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Database: UniProt
Entry: A0A158RBG8_THECL
LinkDB: A0A158RBG8_THECL
Original site: A0A158RBG8_THECL 
ID   A0A158RBG8_THECL        Unreviewed;      1894 AA.
AC   A0A158RBG8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-SEP-2017, entry version 8.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS   Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida;
OC   Thelazioidea; Thelaziidae; Thelazia.
OX   NCBI_TaxID=103827 {ECO:0000313|WBParaSite:TCLT_0000455501-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000455501-mRNA-1}
RP   NUCLEOTIDE SEQUENCE.
RG   Helminth Genomes Consortium;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:TCLT_0000455501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) 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   WBParaSite; TCLT_0000455501-mRNA-1; TCLT_0000455501-mRNA-1; TCLT_0000455501.
DR   Proteomes; UP000046394; Genome Assembly.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000046394};
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:UP000046394};
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      7     29       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    112    128       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    148    169       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    181    197       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    241    263       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    361    383       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    487    505       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    517    535       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    616    636       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    694    716       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    822    840       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    860    881       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    893    919       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    939    969       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1064   1091       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1134   1154       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1175   1194       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1200   1226       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1257   1280       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1351   1375       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1510   1544       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      725    747       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1894 AA;  216715 MW;  07F4E2958A29B593 CRC64;
     MEMLHYFYVL IFFRFFLIRN ISVLASMMAS SAEEDDHHAD DTHKSDLWQQ TLQAAVAATS
     QSEAAKKRQQ QRKPMRQTNV VERSERSLLC LTLSNPLRKA CITVVEWRPF EWLILLMICA
     NCIALAVYQP YPAQDSDTKN TILEQIEYLF IIVFTIECIL KVIALGFLFH PGAYLRNAWN
     ILDFIIVVIG LVSTALSRMN IQGFDVKALR AFRVLRPLRL VSGVPSLQVV LNAILRAMIP
     LLHIALLVMF VIIIYAIIGL ELFCGKLHST CLDPATGQLA QHTPSTCGFA SSAFHCQPNG
     YYEGVNWICT SNTSWQGPNN GITNFDNFGL AMLTVFQCVS LEGWTDVMYW VNDAVGREWP
     WIYFVTLVIL GSFFVLNLVL GVLSGEFSKE REKARARGLF QKFREKQQLE EDLKGYLDWI
     NQAEDIEPVN DDEQEDEQQF NGEELDEEVD EKTDDSRPSW WKKKLRRMQK LNRRCRRGCR
     RLVKSQTFYW LVIILVLLNT LVLTTEHYKQ EPWLDHFQTV ANLFFVILFS MEMILKMYSL
     GLTTYTTSQF NRFDCFVVIS SIIEFVLVHF DLMKPLGVSV LRSARLLRIF KVTKYWTSLR
     NLVSSLLNSL RSIMSLLLLL FLFIVIFALL GMQVFGGKFN FNPMNPKPRA NFDTFNQALL
     TVFQILTGED WNTVMYNGIA SFGGVGSWGV LVSIYYIVLF ICGNYILLNV FLAIAVDNLA
     DADSLTNAEK EEEQAEVEEE VAEEDYEDEK YDENGNEEGR DNSRIVMEED EECGEIITAR
     PRRMSELITA KQQKPIPKAS SLFILSHTNP FRVFCNKIVN HSYFTNSVLI CILVSSAMLA
     AEDPLEAQSP RNTILNYFDY FFTTVFTVEI TLKVVVYGLI FHKGSFCRNA FNLLDILVVA
     VSLVSFVLKS DAISVVKILR VLRVLRPLRA INRAKGLKHV VQCVIVAVKT IGNIMLVTFM
     LQFMFAIIGV QLFKGTFFRC TDESKMTEYE CRGEFLAYED GDPLKPHRMK REWIKNDFNF
     DNVGDAMISL FVVSTFEGWP DLLYVAINSN EEDHGPVYNA RQAVAIFFIT FIVVIAFFMM
     NIFVGFVIVT FQNEGEREYE NCELDKNQRK CIEFALKAKP HRRYIPRNRF QYRVWWFVTS
     QFFEYIIFII ILLNTTTLAM KHYPPDPGMD NVLDVLNLIF TGVFALEAFF IFRWNAFDFV
     IVLGSFIDII YGKLSPGSNI ISINFFRLFR VMRLVKLLSR GEGIRTLLWT FMKSFQALPY
     VALLIVLLFF IYAVIGMQVF GKVALNDETH IHRNNNFHTF PAAVLVLFRS ATGEAWQEIM
     LSCSDRDEVK CDPASDDYKQ NPDAKCGVDF AYPYFISFFM LCSFLVINLF VAVIMDNFDY
     LTRDWSILGP HHLEEFVRLW SEYDPDAKGR IKHLDVVTLL RKISPPLGFG KLCPHRLACK
     RLVSMNMPLN SDGTVCFNAT LFALVRTNLK IYTEGNIDEV NEQLRSAIRR IWKRTPQKML
     DEVVPPAGRD DDVTVGKFYA TFLIQDYFRR FKKRKELESK GIVPQQTSQA MALQAGLRTL
     HEIGPELKRA ISGNLETDFA LDIEEPQHRR PHSLFNNIIS ALGGSTRANQ IYREDRASRL
     LPMIGNHQQI SPTHSLHGND VMSLTAHSGI SANCSFTISP SARSNGGVLQ RRLPKLPPLN
     TSFGGKLLGN DSLQMTRLPI NTQHLYLSAN RNMPVETEEW YERRDPSRLR NDETWMRDAI
     SEKGLKKSFS LARNQAMVIA GLPPDISEAF EGTYRPAPDG KSVRLPFSTR TALRAADGNG
     ESLTERLVGE ALALGRYMDE RVVEAARREI AEAYSLEESE LESAAATLAD ARYMEHLGME
     RSEVRDFNRY SARALLRPAP SQEAPDDDLL VTTL
//
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