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Database: UniProt
Entry: F6REC1_CALJA
LinkDB: F6REC1_CALJA
Original site: F6REC1_CALJA 
ID   F6REC1_CALJA            Unreviewed;      2345 AA.
AC   F6REC1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   25-OCT-2017, entry version 42.
DE   RecName: Full=Voltage-dependent N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1B {ECO:0000313|Ensembl:ENSCJAP00000024932};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000024932, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000024932, ECO:0000313|Proteomes:UP000008225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000024932}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2011) 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: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00448}.
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:ENSCJAP00000024932}.
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DR   EMBL; ACFV01149493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01149494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01149495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01149496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01149497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01149498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01149499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01149500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01149501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01149502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 9483.ENSCJAP00000024932; -.
DR   Ensembl; ENSCJAT00000026358; ENSCJAP00000024932; ENSCJAG00000013488.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; F6REC1; -.
DR   OMA; DSPRNNA; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Proteomes; UP000008225; Chromosome 1.
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:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR002048; EF_hand_dom.
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.
DR   PROSITE; PS50222; EF_HAND_2; 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:UP000008225};
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:UP000008225};
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    141    162       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    174    194       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    229    251       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    306    327       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    339    361       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    491    511       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    517    534       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    616    638       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    694    716       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1158   1176       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1196   1216       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1228   1246       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1289   1311       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1401   1426       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1482   1500       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1512   1535       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1541   1559       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1605   1623       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1692   1715       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1731   1766       EF-hand. {ECO:0000259|PROSITE:PS50222}.
FT   COILED      719    745       {ECO:0000256|SAM:Coils}.
FT   COILED      999   1026       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2345 AA;  263261 MW;  5528EB63B3C4E7B3 CRC64;
     QGRQPSALGG LGGRGPSGTR RSGPGLGSGS GLQPRGLQPG QRVLYKHSIA QRARTMALYN
     PIPVKHNCFT VNRSLFVFSE DNVVRKYAKR ITEWPFLNPR TPFEYMILAT IIANCIVLAL
     EQHLPDGDKT PMSERLDDTE PYFIGIFCFE AGIKIIALGF VFHKGSYLRN GWNVMDFVVV
     LTGILATAGT DFDLRTLRAV RVLRPLKLVS GIPSLQVVLK SIMKAMVPLL QIGLLLFFAI
     LMFAIIGLEF YMGKFHKACF PNSTDAEPVG DFPCGKEAPA RLCEGDTECR EYWPGPNFGI
     TNFDNILFAI LTVFQCITME GWTDILYNTN DAAGNTWNWL YFIPLIIIGS FFMLNLVLGV
     LSGEFAKERE RVENRRAFLK LRRQQQIERE LNGYLEWIFK AEEVMLAEED RNAEEKSPLD
     AVLKRAATKK SRNDLIHAEE GEDRFADLCA VGSPFARASL KSGKTESSSY FRRKEKMFRF
     FIRRMVKAQS FYWVVLCVVA LNTLCVAMVH YNQPRRLTTA LYFAEFVFLG LFLTEMSLKM
     YGLGPRSYFR SSFNCFDFGV IVGSVFEVVW AAIKPGSSFG ISVLRALRLL RIFKVTKYWS
     SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFQDETPT TNFDTFPAAI
     LTVFQILTGE DWNAVMYHGI ESQGGVSKGM FSSFYFIVLT LFGNYTLLNV FLAIAVDNLA
     NAQELTKDEE EMEEAANQKL ALQKAKEVAE VSPMSAANIS IAARQQNSAK ARSVWEQRAS
     QLRLQNLRAS CEALYSEMDP EERLRFATTR HLRPDMKTHL DRPLVVELGR DGARGTVGGK
     ARQEAAEVPE GADPPRRHHR HRDKDRAPAA GDQDRAEAPK AESGEPGARE ERPRPHRSHS
     KEAAGPPEAR SERGRGPGPE GGRRHHRRGS PEEVAEREPR RHRTHRHQDP GKEGAGAKGE
     RRARHRGGPR TGPREAESGE EPARRHRARH KVLPVHEVAE KEAMEKETAE KEAEIVEADK
     EKELRNHQPR EPHCDLETSG TVTVGPVHTL PSTCLQKVEE QPEDADNQRN VTRMGSQPPD
     SSTVVHIPVM LTGPPGEATV VPSGNVDPES QAEGKKEVEA DDVMRSGPRP IVPYSSMFCL
     SPTNLLRRFC HYIVTMRYFE MVILVVIALS SIALAAEDPV RTDSPRNNAL KYLDYIFTGV
     FTFEMVIKMI DLGLLLHPGA YFRDLWNILD FIVVSGALVA FAFSGSKGKD INTIKSLRVL
     RVLRPLKTIK RLPKLKAVFD CVVNSLKNVL NILIVYMLFM FIFAVIAVQL FKGKFFYCTD
     ESKELERDCR GQYLDYEKEE VEAQPRQWKK YDFHYDNVLW ALLTLFTVST GEGWPMVLKH
     SVDATYEEQG PSPGYRMELS IFYVVYFVVF PFFFVNIFVA LIIITFQEQG DKVMSECSLE
     KNERACIDFA ISAKPLTRYM PQNRQSFQYK TWTFVVSPPF EYFIMAMIAL NTVVLMMKFY
     DAPYEYELML KCLNIVFTSM FSMECVLKII AFGVLNYFRD AWNVFDFVTV LGSITDILVT
     EIARTNNFIN LSFLRLFRAA RLIKLLRQGY TIRILLWTFV QSFKALPYVC LLIAMLFFIY
     AIIGMQVFGN IALDDDTSIN RHNNFRTFLQ ALMLLFRSAT GEAWHEIMLS CLSNQACDEQ
     ANATECGSDF AYFYFVSFIF LCSFLMLNLF VAVIMDNFEY LTRDSSILGP HHLDEFIRVW
     AEYDPAACGR ISYNDMFEML KHMSPPLGLG KKCPARVAYK RLVRMNMPIS NEDMTVHFTS
     TLMALIRTAL EIKLAPAGTK QHQCDAELRK EISIVWANLP QKTLDLLVPP HKPDEMTVGK
     VYAALMIFDF YKQNKSTRDQ MQQAPGGLSQ MGPVSLFHPL KATLEQTQPA VLRGARVFLR
     QKSSTSLSNG GAIQNQESGI KESVSWGTQR TQDAPLESRP PLERGHSTEI PVGQSGALAV
     DVQMQSMTRR GPDGEPQPGL ESQGRAASMP RLAAETQPVA DASPMKRSIS TLAQRPRGAH
     LCSTTPDRPP PSQAPHHHHH RCHRRRDRKQ RSLEKGPSLS AETDGAPSSA AGPGLPLGEG
     PTGCKRERER RQERGRSQER RQPSSSSSEK QRFYSCDRFG GREPPKPKPS LSSHPTSPTA
     GQEPGPHPQG SGSVNGSPLL STSGASTPGR GGRRQLPQTP LTPRPSITYK TANSSPVHFA
     GAQTSLPAFS PGRLSRGLSE HNALLQRDPL SQPLAPGSRI GSDPYLGQRL DSEASVHALP
     EDTLTFEEAV ATNSGRSSRT SYVSSLTSQS HPLRRVPNGY HCTLGLSSGG RARHSYHHPD
     QDHWC
//
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