ID AT2A3_MOUSE Reviewed; 999 AA. AC Q64518; O70625; Q64517; Q8VD16; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 02-DEC-2020, sequence version 4. DT 27-MAR-2024, entry version 193. DE RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 3; DE Short=SERCA3; DE Short=SR Ca(2+)-ATPase 3; DE EC=7.2.2.10; DE AltName: Full=Calcium pump 3; GN Name=Atp2a3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SERCA3A AND SERCA3B). RC STRAIN=C57BL/6J; RA Tokuyama Y., Chen X., Roe M.W., Bell G.I.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SERCA3A), AND RP ALTERNATIVE SPLICING. RX PubMed=9593748; DOI=10.1074/jbc.273.22.13982; RA Dode L., De Greef C., Mountian I., Attard M., Town M.M., Casteels R., RA Wuytack F.; RT "Structure of the human sarco/endoplasmic reticulum Ca2+-ATPase 3 gene. RT Promoter analysis and alternative splicing of the SERCA3 pre-mRNA."; RL J. Biol. Chem. 273:13982-13994(1998). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; THR-19; SER-25 AND RP THR-415, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Spleen; 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 expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of CC ATP coupled with the transport of calcium. Transports calcium ions from CC the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. CC Contributes to calcium sequestration involved in muscular CC excitation/contraction. {ECO:0000250|UniProtKB:Q93084}. 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:0000250|UniProtKB:Q93084}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106; CC Evidence={ECO:0000250|UniProtKB:Q93084}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P04191}; CC -!- ACTIVITY REGULATION: Inhibited by sarcolipin (SLN), phospholamban (PLN) CC and myoregulin (MRLN) (By similarity). Enhanced by DWORF; DWORF CC increases activity by displacing sarcolipin (SLN), phospholamban (PLN) CC and myoregulin (MRLN) (By similarity). {ECO:0000250|UniProtKB:P04191, CC ECO:0000250|UniProtKB:Q8R429}. CC -!- SUBUNIT: Interacts with sarcolipin (SLN) (By similarity). Interacts CC with phospholamban (PLN) (By similarity). Interacts with myoregulin CC (MRLN). Interacts with DWORF (By similarity). Interacts with VMP1 (By CC similarity). Interacts with TUNAR; the interaction occurs at low levels CC in low glucose conditions and is increased by high glucose levels (By CC similarity). {ECO:0000250|UniProtKB:P04191, CC ECO:0000250|UniProtKB:Q8R429, ECO:0000250|UniProtKB:Q93084}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q93084}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q93084}. Sarcoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q93084}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q93084}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=SERCA3A; CC IsoId=Q64518-2; Sequence=Displayed; CC Name=SERCA3B; CC IsoId=Q64518-1; Sequence=VSP_060850; CC Name=SERCA3C; CC IsoId=Q64518-3; Sequence=VSP_060851; CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) CC family. Type IIA 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; U49394; AAB04099.1; -; mRNA. DR EMBL; U49393; AAB04098.1; -; mRNA. DR EMBL; CH466596; EDL12704.1; -; Genomic_DNA. DR EMBL; BC017639; AAH17639.1; -; mRNA. DR EMBL; Y15734; CAA75744.1; -; Genomic_DNA. DR EMBL; Y15735; CAA75744.1; JOINED; Genomic_DNA. DR EMBL; Y15734; CAA75745.1; -; Genomic_DNA. DR EMBL; Y15735; CAA75745.1; JOINED; Genomic_DNA. DR EMBL; Y15734; CAA75743.1; -; Genomic_DNA. DR EMBL; Y15735; CAA75743.1; JOINED; Genomic_DNA. DR EMBL; Y15736; CAA75746.1; -; Genomic_DNA. DR CCDS; CCDS24991.1; -. [Q64518-1] DR CCDS; CCDS48843.1; -. [Q64518-2] DR RefSeq; NP_001156808.1; NM_001163336.1. [Q64518-2] DR RefSeq; NP_001156809.1; NM_001163337.1. DR RefSeq; NP_058025.2; NM_016745.3. [Q64518-1] DR AlphaFoldDB; Q64518; -. DR SMR; Q64518; -. DR BioGRID; 207277; 6. DR IntAct; Q64518; 2. DR MINT; Q64518; -. DR STRING; 10090.ENSMUSP00000021142; -. DR BindingDB; Q64518; -. DR ChEMBL; CHEMBL4523338; -. DR GlyGen; Q64518; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q64518; -. DR PhosphoSitePlus; Q64518; -. DR SwissPalm; Q64518; -. DR EPD; Q64518; -. DR jPOST; Q64518; -. DR MaxQB; Q64518; -. DR PaxDb; 10090-ENSMUSP00000021142; -. DR ProteomicsDB; 265125; -. [Q64518-2] DR ProteomicsDB; 265126; -. [Q64518-2] DR ProteomicsDB; 265127; -. [Q64518-3] DR Antibodypedia; 1517; 174 antibodies from 29 providers. DR DNASU; 53313; -. DR Ensembl; ENSMUST00000021142.8; ENSMUSP00000021142.8; ENSMUSG00000020788.16. [Q64518-1] DR Ensembl; ENSMUST00000108485.9; ENSMUSP00000104125.3; ENSMUSG00000020788.16. [Q64518-2] DR GeneID; 53313; -. DR KEGG; mmu:53313; -. DR UCSC; uc007jzo.2; mouse. [Q64518-2] DR AGR; MGI:1194503; -. DR CTD; 489; -. DR MGI; MGI:1194503; Atp2a3. DR VEuPathDB; HostDB:ENSMUSG00000020788; -. DR eggNOG; KOG0202; Eukaryota. DR GeneTree; ENSGT00940000155668; -. DR HOGENOM; CLU_002360_3_2_1; -. DR InParanoid; Q64518; -. DR OMA; GIVDWGC; -. DR OrthoDB; 203629at2759; -. DR PhylomeDB; Q64518; -. DR TreeFam; TF300651; -. DR Reactome; R-MMU-418359; Reduction of cytosolic Ca++ levels. DR Reactome; R-MMU-5578775; Ion homeostasis. DR Reactome; R-MMU-936837; Ion transport by P-type ATPases. DR BioGRID-ORCS; 53313; 6 hits in 78 CRISPR screens. DR ChiTaRS; Atp2a3; mouse. DR PRO; PR:Q64518; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; Q64518; Protein. DR Bgee; ENSMUSG00000020788; Expressed in submandibular gland and 180 other cell types or tissues. DR ExpressionAtlas; Q64518; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0031090; C:organelle membrane; ISO:MGI. DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:MGI. DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0015085; F:calcium ion transmembrane transporter activity; ISO:MGI. DR GO; GO:0030899; F:calcium-dependent ATPase activity; ISO:MGI. DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005388; F:P-type calcium transporter activity; ISO:MGI. DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI. DR GO; GO:0070588; P:calcium ion transmembrane transport; ISO:MGI. DR GO; GO:1903515; P:calcium ion transport from cytosol to endoplasmic reticulum; ISO:MGI. DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; ISO:MGI. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; ISO:MGI. DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISO:MGI. DR CDD; cd02083; P-type_ATPase_SERCA; 1. DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1. DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1. DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. 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; IPR005782; P-type_ATPase_IIA. DR InterPro; IPR001757; P_typ_ATPase. DR InterPro; IPR044492; P_typ_ATPase_HD_dom. DR NCBIfam; TIGR01116; ATPase-IIA1_Ca; 1. DR NCBIfam; TIGR01494; ATPase_P-type; 2. DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1. DR PANTHER; PTHR42861:SF6; SARCOPLASMIC_ENDOPLASMIC RETICULUM CALCIUM ATPASE 3; 1. DR Pfam; PF13246; Cation_ATPase; 1. DR Pfam; PF00689; Cation_ATPase_C; 1. DR Pfam; PF00690; Cation_ATPase_N; 1. DR Pfam; PF00122; E1-E2_ATPase; 1. DR Pfam; PF00702; Hydrolase; 1. DR PRINTS; PR00119; CATATPASE. DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1. DR SFLD; SFLDF00027; p-type_atpase; 1. DR SMART; SM00831; Cation_ATPase_N; 1. DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1. DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1. DR PROSITE; PS00154; ATPASE_E1_E2; 1. DR Genevisible; Q64518; MM. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; ATP-binding; Calcium; Calcium transport; KW Endoplasmic reticulum; Ion transport; Magnesium; Membrane; Metal-binding; KW Nucleotide-binding; Phosphoprotein; Reference proteome; KW Sarcoplasmic reticulum; Translocase; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..999 FT /note="Sarcoplasmic/endoplasmic reticulum calcium ATPase 3" FT /id="PRO_0000046203" FT TOPO_DOM 1..48 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TRANSMEM 49..69 FT /note="Helical; Name=1" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 70..89 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TRANSMEM 90..110 FT /note="Helical; Name=2" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 111..253 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TRANSMEM 254..273 FT /note="Helical; Name=3" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 274..295 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TRANSMEM 296..313 FT /note="Helical; Name=4" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 314..757 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TRANSMEM 758..777 FT /note="Helical; Name=5" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 778..787 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TRANSMEM 788..808 FT /note="Helical; Name=6" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 809..828 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TRANSMEM 829..851 FT /note="Helical; Name=7" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 852..897 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TRANSMEM 898..917 FT /note="Helical; Name=8" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 918..930 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TRANSMEM 931..949 FT /note="Helical; Name=9" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 950..964 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TRANSMEM 965..985 FT /note="Helical; Name=10" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 986..999 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P04191" FT REGION 370..400 FT /note="Interaction with phospholamban 1" FT /evidence="ECO:0000250|UniProtKB:P04191" FT REGION 788..808 FT /note="Interaction with phospholamban 2" FT /evidence="ECO:0000250|UniProtKB:P04191" FT ACT_SITE 351 FT /note="4-aspartylphosphate intermediate" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 304 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 305 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 307 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 309 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 351 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 353 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 353 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 442 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 489 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 515 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 560 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 625 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 626 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 627 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 678 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 684 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 703 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 706 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 768 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 771 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 796 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 799 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 800 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 800 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 908 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P04191" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q93084" FT MOD_RES 17 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 19 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 25 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 415 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 662 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q93084" FT VAR_SEQ 994..999 FT /note="EKKDLK -> GVLGTFMQARSRQLPTTSRTPYHTGKKGPEVNPGSRGESPVW FT PSD (in isoform SERCA3B)" FT /evidence="ECO:0000305" FT /id="VSP_060850" FT VAR_SEQ 994..999 FT /note="EKKDLK -> GVLGTFMQARSRQLPTTSRTPYHTGLACKKKT (in FT isoform SERCA3C)" FT /evidence="ECO:0000305" FT /id="VSP_060851" FT CONFLICT 860 FT /note="T -> A (in Ref. 1; AAB04098/AAB04099)" FT /evidence="ECO:0000305" SQ SEQUENCE 999 AA; 109530 MW; F64B7046E792B6E7 CRC64; MEEAHLLSAA DVLRRFSVTA EGGLSLEQVT DARERYGPNE LPTEEGKSLW ELVVEQFEDL LVRILLLAAL VSFVLAWFEE GEETTTAFVE PLVIMLILVA NAIVGVWQER NAESAIEALK EYEPEMGKVI RSDRKGVQRI RARDIVPGDI VEVAVGDKVP ADLRLIEIKS TTLRVDQSIL TGESVSVTKH TDAIPDPRAV NQDKKNMLFS GTNIASGKAL GVAVATGLQT ELGKIRSQMA AVEPERTPLQ RKLDEFGRQL SHAISVICVA VWVINIGHFA DPAHGGSWLR GAVYYFKIAV ALAVAAIPEG LPAVITTCLA LGTRRMARKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ MSVCRMFVVA EAEAGTCRLH EFTISGTTYT PEGEVRQGEQ PVRCGQFDGL VELATICALC NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTDLK GLSRVERAGA CNSVIKQLMR KEFTLEFSRD RKSMSVYCTP TRADPKVQGS KMFVKGAPES VIERCSSVRV GSRTAPLSTT SREHILAKIR DWGSGSDTLR CLALATRDTP PRKEDMHLDD CSRFVQYETD LTFVGCVGML DPPRPEVAAC ITRCSRAGIR VVMITGDNKG TAVAICRRLG IFGDTEDVLG KAYTGREFDD LSPEQQRQAC RTARCFARVE PAHKSRIVEN LQSFNEITAM TGDGVNDAPA LKKAEIGIAM GSGTAVAKSA AEMVLSDDNF ASIVAAVEEG RAIYNNMKQF IRYLISSNVG EVVCIFLTAI LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMEKP PRNPREALIS GWLFFRYLAI GVYVGLATVA AATWWFLYDT EGPQVTFYQL RNFLKCSEDN PLFAGIDCKV FESRFPTTMA LSVLVTIEMC NALNSVSENQ SLLRMPPWLN PWLLGAVVMS MALHFLILLV PPLPLIFQVT PLSGRQWGVV LQMSLPVILL DEALKYLSRN HMDEKKDLK //