ID AT2A1_RAT Reviewed; 994 AA. AC Q64578; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 192. DE RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 1; DE Short=SERCA1; DE Short=SR Ca(2+)-ATPase 1; DE EC=7.2.2.10 {ECO:0000250|UniProtKB:P04191}; DE AltName: Full=Calcium pump 1; DE AltName: Full=Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform; DE AltName: Full=Endoplasmic reticulum class 1/2 Ca(2+) ATPase; GN Name=Atp2a1; 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], AND TISSUE SPECIFICITY. RC STRAIN=CD Charles River; TISSUE=Skeletal muscle; RX PubMed=8447366; DOI=10.1152/ajpcell.1993.264.2.c333; RA Wu K.D., Lytton J.; RT "Molecular cloning and quantification of sarcoplasmic reticulum Ca(2+)- RT ATPase isoforms in rat muscles."; RL Am. J. Physiol. 264:C333-C341(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 955-994, AND INDUCTION. RC STRAIN=Sprague-Dawley; TISSUE=Kidney; RX PubMed=10329971; DOI=10.1152/ajpcell.1999.276.5.c1218; RA Peters D.G., Mitchell-Felton H., Kandarian S.C.; RT "Unloading induces transcriptional activation of the sarco(endo)plasmic RT reticulum Ca2+-ATPase 1 gene in muscle."; RL Am. J. Physiol. 276:C1218-C1225(1999). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-441; THR-569; SER-581 AND RP SER-643, AND 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). CC -!- FUNCTION: Key regulator of striated muscle performance by acting as the CC major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) CC into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP CC coupled with the translocation of calcium from the cytosol to the CC sarcoplasmic reticulum lumen. Contributes to calcium sequestration CC involved in muscular excitation/contraction. CC {ECO:0000250|UniProtKB:Q8R429}. 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:P04191}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106; CC Evidence={ECO:0000250|UniProtKB:P04191}; 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). Reversibly inhibited by CC phospholamban (PLN) at low calcium concentrations (By similarity). CC Dephosphorylated PLN decreases the apparent affinity of the ATPase for CC calcium. This inhibition is regulated by the phosphorylation of PLN (By CC similarity). Enhanced by DWORF; DWORF increases activity by displacing CC sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN) (By CC 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). {ECO:0000250|UniProtKB:O14983, CC ECO:0000250|UniProtKB:Q8R429}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P04191}. Sarcoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P04191}. CC -!- TISSUE SPECIFICITY: Skeletal muscle, fast twitch muscle (type II) CC fibers. {ECO:0000269|PubMed:8447366}. CC -!- INDUCTION: Increased contractile activity leads to a decrease in SERCA1 CC expression, while decreased contractile activity leads to an increase CC in SERCA1 expression. {ECO:0000269|PubMed:10329971}. CC -!- DOMAIN: Ca(2+) and ATP binding cause major rearrangements of the CC cytoplasmic and transmembrane domains. According to the E1-E2 model, CC Ca(2+) binding to the cytosolic domain of the pump in the high-affinity CC E1 conformation is followed by the ATP-dependent phosphorylation of the CC active site Asp, giving rise to E1P. A conformational change of the CC phosphoenzyme gives rise to the low-affinity E2P state that exposes the CC Ca(2+) ions to the lumenal side and promotes Ca(2+) release. CC Dephosphorylation of the active site Asp mediates the subsequent return CC to the E1 conformation. {ECO:0000250|UniProtKB:P04191}. CC -!- DOMAIN: PLN and SLN both have a single transmembrane helix; both occupy CC a similar binding site on ATP2A1 that is situated between the ATP2A1 CC transmembrane helices. {ECO:0000250|UniProtKB:P04191}. 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; M99223; AAA40991.1; -; mRNA. DR EMBL; AF091853; AAD17802.1; -; Genomic_DNA. DR EMBL; AF091852; AAD17801.1; -; Genomic_DNA. DR PIR; A48849; A48849. DR RefSeq; NP_478120.1; NM_058213.1. DR AlphaFoldDB; Q64578; -. DR SMR; Q64578; -. DR BioGRID; 250515; 1. DR IntAct; Q64578; 1. DR MINT; Q64578; -. DR BindingDB; Q64578; -. DR ChEMBL; CHEMBL3585236; -. DR DrugCentral; Q64578; -. DR iPTMnet; Q64578; -. DR PhosphoSitePlus; Q64578; -. DR SwissPalm; Q64578; -. DR jPOST; Q64578; -. DR Ensembl; ENSRNOT00000106738.1; ENSRNOP00000091865.1; ENSRNOG00000047124.3. DR Ensembl; ENSRNOT00055054479; ENSRNOP00055045048; ENSRNOG00055031226. DR Ensembl; ENSRNOT00060050413; ENSRNOP00060041982; ENSRNOG00060028310. DR Ensembl; ENSRNOT00065027512; ENSRNOP00065021639; ENSRNOG00065016373. DR GeneID; 116601; -. DR KEGG; rno:116601; -. DR AGR; RGD:621293; -. DR CTD; 487; -. DR RGD; 621293; Atp2a1. DR eggNOG; KOG0202; Eukaryota. DR GeneTree; ENSGT00940000159895; -. DR InParanoid; Q64578; -. DR OrthoDB; 203629at2759; -. DR PhylomeDB; Q64578; -. 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:Q64578; -. DR Proteomes; UP000002494; Chromosome 1. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB. DR GO; GO:0031673; C:H zone; ISS:UniProtKB. DR GO; GO:0031674; C:I band; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IEA:GOC. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD. DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:RGD. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0005509; F:calcium ion binding; IDA:RGD. DR GO; GO:0030899; F:calcium-dependent ATPase activity; IDA:ARUK-UCL. DR GO; GO:0005338; F:nucleotide-sugar transmembrane transporter activity; IDA:RGD. DR GO; GO:0005388; F:P-type calcium transporter activity; IDA:ARUK-UCL. DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD. DR GO; GO:0008637; P:apoptotic mitochondrial changes; ISO:RGD. DR GO; GO:0070509; P:calcium ion import; ISO:RGD. DR GO; GO:1990036; P:calcium ion import into sarcoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:ARUK-UCL. DR GO; GO:0006816; P:calcium ion transport; IDA:MGI. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IBA:GO_Central. DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISO:RGD. DR GO; GO:0051659; P:maintenance of mitochondrion location; ISO:RGD. DR GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; ISO:RGD. DR GO; GO:0045988; P:negative regulation of striated muscle contraction; ISS:UniProtKB. DR GO; GO:1901896; P:positive regulation of ATPase-coupled calcium transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:1902082; P:positive regulation of calcium ion import into sarcoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0106134; P:positive regulation of cardiac muscle cell contraction; ISS:UniProtKB. DR GO; GO:0032470; P:positive regulation of endoplasmic reticulum calcium ion concentration; ISO:RGD. DR GO; GO:0031448; P:positive regulation of fast-twitch skeletal muscle fiber contraction; ISS:UniProtKB. DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; ISO:RGD. DR GO; GO:0006942; P:regulation of striated muscle contraction; ISS:UniProtKB. DR GO; GO:0090076; P:relaxation of skeletal muscle; ISO:RGD. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD. DR GO; GO:0043434; P:response to peptide hormone; IDA:UniProtKB. DR GO; GO:0070296; P:sarcoplasmic reticulum calcium ion transport; IDA:RGD. 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; 3. DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1. DR PANTHER; PTHR42861:SF24; SARCOPLASMIC_ENDOPLASMIC RETICULUM CALCIUM ATPASE 1; 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 PRINTS; PR00120; HATPASE. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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. PE 1: Evidence at protein level; KW ATP-binding; Calcium; Calcium transport; Disulfide bond; 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..994 FT /note="Sarcoplasmic/endoplasmic reticulum calcium ATPase 1" FT /id="PRO_0000046190" FT TOPO_DOM 1..48 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" 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:0000305" 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:0000305" 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:0000305" 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:0000305" 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:0000305" 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:0000305" 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:0000305" 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:0000305" 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:0000305" FT TRANSMEM 965..985 FT /note="Helical; Name=10" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 986..994 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT REGION 788..808 FT /note="Interaction with PLN" FT /evidence="ECO:0000250|UniProtKB:P04191" FT REGION 932..943 FT /note="Interaction with PLN" 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="1" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 305 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 307 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 309 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" 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="2" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 771 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 796 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 799 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" 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="2" FT /evidence="ECO:0000250|UniProtKB:P04191" FT MOD_RES 441 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 569 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 581 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 643 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT DISULFID 876..888 FT /evidence="ECO:0000250|UniProtKB:P04191" SQ SEQUENCE 994 AA; 109409 MW; 899F91AD8038A47A CRC64; MEAAHSKSTE ECLSYFGVSE TTGLTPDQVK RHLEKYGPNE LPAEEGKSLW ELVVEQFEDL LVRILLLAAC ISFVLAWFEE GEETVTAFVE PFVILLILIA NAIVGVWQER NAENAIEALK EYEPEMGKVY RADRKSVQRI KARDIVPGDI VEVAVGDKVP ADIRILSIKS TTLRVDQSIL TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAV GIVATTGVST EIGKIRDQMA ATEQDKTPLQ QKLDEFGEQL SKVISLICVA VWLINIGHFN DPVHGGSWFR GAIYYFKIAV ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ MSVCKMFIID KVDGDICSLN EFSITGSTYA PEGEVLKNDK PVRAGQYDGL VELATICALC NDSSLDFNET KGVYEKVGEA TETALTTLVE KMNVFNTEVR SLSKVERANA CNSVIRQLMK KEFTLEFSRD RKSMSVYCSP AKSSRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPLTGP VKEKIMSVIK EWGTGRDTLR CLALATRDTP PKREEMVLDD SAKFMEYEMD LTFVGVVGML DPPRKEVTGS IQLCRDAGIR VIMITGDNKG TAIAICRRIG IFSENEEVAD RAYTGREFDD LPLAEQREAC RRACCFARVE PSHKSKIVEY LQSYDEITAM TGDGVNDAPA LKKAEIGIAM GSGTAVAKTA SEMVLADDNF STIVAAVEEG RAIYNNMKQF IRYLISSNVG EVVCIFLTAA LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMDRP PRSPKEPLIS GWLFFRYMAI GGYVGAATVG AAAWWFLYAE DGPHVSYHQL THFMQCTEHN PEFDGLDCEV FEAPEPMTMA LSVLVTIEMC NALNSLSENQ SLLRMPPWVN IWLLGSICLS MSLHFLILYV DPLPMIFKLR ALDFTQWLMV LKISLPVIGL DELLKFIARN YLEG //