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CAC1B_RAT
ID   CAC1B_RAT               Reviewed;        2336 AA.
AC   Q02294;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Voltage-dependent N-type calcium channel subunit alpha-1B;
DE   AltName: Full=Brain calcium channel III;
DE            Short=BIII;
DE   AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 5;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.2;
GN   Name=Cacna1b; Synonyms=Cach5, Cacnl1a5;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH THE OMEGA-CONOTOXIN
RP   GVIA, AND ACTIVITY REGULATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=1317580; DOI=10.1073/pnas.89.11.5058;
RA   Dubel S.J., Starr T.V.B., Hell J.W., Ahlijanian M.K., Enyeart J.J.,
RA   Catterall W.A., Snutch T.P.;
RT   "Molecular cloning of the alpha-1 subunit of an omega-conotoxin-sensitive
RT   calcium channel.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:5058-5062(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1516-1679 (CLONE RBB-10).
RX   PubMed=1692134; DOI=10.1073/pnas.87.9.3391;
RA   Snutch T.P., Leonard J.P., Gilbert M.M., Lester H.A., Davidson N.;
RT   "Rat brain expresses a heterogeneous family of calcium channels.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:3391-3395(1990).
RN   [3]
RP   PHOSPHORYLATION.
RX   PubMed=8125957; DOI=10.1016/s0021-9258(17)37297-6;
RA   Hell J.W., Appleyard S.M., Yokoyama C.T., Warner C., Catterall W.A.;
RT   "Differential phosphorylation of two size forms of the N-type calcium
RT   channel alpha 1 subunit which have different COOH termini.";
RL   J. Biol. Chem. 269:7390-7396(1994).
RN   [4]
RP   BETA-SUBUNIT BINDING DOMAIN.
RX   PubMed=7509046; DOI=10.1038/368067a0;
RA   Pragnell M., de Waard M., Mori Y., Tanabe T., Snutch T.P., Campbell K.P.;
RT   "Calcium channel beta-subunit binds to a conserved motif in the I-II
RT   cytoplasmic linker of the alpha 1-subunit.";
RL   Nature 368:67-70(1994).
RN   [5]
RP   ACTIVITY REGULATION.
RX   PubMed=10938268; DOI=10.1074/jbc.m002252200;
RA   Lewis R.J., Nielsen K.J., Craik D.J., Loughnan M.L., Adams D.A.,
RA   Sharpe I.A., Luchian T., Adams D.J., Bond T., Thomas L., Jones A.,
RA   Matheson J.-L., Drinkwater R., Andrews P.R., Alewood P.F.;
RT   "Novel omega-conotoxins from Conus catus discriminate among neuronal
RT   calcium channel subtypes.";
RL   J. Biol. Chem. 275:35335-35344(2000).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-746 AND SER-2253,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [7]
RP   FUNCTION.
RX   PubMed=23699505; DOI=10.1523/jneurosci.4288-12.2013;
RA   Kim S.H., Ryan T.A.;
RT   "Balance of calcineurin Aalpha and CDK5 activities sets release probability
RT   at nerve terminals.";
RL   J. Neurosci. 33:8937-8950(2013).
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC       of calcium ions into excitable cells and are also involved in a variety
CC       of calcium-dependent processes, including muscle contraction, hormone
CC       or neurotransmitter release, gene expression, cell motility, cell
CC       division and cell death. This alpha-1B subunit gives rise to N-type
CC       calcium currents. N-type calcium channels belong to the 'high-voltage
CC       activated' (HVA) group. They are involved in pain signaling. Calcium
CC       channels containing alpha-1B subunit may play a role in directed
CC       migration of immature neurons. Mediates Ca(2+) release probability at
CC       hippocampal neuronal soma and synaptic terminals (PubMed:23699505).
CC       {ECO:0000269|PubMed:23699505}.
CC   -!- ACTIVITY REGULATION: Is specifically blocked by omega-conotoxin GVIA
CC       (Probable) (PubMed:10938268). Is specifically blocked by omega-
CC       conotoxin MVIIA (ziconotide) (By similarity). Is insensitive to
CC       dihydropyridines (DHP). {ECO:0000250|UniProtKB:Q00975,
CC       ECO:0000269|PubMed:10938268, ECO:0000305|PubMed:1317580}.
CC   -!- SUBUNIT: Multisubunit complex consisting of alpha-1, alpha-2, beta and
CC       delta subunits in a 1:1:1:1 ratio. The channel activity is directed by
CC       the pore-forming and voltage-sensitive alpha-1 subunit. In many cases,
CC       this subunit is sufficient to generate voltage-sensitive calcium
CC       channel activity. The auxiliary subunits beta and alpha-2/delta linked
CC       by a disulfide bridge regulate the channel activity. Interacts with
CC       RIMS1. Interacts with FMR1 (via C-terminus); this interaction induces a
CC       decrease in the number of presynaptic functional CACNA1B channels at
CC       the cell surface. {ECO:0000250|UniProtKB:O55017}.
CC   -!- INTERACTION:
CC       Q02294; P21707: Syt1; NbExp=2; IntAct=EBI-540038, EBI-458098;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q00975}; Multi-
CC       pass membrane protein {ECO:0000250|UniProtKB:Q00975}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=2 isoforms may be produced.;
CC       Name=1;
CC         IsoId=Q02294-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Central nervous system.
CC   -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC       transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC       transmembrane segment (S4). S4 segments probably represent the voltage-
CC       sensor and are characterized by a series of positively charged amino
CC       acids at every third position.
CC   -!- PTM: Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK.
CC       {ECO:0000269|PubMed:8125957}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. CACNA1B subfamily. {ECO:0000305}.
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DR   EMBL; M92905; AAA42014.1; -; mRNA.
DR   PIR; B35901; B35901.
DR   PDB; 4DEX; X-ray; 2.00 A; B=358-468.
DR   PDBsum; 4DEX; -.
DR   AlphaFoldDB; Q02294; -.
DR   SMR; Q02294; -.
DR   CORUM; Q02294; -.
DR   IntAct; Q02294; 4.
DR   MINT; Q02294; -.
DR   STRING; 10116.ENSRNOP00000006162; -.
DR   BindingDB; Q02294; -.
DR   ChEMBL; CHEMBL5107; -.
DR   DrugCentral; Q02294; -.
DR   GuidetoPHARMACOLOGY; 533; -.
DR   GlyGen; Q02294; 3 sites.
DR   iPTMnet; Q02294; -.
DR   PhosphoSitePlus; Q02294; -.
DR   PaxDb; Q02294; -.
DR   PRIDE; Q02294; -.
DR   UCSC; RGD:628852; rat. [Q02294-1]
DR   RGD; 628852; Cacna1b.
DR   eggNOG; KOG2301; Eukaryota.
DR   InParanoid; Q02294; -.
DR   PhylomeDB; Q02294; -.
DR   Reactome; R-RNO-112308; Presynaptic depolarization and calcium channel opening.
DR   PRO; PR:Q02294; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0043679; C:axon terminus; IDA:RGD.
DR   GO; GO:0030425; C:dendrite; ISO:RGD.
DR   GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; EXP:SynGO.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0043005; C:neuron projection; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; EXP:SynGO.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:RGD.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; IPI:RGD.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:RGD.
DR   GO; GO:0099635; F:voltage-gated calcium channel activity involved in positive regulation of presynaptic cytosolic calcium levels; EXP:SynGO.
DR   GO; GO:0070509; P:calcium ion import; IMP:RGD.
DR   GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; ISO:RGD.
DR   GO; GO:0006816; P:calcium ion transport; IMP:RGD.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0007269; P:neurotransmitter secretion; ISO:RGD.
DR   GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IMP:RGD.
DR   GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR   GO; GO:0051924; P:regulation of calcium ion transport; ISO:RGD.
DR   GO; GO:0008016; P:regulation of heart contraction; ISO:RGD.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:1904645; P:response to amyloid-beta; ISO:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
DR   GO; GO:0048265; P:response to pain; ISO:RGD.
DR   GO; GO:0033574; P:response to testosterone; IMP:RGD.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
DR   Gene3D; 1.20.120.350; -; 4.
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   InterPro; IPR043203; VGCC_Ca_Na.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037; PTHR10037; 1.
DR   PANTHER; PTHR10037:SF289; PTHR10037:SF289; 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   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Calcium; Calcium channel;
KW   Calcium transport; Disulfide bond; Glycoprotein; Ion channel;
KW   Ion transport; Membrane; Metal-binding; Methylation; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..2336
FT                   /note="Voltage-dependent N-type calcium channel subunit
FT                   alpha-1B"
FT                   /id="PRO_0000053924"
FT   TOPO_DOM        1..90
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        91..114
FT                   /note="Helical; Name=S1 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        115..131
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        132..152
FT                   /note="Helical; Name=S2 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        153..163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        164..182
FT                   /note="Helical; Name=S3 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        183..187
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        188..211
FT                   /note="Helical; Name=S4 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        212..221
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        222..244
FT                   /note="Helical; Name=S5 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        245..331
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        332..356
FT                   /note="Helical; Name=S6 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        357..483
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        484..502
FT                   /note="Helical; Name=S1 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        503..512
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        513..535
FT                   /note="Helical; Name=S2 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        536..545
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        546..567
FT                   /note="Helical; Name=S3 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        568..574
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        575..587
FT                   /note="Helical; Name=S4 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        588..605
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        606..631
FT                   /note="Helical; Name=S5 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        632..683
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        684..710
FT                   /note="Helical; Name=S6 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        711..1149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1150..1168
FT                   /note="Helical; Name=S1 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1169..1176
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1177..1201
FT                   /note="Helical; Name=S2 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1202..1215
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1216..1240
FT                   /note="Helical; Name=S3 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1241..1246
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1247..1267
FT                   /note="Helical; Name=S4 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1268..1285
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1286..1305
FT                   /note="Helical; Name=S5 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1306..1392
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1393..1418
FT                   /note="Helical; Name=S6 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1419..1473
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1474..1492
FT                   /note="Helical; Name=S1 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1493..1500
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1501..1525
FT                   /note="Helical; Name=S2 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1526..1535
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1536..1557
FT                   /note="Helical; Name=S3 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1558..1563
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1564..1582
FT                   /note="Helical; Name=S4 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1583..1601
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1602..1621
FT                   /note="Helical; Name=S5 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1622..1683
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1684..1707
FT                   /note="Helical; Name=S6 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1708..2336
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   REPEAT          82..359
FT                   /note="I"
FT   REPEAT          469..713
FT                   /note="II"
FT   REPEAT          1135..1421
FT                   /note="III"
FT   REPEAT          1458..1711
FT                   /note="IV"
FT   DOMAIN          1724..1759
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..396
FT                   /note="Binding to the beta subunit"
FT   REGION          800..1021
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1051..1076
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1981..2202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        800..822
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        873..945
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..1021
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1059..1076
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2014..2031
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2047..2063
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2094..2117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2161..2202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         452..459
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         545
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   BINDING         585
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   BINDING         588
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   BINDING         1737
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000305"
FT   BINDING         1743
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000305"
FT   BINDING         1748
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000305"
FT   SITE            314
FT                   /note="Calcium ion selectivity and permeability"
FT                   /evidence="ECO:0000250"
FT   SITE            664
FT                   /note="Calcium ion selectivity and permeability"
FT                   /evidence="ECO:0000250"
FT   SITE            1367
FT                   /note="Calcium ion selectivity and permeability"
FT                   /evidence="ECO:0000250"
FT   SITE            1655
FT                   /note="Calcium ion selectivity and permeability"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         22
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O55017"
FT   MOD_RES         411
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         746
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         749
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O55017"
FT   MOD_RES         784
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O55017"
FT   MOD_RES         1067
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O55017"
FT   MOD_RES         2065
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O55017"
FT   MOD_RES         2221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O55017"
FT   MOD_RES         2230
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O55017"
FT   MOD_RES         2253
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   CARBOHYD        1563
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1675
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        1538
FT                   /note="N -> D (in Ref. 2; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1579
FT                   /note="C -> L (in Ref. 2; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   HELIX           364..403
FT                   /evidence="ECO:0007829|PDB:4DEX"
SQ   SEQUENCE   2336 AA;  262256 MW;  8D50AF67834FD1BC CRC64;
     MVRFGDELGG RYGGTGGGER ARGGGAGGAG GPGQGGLPPG QRVLYKQSIA QRARTMALYN
     PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD
     GDKTPMSERL DDTEPYFIGI FCFEAGIKII ALGFVFHKGS YLRNGWNVMD FVVVLTEILA
     TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII
     GLEFYMGKFH KACFPNSTDA EPVGDFPCGK EAPARLCDSD TECREYWPGP NFGITNFDNI
     LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA
     KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDKNAEEK SPLDAVLKRA
     ATKKSRNDLI HAEEGEDRFV DLCAAGSPFA RASLKSGKTE SSSYFRRKEK MFRFLIRRMV
     KAQSFYWVVL CVVALNTLCV AMVHYNQPQR LTTALYFAEF VFLGLFLTEM SLKMYGLGPR
     SYFRSSFNCF DFGVIVGSIF EVVWAAIKPG TSFGISVLRA LRLLRIFKVT KYWNSLRNLV
     VSLLNSMKSI ISLLFLLFLF IVVFALLGMQ LFGGQFNFQD ETPTTNFDTF PAAILTVFQI
     LTGEDWNAVM YHGIESQGGV SKGMFSSFYF IVLTLFGNYT LLNVFLAIAV DNLANAQELT
     KDEEEMEEAA NQKLALQKAK EVAEVSPMSA ANISIAARQQ NSAKARSVWE QRASQLRLQN
     LRASCEALYS EMDPEERLRY ASTRHVRPDM KTHMDRPLVV EPGRDGLRGP AGNKSKPEGT
     EATEGADPPR RHHRHRDRDK TSASTPAGGE QDRTDCPKAE STETGAREER ARPRRSHSKE
     APGADTQVRC ERSRRHHRRG SPEEATEREP RRHRAHRHAQ DSSKEGKEGT APVLVPKGER
     RARHRGPRTG PRETENSEEP TRRHRAKHKV PPTLEPPERE VAEKESNVVE GDKETRNHQP
     KEPRCDLEAI AVTGVGSLHM LPSTCLQKVD EQPEDADNQR NVTRMGSQPS DPSTTVHVPV
     TLTGPPGEAT VVPSANTDLE GQAEGKKEAE ADDVLRRGPR PIVPYSSMFC LSPTNLLRRF
     CHYIVTMRYF EMVILVVIAL SSIALAAEDP VRTDSFRNNA LKYMDYIFTG VFTFEMVIKM
     IDLGLLLHPG AYFRDLWNIL DFIVVSGALV AFAFSSFMGG SKGKDINTIK SLRVLRVLRP
     LKTIKRLPKL KAVFDCVVNS LKNVLNILIV YMLFMFIFAV IAVQLFKGKF FYCTDESKEL
     ERDCRGQYLD YEKEEVEAQP RQWKKYDFHY DNVLWALLTL FTVSTGEGWP MVLKHSVDAT
     YEEQGPSPGF RMELSIFYVV YFVVFPFFFV NIFVALIIIT FQEQGDKVMS ECSLEKNERA
     CIDFAISAKP LTRYMPQNKQ SFQYKTWTFV VSPPFEYFIM AMIALNTVVL MMKFYDAPYE
     YELMLKCLNI VFTSMFSLEC ILKIIAFGVL NYFRDAWNVF DFVTVLGSIT DILVTEIANN
     FINLSFLRLF RAARLIKLCR QGYTIRILLW TFVQSFKALP YVCLLIAMLF FIYAIIGMQV
     FGNIALDDGT SINRHNNFRT FLQALMLLFR SATGEAWHEI MLSCLGNRAC DPHANASECG
     SDFAYFYFVS FIFLCSFLML NLFVAVIMDN FEYLTRDSSI LGPHHLDEFI RVWAEYDPAA
     CGRISYNDMF EMLKHMSPPL GLGKKCPARV AYKRLVRMNM PISNEDMTVH FTSTLMALIR
     TALEIKLAPA GTKQHQCDAE LRKEISSVWA NLPQKTLDLL VPPHKPDEMT VGKVYAALMI
     FDFYKQNKTT RDQTHQAPGG LSQMGPVSLF HPLKATLEQT QPAVLRGARV FLRQKSATSL
     SNGGAIQTQE SGIKESLSWG TQRTQDVLYE ARAPLERGHS AEIPVGQPGA LAVDVQMQNM
     TLRGPDGEPQ PGLESQGRAA SMPRLAAETQ PAPNASPMKR SISTLAPRPH GTQLCNTVLD
     RPPPSQVSHH HHHRCHRRRD KKQRSLEKGP SLSVDTEGAP STAAGSGLPH GEGSTGCRRE
     RKQERGRSQE RRQPSSSSSE KQRFYSCDRF GSREPPQPKP SLSSHPISPT AALEPGPHPQ
     GSGSVNGSPL MSTSGASTPG RGGRRQLPQT PLTPRPSITY KTANSSPVHF AEGQSGLPAF
     SPGRLSRGLS EHNALLQKEP LSQPLASGSR IGSDPYLGQR LDSEASAHNL PEDTLTFEEA
     VATNSGRSSR TSYVSSLTSQ SHPLRRVPNG YHCTLGLSTG VRARHSYHHP DQDHWC
 
 
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