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Database: UniProt
Entry: H2VGV8_CAEJA
LinkDB: H2VGV8_CAEJA
Original site: H2VGV8_CAEJA 
ID   H2VGV8_CAEJA            Unreviewed;      1874 AA.
AC   H2VGV8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-SEP-2017, entry version 31.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS   Caenorhabditis japonica.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=281687 {ECO:0000313|EnsemblMetazoa:CJA00370};
RN   [1] {ECO:0000313|EnsemblMetazoa:CJA00370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DF5081 {ECO:0000313|EnsemblMetazoa:CJA00370};
RG   Caenorhabditis japonica Sequencing Consortium;
RA   Wilson R.K.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:CJA00370}
RP   IDENTIFICATION.
RC   STRAIN=DF5081 {ECO:0000313|EnsemblMetazoa:CJA00370};
RG   EnsemblMetazoa;
RL   Submitted (NOV-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}.
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DR   STRING; 281687.CJA00370; -.
DR   EnsemblMetazoa; CJA00370; CJA00370; WBGene00119574.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   InParanoid; H2VGV8; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   Proteomes; UP000005237; 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; 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:UP000005237};
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:UP000005237};
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     90    108       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    128    149       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    161    177       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    222    240       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    343    365       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    472    490       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    502    523       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    595    615       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    672    693       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    796    814       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    834    854       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    912    941       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1037   1064       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1115   1133       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1145   1166       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1178   1195       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1242   1265       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1338   1362       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1497   1531       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1874 AA;  212434 MW;  A9E16C01960833B3 CRC64;
     MSVLASMMSS GEDEEQAAAD EQERSDLWQQ TLQAAVAASG SQDATKKRPA QRKPLRQTNV
     VERSERSLLC LSLNNPIRKL CISIVEWKPF EFLILFMICA NCIALAIYQP YPAQDSDYKN
     TLLETIEYVF IVVFTIECVL KIVAFGFLFH PSAYLRNAWN ILDFIIVVIG LVSTILSKMS
     IQGFDVKALR AFRVLRPLRL VSGVPSLQVV LNAILRAMIP LLHIALLVLF VILIYAIIGL
     ELFCGKLHST CIDPATGQLA QKDPTPCGND GTAFKCRPSD SLSSMGVRWE CSSNTSWTGP
     NNGITNFDNF GLAMLTVFQC VSLEGWTDVM YWVNDAVGRE WPWIYFVTLV ILGSFFVLNL
     VLGVLSGEFS KEREKARARG LFQKFREKQQ LEEDLKGYLD WITQAEDIEP VNEDEQEDEP
     AAQTVVGEEA DEEGEERVED VRPSKWAARI KRLEKLNRRC RRACRRLVKS QTFYWLVILL
     VLLNTLVLTS EHYGQSEWLD HFQTMANLFF VILFSMEMLL KMYSLGFTTY TTSQFNRFDC
     FVVISSILEF VLVYFDLMKP LGVSVLRSAR LLRIFKVTKY WTSLRNLVSS LLNSLRSIIS
     LLLLLFLFIV IFALLGMQVF GGKFNFNPQQ PKPRANFDTF VQALLTVFQI LTGEDWNTVM
     YHGIESFGGV GTLGVIVCIY YIVLFICGNY ILLNVFLAIA VDNLADADSL TNAEKEEEQQ
     EIEGEDEEFD EGDEGEDEHG LEEPDGDEEV SARPRRMSEV PAASTIKPIP KASSLFILSH
     TNSFRVFCNM VVNHSYFTNA VLFCILVSSA MLAAEDPLQA NSTRNMVLNY FDYFFTSVFT
     VEITLKVIVF GLVFHKGSFC RNAFNLLDIL VVAVSLTSFV LRTDAMSVVK ILRVLRVLRP
     LRAINRAKGL KHVVQCVIVA VKTIGNIMLV TFMLQFMFAI IGVQLFKGTF FLCNDLSKMT
     EAECRGEYIH YEDGDPTKPV SKKRVWSNND FNFDNVGDAM VSLFVVSTFE GWPQLLYVAI
     DSNEEDKGPI HNSRQAVALF FIAFIIVIAF FMMNIFVGFV IVTFQNEGER EYENCELDKN
     QRKCIEFALK AKPHRRYIPR NRLQYRVWWF VTSRAFEYVI FLIIVMNTVS LACKHYPSSR
     GFEDFLDVFN LIFTGVFAFE AVLKIVALNP KNYISDRWNV FDLLVVVGSF IDITYGKLNP
     GGTNLISINF FRLFRVMRLV KLLSRGEGIR TLLWTFMKSF QALPYVALLI VLLFFIYAVI
     GMQFFGKVAL DDSTSIHRNN NFHSFPAAIL VLFRSATGEA WQDIMLSCSD REDVRCDPMS
     DDYSKGGFNE SRCGNNFAYP YFISFFMLCS FLVINLFVAV IMDNFDYLTR DWSILGPHHL
     EEFVRLWSEY DPDAKGRIKH LDVVTLLRKI SPPLGFGKLC PHRLACKRLV SMNMPLNSDG
     TVCFNATLFA LVRTNLKIYT EGNIDEANEQ LRSAIKRIWK RTHKDLLDEV VPPAGKEDDV
     TVGKFYATFL IQDYFRRFKK RKELEAKGVV PAQTPQAMAL QAGLRTLHEI GPELKRAISG
     NLETDFNFDD AEPQHRRPHS LFNNLVHRLS GARSPTEHER MERGSTLLPY HPRSFSPTHS
     LAGTDDSPVP SQIQRNAPVN QSINLPPVNG SVRRLPALPP YANHIHDETD DGPRYRDTGD
     RPGYDQSHGR MVVANRNLPV DPDEEEAYRG GGIRSNRTDR RTLPPIREPM LVARGAALAL
     AGMSSEAFEG TYRPVGEGKS VRLPFSSRPV LRPAEDPRPI DRLIGQSLGL GRYADARVVG
     AARREIEEAY SLGEQEIDLA ADSLAPLMQH VGMHDIRDIN ENSRSALLRP ADSSSRQRDS
     HGGSQEDLLL VTTL
//
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