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Database: UniProt
Entry: CAC1B_MOUSE
LinkDB: CAC1B_MOUSE
Original site: CAC1B_MOUSE 
ID   CAC1B_MOUSE             Reviewed;        2327 AA.
AC   O55017; Q60609;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-SEP-2017, entry version 170.
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, Cchn1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Hong T., Birnbaumer L.;
RT   "Nucleotide sequence polymorphism of mouse alpha1 B.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS NB1 AND NB2).
RC   TISSUE=Neuroblastoma;
RX   PubMed=8307146; DOI=10.1016/0014-5793(94)80105-3;
RA   Coppola T., Waldmann R., Borsotto M., Heurteaux C., Romey G.,
RA   Mattei M.-G., Lazdunski M.;
RT   "Molecular cloning of a murine N-type calcium channel alpha 1 subunit.
RT   Evidence for isoforms, brain distribution, and chromosomal
RT   localization.";
RL   FEBS Lett. 338:1-5(1994).
RN   [3]
RP   INTERACTION WITH RIMS1.
RC   TISSUE=Brain;
RX   PubMed=11438518; DOI=10.1074/jbc.M100929200;
RA   Coppola T., Magnin-Luethi S., Perret-Menoud V., Gattesco S.,
RA   Schiavo G., Regazzi R.;
RT   "Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-
RT   25, and synaptotagmin.";
RL   J. Biol. Chem. 276:32756-32762(2001).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-745; SER-748;
RP   SER-783; SER-1058; SER-2056; SER-2212; SER-2221 AND SER-2244, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-22, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.O113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [8]
RP   INTERACTION WITH FMR1.
RX   PubMed=24709664; DOI=10.1038/ncomms4628;
RA   Ferron L., Nieto-Rostro M., Cassidy J.S., Dolphin A.C.;
RT   "Fragile X mental retardation protein controls synaptic vesicle
RT   exocytosis by modulating N-type calcium channel density.";
RL   Nat. Commun. 5:3628-3628(2014).
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   -!- SUBUNIT: Multisubunit complex consisting of alpha-1, alpha-2, beta
CC       and delta subunits in a 1:1:1:1 ratio. The channel activity is
CC       directed by the pore-forming and voltage-sensitive alpha-1
CC       subunit. In many cases, this subunit is sufficient to generate
CC       voltage-sensitive calcium channel activity. The auxiliary subunits
CC       beta and alpha-2/delta linked by a disulfide bridge regulate the
CC       channel activity. Interacts with RIMS1 (PubMed:11438518).
CC       Interacts with FMR1 (via C-terminus); this interaction induces a
CC       deacrease in the number of presynaptic functional CACNA1B channels
CC       at the cell surface (PubMed:24709664).
CC       {ECO:0000269|PubMed:11438518, ECO:0000269|PubMed:24709664}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=NB1;
CC         IsoId=O55017-1; Sequence=Displayed;
CC       Name=NB2;
CC         IsoId=O55017-2; Sequence=VSP_000883;
CC   -!- TISSUE SPECIFICITY: Widespread expression throughout the brain.
CC       Highest levels in pyramidal cell layers C1, C2 and C3 of the
CC       hippocampus, in the dentate gyrus, in the cortex layers 2 et 4, in
CC       the subiculum and the habenula.
CC   -!- DOMAIN: Each of the four internal repeats contains five
CC       hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
CC       positively charged transmembrane segment (S4). S4 segments
CC       probably represent the voltage-sensor and are characterized by a
CC       series of positively charged amino acids at every third position.
CC   -!- PTM: Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. CACNA1B subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB60437.1; Type=Frameshift; Positions=1924, 1934, 2121, 2127; Evidence={ECO:0000305};
DR   EMBL; AF042317; AAB97840.1; -; mRNA.
DR   EMBL; U04999; AAB60437.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS38065.1; -. [O55017-1]
DR   PIR; S41080; S41080.
DR   RefSeq; NP_001035993.1; NM_001042528.2. [O55017-1]
DR   UniGene; Mm.4424; -.
DR   ProteinModelPortal; O55017; -.
DR   BioGrid; 198431; 5.
DR   IntAct; O55017; 2.
DR   STRING; 10090.ENSMUSP00000037416; -.
DR   ChEMBL; CHEMBL3637936; -.
DR   TCDB; 1.A.1.11.9; the voltage-gated ion channel (vic) superfamily.
DR   iPTMnet; O55017; -.
DR   PhosphoSitePlus; O55017; -.
DR   MaxQB; O55017; -.
DR   PaxDb; O55017; -.
DR   PRIDE; O55017; -.
DR   Ensembl; ENSMUST00000041342; ENSMUSP00000037416; ENSMUSG00000004113. [O55017-1]
DR   GeneID; 12287; -.
DR   KEGG; mmu:12287; -.
DR   UCSC; uc008ipe.2; mouse. [O55017-1]
DR   CTD; 774; -.
DR   MGI; MGI:88296; Cacna1b.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   HOGENOM; HOG000231530; -.
DR   HOVERGEN; HBG050763; -.
DR   InParanoid; O55017; -.
DR   KO; K04849; -.
DR   TreeFam; TF312805; -.
DR   Reactome; R-MMU-112308; Presynaptic depolarization and calcium channel opening.
DR   PRO; PR:O55017; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000004113; -.
DR   ExpressionAtlas; O55017; baseline and differential.
DR   Genevisible; O55017; MM.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
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:MGI.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:MGI.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IMP:MGI.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR   GO; GO:0007269; P:neurotransmitter secretion; IMP:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0051924; P:regulation of calcium ion transport; IMP:MGI.
DR   GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR   GO; GO:0048265; P:response to pain; IMP:MGI.
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:SF246; PTHR10037:SF246; 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   Alternative splicing; ATP-binding; Calcium; Calcium channel;
KW   Calcium transport; Complete proteome; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Metal-binding; Methylation;
KW   Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1   2327       Voltage-dependent N-type calcium channel
FT                                subunit alpha-1B.
FT                                /FTId=PRO_0000053922.
FT   TOPO_DOM      1     95       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     96    114       Helical; Name=S1 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    115    133       Extracellular. {ECO:0000255}.
FT   TRANSMEM    134    151       Helical; Name=S2 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    152    164       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    165    179       Helical; Name=S3 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    180    186       Extracellular. {ECO:0000255}.
FT   TRANSMEM    187    205       Helical; Name=S4 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    206    225       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    226    245       Helical; Name=S5 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    246    331       Extracellular. {ECO:0000255}.
FT   TRANSMEM    332    356       Helical; Name=S6 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    357    482       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    483    502       Helical; Name=S1 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    503    516       Extracellular. {ECO:0000255}.
FT   TRANSMEM    517    536       Helical; Name=S2 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    537    544       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    545    563       Helical; Name=S3 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    564    574       Extracellular. {ECO:0000255}.
FT   TRANSMEM    575    592       Helical; Name=S4 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    593    611       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    612    631       Helical; Name=S5 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    632    684       Extracellular. {ECO:0000255}.
FT   TRANSMEM    685    709       Helical; Name=S6 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    710   1134       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1135   1158       Helical; Name=S1 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1159   1175       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1176   1195       Helical; Name=S2 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1196   1203       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1204   1226       Helical; Name=S3 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1227   1241       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1242   1256       Helical; Name=S4 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1257   1277       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1278   1297       Helical; Name=S5 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1298   1383       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1384   1408       Helical; Name=S6 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1409   1465       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1466   1484       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1485   1498       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1499   1518       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1519   1527       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1528   1546       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1547   1554       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1555   1573       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1574   1592       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1593   1612       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1613   1674       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1675   1694       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1695   2327       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       82    359       I.
FT   REPEAT      468    712       II.
FT   REPEAT     1126   1412       III.
FT   REPEAT     1449   1702       IV.
FT   DOMAIN     1715   1750       EF-hand. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   NP_BIND     451    458       ATP. {ECO:0000255}.
FT   CA_BIND    1728   1739       {ECO:0000255|PROSITE-ProRule:PRU00448}.
FT   REGION      379    396       Binding to the beta subunit.
FT                                {ECO:0000250}.
FT   COMPBIAS   2040   2044       Poly-His.
FT   COMPBIAS   2106   2110       Poly-Ser.
FT   SITE        314    314       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE        663    663       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1358   1358       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1646   1646       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   MOD_RES      22     22       Omega-N-methylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     411    411       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     745    745       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     748    748       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     783    783       Phosphoserine.
FT                                {ECO:0000244|PubMed:16452087,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1058   1058       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1710   1710       Phosphoserine; by PKA. {ECO:0000255}.
FT   MOD_RES    2056   2056       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    2212   2212       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    2221   2221       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    2244   2244       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CARBOHYD    256    256       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1554   1554       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1666   1666       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ     756    756       A -> AFVKQTRGTVSRSSSVSSVNSP (in isoform
FT                                NB2). {ECO:0000303|PubMed:8307146}.
FT                                /FTId=VSP_000883.
FT   VARIANT     414    414       D -> DA.
FT   CONFLICT    238    238       A -> G (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT    645    645       N -> I (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT    757    759       RQQ -> QE (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT    880    880       A -> P (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   1128   1128       L -> F (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   1173   1173       K -> E (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   1185   1185       F -> C (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   1227   1230       Missing (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   1388   1388       F -> L (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   1549   1549       A -> AET (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   1615   1615       I -> S (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   1636   1636       L -> I (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   1657   1657       G -> D (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   1802   1837       Missing (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   1942   1942       A -> G (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   1949   1949       G -> D (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   1963   1963       A -> L (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   1979   1979       E -> D (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   1994   1994       P -> L (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   2021   2021       H -> D (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   2075   2075       A -> AA (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   2141   2141       T -> A (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   2168   2168       S -> I (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   2309   2309       S -> N (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   2313   2313       R -> G (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
FT   CONFLICT   2316   2316       H -> A (in Ref. 2; AAB60437).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2327 AA;  261481 MW;  AD42CDD38482895A CRC64;
     MVRFGDELGG RYGGTGGGER ARGGGAGGAG GPGQGGLPPG QRVLYKQSIA QRARTMALYN
     PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD
     GDKTPMSERL DDTEPYFIGI FCFEAGIKII ALGFVFHKGS YLRNGWNVMD FVVVLTGILA
     TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII
     GLEFYMGKFH KACFPNSTDT EPVGDFPCGK DPPARQCDGD TECREYWPGP NFGITNFDNI
     LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA
     KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDKNAEEK SPLDVLKRAA
     TKKSRNDLIH AEEGEDRFVD LCAVGSPFAR ASLKSGKTES SSYFRRKEKM FRFFIRRMVK
     AQSFYWVVLC VVALNTLCVA MVHYNQPQRL TTALYFAEFV FLGLFLTEMS LKMYGLGPRS
     YFRSSFNCFD FGVIVGSIFE VVWAAIKPGT SFGISVLRAL RLLRIFKVTK YWNSLRNLVV
     SLLNSMKSII SLLFLLFLFI VVFALLGMQL FGGQFNFQDE TPTTNFDTFP AAILTVFQIL
     TGEDWNAVMY HGIESQGGVS KGMFSSFYFI VLTLFGNYTL LNVFLAIAVD NLANAQELTK
     DEEEMEEAAN QKLALQKAKE VAEVSPMSAA NISIAARQQN SAKARSVWEQ RASQLRLQNL
     RASCEALYSE MDPEERLRYA STRHVRPDMK THMDRPLVVE PGRDGLRGPV GSKSKPEGTE
     ATESADLPRR HHRHRDRDKT SATAPAGGEQ DRTESTETGA REERARPRRS HSKETPGADT
     QVRCERSRRH HRRGSPEEAT EREPRRHRAH RHAQDSSKEG TAPVLVPKGE RRARHRGPRT
     GPREAENNEE PTRRHRARHK VPPTLQPPER EAAEKESNAV EGDKETRNHQ PKEPHCDLEA
     IAVTGVGPLH MLPSTCLQKV DEQPEDADNQ RNVTRMGSQP SDPSTTVHVP VTLTGPPGET
     PVVPSGNMNL EGQAEGKKEA EADDVLRRGP RPIVPYSSMF CLSPTNLLRR FCHYIVTMRY
     FEMVILVVIA LSSIALAAED PVRTDSFRNN ALKYMDYIFT GVFTFEMVIK MIDLGLLLHP
     GAYFRDLWNI LDFIVVSGAL VAFAFSSFMG GSKGKDINTI KSLRVLRVLR PLKTIKRLPK
     LKAVFDCVVN SLKNVLNILI VYMLFMFIFA VIAVQLFKGK FFYCTDESKE LERDCRGQYL
     DYEKEEVEAQ PRQWKKYDFH YDNVLWALLT LFTVSTGEGW PMVLKHSVDA TYEEQGPSPG
     FRMELSIFYV VYFVVFPFFF VNIFVALIII TFQEQGDKVM SECSLEKNER ACIDFAISAK
     PLTRYMPQNK QSFQYKTWTF VVSPPFEYFI MAMIALNTVV LMMKFYDAPY EYELMLKCLN
     IVFTSMFSME CILKIIAFGV LNYFRDAWNV FDFVTVLGSI TDILVTEIAN NFINLSFLRL
     FRAARLIKLL RQGYTIRILL WTFVQSFKAL PYVCLLIAML FFIYAIIGMQ VFGNIALDDD
     TSINRHNNFR TFLQALMLLF RSATGEAWHE IMLSCLGNRA CDPHANASEC GSDFAYFYFV
     SFIFLCSFLM LNLFVAVIMD NFEYLTRDSS ILGPHHLDEF IRVWAEYDPA ACGRISYNDM
     FEMLKHMSPP LGLGKKCPAR VAYKRLVRMN MPISNEDMTV HFTSTLMALI RTALEIKLAP
     AGTKQHQCDA ELRKEISSVW ANLPQKTLDL LVPPHKPDEM TVGKVYAALM IFDFYKQNKT
     TRDQTHQAPG GLSQMGPVSL FHPLKATLEQ TQPAVLRGAR VFLRQKSATS LSNGGAIQTQ
     ESGIKESLSW GTQRTQDALY EARAPLERGH SAEIPVGQSG TLAVDVQMQN MTLRGPDGEP
     QPGLESQGRA ASMPRLAAET QPAPNASPMK RSISTLAPRP HGTQLCSTVL DRPPPSQASH
     HHHHRCHRRR DKKQRSLEKG PSLSVDPEGA PSTAAGPGLP HGEGSTACRR DRKQERGRSQ
     ERRQPSSSSS EKQRFYSCDR FGSREPPQLM PSLSSHPTSP TAALEPAPHP QGSGSVNGSP
     LMSTSGASTP GRGGRRQLPQ TPLTPRPSIT YKTANSSPVH FAEGQSGLPA FSPGRLSRGL
     SEHNALLQKE PLSQPLAPGS RIGSDPYLGQ RLDSEASAHT LPEDTLTFEE AVATNSGRSS
     RTSYVSSLTS QSHPLRRVPN GYHCTLGLST GVRARHSYHH PDQDHWC
//
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