIL
     GPHHLEEFVR LWSEYDPDAK GRIKHLDVVT LLRKISPPLG FGKLCPHRLA CKRLVSMNMP
     LNSDGTVCFN ATLFALVRTN LKIYTEGNID EANEQLRSAI KRIWKRTHKD LLDEVVPPAG
     KEDDVTVGKF YATFLIQDYF RRFKKRKEME AKGVLPAQTP QAMALQAGLR TLHEIGPELK
     RAISGNLETD FNFDEPEPQH RRPHTLFNNL VHRLSQVGQK SPTEHEQLER GAKLLPYDSR
     SFSPTHSLAG AEGSPVPSQM HRGAPINQSI NLPPVNGSAR RLPALPPYAN HIHDETDDGP
     RYRDTGDRAG YDQSQNRMVV ANRNLPVDPD EEEQWMRGGP SNRSDRRNLP IRDPILMARG
     AALSLAGMSS EAYEGTYRPV GEGKSVRLPF SSRPVLRPAE DSRPADRLIG QSLGLGRYAD
     ARVVGAARRE IEEAYSLGEQ EIDMAADSLA PLMQHVGMHD IRDINENSRS ALLRPAENSS
     RQHDSQGGSQ EDLLLVTTL
//
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