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Database: UniProt
Entry: A0A0Q9XH61_DROMO
LinkDB: A0A0Q9XH61_DROMO
Original site: A0A0Q9XH61_DROMO 
ID   A0A0Q9XH61_DROMO        Unreviewed;      2452 AA.
AC   A0A0Q9XH61;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-SEP-2017, entry version 13.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=Dmoj\GI17378 {ECO:0000313|EMBL:KRG02952.1};
GN   ORFNames=Dmoj_GI17378 {ECO:0000313|EMBL:KRG02952.1}, GI17378
GN   {ECO:0000313|FlyBase:FBgn0140122};
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230 {ECO:0000313|EMBL:KRG02952.1, ECO:0000313|Proteomes:UP000009192};
RN   [1] {ECO:0000313|EMBL:KRG02952.1, ECO:0000313|Proteomes:UP000009192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22 {ECO:0000313|Proteomes:UP000009192};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 Genomes Consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B.,
RA   Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N.,
RA   Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P.,
RA   Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W.,
RA   Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A.,
RA   Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D.,
RA   Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D.,
RA   Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A.,
RA   Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H.,
RA   Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S.,
RA   Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A.,
RA   Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S.,
RA   Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J.,
RA   Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W.,
RA   Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A.,
RA   Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S.,
RA   Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H.,
RA   Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F.,
RA   Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S.,
RA   Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J.,
RA   Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A.,
RA   Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A.,
RA   Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B.,
RA   McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P.,
RA   Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B.,
RA   Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S.,
RA   Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D.,
RA   Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H.,
RA   Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A.,
RA   Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H.,
RA   Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L.,
RA   Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C.,
RA   Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M.,
RA   Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E.,
RA   Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D.,
RA   Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N.,
RA   Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C.,
RA   Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B.,
RA   Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A.,
RA   Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D.,
RA   Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P.,
RA   Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A.,
RA   An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P.,
RA   Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J.,
RA   Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A.,
RA   Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M.,
RA   Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G.,
RA   DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M.,
RA   Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D.,
RA   Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F.,
RA   LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T.,
RA   Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V.,
RA   Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J.,
RA   Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V.,
RA   Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T.,
RA   Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B.,
RA   Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P.,
RA   Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C.,
RA   Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L.,
RA   Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N.,
RA   Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T.,
RA   Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A.,
RA   Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C.,
RA   Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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; CH933807; KRG02952.1; -; Genomic_DNA.
DR   RefSeq; XP_015020659.1; XM_015165173.1.
DR   GeneID; 6576426; -.
DR   KEGG; dmo:Dmoj_GI17378; -.
DR   FlyBase; FBgn0140122; Dmoj\GI17378.
DR   Proteomes; UP000009192; Unassembled WGS sequence.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0008332; F:low voltage-gated calcium channel activity; IEA:EnsemblMetazoa.
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; 5.
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:UP000009192};
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:UP000009192};
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    611    629       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    649    670       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    682    701       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    742    764       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    851    871       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    980    998       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1010   1028       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1109   1128       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1180   1208       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1340   1357       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1377   1397       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1409   1435       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1470   1493       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1505   1525       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1620   1644       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1665   1690       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1757   1775       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1850   1871       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     2006   2040       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   2452 AA;  269711 MW;  6EA302822E389834 CRC64;
     MGGGELVNCI AYDDNTLIIE RKPSPTSPAS ARRYMKAETQ TRGSRKYNRK SSTARSELEV
     IVVKPEHRHQ HRSPTITLPV PATSAATLAT ATTPATAAAA AAAATTTGPT VLQQSCSPRE
     VIAFSEETPA SSSSRIRAAA NNTELALSTV TSQIVNNTTY KLDFKQRRHK SNNNNNNNGS
     EAHSSNGGSK RQRRKSSCNS CGGTASQRLT PEEAATSAAA AAAPSAAESS YSAVGGDSSS
     SNSCNCDITG DNSTLHGFGV GDISSFIGDD DCEEDEDDDP DNPDAADVSS QTLRTAAIVA
     AVAAAAKEQQ GAAASATATA GSAGGGNTDC ESLSERRQDA DDDADDEIRI IAGAVRSGND
     SLEDVGDVDD NADVIVRRNT RNQRPSIRRT CRITEEDDDG AEITDDDDDD YDEEDEPEGT
     TIDIDDQEQL AQQQHDYQHH DDDEEVDDDD DEEADEYYEE EEDNTQAFSP FYSSSAELID
     NFGGGAGKYF NIMDFERGAA GGGTFTPNGN GGAGAVGGDM SSAHNPQADM GGGNNIMGID
     SMGIANIPET MNGTTIGPSG GGGQKAGAAG QKRPQRRGKP QPDRPQRALF CLGLKNPIRA
     LCIRIVEWKP FEFLILLTIF ANCIALAVYT PYPGSDSNVT NQTLEKVEYI FLVIFTAECV
     MKILAYGFVL HNGAYLRNGW NLLDFTIVVI GAISTALSHL MKDAFDVKAL RAFRVLRPLR
     LVSGVPSLQV VLNSILKAMV PLFHIALLVI FVIIIYAIIG LELFSGKLHK TCRDEVTGEY
     EEDVRPCGIG RLCPEGMKCY GNWAGPNSGI TNFDNFGLAM LTVFQCVTLE GWTDVLYYIQ
     DAMGSDWQWM YFISMVILGA FFVMNLILGV LSGEFSKERN KAKNRGDFQK LREKQQIEED
     LRGYLDWITQ AEDIEPDATG GLMPDGKSKQ PNDMDSTENM GEEMPEMQVT ESRWRKMKKD
     FDRVNRRMRR ACRKAVKSQA FYWLIIVLVF LNTGVLATEH YGQVDWLDEF QEYTNIVFIG
     LFTCEMLLKM YSLGFQGYFV SLFNRFDCFV VIGSISETLL TKTGMMPPLG VSVLRCVRLL
     RVFKVTKYWR SLSNLVCSLL NSIQSIASLL LLLFLFIVIF ALLGMQVFGG KFNYNEEEKY
     RTNFDCFWQS LLTVFQIMTG EDWNAVMYVG INAYGGVSSY GALACIYFII LFICGNYILL
     NVFLAIAVDN LADADSLSEV EKDEEPHDEG ALKKEHSPTP TIDGMDDEHL SIDMDMDMEN
     NDMDDDKDHE TLSDEEVREM CEDEEEVDEE DIITARPRRM SEINTATKIL PIPPGTSFFL
     FSQTNRFRVF CHWLCNHSNF GNIILCCIMF SSAMLAAENP LRANDELNKV LLKFDYFFTA
     VFTIELILKL ISYGFVLHDG AFCRSAFNLL DLVVVCVSLI SVAFSSNAIS VVKILRVLRV
     LRPLRAINRA KGLKHVVQCV IVAVKTIGNI VLVTCLLQFM FAVIGVQLFK YVVKCVVVAI
     KTIGNIMLVT YLLQFMFAVI GVQLFKGKFF SCSDGSKMVR EECFGTYLVY EGGDMNKPRL
     KEREWKNNGF HFDDVAKGML TLFTVSTFEG WPSLLYVSID SNKEDGGPIH NFRPIVAAYY
     IIYIIIIAFF MVNIFVGFVI VTFQNEGEQE YKNCDLDRSA YCIEFAIYFG DAWYVFDFII
     VLGSVIDIVY SEIKSKNPPQ THCDIVEGCK AKVKEAGSNL ISINFFRLFR VMRLVKLLSK
     GEGIRTLLWT FIKSFQALPY VALLIVLLFF IYAVVGMQMF GKIAINGGTA ITRNNNFQTF
     QQAVLVLFRS ATGEAWQDIM MACSAQPEVR CDELSDTPNA QCGSSIAYPY FISFYVLCSF
     LIINLFVAVI MDNFDYLTRD WSILGPHHLD EFIRLWSEYD PDAKGRIKHL DVVTLLRKIS
     PPLGFGKLCP HRMACKRLVS MNMPLNSDGT VLFNATLFAV VRTSLSIKTE GNIDDANAEL
     RATIKQIWKR TNPKLLDQVV PPPGNDDEVT VGKFYATYLI QDYFRRFKKR KEQEGKEGHP
     DSNTVTLQAG LRTLHEVSPA LKRAISGNLD ELAEEPEPMH RRHHTLFGSV WSSIRRHGNG
     TFRRSAKASQ SNGALTIGGS SLAAAGVGGS TMVLGSADAG GTDYLYDNLN RSVADGVNHI
     TRNIMQARLA ASGKLQDELH ASSGGELRTF GESISMRPLA KNGGGASTVT GTLPPEANAL
     SYDNRNRGIL LHPYNNVYAA NGAIPGHERM IQSTPASPYD QRRLPTSSDM NGLAESLIGG
     VLAAEGLGKY CDSEFVGTAA REMREALDMT PEEMNLAAHQ ILSNEHSLSL IGSSNGSIFG
     SVGGVGGGGG GGVGSSSIAG AFGGSGSGPS AFSPREDSGT LQSPPIPDNR LRRVATISTT
     NNNTKSQFSQ NNNTNNLNSR TMSPTQQQQQ QQQQLSPQRN LGSGQNNPAS FS
//
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