PURA1_MOUSE
ID PURA1_MOUSE Reviewed; 457 AA.
AC P28650; Q8CHQ1;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Adenylosuccinate synthetase isozyme 1 {ECO:0000255|HAMAP-Rule:MF_03126};
DE Short=AMPSase 1 {ECO:0000255|HAMAP-Rule:MF_03126};
DE Short=AdSS 1 {ECO:0000255|HAMAP-Rule:MF_03126};
DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_03126};
DE AltName: Full=Adenylosuccinate synthetase like 1 {ECO:0000312|MGI:MGI:87947};
DE AltName: Full=Adenylosuccinate synthetase, basic isozyme {ECO:0000255|HAMAP-Rule:MF_03126};
DE AltName: Full=Adenylosuccinate synthetase, muscle isozyme {ECO:0000255|HAMAP-Rule:MF_03126, ECO:0000303|PubMed:11560929, ECO:0000303|PubMed:12482871};
DE Short=M-type adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_03126};
DE AltName: Full=IMP--aspartate ligase 1 {ECO:0000255|HAMAP-Rule:MF_03126};
GN Name=Adss1; Synonyms=Adssl1 {ECO:0000312|MGI:MGI:87947};
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).
RC TISSUE=Muscle;
RX PubMed=1939273; DOI=10.1016/s0021-9258(18)54611-1;
RA Guicherit O.M., Rudolph F.B., Kellems R.E., Cooper B.F.;
RT "Molecular cloning and expression of a mouse muscle cDNA encoding
RT adenylosuccinate synthetase.";
RL J. Biol. Chem. 266:22582-22587(1991).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=8308018; DOI=10.1016/s0021-9258(17)41805-9;
RA Guicherit O.M., Cooper B.F., Rudolph F.B., Kellems R.E.;
RT "Amplification of an adenylosuccinate synthetase gene in alanosine-
RT resistant murine T-lymphoma cells. Molecular cloning of a cDNA encoding the
RT 'non-muscle' isozyme.";
RL J. Biol. Chem. 269:4488-4496(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12482871; DOI=10.1074/jbc.m210838200;
RA Borza T., Iancu C.V., Pike E., Honzatko R.B., Fromm H.J.;
RT "Variations in the response of mouse isozymes of adenylosuccinate
RT synthetase to inhibitors of physiological relevance.";
RL J. Biol. Chem. 278:6673-6679(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, 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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
RX PubMed=11560929; DOI=10.1074/jbc.m106294200;
RA Iancu C.V., Borza T., Choe J.Y., Fromm H.J., Honzatko R.B.;
RT "Recombinant mouse muscle adenylosuccinate synthetase: overexpression,
RT kinetics, and crystal structure.";
RL J. Biol. Chem. 276:42146-42152(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH IMP AND GTP.
RX PubMed=12004071; DOI=10.1074/jbc.m203730200;
RA Iancu C.V., Borza T., Fromm H.J., Honzatko R.B.;
RT "IMP, GTP, and 6-phosphoryl-IMP complexes of recombinant mouse muscle
RT adenylosuccinate synthetase.";
RL J. Biol. Chem. 277:26779-26787(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RX PubMed=12186864; DOI=10.1074/jbc.m204952200;
RA Iancu C.V., Borza T., Fromm H.J., Honzatko R.B.;
RT "Feedback inhibition and product complexes of recombinant mouse muscle
RT adenylosuccinate synthetase.";
RL J. Biol. Chem. 277:40536-40543(2002).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RX PubMed=16981730; DOI=10.1021/bi0607498;
RA Iancu C.V., Zhou Y., Borza T., Fromm H.J., Honzatko R.B.;
RT "Cavitation as a mechanism of substrate discrimination by adenylosuccinate
RT synthetases.";
RL Biochemistry 45:11703-11711(2006).
CC -!- FUNCTION: Component of the purine nucleotide cycle (PNC), which
CC interconverts IMP and AMP to regulate the nucleotide levels in various
CC tissues, and which contributes to glycolysis and ammoniagenesis.
CC Catalyzes the first committed step in the biosynthesis of AMP from IMP.
CC {ECO:0000269|PubMed:12482871}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-
CC dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03126};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- ACTIVITY REGULATION: Weakly inhibited by AMP non-competitively to all
CC substrates. Inhibited by IMP non-competitively with respect to GTP.
CC Inhibited by fructose 1,6-bisphosphate competitively with respect to
CC IMP.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 uM for GTP {ECO:0000269|PubMed:12482871};
CC KM=45 uM for IMP {ECO:0000269|PubMed:12482871};
CC KM=140 uM for L-aspartate {ECO:0000269|PubMed:12482871};
CC pH dependence:
CC Optimum pH is 6.6-6.9. {ECO:0000269|PubMed:12482871};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_03126}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03126,
CC ECO:0000269|PubMed:12004071}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC Note=Partially associated with particulate fractions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P28650-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28650-2; Sequence=VSP_008422;
CC -!- TISSUE SPECIFICITY: High levels in muscle.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03126}.
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DR EMBL; M74495; AAA82870.1; -; mRNA.
DR EMBL; BC039943; AAH39943.1; -; mRNA.
DR CCDS; CCDS26192.1; -. [P28650-1]
DR PIR; A39317; AJMSDS.
DR RefSeq; NP_031447.1; NM_007421.2. [P28650-1]
DR PDB; 1IWE; X-ray; 2.10 A; A/B=1-457.
DR PDB; 1J4B; X-ray; 2.50 A; A=1-457.
DR PDB; 1LNY; X-ray; 2.20 A; A/B=1-457.
DR PDB; 1LON; X-ray; 2.10 A; A=1-457.
DR PDB; 1LOO; X-ray; 2.20 A; A=1-457.
DR PDB; 1MEZ; X-ray; 2.40 A; A=1-457.
DR PDB; 1MF0; X-ray; 2.50 A; A=1-457.
DR PDB; 1MF1; X-ray; 2.70 A; A=1-457.
DR PDB; 2DGN; X-ray; 2.40 A; A=1-457.
DR PDBsum; 1IWE; -.
DR PDBsum; 1J4B; -.
DR PDBsum; 1LNY; -.
DR PDBsum; 1LON; -.
DR PDBsum; 1LOO; -.
DR PDBsum; 1MEZ; -.
DR PDBsum; 1MF0; -.
DR PDBsum; 1MF1; -.
DR PDBsum; 2DGN; -.
DR AlphaFoldDB; P28650; -.
DR SMR; P28650; -.
DR BioGRID; 198010; 6.
DR STRING; 10090.ENSMUSP00000136572; -.
DR iPTMnet; P28650; -.
DR PhosphoSitePlus; P28650; -.
DR SwissPalm; P28650; -.
DR jPOST; P28650; -.
DR MaxQB; P28650; -.
DR PaxDb; P28650; -.
DR PeptideAtlas; P28650; -.
DR PRIDE; P28650; -.
DR ProteomicsDB; 302033; -. [P28650-1]
DR ProteomicsDB; 302034; -. [P28650-2]
DR Antibodypedia; 28209; 98 antibodies from 17 providers.
DR DNASU; 11565; -.
DR Ensembl; ENSMUST00000021726; ENSMUSP00000021726; ENSMUSG00000011148. [P28650-1]
DR GeneID; 11565; -.
DR KEGG; mmu:11565; -.
DR UCSC; uc007peu.2; mouse. [P28650-1]
DR CTD; 11565; -.
DR MGI; MGI:87947; Adssl1.
DR VEuPathDB; HostDB:ENSMUSG00000011148; -.
DR eggNOG; KOG1355; Eukaryota.
DR GeneTree; ENSGT00390000015553; -.
DR HOGENOM; CLU_029848_0_0_1; -.
DR InParanoid; P28650; -.
DR OMA; RYAHMLN; -.
DR PhylomeDB; P28650; -.
DR BRENDA; 6.3.4.4; 3474.
DR Reactome; R-MMU-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00075; UER00335.
DR BioGRID-ORCS; 11565; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Adssl1; mouse.
DR EvolutionaryTrace; P28650; -.
DR PRO; PR:P28650; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P28650; protein.
DR Bgee; ENSMUSG00000011148; Expressed in triceps brachii and 212 other tissues.
DR ExpressionAtlas; P28650; baseline and differential.
DR Genevisible; P28650; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006167; P:AMP biosynthetic process; ISO:MGI.
DR GO; GO:0044209; P:AMP salvage; IDA:MGI.
DR GO; GO:0006531; P:aspartate metabolic process; ISO:MGI.
DR GO; GO:0046040; P:IMP metabolic process; ISO:MGI.
DR GO; GO:0006163; P:purine nucleotide metabolic process; IDA:MGI.
DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; ISO:MGI.
DR CDD; cd03108; AdSS; 1.
DR Gene3D; 1.10.300.10; -; 1.
DR Gene3D; 3.40.440.10; -; 1.
DR Gene3D; 3.90.170.10; -; 1.
DR HAMAP; MF_00011; Adenylosucc_synth; 1.
DR HAMAP; MF_03126; Adenylosucc_synth_vert_basic; 1.
DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
DR InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR InterPro; IPR042110; Adenylosuccinate_synth_dom2.
DR InterPro; IPR042111; Adenylosuccinate_synth_dom3.
DR InterPro; IPR001114; Adenylosuccinate_synthetase.
DR InterPro; IPR027509; AdSS_1_vert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11846; PTHR11846; 1.
DR Pfam; PF00709; Adenylsucc_synt; 1.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00184; purA; 1.
DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; GTP-binding; Ligase;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1..457
FT /note="Adenylosuccinate synthetase isozyme 1"
FT /id="PRO_0000095133"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 43
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT ACT_SITE 71
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126"
FT BINDING 42..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126,
FT ECO:0000269|PubMed:12004071"
FT BINDING 43..46
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 43
FT /ligand="substrate"
FT BINDING 68..71
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 70..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126,
FT ECO:0000269|PubMed:12004071"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 163
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126,
FT ECO:0000269|PubMed:12004071"
FT BINDING 177
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126,
FT ECO:0000269|PubMed:12004071"
FT BINDING 256
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126,
FT ECO:0000269|PubMed:12004071"
FT BINDING 271
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126,
FT ECO:0000269|PubMed:12004071"
FT BINDING 331..337
FT /ligand="substrate"
FT BINDING 335
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126,
FT ECO:0000269|PubMed:12004071"
FT BINDING 337
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126,
FT ECO:0000269|PubMed:12004071"
FT BINDING 363..365
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126,
FT ECO:0000269|PubMed:12004071"
FT BINDING 445..448
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03126,
FT ECO:0000269|PubMed:12004071"
FT VAR_SEQ 136
FT /note="L -> LENEVPHEPLPSASLLPMCWLLAP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008422"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1J4B"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:1IWE"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 139..155
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 189..205
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 214..228
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:1IWE"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 278..284
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 291..304
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:1IWE"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 371..381
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:1LOO"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 400..407
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:1IWE"
FT HELIX 424..437
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:1IWE"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:1IWE"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:1IWE"
SQ SEQUENCE 457 AA; 50254 MW; EBEC85BF907B7FED CRC64;
MSGTRASNDR PPGTGGVKRG RLQQEAAATG SRVTVVLGAQ WGDEGKGKVV DLLATDADIV
SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NTKAVSFIGN GVVIHLPGLF EEAEKNEKKG
LKDWEKRLII SDRAHLVFDF HQAVDGLQEV QRQAQEGKNI GTTKKGIGPT YSSKAARTGL
RICDLLSDFD EFSARFKNLA HQHQSMFPTL EIDVEGQLKR LKGFAERIRP MVRDGVYFMY
EALHGPPKKV LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGDVYGVVKA
YTTRVGIGAF PTEQINEIGD LLQNRGHEWG VTTGRKRRCG WLDLMILRYA HMVNGFTALA
LTKLDILDVL SEIKVGISYK LNGKRIPYFP ANQEILQKVE VEYETLPGWK ADTTGARKWE
DLPPQAQSYV RFVENHMGVA VKWVGVGKSR ESMIQLF
