AT2B4_MOUSE
ID AT2B4_MOUSE Reviewed; 1205 AA.
AC Q6Q477; Q32ME1;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Plasma membrane calcium-transporting ATPase 4 {ECO:0000305};
DE Short=PMCA4 {ECO:0000303|PubMed:15078889};
DE EC=7.2.2.10 {ECO:0000250|UniProtKB:P23634};
GN Name=Atp2b4 {ECO:0000312|MGI:MGI:88111};
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] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=15078889; DOI=10.1074/jbc.m312599200;
RA Schuh K., Cartwright E.J., Jankevics E., Bundschu K., Liebermann J.,
RA Williams J.C., Armesilla A.L., Emerson M., Oceandy D., Knobeloch K.P.,
RA Neyses L.;
RT "Plasma membrane Ca2+ ATPase 4 is required for sperm motility and male
RT fertility.";
RL J. Biol. Chem. 279:28220-28226(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1145, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
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).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1072, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Calcium/calmodulin-regulated and magnesium-dependent enzyme
CC that catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium out of the cell (By similarity). By regulating sperm cell
CC calcium homeostasis, may play a role in sperm motility
CC (PubMed:15078889). {ECO:0000250|UniProtKB:P23634,
CC ECO:0000269|PubMed:15078889}.
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:P23634};
CC -!- ACTIVITY REGULATION: Activated by calcium/calmodulin.
CC {ECO:0000250|UniProtKB:P23634}.
CC -!- SUBUNIT: Interacts with PDZD11. Interacts with SLC35G1 and STIM1.
CC Interacts with calmodulin. {ECO:0000250|UniProtKB:P23634}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P23634}; Multi-
CC pass membrane protein {ECO:0000255}. Cell projection, cilium, flagellum
CC membrane {ECO:0000269|PubMed:15078889}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PMCA4b;
CC IsoId=Q6Q477-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6Q477-2; Sequence=VSP_058018, VSP_058019;
CC -!- TISSUE SPECIFICITY: Specifically expressed by sperm in testis (at
CC protein level). {ECO:0000269|PubMed:15078889}.
CC -!- DISRUPTION PHENOTYPE: Male mice lacking Atp2b4 are infertile with
CC severe reduction of sperm motility. {ECO:0000269|PubMed:15078889}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000305}.
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DR EMBL; AY560895; AAT01506.1; -; mRNA.
DR EMBL; AC124338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC157924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC109172; AAI09173.1; -; mRNA.
DR EMBL; BC109173; AAI09174.1; -; mRNA.
DR CCDS; CCDS15298.1; -. [Q6Q477-1]
DR RefSeq; NP_001161421.1; NM_001167949.2.
DR RefSeq; NP_998781.1; NM_213616.4. [Q6Q477-1]
DR RefSeq; XP_006529786.1; XM_006529723.2. [Q6Q477-1]
DR RefSeq; XP_006529787.1; XM_006529724.3. [Q6Q477-1]
DR RefSeq; XP_006529788.1; XM_006529725.2. [Q6Q477-1]
DR AlphaFoldDB; Q6Q477; -.
DR SMR; Q6Q477; -.
DR CORUM; Q6Q477; -.
DR DIP; DIP-46143N; -.
DR IntAct; Q6Q477; 5.
DR MINT; Q6Q477; -.
DR STRING; 10090.ENSMUSP00000119242; -.
DR iPTMnet; Q6Q477; -.
DR PhosphoSitePlus; Q6Q477; -.
DR EPD; Q6Q477; -.
DR jPOST; Q6Q477; -.
DR MaxQB; Q6Q477; -.
DR PaxDb; Q6Q477; -.
DR PRIDE; Q6Q477; -.
DR ProteomicsDB; 277123; -. [Q6Q477-1]
DR ProteomicsDB; 277124; -. [Q6Q477-2]
DR Antibodypedia; 4241; 158 antibodies from 23 providers.
DR DNASU; 381290; -.
DR Ensembl; ENSMUST00000112264; ENSMUSP00000107883; ENSMUSG00000026463. [Q6Q477-2]
DR Ensembl; ENSMUST00000143567; ENSMUSP00000119242; ENSMUSG00000026463. [Q6Q477-1]
DR Ensembl; ENSMUST00000165602; ENSMUSP00000133187; ENSMUSG00000026463. [Q6Q477-1]
DR GeneID; 381290; -.
DR KEGG; mmu:381290; -.
DR UCSC; uc007cqv.3; mouse. [Q6Q477-1]
DR UCSC; uc007cqw.1; mouse.
DR CTD; 493; -.
DR MGI; MGI:88111; Atp2b4.
DR VEuPathDB; HostDB:ENSMUSG00000026463; -.
DR eggNOG; KOG0204; Eukaryota.
DR GeneTree; ENSGT00940000154527; -.
DR InParanoid; Q6Q477; -.
DR OMA; IMGQNIY; -.
DR OrthoDB; 115892at2759; -.
DR PhylomeDB; Q6Q477; -.
DR TreeFam; TF300330; -.
DR BRENDA; 7.2.2.10; 3474.
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; 381290; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Atp2b4; mouse.
DR PRO; PR:Q6Q477; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6Q477; protein.
DR Bgee; ENSMUSG00000026463; Expressed in spermatocyte and 138 other tissues.
DR ExpressionAtlas; Q6Q477; baseline and differential.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR GO; GO:0097228; C:sperm principal piece; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
DR GO; GO:0030018; C:Z disc; ISO:MGI.
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:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050998; F:nitric-oxide synthase binding; ISO:MGI.
DR GO; GO:0036487; F:nitric-oxide synthase inhibitor activity; ISO:MGI.
DR GO; GO:0005388; F:P-type calcium transporter activity; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030346; F:protein phosphatase 2B binding; ISO:MGI.
DR GO; GO:1901660; P:calcium ion export; ISO:MGI.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006816; P:calcium ion transport; ISO:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:1905145; P:cellular response to acetylcholine; IMP:UniProtKB.
DR GO; GO:0071872; P:cellular response to epinephrine stimulus; ISO:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0140199; P:negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process; ISO:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:ARUK-UCL.
DR GO; GO:1900082; P:negative regulation of arginine catabolic process; ISO:MGI.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IMP:ARUK-UCL.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IMP:ARUK-UCL.
DR GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; IMP:BHF-UCL.
DR GO; GO:1902548; P:negative regulation of cellular response to vascular endothelial growth factor stimulus; ISO:MGI.
DR GO; GO:1903249; P:negative regulation of citrulline biosynthetic process; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; ISO:MGI.
DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; ISO:MGI.
DR GO; GO:0098736; P:negative regulation of the force of heart contraction; ISO:MGI.
DR GO; GO:0003407; P:neural retina development; IEA:Ensembl.
DR GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; ISO:MGI.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0051599; P:response to hydrostatic pressure; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; IMP:UniProtKB.
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; 1.
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; Cilium; Flagellum;
KW Ion transport; Magnesium; Membrane; Metal-binding; Methylation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1205
FT /note="Plasma membrane calcium-transporting ATPase 4"
FT /id="PRO_0000435124"
FT TOPO_DOM 1..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..147
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..409
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..844
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 845..865
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 866..872
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 873..893
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 894..919
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 920..942
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 943..956
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 957..979
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 980..995
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 996..1016
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1017..1029
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1030..1050
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1051..1205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 294..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1104
FT /note="Calmodulin-binding subdomain A"
FT /evidence="ECO:0000250|UniProtKB:P20020,
FT ECO:0000250|UniProtKB:P23634"
FT REGION 1105..1114
FT /note="Calmodulin-binding subdomain B"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT COMPBIAS 294..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 466
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 786
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 790
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64542"
FT MOD_RES 1065
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64542"
FT MOD_RES 1071
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64542"
FT MOD_RES 1072
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1103
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 1145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1104..1107
FT /note="QIRV -> QEGN (in isoform 2)"
FT /id="VSP_058018"
FT VAR_SEQ 1108..1205
FT /note="Missing (in isoform 2)"
FT /id="VSP_058019"
SQ SEQUENCE 1205 AA; 133069 MW; 75E39DB859951DF0 CRC64;
MTNPPGQSVS ANTVAESHEG EFGCTLMDLR KLMELRGADA VAQISAHYGG VQEICTRLKT
SPIEGLSGNP ADLEKRRLVF GKNVIPPKRP KTFLELVWEA LQDVTLIILE IAAIISLVLS
FYRPPGGDNE ICGHIASSPE EEEEGETGWI EGAAILASVI IVVLVTAFND WSKEKQFRGL
QSRIELEQKF SIIRNGQLIQ LPVAEIVVGD IAQIKYGDLL PADGILIQGN DLKIDESSLT
GESDHVKKTL DKDPMLLSGT HVMEGSGRMV VTAVGVNSQT GIIFTLLGAS EEEDDDDKKK
KGKKQGAPEN RNKAKTQDGV ALEIQPLNSQ EGLDSEDKEK KIARIPKKEK SVLQGKLTRL
AVQIGKAGLI MSVLTVVILI LYFVVDNFVI QRREWLPECT PVYIQYFVKF FIIGVTVLVV
AVPEGLPLAV TISLAYSVKK MMKDNNLVRH LDACETMGNA TAICSDKTGT LTMNRMTVVQ
AYIGGTHYRQ IPQPDVFPPK VLELIVNGIS INCAYTSKIQ PPEKEGGLPR QVGNKTECGL
LGFVTDLKQD YQAVRNEVPE EKLFKVYTFN SVRKSMSTVI RKPEGGFRMF SKGASEIMLR
RCDRILNKEG EIKSFRSKDR DNMVRNVIEP MASEGLRTIC LAYRDFDGTE PSWDIEGEIL
TSLICIAVVG IEDPVRPEVP DAIAKCKRAG ITVRMVTGDN VNTARAIATK CGILTPKDDF
LCLEGKEFNS LIRNEKGEVE QEKLDKIWPK LRVLARSSPT DKHTLVKGII DSTAGEQRQV
VAVTGDGTND GPALKKADVG FAMGIAGTDV AKEASDIILT DDNFTSIVKA VMWGRNVYDS
ISKFLQFQLT VNVVAVIVAF TGACITQDSP LKAVQMLWVN LIMDTFASLA LATEPPTESL
LRRRPYGRNK PLISRTMMKN ILGHAVYQLL IVFLLVFAGD TLFDIDSGRK APLNSPPSQH
YTIVFNTFVL MQLFNEINAR KIHGEKNVFA GVYRNIIFCT VVLGTFFCQI MIVELGGKPF
SCTSLTMEQW MWCLFIGIGE LLWGQVISAI PTKSLKFLKE AGHGSDKEDI SRDTEGMDEI
DLAEMELRRG QILWVRGLNR IQTQIRVVKL FHNNHEVAHK PKNRSSIHTF MTQPEYPADD
ELSQSFLDIQ EGNPELVSKA GTSVLLLDGE AASHDNINNN AVDCHQVQIV ASHSDSPLPS
LETPV
