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Database: UniProt
Entry: K7FUT3_PELSI
LinkDB: K7FUT3_PELSI
Original site: K7FUT3_PELSI 
ID   K7FUT3_PELSI            Unreviewed;      2334 AA.
AC   K7FUT3;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   25-OCT-2017, entry version 39.
DE   RecName: Full=Voltage-dependent N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1B {ECO:0000313|Ensembl:ENSPSIP00000011793};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudines; Cryptodira; Trionychia; Trionychidae;
OC   Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000011793, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Ensembl:ENSPSIP00000011793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17381049; DOI=10.1080/10425170600760091;
RA   Jung S.-O., Lee Y.-M., Kartavtsev Y., Park I.-S., Kim D.S., Lee J.-S.;
RT   "The complete mitochondrial genome of the Korean soft-shelled turtle
RT   Pelodiscus sinensis (Testudines, Trionychidae).";
RL   DNA Seq. 17:471-483(2006).
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000011793}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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-1B
CC       gives rise to N-type calcium currents. N-type calcium channels
CC       belong to the 'high-voltage activated' (HVA) group and are blocked
CC       by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin-
CC       IIIA (omega-Aga-IIIA). They are however insensitive to
CC       dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA).
CC       Calcium channels containing alpha-1B subunit may play a role in
CC       directed migration of immature neurons.
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:ENSPSIP00000011793}.
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DR   EMBL; AGCU01190440; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01190441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01190442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01190443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01190444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01190445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01190446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01190447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01190448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01190449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 13735.ENSPSIP00000011793; -.
DR   Ensembl; ENSPSIT00000011850; ENSPSIP00000011793; ENSPSIG00000010322.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   OMA; DSPRNNA; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:Ensembl.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IEA:Ensembl.
DR   GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0007269; P:neurotransmitter secretion; IEA:Ensembl.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
DR   GO; GO:0008016; P:regulation of heart contraction; IEA:Ensembl.
DR   GO; GO:0048265; P:response to pain; IEA:Ensembl.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005447; VDCC_N_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF161; PTHR10037:SF161; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01631; NVDCCALPHA1.
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:UP000007267};
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:UP000007267};
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     63     80       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    101    122       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    134    154       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    189    211       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    265    286       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    298    320       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    473    493       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    499    516       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    598    620       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    676    698       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1146   1164       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1184   1204       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1216   1234       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1277   1299       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1389   1414       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1470   1488       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1500   1523       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1583   1612       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1682   1706       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1844   1878       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      707    734       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2334 AA;  264695 MW;  33860BE552D07A51 CRC64;
     GGPPPGQRMY KQSMAQRART MALYNPIPVK QNCFTVNRSL FIFSEDNVIR KYAKRITEWP
     YPVEYMILAT IIANCIVLAL EQHLPEDDKT PMSERLDDTE PYFIGIFCFE AGIKIIALGF
     VFHKGSYLRN GWNVMDFVVV LTGILATAGT DFDLRTLRAV RVLRPLKLVS GIPSLQVVLK
     SIMKAMVPLL QIGLLLFFAI VMFAIIGLEF YMGKFHKTCF SNETGEEIGD FPCGEDPPAR
     QCENGTTCRK YWPGPNYGIT NFDNILFAVL TVFQCITMEG WTDILYNTND AAGNTWNWLY
     FIPLIIIGSF FMLNLVLGVL SGEFAKERER VENRRAFLKL RRQQQIEREL NGYLEWIFKA
     EEVMLAEEDK NAEEKSPLDG RAASEGPVQQ GTASTEPGSG SYNMLKRATI KKSKNDLIHA
     EEAEDHFTDI CSVGSPFARA SLKSGKNESS SYFRRKEKMF RFFIRRMVKA QSFYWIVLCV
     VTLNTLCVAM VHYDQPEGLT NALYFAEFVF LGLFLTEMSL KMYGLGPRNY FHSSFNCFDF
     GVIVGSIFEV IWAAVKPGTS FGISVLRALR LLRIFKVTKY WNSLRNLVVS LLNSMKSIIS
     LLFLLFLFIV VFALLGMQLF GGQFNFQDET PTTNFDTFPA AILTVFQILT GEDWNAVMYH
     GIVSQGGVHS GMFSSIYFII LTLFGNYTLL NVFLAIAVDN LANAQELTKD EEEMEEATNQ
     KLALQKAKEV AEVSPMSAAN ISIAAKQQNS SKSKSVWEQR TSQIRMHNFR ASCEALYNEL
     NPEERVLYAT TLHIRPDMKT HLDRPLVVEP RTDGRNNVSK LSPGDIQETE QAKVTAADSA
     EVPRKHHRHR DRDKVGEQEK SDMAKDENGE SGTNSKEERH RQHRSRSKEA EGGSKEGKSE
     RNRSQEGGKR HHRRGSVEEG AEKEYRRHRP HRHAAERQAK EGNGTINGAR SERRSRHRGG
     SRSGNRESDP GMKGENGEEP HRRHKMRQKA LSTYDSVEKE NGEKEGETGE KDLRNHQPKV
     GTTIEAGGSV SVVPAHTLPS TYLQKVPEQP EDADNQKNVT RMTQPPLDKT TTVNIPVTIT
     APPGETTVIP MNNVEFESKT EEKKDMEVDD LTKNGPKPIL PYSSMFILSP TNPIRRLFHY
     IVNMRYFEMV ILIVIALSSI ALAAEDPVQA ESPRNDALKY LDYIFTGVFT FEMVIKMIDL
     GLLLHPGSYF RDLWNILDFI VVSGALVAFA FSGSKGKDIN TIKSLRVLRV LRPLKTIKRL
     PKLKAVFDCV VNSLKNVLNI LIVYMLFMFI FAVIAVQLFK GKFFYCTDES KELEKDCRGQ
     YLDYEKSEVE AQPRQWQKYE FHYDNVLWAL LTLFTVSTGE GWPTVLKHSV DATHEDQGPS
     PGYRMEMSIF YVVYFVVFPF FFVNIFVALI IITFQEQGDK VMSECSLEKN ERACIDFAIS
     AKPLTRYMPQ NKQSFQYKMW KFVVSPPFEY FIMAMIALNT IVLMMKFYDA PETYEEMLKC
     LNIVFTSMFS MECVLKIIAF GVLNYFRDAW NVFDFVTVLG SITDILVTEI AVSTDNFINL
     SFLRLFRAAR LIKLLRQGYT IRILLWTFVQ SFKALPYVCL LIAMLFFIYA IIGMQVFGNI
     ALDDDTSINR HNNFRTFLQA LMLLFRSATG EAWHEIMLSC LSNRACDKLS GLTKNECGSD
     FAYFYFVSFI FLCSFLMLNL FVAVIMDNFE YLTRDSSILG PHHLDEFIRV WAEYDPAACC
     RIHYKDMYNL LRVIAPPLGL GKKCPHRVAY KRLVRMNMPI SDQDLTVHFT STLMALIRTA
     LEIKLATAGV QQHQCDSELR KEISLVWPNL SQKTLDLLVP PHKQDEMTVG KVYAALMIFD
     FYKQNKNSRD QAHQPPGGLC QTGPVSLFHP LKATLEQTQP LVFNNAKAFL RQKSSASLNN
     GGTLPAPESG IKESVSWGTQ HTQDVFYETR TPAFERGHSE EIPIERVVEM REISPTLANG
     DHQPGLESQG RAASMPRLAA ETQRSKTRSP GSYLAPIPDT SPMKRSISTL TPQRPHPMHL
     YEYSLERMPP DHTHHHHHHR CHRRKDKKQK SLDKPPNQLA DGDAVARPGE ASSKDKKQER
     GRSQERKLHS SSSSEKQRFY SCDRYGSRDR SQPKSADHSR PTSPNGGLEP GPHRQGSGSV
     NGSPLLSTSG ASTPCRGRRQ LPQTPLTPRP SITYKTANSS PVHFTSFQTS LPTFSPGRLS
     RGLSEHNALL QRDSQSHAHS MVARIGSDPY LGHRDDSDSP YRVVPEDTLT FEEAVATNSG
     RSSRTSYVSS LTSQSHQIRR VPNGYHYTLG LSTGPGTCAR ARSYYHEADE DDWC
//
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