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Database: UniProt
Entry: A0A139WPC9_TRICA
LinkDB: A0A139WPC9_TRICA
Original site: A0A139WPC9_TRICA 
ID   A0A139WPC9_TRICA        Unreviewed;      1992 AA.
AC   A0A139WPC9;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-SEP-2017, entry version 12.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=TcasGA2_TC004715 {ECO:0000313|EMBL:KYB29717.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Coleoptera; Polyphaga;
OC   Cucujiformia; Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:KYB29717.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:KYB29717.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB29717.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G.,
RA   Friedrich M., Grimmelikhuijzen C.J., Klingler M., Lorenzen M.,
RA   Richards S., Roth S., Schroder R., Tautz D., Zdobnov E.M., Muzny D.,
RA   Gibbs R.A., Weinstock G.M., Attaway T., Bell S., Buhay C.J.,
RA   Chandrabose M.N., Chavez D., Clerk-Blankenburg K.P., Cree A., Dao M.,
RA   Davis C., Chacko J., Dinh H., Dugan-Rocha S., Fowler G., Garner T.T.,
RA   Garnes J., Gnirke A., Hawes A., Hernandez J., Hines S., Holder M.,
RA   Hume J., Jhangiani S.N., Joshi V., Khan Z.M., Jackson L., Kovar C.,
RA   Kowis A., Lee S., Lewis L.R., Margolis J., Morgan M., Nazareth L.V.,
RA   Nguyen N., Okwuonu G., Parker D., Richards S., Ruiz S.J.,
RA   Santibanez J., Savard J., Scherer S.E., Schneider B., Sodergren E.,
RA   Tautz D., Vattahil S., Villasana D., White C.S., Wright R., Park Y.,
RA   Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J.,
RA   Brown S.J., Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H.,
RA   Lorenzen M., Maselli V., Osanai M., Park Y., Robertson H.M., Tu Z.,
RA   Wang J.J., Wang S., Richards S., Song H., Zhang L., Sodergren E.,
RA   Werner D., Stanke M., Morgenstern B., Solovyev V., Kosarev P.,
RA   Brown G., Chen H.C., Ermolaeva O., Hlavina W., Kapustin Y.,
RA   Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P.,
RA   Aranda M., Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F.,
RA   Bopp D., Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E.,
RA   Ferrier D.E., Friedrich M., Gordon C.M., Jindra M., Klingler M.,
RA   Lan Q., Lattorff H.M., Laudet V., von Levetsow C., Liu Z., Lutz R.,
RA   Lynch J.A., da Fonseca R.N., Posnien N., Reuter R., Roth S.,
RA   Savard J., Schinko J.B., Schmitt C., Schoppmeier M., Schroder R.,
RA   Shippy T.D., Simonnet F., Marques-Souza H., Tautz D., Tomoyasu Y.,
RA   Trauner J., Van der Zee M., Vervoort M., Wittkopp N., Wimmer E.A.,
RA   Yang X., Jones A.K., Sattelle D.B., Ebert P.R., Nelson D., Scott J.G.,
RA   Beeman R.W., Muthukrishnan S., Kramer K.J., Arakane Y., Beeman R.W.,
RA   Zhu Q., Hogenkamp D., Dixit R., Oppert B., Jiang H., Zou Z.,
RA   Marshall J., Elpidina E., Vinokurov K., Oppert C., Zou Z., Evans J.,
RA   Lu Z., Zhao P., Sumathipala N., Altincicek B., Vilcinskas A.,
RA   Williams M., Hultmark D., Hetru C., Jiang H., Grimmelikhuijzen C.J.,
RA   Hauser F., Cazzamali G., Williamson M., Park Y., Li B., Tanaka Y.,
RA   Predel R., Neupert S., Schachtner J., Verleyen P., Raible F., Bork P.,
RA   Friedrich M., Walden K.K., Robertson H.M., Angeli S., Foret S.,
RA   Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:KYB29717.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB29717.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic
RT   information for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
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; KQ971307; KYB29717.1; -; Genomic_DNA.
DR   STRING; 7070.TC004715-PA; -.
DR   EnsemblMetazoa; TC004715_005; TC004715_005; TC004715.
DR   Proteomes; UP000007266; 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; IPR031688; CAC1F_C.
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; PF16885; CAC1F_C; 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:UP000007266};
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:UP000007266};
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    107    125       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    145    165       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    177    197       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    231    255       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    323    344       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    356    378       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    484    505       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    517    535       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    599    627       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    676    699       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    850    874       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    894    915       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    927    952       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    972   1001       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1059   1080       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1100   1124       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1178   1197       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1209   1230       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1251   1273       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1321   1339       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1418   1439       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1574   1608       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED     1950   1977       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1992 AA;  225746 MW;  33479FD2C4811A1F CRC64;
     MDPTLYCPGL QYELRESADN RLWSVQPPYT GCAWQGPISA TATAMSTVGA GVTSPGQTGA
     RTTTAPRRPM RRGGKPPPDR PQRALFCLYL KNPIRKLCID VVEWKPFEYL ILLTIFANCV
     ALAVYTPFPN GDSNVTNGIL EKIEYIFLVI FTVECIMKII AYGFLMHQGA YLRNGWNLLD
     FTIVVIGMIS TALSTLIGDS FDVKALRAFR VLRPLRLVSG VPSLQVVLNS ILRAMVPLLH
     IALLVLFVII IYAIIGLELF SGKMHNTCWN EKKEAFMDEP HPCGANGFNC TEHDSDMVCS
     EFVPGINNTW EGPNSGITNF DNFGLSMLTV FQCITLEGWT DVLYNIQDAM GRTWQWSYFV
     SMVILGAFFV MNLILGVLSG EFSKEREKAK ARGDFHKLRE KQQIEEDLKG YLDWITQAED
     IEPEGEDQSN QDARNNPANE MESTDQLGEE EIQQESWFKK RKKDFERINR RMRRSCRKAV
     KSQTFYWLII VLVFLNTGVL ATEHYNQPLW LDRFQEYTNM FFIALFTMEM LLKLYSLGFQ
     GYFVSLFNRF DCFVVIGSIS EMILTHTNVM PPLGISVLRC VRLLRVFKVT KYWRSLSNLV
     ASLLNSIQSI ASLLLLLFLF IVIFALLGMQ VFGGRFNFND TQDKPRSNFD SFWQSLLTVF
     QILTGEDWNA VMYTGIAAYG GVHGFGVLAC IYFIILFICG NYILLNVFLA IAVDNLADAE
     SLTAIEKEEE EEAQNKSKSP TPHEEENVEE EEEEEHSVEE EETEEDGQYD GERSEHDEEA
     ESQTKMTLDN EEEYEEEQNS QDEQVEVTKD SARPRRLSEV TIVKKIRPIP KGSAFFIFSS
     KNRFRIFCHW LCNHSVFGNV ILVCIMVSSA LLALEDPIPA PGSEMGNILK IFDYVFTAIF
     SAELLLKTIS YGCILHDGAF LRSAFNVLDL VVVCVSIVSI YSQGAMSVVK ILRVLRVLRP
     LRAINRAKGL KHVVQCVIVA VKTIGNIVLV TCLLQFMFAV IGVQLFKGKF SSCTDRSKLT
     ASECNGTYLI YLEGDINKPE MKERNWEPNP FHFDNVAKAM LTLFTVSTFE GWPALLYVSI
     DSNDENRGLI HNYRPIVAAY YIIYIIIIAF FMVNIFVGFV IVTFQNEGEQ EYKNCELDKN
     QRNCIEFALK AKPVRRYIPK HRIQYKVWWF VTSRPFEYAI FMLILTNTIT LAMRFHGQDK
     TYESVLDTLN MIFTAIFAME FVFKLAAFRI KVDQLKISLR IHYIVFNFQN YFGDAWNVFD
     FIIVLGSFID IVYQDVNPGG TKLQISSNFF RLFRVMRLIK LLNKGEGIRT LLWTFLKSFQ
     ALPYVALLIV MLFFIYAVIG MQMFGKIENV DSDTHINRNN NFGSFFQAVL VLFRSATGEG
     WQEIMLACAD TENAKCDSRV ELKQGDSPYC GSDIAYPYFI SFYVLCSFLI INLFVAVIMD
     NFDYLTRDWS ILGPHHLDEF IRLWSEYDPD AKGRIKHLDV VTLLRKISPP LGFGKLCPHR
     VACKRLVSMN MPLNSDGTVL FNATLFAVVR TSLRIKTEGN IDDANAELRA VIKKIWKRTN
     PKLLDQVVPP PGVDDEVTVG KFYATFLIQD YFRRFKKRKE QELKEGDTET HNTVTLQAGL
     RTLHEAGPEL KRAISGNLDE LVDDNPEPMH RRNHSLFGSV WSSMRRGHSF NRAKSLKANS
     TQIKITPASS VDYLPYNSIH RTVTEGMNHI TSMTKSVVQN RASATSLHNQ EGLKDEEIPL
     RSLSNLHNGD TEKNFQVIDK SGFLHPNYKG KRKRILQGDH TELMPPTPPP RRVRLGLGAL
     GNLGGGCMTA TPSPVQHAPS FSRIASGLKL AQAQAMAVAG FLPEPLPYEC SVLGAPGSLQ
     PFTSDSEGDG RHARCSLLNH RASFHGRAPA GEPNGHVGSE RLSHSLPGSP ADRRPTSFEV
     VGSAESLVGR ILVEQGLGKY CDPDFVRNTS KEMQEALDMT QEEMDLAAHQ LLQQERRIHA
     QAPTIDALHP QL
//
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