NAC3_RAT
ID NAC3_RAT Reviewed; 927 AA.
AC P70549;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Sodium/calcium exchanger 3;
DE AltName: Full=Na(+)/Ca(2+)-exchange protein 3;
DE AltName: Full=Solute carrier family 8 member 3;
DE Flags: Precursor;
GN Name=Slc8a3; Synonyms=Ncx3 {ECO:0000303|PubMed:8798769};
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, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
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 [2]
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 [3]
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 [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=21959935; DOI=10.1038/cdd.2011.125;
RA Boscia F., D'Avanzo C., Pannaccione A., Secondo A., Casamassa A.,
RA Formisano L., Guida N., Sokolow S., Herchuelz A., Annunziato L.;
RT "Silencing or knocking out the Na(+)/Ca(2+) exchanger-3 (NCX3) impairs
RT oligodendrocyte differentiation.";
RL Cell Death Differ. 19:562-572(2012).
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:8798769, PubMed:9486131). Contributes to cellular
CC Ca(2+) homeostasis in excitable cells, both in muscle and in brain. In
CC a first phase, voltage-gated channels mediate the rapid increase of
CC cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the
CC endoplasmic reticulum. SLC8A3 mediates the export of Ca(2+) from the
CC cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly
CC return to baseline. Contributes to Ca(2+) transport during excitation-
CC contraction coupling in muscle. In neurons, contributes to the rapid
CC decrease of cytoplasmic Ca(2+) levels back to baseline after neuronal
CC activation, and thereby contributes to modulate synaptic plasticity,
CC learning and memory. Required for normal oligodendrocyte
CC differentiation and for normal myelination. Mediates Ca(2+) efflux from
CC mitochondria and contributes to mitochondrial Ca(2+) ion homeostasis.
CC {ECO:0000250|UniProtKB:S4R2P9, ECO:0000269|PubMed:8798769,
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:0000305|PubMed:8798769, ECO:0000305|PubMed:9486131};
CC -!- ACTIVITY REGULATION: Calcium transport is down-regulated by Na(+) and
CC stimulated by Ca(2+). {ECO:0000269|PubMed:9486131}.
CC -!- SUBUNIT: Interacts with AKAP1. {ECO:0000250|UniProtKB:S4R2P9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16914199,
CC ECO:0000269|PubMed:8798769, ECO:0000269|PubMed:9486131}; Multi-pass
CC membrane protein {ECO:0000305}. Perikaryon
CC {ECO:0000269|PubMed:16914199}. Cell projection, dendrite
CC {ECO:0000269|PubMed:16914199}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:16914199}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:S4R2P9}. Cytoplasm, sarcoplasm
CC {ECO:0000250|UniProtKB:S4R2P9}. Cell junction
CC {ECO:0000250|UniProtKB:S4R2P9}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:16914199}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:S4R2P9}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16914199}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:S4R2P9}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P57103}. Note=Detected at neuromuscular
CC junctions. {ECO:0000250|UniProtKB:S4R2P9}.
CC -!- TISSUE SPECIFICITY: Detected in neurons in brain cortex and
CC hippocampus. Detected in pyramidal cell bodies and processes, in
CC granule cells and interneurons in the CA1 and CA3 region of the
CC hippocampus. Detected on astrocyte processes in brain cortex. Detected
CC on endothelial cells in hippocampus capillaries (at protein level)
CC (PubMed:16914199). Restricted to brain and skeletal muscle
CC (PubMed:8798769). {ECO:0000269|PubMed:16914199,
CC ECO:0000269|PubMed:8798769}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during in vitro differentiation of
CC oligodendrocytes (at protein level). {ECO:0000269|PubMed:21959935}.
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; U53420; AAC52817.1; -; mRNA.
DR RefSeq; NP_511175.1; NM_078620.2.
DR RefSeq; XP_017449476.1; XM_017593987.1.
DR RefSeq; XP_017449477.1; XM_017593988.1.
DR RefSeq; XP_017449478.1; XM_017593989.1.
DR RefSeq; XP_017449479.1; XM_017593990.1.
DR RefSeq; XP_017449480.1; XM_017593991.1.
DR AlphaFoldDB; P70549; -.
DR SMR; P70549; -.
DR IntAct; P70549; 1.
DR MINT; P70549; -.
DR STRING; 10116.ENSRNOP00000041987; -.
DR GlyGen; P70549; 2 sites.
DR PaxDb; P70549; -.
DR PRIDE; P70549; -.
DR Ensembl; ENSRNOT00000102013; ENSRNOP00000093954; ENSRNOG00000029871.
DR GeneID; 140448; -.
DR KEGG; rno:140448; -.
DR UCSC; RGD:620197; rat.
DR CTD; 6547; -.
DR RGD; 620197; Slc8a3.
DR eggNOG; KOG1306; Eukaryota.
DR GeneTree; ENSGT00940000157547; -.
DR HOGENOM; CLU_012872_1_0_1; -.
DR InParanoid; P70549; -.
DR OMA; VEMANYH; -.
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:P70549; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000029871; Expressed in quadriceps femoris and 9 other tissues.
DR Genevisible; P70549; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0043679; C:axon terminus; ISO:RGD.
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:SynGO.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
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:0031226; C:intrinsic component of plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IDA:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0016528; C:sarcoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0015368; F:calcium:cation antiporter 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:0099580; F:ion antiporter activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IGI: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:0071320; P:cellular response to cAMP; IDA:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; 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; ISO:RGD.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0048709; P:oligodendrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0014819; P:regulation of skeletal muscle contraction; ISS:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:RGD.
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 junction;
KW Cell membrane; Cell projection; Cytoplasm; Endoplasmic reticulum;
KW Glycoprotein; Ion transport; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Repeat; Signal; Sodium;
KW Sodium transport; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..927
FT /note="Sodium/calcium exchanger 3"
FT /id="PRO_0000019385"
FT TOPO_DOM 31..73
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..726
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 727..747
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 748..754
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 755..775
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 776..778
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 800..828
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 829..849
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 850..860
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 861..881
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 882..903
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 904..924
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 925..927
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 140..180
FT /note="Alpha-1"
FT DOMAIN 386..485
FT /note="Calx-beta 1"
FT DOMAIN 519..619
FT /note="Calx-beta 2"
FT REPEAT 796..832
FT /note="Alpha-2"
FT REGION 253..272
FT /note="Putative calmodulin-binding region"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
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 475
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 475
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 475
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 478
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 525
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 526
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 527
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 527
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 543
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 579
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 606
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 607
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 607
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 672
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 823
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 927 AA; 103163 MW; EAB35F9620DBE69E CRC64;
MAWLRLQPLT SAFLHFGLVT FVLFLNGLRA EAGDLRDVPS AGQNNESCSG SSDCKEGVIL
PIWYPENPSL GDKIARVIVY FVALIYMFLG VSIIADRFMA SIEVITSQER EVTIKKPNGE
TSTTTIRVWN ETVSNLTLMA LGSSAPEILL SLIEVCGHGF IAGDLGPSTI VGSAAFNMFI
IIGICVYVIP DGETRKIKHL RVFFVTAAWS VFAYIWLYMI LAVFSPGVVQ VWEGLLTLFF
FPVCVLLAWV ADKRLLFYKY MHKRYRTDKH RGIIIETEGE HPKGIEMDGK MMNSHFLDGN
LIPLEGKEVD ESRREMIRIL KDLKQKHPEK DLDQLVEMAN YYALSHQQKS RAFYRIQATR
MMTGAGNILK KHAAEQAKKT ASMSEVHTDE PEDFASKVFF DPCSYQCLEN CGAVLLTVVR
KGGDISKTMY VDYKTEDGSA NAGADYEFTE GTVVLKPGET QKEFSVGIID DDIFEEDEHF
FVRLSNVRVE EEQLEEGMTP AILNSLPLPR AVLASPCVAT VTILDDDHAG IFTFECDTIH
VSESIGVMEV KVLRTSGARG TVIVPFRTVE GTAKGGGEDF EDTYGELEFK NDETVKTIRV
KIVDEEEYER QENFFIALGE PKWMERGISA LLLSPEVTDR KLTMEEEEAK RIAEMGKPVL
GEHPKLEVII EESYEFKSTV DKLIKKTNLA LVVGTHSWRD QFMEAITVSA AGDEEEDESG
EERLPSCFDY VMHFLTVFWK VLFACVPPTE YCHGWACFVV SILIIGMLTA IIGDLASHFG
CTIGLKDSVT AVVFVAFGTS VPDTFASKAA ALQDVYADAS IGNVTGSNAV NVFLGIGLAW
SVAAIYWAMQ GQEFHVSAGT LAFSVTLFTI FAFVCLSVLL YRRRPHLGGE LGGPRGCKLA
TTWLFVSLWL LYVLFATLEA YCYIKGF
