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Database: UniProt
Entry: CAC1A_MOUSE
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Original site: CAC1A_MOUSE 
ID   CAC1A_MOUSE             Reviewed;        2368 AA.
AC   P97445; Q2TPN3;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   25-OCT-2017, entry version 167.
DE   RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha-1A;
DE   AltName: Full=Brain calcium channel I;
DE            Short=BI;
DE   AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 4;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.1;
GN   Name=Cacna1a; Synonyms=Caca1a, Cach4, Cacn3, Cacnl1a4, Ccha1a;
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=Swiss Webster; TISSUE=Brain;
RA   Richards K.S., Swensen A.M., Lipscombe D.;
RT   "Molecular identity of P-type calcium current in Purkinje neurons.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 49-2212, AND VARIANT TG LEU-649.
RC   STRAIN=DBA/2J;
RX   PubMed=8929530; DOI=10.1016/S0092-8674(00)81381-1;
RA   Fletcher C.F., Lutz C.M., O'Sullivan T.N., Shaughnessy J.D. Jr.,
RA   Hawkes R., Frankel W.N., Copeland N.G., Jenkins N.A.;
RT   "Absence epilepsy in tottering mutant mice is associated with calcium
RT   channel defects.";
RL   Cell 87:607-617(1996).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-792, 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   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-450; SER-453;
RP   SER-752; SER-755; SER-1038; SER-1042; SER-1051; THR-1935; SER-2016 AND
RP   SER-2071, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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).
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-1A
CC       gives rise to P and/or Q-type calcium currents. P/Q-type calcium
CC       channels belong to the 'high-voltage activated' (HVA) group and
CC       are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-
CC       IVA (omega-Aga-IVA). They are however insensitive to
CC       dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).
CC       {ECO:0000250|UniProtKB:O00555}.
CC   -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit
CC       complexes, consisting of alpha-1, alpha-2, beta and delta subunits
CC       in a 1:1:1:1 ratio. The channel activity is directed by the pore-
CC       forming and voltage-sensitive alpha-1 subunit. In many cases, this
CC       subunit is sufficient to generate voltage-sensitive calcium
CC       channel activity. The auxiliary subunits beta and alpha-2/delta
CC       linked by a disulfide bridge regulate the channel activity.
CC       Interacts with CABP1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:O00555}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Brain specific; mainly found in the
CC       cerebellum, olfactory bulb, cerebral cortex, hippocampus, and
CC       inferior colliculus. In the hippocampus, expression occurs in
CC       pyramidal and granule neurons, as well as in interneurons.
CC       Purkinje cells contain predominantly P-type VSCC, the Q-type being
CC       a prominent calcium current in cerebellar granule cells.
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   -!- DISEASE: Note=Defects in Cacna1a are the cause of a delayed-onset,
CC       recessive neurological disorder seen in tottering (tg) mutants,
CC       resulting in ataxia, motor seizures and behavioral absence
CC       seizures resembling petit mal epilepsy (or absence epilepsy) in
CC       humans. There are two more alleles, leaner (tg(lA)), that is
CC       characterized by severe ataxia and frequent death past weaning,
CC       but no motor seizures; and rolling Nagoya (tg(rol)), that presents
CC       an intermediary phenotype, the ataxia being somewhat more severe
CC       that with tg, but without motors seizures. Selective degeneration
CC       of cerebellar Purkinje cells has been shown for all these types of
CC       mutants. Selective degeneration of cerebellar Purkinje cells has
CC       been shown for all these types of mutants.
CC       {ECO:0000269|PubMed:8929530}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. CACNA1A subfamily. {ECO:0000305}.
DR   EMBL; AY714490; AAW56205.1; -; mRNA.
DR   EMBL; U76716; AAC52940.1; -; mRNA.
DR   CCDS; CCDS52618.1; -.
DR   RefSeq; NP_031604.3; NM_007578.3.
DR   UniGene; Mm.334658; -.
DR   ProteinModelPortal; P97445; -.
DR   BioGrid; 198430; 4.
DR   IntAct; P97445; 1.
DR   MINT; MINT-4997013; -.
DR   STRING; 10090.ENSMUSP00000112436; -.
DR   iPTMnet; P97445; -.
DR   PhosphoSitePlus; P97445; -.
DR   EPD; P97445; -.
DR   MaxQB; P97445; -.
DR   PaxDb; P97445; -.
DR   PeptideAtlas; P97445; -.
DR   PRIDE; P97445; -.
DR   Ensembl; ENSMUST00000121390; ENSMUSP00000112436; ENSMUSG00000034656.
DR   GeneID; 12286; -.
DR   KEGG; mmu:12286; -.
DR   UCSC; uc009mmn.2; mouse.
DR   CTD; 773; -.
DR   MGI; MGI:109482; Cacna1a.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   HOGENOM; HOG000231530; -.
DR   HOVERGEN; HBG050763; -.
DR   InParanoid; P97445; -.
DR   KO; K04344; -.
DR   OMA; EKDCRGK; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   PhylomeDB; P97445; -.
DR   TreeFam; TF312805; -.
DR   Reactome; R-MMU-112308; Presynaptic depolarization and calcium channel opening.
DR   Reactome; R-MMU-422356; Regulation of insulin secretion.
DR   ChiTaRS; Cacna1a; mouse.
DR   PRO; PR:P97445; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000034656; -.
DR   ExpressionAtlas; P97445; baseline and differential.
DR   Genevisible; P97445; MM.
DR   GO; GO:0042995; C:cell projection; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IMP:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR   GO; GO:0017156; P:calcium ion regulated exocytosis; IMP:MGI.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IMP:MGI.
DR   GO; GO:0008219; P:cell death; ISO:MGI.
DR   GO; GO:0016049; P:cell growth; IMP:MGI.
DR   GO; GO:0030644; P:cellular chloride ion homeostasis; IMP:MGI.
DR   GO; GO:0021953; P:central nervous system neuron differentiation; IMP:MGI.
DR   GO; GO:0021679; P:cerebellar molecular layer development; IMP:MGI.
DR   GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:MGI.
DR   GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:MGI.
DR   GO; GO:0021590; P:cerebellum maturation; IMP:MGI.
DR   GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR   GO; GO:0014051; P:gamma-aminobutyric acid secretion; IMP:MGI.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IMP:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0051899; P:membrane depolarization; IMP:MGI.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR   GO; GO:0050883; P:musculoskeletal movement, spinal reflex action; IMP:MGI.
DR   GO; GO:0032353; P:negative regulation of hormone biosynthetic process; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR   GO; GO:0050877; P:nervous system process; IMP:MGI.
DR   GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR   GO; GO:0007270; P:neuron-neuron synaptic transmission; IMP:MGI.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:MGI.
DR   GO; GO:0043113; P:receptor clustering; IMP:MGI.
DR   GO; GO:0014056; P:regulation of acetylcholine secretion, neurotransmission; IMP:MGI.
DR   GO; GO:0050770; P:regulation of axonogenesis; IMP:MGI.
DR   GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IDA:MGI.
DR   GO; GO:0010817; P:regulation of hormone levels; IMP:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR   GO; GO:0001505; P:regulation of neurotransmitter levels; IMP:MGI.
DR   GO; GO:0031335; P:regulation of sulfur amino acid metabolic process; IMP:MGI.
DR   GO; GO:0048265; P:response to pain; IMP:MGI.
DR   GO; GO:0060024; P:rhythmic synaptic transmission; IMP:MGI.
DR   GO; GO:0021522; P:spinal cord motor neuron differentiation; IMP:MGI.
DR   GO; GO:0007416; P:synapse assembly; IMP:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR   GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
DR   GO; GO:0021750; P:vestibular nucleus development; IMP:MGI.
DR   InterPro; IPR005448; CACNA1A.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01632; PQVDCCALPHA1.
DR   SMART; SM01062; Ca_chan_IQ; 1.
PE   1: Evidence at protein level;
KW   Calcium; Calcium channel; Calcium transport; Cell membrane;
KW   Complete proteome; Disease mutation; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW   Transport; Voltage-gated channel.
FT   CHAIN         1   2368       Voltage-dependent P/Q-type calcium
FT                                channel subunit alpha-1A.
FT                                /FTId=PRO_0000053917.
FT   TOPO_DOM      1    100       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    101    119       Helical; Name=S1 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    120    138       Extracellular. {ECO:0000255}.
FT   TRANSMEM    139    156       Helical; Name=S2 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    157    168       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    169    184       Helical; Name=S3 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    185    192       Extracellular. {ECO:0000255}.
FT   TRANSMEM    193    211       Helical; Name=S4 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    212    230       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    231    250       Helical; Name=S5 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    251    337       Extracellular. {ECO:0000255}.
FT   TRANSMEM    338    362       Helical; Name=S6 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    363    489       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    490    509       Helical; Name=S1 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    510    523       Extracellular. {ECO:0000255}.
FT   TRANSMEM    524    543       Helical; Name=S2 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    544    551       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    552    570       Helical; Name=S3 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    571    580       Extracellular. {ECO:0000255}.
FT   TRANSMEM    581    599       Helical; Name=S4 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    600    618       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    619    638       Helical; Name=S5 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    639    691       Extracellular. {ECO:0000255}.
FT   TRANSMEM    692    716       Helical; Name=S6 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    717   1190       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1191   1214       Helical; Name=S1 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1215   1231       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1232   1251       Helical; Name=S2 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1252   1258       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1259   1282       Helical; Name=S3 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1283   1293       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1294   1311       Helical; Name=S4 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1312   1330       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1331   1350       Helical; Name=S5 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1351   1437       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1438   1462       Helical; Name=S6 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1463   1518       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1519   1537       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1538   1551       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1552   1573       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1574   1580       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1581   1600       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1601   1607       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1608   1626       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1627   1645       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1646   1665       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1666   1737       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1738   1763       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1764   2368       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       65    365       I.
FT   REPEAT      475    719       II.
FT   REPEAT     1182   1465       III.
FT   REPEAT     1502   1765       IV.
FT   CA_BIND    1791   1802       {ECO:0000250}.
FT   REGION      385    402       Binding to the beta subunit.
FT                                {ECO:0000250}.
FT   COMPBIAS    729    734       Poly-Glu.
FT   COMPBIAS   1155   1158       Poly-Glu.
FT   SITE        320    320       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE        670    670       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1411   1411       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1600   1600       Binds to omega-Aga-IVA. {ECO:0000250}.
FT   SITE       1707   1707       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   MOD_RES     411    411       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     450    450       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     453    453       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     752    752       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     755    755       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     792    792       Phosphoserine.
FT                                {ECO:0000244|PubMed:16452087}.
FT   MOD_RES    1038   1038       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1042   1042       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1051   1051       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1935   1935       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1998   1998       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P54282}.
FT   MOD_RES    2016   2016       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    2028   2028       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P54282}.
FT   MOD_RES    2030   2030       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P54282}.
FT   MOD_RES    2071   2071       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    2091   2091       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P54282}.
FT   CARBOHYD    285    285       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1607   1607       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VARIANT     649    649       P -> L (in tg).
FT                                {ECO:0000269|PubMed:8929530}.
FT   CONFLICT     79     79       S -> P (in Ref. 2; AAC52940).
FT                                {ECO:0000305}.
FT   CONFLICT     82     82       L -> F (in Ref. 2; AAC52940).
FT                                {ECO:0000305}.
FT   CONFLICT    884    884       P -> L (in Ref. 2; AAC52940).
FT                                {ECO:0000305}.
FT   CONFLICT    888    888       E -> D (in Ref. 1; AAW56205).
FT                                {ECO:0000305}.
FT   CONFLICT   1083   1083       N -> D (in Ref. 2; AAC52940).
FT                                {ECO:0000305}.
FT   CONFLICT   1349   1349       L -> F (in Ref. 2; AAC52940).
FT                                {ECO:0000305}.
FT   CONFLICT   1373   1373       L -> F (in Ref. 2; AAC52940).
FT                                {ECO:0000305}.
FT   CONFLICT   2161   2161       P -> PH (in Ref. 1; AAW56205).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2368 AA;  267647 MW;  E7B573BA005E5CB1 CRC64;
     MARFGDEMPG RYGAGGGGSG PAAGVVVGAA GGRGAGGSRQ GGQPGAQRMY KQSMAQRART
     MALYNPIPVR QNCLTVNRSL FLFSEDNVVR KYAKKITEWP PFEYMILATI IANCIVLALE
     QHLPDDDKTP MSERLDDTEP YFIGIFCFEA GIKIVALGFA FHKGSYLRNG WNVMDFVVVL
     TGILATVGTE FDLRTLRAVR VLRPLKLVSG IPSLQVVLKS IMKAMIPLLQ IGLLLFFAIL
     IFAIIGLEFY MGKFHTTCFE EGTDDIQGES PAPCGTEEPA RTCPNGTKCQ PYWEGPNNGI
     TQFDNILFAV LTVFQCITME GWTDLLYNSN DASGNTWNWL YFIPLIIIGS FFMLNLVLGV
     LSGEFAKERE RVENRRAFLK LRRQQQIERE LNGYMEWISK AEEVILAEDE TDVEQRHPFD
     GALRRATLKK SKTDLLNPEE AEDQLADIAS VGSPFARASI KSAKLENSTF FHKKERRMRF
     YIRRMVKTQA FYWTVLSLVA LNTLCVAIVH YNQPEWLSDF LYYAEFIFLG LFMSEMFIKM
     YGLGTRPYFH SSFNCFDCGV IIGSIFEVIW AVIKPGTSFG ISVLRALRLL RIFKVTKYWA
     SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFDEGTPP TNFDTFPAAI
     MTVFQILTGE DWNEVMYDGI KSQGGVQGGM VFSIYFIVLT LFGNYTLLNV FLAIAVDNLA
     NAQELTKDEQ EEEEAANQKL ALQKAKEVAE VSPLSAANMS IAVKEQQKNQ KPTKSVWEQR
     TSEMRKQNLL ASREALYGDA AERWPTPYAR PLRPDVKTHL DRPLVVDPQE NRNNNTNKSR
     APEALRPTAR PRESARDPDA RRAWPGSPER APGREGPYGR ESEPQQREHA PPREHAPWDA
     DTERAKAGDA PRRHTHRPVA EGEPRRHRAR RRPGDEPDDR PERRPRPRDA TRPARAADGE
     GDDGERKRRH RHGPPAHDDR ERRHRRRKEN QGSGVPVSGP NLSTTRPIQQ DLGRQDLPLA
     EDLDNMKNNK LATGEPASPH DSLGHSGLPP SPAKIGNSTN PGPALATNPQ NAASRRTPNN
     PGNPSNPGPP KTPENSLIVT NPSSTQPNSA KTARKPEHMA VEIPPACPPL NHTVVQVNKN
     ANPDPLPKKE EEKKEEEEAD PGEDGPKPMP PYSSMFILST TNPLRRLCHY ILNLRYFEMC
     ILMVIAMSSI ALAAEDPVQP NAPRNNVLRY FDYVFTGVFT FEMVIKMIDL GLVLHQGAYF
     RDLWNILDFI VVSGALVAFA FTGNSKGKDI NTIKSLRVLR VLRPLKTIKR LPKLKAVFDC
     VVNSLKNVFN ILIVYMLFMF IFAVVAVQLF KGKFFHCTDE SKEFERDCRG KYLLYEKNEV
     KARDREWKKY EFHYDNVLWA LLTLFTVSTG EGWPQVLKHS VDATFENQGP SPGYRMEMSI
     FYVVYFVVFP FFFVNIFVAL IIITFQEQGD KMMEEYSLEK NERACIDFAI SAKPLTRHMP
     QNKQSFQYRM WQFVVSPPFE YTIMAMIALN TIVLMMKFYG ASVAYENALR VFNIVFTSLF
     SLECVLKVMA FGILNYFRDA WNIFDFVTVL GSITDILVTE FGNNFINLSF LRLFRAARLI
     KLLRQGYTIR ILLWTFVQSF KALPYVCLLI AMLFFIYAII GMQVFGNIGI DGEDEDSDED
     EFQITEHNNF RTFFQALMLL FRSATGEAWH NIMLSCLSGK PCDKNSGILT ADCGNEFAYF
     YFVSFIFLCS FLMLNLFVAV IMDNFEYLTR DSSILGPHHL DEYVRVWAEY DPAACGRIHY
     KDMYSLLRVI SPPLGLGKKC PHRVACKRLL RMDLPVADDN TVHFNSTLMA LIRTALDIKI
     AKGGADKQQM DAELRKEMMA IWPNLSQKTL DLLVTPHKST DLTVGKIYAA MMIMEYYRQS
     KAKKLQAMRE EQNRTPLMFQ RMEPPSPTQE GGPSQNALPS TQLDPGGGLM AHEGGMKESP
     SWVTQRAQEM FQKTGTWSPE RGPPIDMPNS QPNSQSVEMR EMGTDGYSDS EHYLPMEGQT
     RAASMPRLPA ENQRRRGRPR GNDLSTISDT SPMKRSASVL GPKARRLDDY SLERVPPEEN
     QRYHQRRRDR GHRTSERSLG RYTDVDTGLG TDLSMTTQSG DLPSKDRDQD RGRPKDRKHR
     PHHHHHHHHH HPPAPDRDRY AQERPDTGRA RAREQRWSRS PSEGREHTTH RQGSSSVSGS
     PAPSTSGTST PRRGRRQLPQ TPCTPRPLVS YSPAPRRPAA RRMAGPAAPP GGSPRGCRRA
     PRWPAHAPEG PRPRGADYTE PDSPREPPGG AHDPAPRSPR TPRAAGCASP RHGRRLPNGY
     YAGHGAPRPR TARRGAHDAY SESEDDWC
//
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