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Database: UniProt
Entry: A0A091D0B2_FUKDA
LinkDB: A0A091D0B2_FUKDA
Original site: A0A091D0B2_FUKDA 
ID   A0A091D0B2_FUKDA        Unreviewed;      1906 AA.
AC   A0A091D0B2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   25-OCT-2017, entry version 16.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=H920_14230 {ECO:0000313|EMBL:KFO24422.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricomorpha; Bathyergidae; Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO24422.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO24422.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO24422.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) 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; KN123586; KFO24422.1; -; Genomic_DNA.
DR   Proteomes; UP000028990; 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; IPR005450; VDCC_L_a1ssu.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF190; PTHR10037:SF190; 2.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 5.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01634; LVDCCALPHA1S.
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:UP000028990};
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:UP000028990};
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     55     72       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     92    112       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    124    145       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    196    218       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    278    299       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    311    333       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    433    450       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    470    488       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    562    581       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    634    661       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    795    817       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    837    858       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    870    896       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    916    945       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1042   1068       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1122   1140       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1152   1172       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1248   1265       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1383   1406       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1540   1573       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1906 AA;  215976 MW;  7ED396CED630C37B CRC64;
     MEPSSPQDES QRKKQSKKPV PEVLPRPPRA LFCLTLQNPL RKACISIVEW KPFETIILLT
     IFANCVALAV YLPMPEDDNN TLNLGLEKLE YFFLIVFSIE AAMKIIAYGF LFHQDAYLRS
     GWNVLDFTIV FLGVFTVSLE QVNIIQSNTA PMSSKGAGLD VKALRAFRVL RPLRLVSGVP
     SLQVVLNSIF KAVLPLFHIA LLVLFMVIIY AIIGLELFKG KMHKACYFVG TDILATVENE
     QPSPCARTGS GRPCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIT MEGWTDVLYW
     VNDAIGKEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF QKLREKQQLE
     EDLRGYMSWI TQGEVMDVED LREGKLSLDE GGSDTESLYE IEGLNKIIQF IRHWRQWNRV
     FRRKCHDVVK SKVFYWLVIL IVALNTLSIA SEHHSQPLWL THLQDVANRV LLALFTIEML
     MKMYGLGLRQ YFMSVFNRFD CFVVCSGILE ILLVESGAMT PLGISVLRCV RLLRIFKVTK
     YWTSLSNLVA SLLNSIRSIA SLLLLLFLFI VIFALLGMQL FGGRYDFEDT EVRRSNFDNF
     PQALISVFQV LTGEDWTSVM YNGIMAYGGP SYPGVLVCIY FIILFVCGNY ILLNVFLAIA
     VDNLAEAESL TSAQKAKAEE RKRRKMSRGL PEKSEEEKST MAKKLEQKPK GEGIPTTAKL
     KIDEFESNVN EVKDPYPSAD FPGDDEEDEP EIPVSPRPRP LAELQLKEKA VPIPEASSFF
     IFSPTNKIRV LCHRIVNATW FTNFILLFIL LSSAALAAED PIRAESTRNQ ILEYFDIVFT
     SVFTVEIVLK MTTYGAFLHK GSFCRNYFNI LDLLVVAVSL ISMGLESSTI SVVKILRVLR
     VLRPLRAINR AKGLKHVVQC VFVALRTIGN IVLVTTLLQF MFACIGVQLF KGKFFSCNDL
     SKMTEEQCKG SYYVYKDGDP TQIELHPRQW LHNDFHFDNV LSAMMSLFTV STFEGWPQLL
     YKAIDANEED VGPIYNNRVE MAIFFIIYII LIAFFMMNIF VGFVIVTFQE QGETEYKNCE
     LDKNQRQCVQ YALKARPLRC YIPKNPYQYQ VWYVVTSSYF EYLMFALIML NTICLGMQHY
     NQSEQMNHIS DILNVAFTII FTLEMILKLM AFKARGYFGD PWNVFDFLIV IGSIIDVILS
     EIDDPDESAR ISSAFFRLFR VMRLIKLLSR AEGVRTLLWT FIKSFQALPY VALLIVMLFF
     IYAVIGMQMF GKIAMLDGTQ INRNNNFQTF PQAVLLLFRQ ECPRPAPDSP CFALICTGSA
     SPTVGSPAGF LPCSSLLDDF SHLCATGEAW QEILLACSYG KLCDPESDYA PGEEYTCGTN
     FAYYYFISFY MLCAFLIINL FVAVIMDNFD YLTRDWSILG PHHLDEFKAI WAEYDPEAKG
     RIKHLDVVTL LRRIQPPLGF GKFCPHRVAC KRLVGMNMPL NSDGTVTFNA TLFALVRTAL
     KIKTEGNFEQ ANEELRAIIK KIWKRTSMKL LDQVIPPIGD DEVTVGKFYA TFLIQEHFRK
     FMKRQEEYYG YRPKKDTVQI QAGLRTIEEE AAPEIHRTIS GDLTAEEELE RAMVEAAMEE
     GIFRRTGGLF GQVDNFLERT NSLPAAMANQ RPLQFTEIDM EELESPVFLE DFPHDPRTNP
     LARANANNAN ANVACGNSSH SNSQAFFSVH YEREFLEETE TPAARGGAFG QACRELGAHN
     KPLMERLRGQ LTTRGMPGGQ APPAPCQHLR METFTSEEKS STPGPLHEEA HHSRRSREGD
     ARCQAPATTL LIQEALVRGG LGSLAADANF VMATGQALAD ACQMEPEEVE VAATELLRGR
     ESPEGMARTQ SLRSSLDSLD QRQGSRETLI PPKRCKLWSQ PGSELD
//
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