NAC2_RAT
ID NAC2_RAT Reviewed; 921 AA.
AC P48768;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Sodium/calcium exchanger 2;
DE AltName: Full=Na(+)/Ca(2+)-exchange protein 2;
DE AltName: Full=Solute carrier family 8 member 2;
DE Flags: Precursor;
GN Name=Slc8a2; Synonyms=Ncx2;
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, SUBCELLULAR LOCATION, ACTIVITY
RP REGULATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain stem;
RX PubMed=8021246; DOI=10.1016/s0021-9258(17)32458-4;
RA Li Z., Matsuoka S., Hryshko L.V., Nicoll D.A., Bershon M.M., Burke E.P.,
RA Lifton R.P., Philipson K.D.;
RT "Cloning of the NCX2 isoform of the plasma membrane Na(+)-Ca2+ exchanger.";
RL J. Biol. Chem. 269:17434-17439(1994).
RN [2]
RP TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=8798769; DOI=10.1074/jbc.271.40.24914;
RA Nicoll D.A., Quednau B.D., Qui Z., Xia Y.-R., Lusis A.J., Philipson K.D.;
RT "Cloning of a third mammalian Na+-Ca2+ exchanger, NCX3.";
RL J. Biol. Chem. 271:24914-24921(1996).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=9486131; DOI=10.1152/ajpcell.1998.274.2.c415;
RA Linck B., Qiu Z., He Z., Tong Q., Hilgemann D.W., Philipson K.D.;
RT "Functional comparison of the three isoforms of the Na+/Ca2+ exchanger
RT (NCX1, NCX2, NCX3).";
RL Am. J. Physiol. 274:C415-C423(1998).
RN [4]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16914199; DOI=10.1016/j.ceca.2006.06.004;
RA Minelli A., Castaldo P., Gobbi P., Salucci S., Magi S., Amoroso S.;
RT "Cellular and subcellular localization of Na+-Ca2+ exchanger protein
RT isoforms, NCX1, NCX2, and NCX3 in cerebral cortex and hippocampus of adult
RT rat.";
RL Cell Calcium 41:221-234(2007).
RN [5]
RP REVIEW.
RX PubMed=23506867; DOI=10.1016/j.mam.2012.07.003;
RA Khananshvili D.;
RT "The SLC8 gene family of sodium-calcium exchangers (NCX) - structure,
RT function, and regulation in health and disease.";
RL Mol. Aspects Med. 34:220-235(2013).
CC -!- FUNCTION: Mediates the electrogenic exchange of Ca(2+) against Na(+)
CC ions across the cell membrane, and thereby contributes to the
CC regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular
CC processes (PubMed:8021246, PubMed:9486131). Contributes to cellular
CC Ca(2+) homeostasis in excitable cells (By similarity). Contributes to
CC the rapid decrease of cytoplasmic Ca(2+) levels back to baseline after
CC neuronal activation, and thereby contributes to modulate synaptic
CC plasticity, learning and memory (By similarity). Plays a role in
CC regulating urinary Ca(2+) and Na(+) excretion (By similarity).
CC {ECO:0000250|UniProtKB:Q8K596, ECO:0000269|PubMed:8021246,
CC ECO:0000269|PubMed:9486131}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:69955, ChEBI:CHEBI:29101, ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:9486131};
CC -!- ACTIVITY REGULATION: Calcium transport is down-regulated by Na(+) and
CC stimulated by Ca(2+). {ECO:0000269|PubMed:8021246,
CC ECO:0000269|PubMed:9486131}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16914199,
CC ECO:0000269|PubMed:8021246, ECO:0000269|PubMed:9486131}; Multi-pass
CC membrane protein {ECO:0000305}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q8K596}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8K596}. Perikaryon
CC {ECO:0000269|PubMed:16914199}. Cell projection, dendrite
CC {ECO:0000269|PubMed:16914199}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:16914199}.
CC -!- TISSUE SPECIFICITY: Detected in neocortex and hippocampus on pyramidal
CC cells, astrocyte processes and dendrites (at protein level)
CC (PubMed:16914199). Brain and skeletal muscle.
CC {ECO:0000269|PubMed:8021246, ECO:0000269|PubMed:8798769}.
CC -!- DOMAIN: The cytoplasmic Calx-beta domains bind the regulatory Ca(2+).
CC The first Calx-beta domain can bind up to four Ca(2+) ions. The second
CC domain can bind another two Ca(2+) ions that are essential for calcium-
CC regulated ion exchange. {ECO:0000250|UniProtKB:P23685}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. SLC8 subfamily. {ECO:0000305}.
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DR EMBL; U08141; AAA19920.1; -; mRNA.
DR PIR; A54139; A54139.
DR RefSeq; NP_511174.1; NM_078619.1.
DR AlphaFoldDB; P48768; -.
DR SMR; P48768; -.
DR BioGRID; 250785; 2.
DR IntAct; P48768; 2.
DR MINT; P48768; -.
DR STRING; 10116.ENSRNOP00000042012; -.
DR GuidetoPHARMACOLOGY; 946; -.
DR GlyGen; P48768; 2 sites.
DR iPTMnet; P48768; -.
DR SwissPalm; P48768; -.
DR PaxDb; P48768; -.
DR PRIDE; P48768; -.
DR GeneID; 140447; -.
DR KEGG; rno:140447; -.
DR UCSC; RGD:620194; rat.
DR CTD; 6543; -.
DR RGD; 620194; Slc8a2.
DR eggNOG; KOG1306; Eukaryota.
DR InParanoid; P48768; -.
DR OrthoDB; 490546at2759; -.
DR Reactome; R-RNO-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-RNO-425561; Sodium/Calcium exchangers.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR PRO; PR:P48768; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0043679; C:axon terminus; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:ARUK-UCL.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0015085; F:calcium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:1905060; F:calcium:cation antiporter activity involved in regulation of postsynaptic cytosolic calcium ion concentration; IMP:SynGO.
DR GO; GO:0005432; F:calcium:sodium antiporter activity; IDA:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0015491; F:cation:cation antiporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:1990034; P:calcium ion export across plasma membrane; IDA:RGD.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IDA:RGD.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0060402; P:calcium ion transport into cytosol; IDA:RGD.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:ARUK-UCL.
DR GO; GO:0050890; P:cognition; ISO:RGD.
DR GO; GO:0007612; P:learning; ISS:UniProtKB.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; ISS:UniProtKB.
DR GO; GO:0030001; P:metal ion transport; IBA:GO_Central.
DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0070050; P:neuron cellular homeostasis; ISO:RGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0099608; P:regulation of action potential firing pattern; ISO:RGD.
DR GO; GO:0106056; P:regulation of calcineurin-mediated signaling; ISO:RGD.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; ISO:RGD.
DR GO; GO:0033280; P:response to vitamin D; IEP:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0006814; P:sodium ion transport; IDA:RGD.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR GO; GO:0021537; P:telencephalon development; IEP:RGD.
DR Gene3D; 1.20.1420.30; -; 2.
DR Gene3D; 2.60.40.2030; -; 2.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR004836; Na_Ca_Ex.
DR InterPro; IPR032452; Na_Ca_Ex_C-exten.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR Pfam; PF03160; Calx-beta; 2.
DR Pfam; PF01699; Na_Ca_ex; 2.
DR Pfam; PF16494; Na_Ca_ex_C; 1.
DR PRINTS; PR01259; NACAEXCHNGR.
DR SMART; SM00237; Calx_beta; 2.
DR SUPFAM; SSF141072; SSF141072; 2.
DR TIGRFAMs; TIGR00845; caca; 1.
PE 1: Evidence at protein level;
KW Antiport; Calcium; Calcium transport; Calmodulin-binding; Cell membrane;
KW Cell projection; Glycoprotein; Ion transport; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Sodium;
KW Sodium transport; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..921
FT /note="Sodium/calcium exchanger 2"
FT /id="PRO_0000019383"
FT TOPO_DOM 21..68
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..164
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..222
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..720
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 721..740
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 741..747
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 748..770
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 771..772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..791
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 792..822
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 823..843
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 844..854
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 855..875
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 876..892
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 893..909
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 910..921
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 135..175
FT /note="Alpha-1"
FT DOMAIN 384..483
FT /note="Calx-beta 1"
FT DOMAIN 512..612
FT /note="Calx-beta 2"
FT REPEAT 790..826
FT /note="Alpha-2"
FT REGION 23..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..267
FT /note="Putative calmodulin-binding region"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT REGION 372..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 518
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 520
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 520
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 536
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 598
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 598
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 599
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 600
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 600
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 665
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K596"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 921 AA; 100523 MW; 0CDB26BEACBCF6B1 CRC64;
MAPLALVGVA LLLGAPHCLG EATPTPSLPP PPANDSDASP GGCQGSYRCQ PGVLLPVWEP
DDPSLGDKAA RAVVYFVAMV YMFLGLSIIA DRFMASIEVI TSKEKEITIT KANGETSVGT
VRIWNETVSN LTLMALGSSA PEILLSVIEV CGHNFQAGEL GPGTIVGSAA FNMFVVIAVC
VYVIPAGESR KIKHLRVFFV TASWSIFAYV WLYLILAVFS PGVVQVWEAL LTLVFFPVCV
VFAWMADKRL LFYKYVYKRY RTDPRSGIII GAEGDPPKSI ELDGTFVGTE VPGELGALGT
GPAEARELDA SRREVIQILK DLKQKHPDKD LEQLVGIAKY YALLHQQKSR AFYRIQATRL
MTGAGNVLRR HAADAARRPG ANDGAPDDED DGASRIFFEP SLYHCLENCG SVLLSVACQG
GEGNSTFYVD YRTEDGSAKA GSDYEYSEGT LVFKPGETQK ELRIGIIDDD IFEEDEHFFV
RLLNLRVGDA QGMFEPDGGG RPKGRLVAPL LATVTILDDD HAGIFSFQDR LLHVSECMGT
VDVRVVRSSG ARGTVRLPYR TVDGTARGGG VHYEDACGEL EFGDDETMKT LQVKIVDDEE
YEKKDNFFIE LGQPQWLKRG ISALLLNQGD GDRKLTAEEE EAQRIAEMGK PVLGENCRLE
VIIEESYDFK NTVDKLIKKT NLALVIGTHS WREQFLEAVT VSAGDEEEDE DGSREERLPS
CFDYVMHFLT VFWKVLFACL PPTEYCHGWA CFGVCILVIG LLTALIGDLA SHFGCTVGLK
DSVNAVVFVA LGTSIPDTFA SKVAALQDQC ADASIGNVTG SNAVNVFLGL GVAWSVAAVY
WAVQGRPFEV RTGTLAFSVT LFTVFAFVGI AVLLYRRRPH IGGELGGPRG PKLATTALFL
GLWFLYILFA SLEAYCHIRG F
