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Database: UniProt
Entry: H2RNR0_TAKRU
LinkDB: H2RNR0_TAKRU
Original site: H2RNR0_TAKRU 
ID   H2RNR0_TAKRU            Unreviewed;      1940 AA.
AC   H2RNR0;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-SEP-2017, entry version 35.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae;
OC   Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000001773, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000001773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A.,
RA   Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu
RT   facilitates insights into distinct features of genome evolution in
RT   teleosts and mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000001773}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-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}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSTRUP00000001773}.
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DR   Ensembl; ENSTRUT00000001781; ENSTRUP00000001773; ENSTRUG00000000739.
DR   GeneTree; ENSGT00830000128247; -.
DR   Proteomes; UP000005226; Unplaced.
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   Complete proteome {ECO:0000313|Proteomes:UP000005226};
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:UP000005226};
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     71     90       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    110    129       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    141    158       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    216    239       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    295    316       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    328    350       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    503    521       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    541    568       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    627    647       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    708    732       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    843    861       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    873    896       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    916    939       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    960    993       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1084   1111       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1163   1183       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1195   1214       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1298   1321       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1389   1412       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1547   1581       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1940 AA;  217803 MW;  B94D7D5CD906E89A CRC64;
     PCWSLWDAPP VGDVGKSDTL GSTGSARKRG GGAKKAMQAN KSALRAPRAL CCLTLSNPIR
     MAALALVEWK PFDIFILLAI FANCVAMGVT KPFPDDDSNA TNHKLEQVEY VFLVIFTIET
     FTKILAYGLV MHPSAYIRSG WNLLDFVIVI VGLFSVIAEG MTDHKPGEAH HAAGKPGGLD
     VKALRAFRVL RPLRLVSGVP SLQIVLNSIM KAMVPLLHIG MLVMFVIIIY AIIGLELFIG
     RMHKTCYSST TGLMMEDDAS PCAFAGSGRF CVENGTECRG KWEGPNGGIT NFDNIFFAML
     TVFQCITMEG WTDVLYWMND AIGFEIPWIY FVSLVIFGSF FIINLVLGVL SGEFSKEREK
     AVARGELQKA QESKQMEEDM IGYMDWLIEA EDVDEEGNKP SRHSLSPPSR HSLSPPSRHS
     LSPLAHAIRS LHPRSLHPHA IRSPPSLSPP SQSDSDDDIA YLDDDSGFCA SLMAKMMANS
     FCDQLCQINH TMRKNSRVAV KTTNFYWLVL LLVFLNTVAS ASEHYGQPKW LTEMQERANK
     VLLLLFTLEM LMKMYAFGLQ IYFMALFNRF DCFVVCGGIL EMLLVEMEVI PPIGIAVLRC
     IRLLRIFKMT RHWAALSDLV NSLLNSMKAI CSLLLLLFLF LIIFALLGMQ LFGGKFNFDE
     TQMKRSTFDS FPQALLTCFQ ILTGEDWNAV MYDGIMAYGG PIFPNMVVCI YFVILFVCGN
     YILLNVFLAI AVDNLAGGGG KNKVENQKTR HFRVIVPFYH LERKRKMRKS GMTMRRMQNE
     DDDWQENEEL RAIEGLEGVA PLKPDFSGPK EKIVPIPDGS SFFILGKKNC LRVACHNLIH
     HPYFTNFILI FIILSSISLA AEDPIKSHSF RNIVLGYADY VFTSVFTVEI VLKMTVYGAF
     LHTGSFCRNA FNLLDLLVVG VSLTSFFLHS SAISVVKILR VLRVLRPLRA INRAKGLKNV
     VQCVFVAIRT IGNILIVTTL LQFMFACIGV QLFKGRFYSC TDEAKQTPEE CKGTFVIYKD
     GDINHPMVRE RVWENSDFNF DNVLNGMLAL FTVSTFEGWP QLLYRAVDAN AINRGPIYNY
     RVEISIFFII YIIIIAFFMM NIFVGFVIIT FREQGEAEFK NCELNKNQRQ CVYYALKAQP
     IKIYIPKNQS QLKFWKIINS SQFEYIMFVL ILGNTLTLAI QHYEQSKLFT SIMDILNMIF
     TVVFTVEMVI KLLALRAHHY FIDPWNSFDA LIVVGSVLDI AVSEFSGGGG HGEGSKGESG
     KVSITFFRLF RVLRLVKLLS KGEGIRTLLW TFVKSLQALP YVGLLIAMIF FIYAVIGMQM
     FGKVAVDDNT NINRNCNFQT FFMAVLVLFR CATGEQWQEI MLGALPGRRC DPESDIEPGE
     EYTCGSNLAY LYFISFFMLC AYLIINLFIA VIMDNFEYLT RDWTVLGTHH LDEFKRVWSD
     YDPEATGRIK HIDVVTMLRR IQPPLGFGKL CPHRVACKRL VDMNVPLHPD GTVTFNATLF
     ALVRTSLKIK TEGPIDQQNE ELKIIIKKLW KRTKPKLIDE VIPPPRGDEV TCGKFYASFL
     IQDYFKKFRK RKERERKSKR KDKAAALQQG LRSLQDLAPE MRLAMASDLE DEEGADGEMT
     GDEEPEPEAE KEEVITEQVK EDTSGVVVEE PAVAVLTTET EAGYSREGDD ASAASVNSNG
     YNDSNVNGGS VATSPTPYDT NGYNGNGYNR NGYNGYSENG SLFSTNTNGN ACNENGSGYA
     DSKNVRRRLL PAIPKGRRPA FNFQCLKPQR SLDEQTPIPG TYHGNSSPSR SRLQGITHPS
     GRRGKLIYTP MMLVDEATGT RQPLWTDGTT SLPAGNRPGW YPTQARTFNS MRIPPVNQGY
     VSKGGADGLV ESILISEGLG VFARDPKFVS FAKREIAEAC HMSMDEMESA ATDLIARGAT
     RSISRFEDEL ADEMNCVVSY
//
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