AT2B3_RAT
ID AT2B3_RAT Reviewed; 1258 AA.
AC Q64568; Q01489; Q63444;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Plasma membrane calcium-transporting ATPase 3;
DE Short=PMCA3;
DE EC=7.2.2.10 {ECO:0000305|PubMed:25014339, ECO:0000305|PubMed:9880546};
DE AltName: Full=Plasma membrane calcium ATPase isoform 3;
DE AltName: Full=Plasma membrane calcium pump isoform 3;
GN Name=Atp2b3; Synonyms=Pmca3;
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] (ISOFORM ZA), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=2530223; DOI=10.1016/s0021-9258(18)51505-2;
RA Greeb J., Shull G.E.;
RT "Molecular cloning of a third isoform of the calmodulin-sensitive plasma
RT membrane Ca2+-transporting ATPase that is expressed predominantly in brain
RT and skeletal muscle.";
RL J. Biol. Chem. 264:18569-18576(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1016-1258 (ISOFORMS XF/ZF), AND ALTERNATIVE
RP SPLICING.
RC STRAIN=CD Charles River;
RX PubMed=1388171; DOI=10.1016/s0021-9258(18)41829-7;
RA Burk S.E., Shull G.E.;
RT "Structure of the rat plasma membrane Ca(2+)-ATPase isoform 3 gene and
RT characterization of alternative splicing and transcription products.
RT Skeletal muscle-specific splicing results in a plasma membrane Ca(2+)-
RT ATPase with a novel calmodulin-binding domain.";
RL J. Biol. Chem. 267:19683-19690(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1054-1258, ALTERNATIVE SPLICING
RP (ISOFORMS XA/ZA), AND TISSUE SPECIFICITY (ISOFORMS XA AND XB).
RC STRAIN=CD Charles River;
RX PubMed=8428948; DOI=10.1016/s0021-9258(18)53836-9;
RA Keeton T.P., Burk S.E., Shull G.E.;
RT "Alternative splicing of exons encoding the calmodulin-binding domains and
RT C termini of plasma membrane Ca(2+)-ATPase isoforms 1, 2, 3, and 4.";
RL J. Biol. Chem. 268:2740-2748(1993).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9880546; DOI=10.1074/jbc.274.3.1667;
RA Guerini D., Garcia-Martin E., Gerber A., Volbracht C., Leist M.,
RA Merino C.G., Carafoli E.;
RT "The expression of plasma membrane Ca2+ pump isoforms in cerebellar granule
RT neurons is modulated by Ca2+.";
RL J. Biol. Chem. 274:1667-1676(1999).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17183553; DOI=10.1002/cne.21237;
RA Burette A., Weinberg R.J.;
RT "Perisynaptic organization of plasma membrane calcium pumps in cerebellar
RT cortex.";
RL J. Comp. Neurol. 500:1127-1135(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; THR-1079 AND SER-1126, AND
RP 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, AND CATALYTIC ACTIVITY.
RX PubMed=25014339; DOI=10.1371/journal.pone.0102352;
RA Boczek T., Lisek M., Ferenc B., Kowalski A., Stepinski D., Wiktorska M.,
RA Zylinska L.;
RT "Plasma membrane Ca2+-ATPase isoforms composition regulates cellular pH
RT homeostasis in differentiating PC12 cells in a manner dependent on
RT cytosolic Ca2+ elevations.";
RL PLoS ONE 9:e102352-e102352(2014).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27035656; DOI=10.1210/en.2015-2029;
RA Tauber P., Aichinger B., Christ C., Stindl J., Rhayem Y., Beuschlein F.,
RA Warth R., Bandulik S.;
RT "Cellular Pathophysiology of an Adrenal Adenoma-Associated Mutant of the
RT Plasma Membrane Ca(2+)-ATPase ATP2B3.";
RL Endocrinology 157:2489-2499(2016).
CC -!- FUNCTION: ATP-driven Ca(2+) ion pump involved in the maintenance of
CC basal intracellular Ca(2+) levels at the presynaptic terminals. Uses
CC ATP as an energy source to transport cytosolic Ca(2+) ions across the
CC plasma membrane to the extracellular compartment (PubMed:25014339,
CC PubMed:9880546). May counter-transport protons, but the mechanism and
CC the stoichiometry of this Ca(2+)/H(+) exchange remains to be
CC established (PubMed:25014339, PubMed:9880546).
CC {ECO:0000269|PubMed:25014339, ECO:0000269|PubMed:9880546}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000305|PubMed:25014339, ECO:0000305|PubMed:9880546};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000305|PubMed:25014339, ECO:0000305|PubMed:9880546};
CC -!- SUBUNIT: Interacts with PDZD11. Interacts (via N-terminus) with YWHAE.
CC {ECO:0000250|UniProtKB:Q16720}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27035656};
CC Multi-pass membrane protein {ECO:0000255}. Presynaptic cell membrane
CC {ECO:0000269|PubMed:17183553}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localized at parallel fiber terminals.
CC {ECO:0000269|PubMed:17183553}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=12;
CC Comment=There is a combination of two alternative spliced domains at
CC N-terminal site A (X and Z) and at C-terminal site C (A, B, C, D, E
CC and F). So far the splice sites have been studied independently.
CC Experimental confirmation may be lacking for some isoforms.;
CC Name=XD; Synonyms=AIICIV;
CC IsoId=Q64568-1; Sequence=Displayed;
CC Name=XA; Synonyms=AIICII;
CC IsoId=Q64568-2; Sequence=VSP_000400;
CC Name=ZA; Synonyms=AICII;
CC IsoId=Q64568-3; Sequence=VSP_000396, VSP_000400;
CC Name=XB; Synonyms=AIICI;
CC IsoId=Q64568-4; Sequence=VSP_000397;
CC Name=ZB; Synonyms=AICI;
CC IsoId=Q64568-5; Sequence=VSP_000396, VSP_000397;
CC Name=XC; Synonyms=AIICIII;
CC IsoId=Q64568-6; Sequence=VSP_000399;
CC Name=ZC; Synonyms=AICIII;
CC IsoId=Q64568-7; Sequence=VSP_000396, VSP_000399;
CC Name=ZD; Synonyms=AICIV;
CC IsoId=Q64568-8; Sequence=VSP_000396;
CC Name=XE; Synonyms=AIICV;
CC IsoId=Q64568-9; Sequence=VSP_000401;
CC Name=ZE; Synonyms=AICV;
CC IsoId=Q64568-10; Sequence=VSP_000396, VSP_000401;
CC Name=XF; Synonyms=AIICVI;
CC IsoId=Q64568-11; Sequence=VSP_000398;
CC Name=ZF; Synonyms=AICVI;
CC IsoId=Q64568-12; Sequence=VSP_000396, VSP_000398;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in brain and skeletal
CC muscle (PubMed:2530223). Expressed in the molecular layer of the
CC cerebellar cortex, in particular in granule cells (at protein level)
CC (PubMed:27035656, PubMed:17183553, PubMed:9880546). Expressed in
CC aldosterone producing glomerulosa cells of adrenal glands (at protein
CC level) (PubMed:27035656). Detected at low levels in various tissues
CC including testis, stomach, small intestine, and large intestine
CC (PubMed:2530223). {ECO:0000269|PubMed:17183553,
CC ECO:0000269|PubMed:2530223, ECO:0000269|PubMed:27035656,
CC ECO:0000269|PubMed:9880546}.
CC -!- TISSUE SPECIFICITY: [Isoform XA]: Most abundant form in brain and most
CC other tissues. {ECO:0000269|PubMed:8428948}.
CC -!- TISSUE SPECIFICITY: [Isoform XB]: Most abundant form in skeletal muscle
CC and is also found in brain and at low levels in testis and kidney.
CC {ECO:0000269|PubMed:8428948}.
CC -!- INDUCTION: Up-regulated upon activation of glutamate-operated calcium
CC channels. {ECO:0000269|PubMed:9880546}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L05565; AAA53650.1; -; Genomic_DNA.
DR EMBL; L05558; AAA53650.1; JOINED; Genomic_DNA.
DR EMBL; L05564; AAA53650.1; JOINED; Genomic_DNA.
DR EMBL; J05087; AAA69667.1; -; mRNA.
DR EMBL; M96626; AAA50821.1; -; mRNA.
DR PIR; A34308; A34308.
DR PIR; C44525; C44525.
DR RefSeq; NP_579822.1; NM_133288.1. [Q64568-3]
DR RefSeq; XP_008771842.1; XM_008773620.2. [Q64568-7]
DR RefSeq; XP_017457435.1; XM_017601946.1. [Q64568-5]
DR RefSeq; XP_017457436.1; XM_017601947.1. [Q64568-3]
DR RefSeq; XP_017457437.1; XM_017601948.1. [Q64568-3]
DR AlphaFoldDB; Q64568; -.
DR SMR; Q64568; -.
DR BioGRID; 248231; 2.
DR IntAct; Q64568; 1.
DR MINT; Q64568; -.
DR STRING; 10116.ENSRNOP00000035695; -.
DR iPTMnet; Q64568; -.
DR PhosphoSitePlus; Q64568; -.
DR SwissPalm; Q64568; -.
DR jPOST; Q64568; -.
DR PaxDb; Q64568; -.
DR PRIDE; Q64568; -.
DR Ensembl; ENSRNOT00000098998; ENSRNOP00000083651; ENSRNOG00000061304. [Q64568-7]
DR GeneID; 29599; -.
DR KEGG; rno:29599; -.
DR CTD; 492; -.
DR RGD; 621304; Atp2b3.
DR VEuPathDB; HostDB:ENSRNOG00000061304; -.
DR eggNOG; KOG0204; Eukaryota.
DR GeneTree; ENSGT00940000160765; -.
DR InParanoid; Q64568; -.
DR OrthoDB; 115892at2759; -.
DR PhylomeDB; Q64568; -.
DR Reactome; R-RNO-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR Reactome; R-RNO-936837; Ion transport by P-type ATPases.
DR PRO; PR:Q64568; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000061304; Expressed in cerebellum and 12 other tissues.
DR ExpressionAtlas; Q64568; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:1990032; C:parallel fiber; IDA:UniProtKB.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015085; F:calcium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
DR GO; GO:1905056; F:P-type calcium transporter activity involved in regulation of presynaptic cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:1990034; P:calcium ion export across plasma membrane; ISS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0003407; P:neural retina development; IEP:RGD.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:RGD.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR022141; ATP_Ca_trans_C.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF12424; ATP_Ca_trans_C; 2.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Calcium; Calcium transport;
KW Calmodulin-binding; Cell membrane; Cell projection; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Synapse; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1258
FT /note="Plasma membrane calcium-transporting ATPase 3"
FT /id="PRO_0000046219"
FT TOPO_DOM 1..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..155
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..849
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 850..869
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 870..879
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 880..900
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 901..920
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 921..943
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 944..961
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 962..983
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 984..1002
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1003..1024
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1025..1034
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1035..1056
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1057..1258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1114
FT /note="Calmodulin-binding subdomain A"
FT /evidence="ECO:0000250"
FT REGION 1115..1124
FT /note="Calmodulin-binding subdomain B"
FT /evidence="ECO:0000250"
FT REGION 1204..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 473
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 794
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 798
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1079
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1113
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 1126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 306..319
FT /note="Missing (in isoform ZA, isoform ZB, isoform ZC,
FT isoform ZD, isoform ZE and isoform ZF)"
FT /evidence="ECO:0000303|PubMed:2530223"
FT /id="VSP_000396"
FT VAR_SEQ 1115..1258
FT /note="MEVVSTFKRSGSFQGAVRRRSSVLSQLHDVTNLSTPTHIRVVKAFRSSLYEG
FT LEKPESKSCIHNFMATPEFLINDYTHNIPLIDDTDVDENEERLRAPPPPPPNQNNNAID
FT SGIYLTTHATKSATSSAFSSRPGSPLHSMETSL -> VCWDGKKMLRTTEVG (in
FT isoform XF and isoform ZF)"
FT /evidence="ECO:0000305"
FT /id="VSP_000398"
FT VAR_SEQ 1115..1152
FT /note="Missing (in isoform XB and isoform ZB)"
FT /evidence="ECO:0000305"
FT /id="VSP_000397"
FT VAR_SEQ 1144..1152
FT /note="Missing (in isoform XC and isoform ZC)"
FT /evidence="ECO:0000305"
FT /id="VSP_000399"
FT VAR_SEQ 1153..1258
FT /note="IRVVKAFRSSLYEGLEKPESKSCIHNFMATPEFLINDYTHNIPLIDDTDVDE
FT NEERLRAPPPPPPNQNNNAIDSGIYLTTHATKSATSSAFSSRPGSPLHSMETSL -> V
FT TLSAAKPTSAAGNPSGESIP (in isoform XA and isoform ZA)"
FT /evidence="ECO:0000303|PubMed:2530223"
FT /id="VSP_000400"
FT VAR_SEQ 1153..1258
FT /note="IRVVKAFRSSLYEGLEKPESKSCIHNFMATPEFLINDYTHNIPLIDDTDVDE
FT NEERLRAPPPPPPNQNNNAIDSGIYLTTHATKSATSSAFSSRPGSPLHSMETSL -> V
FT TLSAAKPTSAAGSES (in isoform XE and isoform ZE)"
FT /evidence="ECO:0000305"
FT /id="VSP_000401"
SQ SEQUENCE 1258 AA; 138559 MW; 3A13781D21042BA6 CRC64;
MGDMANSSIE FHPKPQQQRE VPHVGGFGCT LAELRSLMEL RGAEALQKIQ EAYGDVSGLC
RRLKTSPTEG LADNTNDLEK RRQIYGQNFI PPKQPKTFLQ LVWEALQDVT LIILEVAAIV
SLGLSFYAPP GEESEACGNV SGGAEDEGEA EAGWIEGAAI LLSVICVVLV TAFNDWSKEK
QFRGLQSRIE QEQKFTVIRN GQLLQVPVAA LVVGDIAQVK YGDLLPADGV LIQGNDLKID
ESSLTGESDH VRKSADKDPM LLSGTHVMEG SGRMVVTAVG VNSQTGIIFT LLGAGGEEEE
KKDKKGKQQD GAMESSQTKA KKQDGAVAME MQPLKSAEGG EMEEREKKKA NVPKKEKSVL
QGKLTKLAVQ IGKAGLVMSA ITVIILVLYF VIETFVVDGR VWLAECTPVY VQYFVKFFII
GVTVLVVAVP EGLPLAVTIS LAYSVKKMMK DNNLVRHLDA CETMGNATAI CSDKTGTLTT
NRMTVVQSYL GDTHYKEIPA PSALTPKILD LLVHAISINS AYTTKILPPE KEGALPRQVG
NKTECALLGF ILDLKRDFQP VREQIPEDQL YKVYTFNSVR KSMSTVIRMP DGGFRLFSKG
ASEILLKKCT NILNSNGELR GFRPRDRDDM VKKIIEPMAC DGLRTICIAY RDFSAIQEPD
WDNENEVVGD LTCIAVVGIE DPVRPEVPEA IRKCQRAGIT VRMVTGDNIN TARAIAAKCG
IIQPGEDFLC LEGKEFNRRI RNEKGEIEQE RLDKVWPKLR VLARSSPTDK HTLVKGIIDS
TTGEQRQVVA VTGDGTNDGP ALKKADVGFA MGIAGTDVAK EASDIILTDD NFTSIVKAVM
WGRNVYDSIS KFLQFQLTVN VVAVIVAFTG ACITQDSPLK AVQMLWVNLI MDTFASLALA
TEPPTESLLL RKPYGRDKPL ISRTMMKNIL GHAVYQLTII FTLLFVGELF FDIDSGRNAP
LHSPPSEHYT IIFNTFVMMQ LFNEINARKI HGERNVFDGI FSNPIFCTIV LGTFGIQIVI
VQFGGKPFSC SPLSTEQWLW CLFVGVGELV WGQVIATIPT SQLKCLKEAG HGPGKDEMTD
EELAEGEEEI DHAERELRRG QILWFRGLNR IQTQMEVVST FKRSGSFQGA VRRRSSVLSQ
LHDVTNLSTP THIRVVKAFR SSLYEGLEKP ESKSCIHNFM ATPEFLINDY THNIPLIDDT
DVDENEERLR APPPPPPNQN NNAIDSGIYL TTHATKSATS SAFSSRPGSP LHSMETSL
