NADC_HUMAN
ID NADC_HUMAN Reviewed; 297 AA.
AC Q15274; Q53XW7; Q96G22; Q9BSG6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating];
DE EC=2.4.2.19 {ECO:0000269|PubMed:17868694, ECO:0000269|PubMed:24038671, ECO:0000269|PubMed:9473669};
DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating];
DE Short=QAPRTase;
DE Short=QPRTase;
GN Name=QPRT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP VARIANT ALA-195.
RC TISSUE=Brain;
RX PubMed=9473669; DOI=10.1016/s0167-4781(97)00143-7;
RA Fukuoka S., Nyaruhucha C.M., Shibata K.;
RT "Characterization and functional expression of the cDNA encoding human
RT brain quinolinate phosphoribosyltransferase.";
RL Biochim. Biophys. Acta 1395:192-201(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-195.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-195.
RC TISSUE=Kidney, Muscle, and Placenta;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP MUTAGENESIS OF ARG-102; ARG-138; LYS-139; ARG-161 AND LYS-171, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, AND SUBUNIT.
RX PubMed=17868694; DOI=10.1016/j.jmb.2007.08.043;
RA Liu H., Woznica K., Catton G., Crawford A., Botting N., Naismith J.H.;
RT "Structural and kinetic characterization of quinolinate
RT phosphoribosyltransferase (hQPRTase) from homo sapiens.";
RL J. Mol. Biol. 373:755-763(2007).
RN [6] {ECO:0007744|PDB:4KWV, ECO:0007744|PDB:4KWW}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN APO FORM AND IN COMPLEX WITH
RP INHIBITOR PHT, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY,
RP AND SUBUNIT.
RX PubMed=24038671; DOI=10.1002/prot.24406;
RA Malik S.S., Patterson D.N., Ncube Z., Toth E.A.;
RT "The crystal structure of human quinolinic acid phosphoribosyltransferase
RT in complex with its inhibitor phthalic acid.";
RL Proteins 82:405-414(2014).
RN [7] {ECO:0007744|PDB:5AYX, ECO:0007744|PDB:5AYY, ECO:0007744|PDB:5AYZ}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN APO FORM; IN COMPLEX WITH
RP QUINOLINATE AND IN COMPLEX WITH NICOTINATE MONONUCLEOTIDE, SUBUNIT, AND
RP MUTAGENESIS OF 1-MET--GLU-4; 1-MET--LEU-8; 1-MET--LEU-9; 1-MET--LEU-10 AND
RP 1-MET--PRO-12.
RX PubMed=26805589; DOI=10.1038/srep19681;
RA Youn H.S., Kim T.G., Kim M.K., Kang G.B., Kang J.Y., Lee J.G., An J.Y.,
RA Park K.R., Lee Y., Im Y.J., Lee J.H., Eom S.H.;
RT "Structural Insights into the Quaternary Catalytic Mechanism of Hexameric
RT Human Quinolinate Phosphoribosyltransferase, a Key Enzyme in de novo NAD
RT Biosynthesis.";
RL Sci. Rep. 6:19681-19681(2016).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-195, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC {ECO:0000269|PubMed:17868694, ECO:0000269|PubMed:24038671,
CC ECO:0000269|PubMed:9473669}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CO2 + diphosphate + nicotinate beta-D-ribonucleotide = 5-
CC phospho-alpha-D-ribose 1-diphosphate + 2 H(+) + quinolinate;
CC Xref=Rhea:RHEA:12733, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:29959, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC ChEBI:CHEBI:58017; EC=2.4.2.19;
CC Evidence={ECO:0000269|PubMed:17868694, ECO:0000269|PubMed:24038671,
CC ECO:0000269|PubMed:9473669};
CC -!- ACTIVITY REGULATION: Activity toward QA is slightly repressed by
CC phosphoribosylpyrophosphate (PRPP) in both a competitive and a non-
CC competitive manner (PubMed:17868694). Competitively inhibited by
CC phthalic acid (PHT) (PubMed:24038671). {ECO:0000269|PubMed:17868694,
CC ECO:0000269|PubMed:24038671}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for QA (at 0.1 mM PRPP) {ECO:0000269|PubMed:17868694};
CC KM=23 uM for QA (at 0.3 mM PRPP) {ECO:0000269|PubMed:17868694};
CC Vmax=1.2 uM/min/mg enzyme (at 0.3 mM QA and 0.1 mM PRPP)
CC {ECO:0000269|PubMed:17868694};
CC Vmax=0.93 uM/min/mg enzyme (at 0.3 mM QA and 0.3 mM PRPP)
CC {ECO:0000269|PubMed:17868694};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from quinolinate: step 1/1.
CC {ECO:0000269|PubMed:17868694, ECO:0000269|PubMed:24038671,
CC ECO:0000269|PubMed:9473669}.
CC -!- SUBUNIT: Hexamer formed by 3 homodimers. {ECO:0000269|PubMed:17868694,
CC ECO:0000269|PubMed:24038671, ECO:0000269|PubMed:26805589}.
CC -!- INTERACTION:
CC Q15274; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-739851, EBI-10173507;
CC Q15274; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-739851, EBI-11959885;
CC Q15274; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-739851, EBI-10171774;
CC Q15274; Q9NZ94-2: NLGN3; NbExp=4; IntAct=EBI-739851, EBI-16423037;
CC Q15274; Q15274: QPRT; NbExp=3; IntAct=EBI-739851, EBI-739851;
CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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DR EMBL; D78177; BAA11242.1; -; mRNA.
DR EMBL; BT007231; AAP35895.1; -; mRNA.
DR EMBL; BC005060; AAH05060.1; -; mRNA.
DR EMBL; BC010033; AAH10033.1; -; mRNA.
DR EMBL; BC018910; AAH18910.1; -; mRNA.
DR CCDS; CCDS10651.1; -.
DR PIR; T46864; T46864.
DR RefSeq; NP_001305178.1; NM_001318249.1.
DR RefSeq; NP_001305179.1; NM_001318250.1.
DR RefSeq; NP_055113.2; NM_014298.4.
DR PDB; 2JBM; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-297.
DR PDB; 4KWV; X-ray; 2.80 A; A/B/C/D/E/F=1-297.
DR PDB; 4KWW; X-ray; 2.55 A; A/B/C/D/E/F=1-297.
DR PDB; 5AYX; X-ray; 2.80 A; A/B/C/D/E/F=1-297.
DR PDB; 5AYY; X-ray; 3.09 A; A/B/C/D/E/F/G/H/I=1-297.
DR PDB; 5AYZ; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=1-297.
DR PDBsum; 2JBM; -.
DR PDBsum; 4KWV; -.
DR PDBsum; 4KWW; -.
DR PDBsum; 5AYX; -.
DR PDBsum; 5AYY; -.
DR PDBsum; 5AYZ; -.
DR AlphaFoldDB; Q15274; -.
DR SMR; Q15274; -.
DR BioGRID; 117035; 84.
DR IntAct; Q15274; 40.
DR STRING; 9606.ENSP00000378782; -.
DR DrugBank; DB00627; Niacin.
DR DrugCentral; Q15274; -.
DR iPTMnet; Q15274; -.
DR PhosphoSitePlus; Q15274; -.
DR BioMuta; QPRT; -.
DR DMDM; 296439291; -.
DR EPD; Q15274; -.
DR jPOST; Q15274; -.
DR MassIVE; Q15274; -.
DR MaxQB; Q15274; -.
DR PaxDb; Q15274; -.
DR PeptideAtlas; Q15274; -.
DR PRIDE; Q15274; -.
DR ProteomicsDB; 60508; -.
DR Antibodypedia; 26777; 334 antibodies from 26 providers.
DR DNASU; 23475; -.
DR Ensembl; ENST00000395384.9; ENSP00000378782.4; ENSG00000103485.19.
DR Ensembl; ENST00000449759.2; ENSP00000404873.3; ENSG00000103485.19.
DR GeneID; 23475; -.
DR KEGG; hsa:23475; -.
DR MANE-Select; ENST00000395384.9; ENSP00000378782.4; NM_014298.6; NP_055113.3.
DR UCSC; uc002dto.4; human.
DR CTD; 23475; -.
DR DisGeNET; 23475; -.
DR GeneCards; QPRT; -.
DR HGNC; HGNC:9755; QPRT.
DR HPA; ENSG00000103485; Tissue enhanced (kidney, liver).
DR MIM; 606248; gene.
DR neXtProt; NX_Q15274; -.
DR OpenTargets; ENSG00000103485; -.
DR PharmGKB; PA34096; -.
DR VEuPathDB; HostDB:ENSG00000103485; -.
DR eggNOG; KOG3008; Eukaryota.
DR GeneTree; ENSGT00390000002761; -.
DR HOGENOM; CLU_039622_1_1_1; -.
DR InParanoid; Q15274; -.
DR OMA; DMIMLKD; -.
DR OrthoDB; 1263431at2759; -.
DR PhylomeDB; Q15274; -.
DR TreeFam; TF300845; -.
DR BioCyc; MetaCyc:HS02508-MON; -.
DR BRENDA; 2.4.2.19; 2681.
DR PathwayCommons; Q15274; -.
DR Reactome; R-HSA-196807; Nicotinate metabolism.
DR SignaLink; Q15274; -.
DR UniPathway; UPA00253; UER00331.
DR BioGRID-ORCS; 23475; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; QPRT; human.
DR EvolutionaryTrace; Q15274; -.
DR GenomeRNAi; 23475; -.
DR Pharos; Q15274; Tbio.
DR PRO; PR:Q15274; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q15274; protein.
DR Bgee; ENSG00000103485; Expressed in right adrenal gland cortex and 165 other tissues.
DR ExpressionAtlas; Q15274; baseline and differential.
DR Genevisible; Q15274; HS.
DR GO; GO:1902494; C:catalytic complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IDA:UniProtKB.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR GO; GO:0019674; P:NAD metabolic process; TAS:Reactome.
DR GO; GO:0034213; P:quinolinate catabolic process; IDA:UniProtKB.
DR CDD; cd01572; QPRTase; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.90.1170.20; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004393; NadC.
DR InterPro; IPR027277; NadC/ModD.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf.
DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR InterPro; IPR022412; Quinolinate_PRibosylTrfase_N.
DR PANTHER; PTHR32179; PTHR32179; 1.
DR Pfam; PF01729; QRPTase_C; 1.
DR Pfam; PF02749; QRPTase_N; 1.
DR PIRSF; PIRSF006250; NadC_ModD; 1.
DR SUPFAM; SSF51690; SSF51690; 1.
DR TIGRFAMs; TIGR00078; nadC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Pyridine nucleotide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..297
FT /note="Nicotinate-nucleotide pyrophosphorylase
FT [carboxylating]"
FT /id="PRO_0000155954"
FT REGION 8..12
FT /note="Important for hexamer formation"
FT /evidence="ECO:0000269|PubMed:26805589"
FT BINDING 102
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000269|PubMed:26805589,
FT ECO:0000305|PubMed:17868694, ECO:0000305|PubMed:24038671,
FT ECO:0007744|PDB:2JBM, ECO:0007744|PDB:4KWW,
FT ECO:0007744|PDB:5AYY"
FT BINDING 138..139
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000269|PubMed:26805589,
FT ECO:0000305|PubMed:17868694, ECO:0000305|PubMed:24038671,
FT ECO:0007744|PDB:2JBM, ECO:0007744|PDB:4KWW,
FT ECO:0007744|PDB:5AYY, ECO:0007744|PDB:5AYZ"
FT BINDING 160..161
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000269|PubMed:26805589,
FT ECO:0000305|PubMed:17868694, ECO:0000305|PubMed:24038671,
FT ECO:0007744|PDB:2JBM, ECO:0007744|PDB:4KWW,
FT ECO:0007744|PDB:5AYY, ECO:0007744|PDB:5AYZ"
FT BINDING 171
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000269|PubMed:26805589,
FT ECO:0000305|PubMed:24038671, ECO:0007744|PDB:2JBM,
FT ECO:0007744|PDB:4KWW, ECO:0007744|PDB:5AYY,
FT ECO:0007744|PDB:5AYZ"
FT BINDING 201
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000269|PubMed:26805589,
FT ECO:0007744|PDB:5AYZ"
FT BINDING 222
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000269|PubMed:26805589,
FT ECO:0007744|PDB:5AYZ"
FT BINDING 248..250
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000269|PubMed:26805589,
FT ECO:0007744|PDB:5AYZ"
FT BINDING 270
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000269|PubMed:26805589,
FT ECO:0007744|PDB:5AYZ"
FT VARIANT 158
FT /note="A -> V (in dbSNP:rs2303255)"
FT /id="VAR_021915"
FT VARIANT 195
FT /note="T -> A (in dbSNP:rs9932770)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9473669, ECO:0000269|Ref.2,
FT ECO:0007744|PubMed:21269460"
FT /id="VAR_050219"
FT MUTAGEN 1..12
FT /note="Missing: Forms dimers instead of hexamers."
FT /evidence="ECO:0000269|PubMed:26805589"
FT MUTAGEN 1..10
FT /note="Missing: Forms dimers instead of hexamers."
FT /evidence="ECO:0000269|PubMed:26805589"
FT MUTAGEN 1..9
FT /note="Missing: Forms dimers instead of hexamers."
FT /evidence="ECO:0000269|PubMed:26805589"
FT MUTAGEN 1..8
FT /note="Missing: Forms dimers instead of hexamers."
FT /evidence="ECO:0000269|PubMed:26805589"
FT MUTAGEN 1..4
FT /note="Missing: No effect on hexamer formation."
FT /evidence="ECO:0000269|PubMed:26805589"
FT MUTAGEN 102
FT /note="R->A,Q: Reduced activity."
FT /evidence="ECO:0000269|PubMed:17868694"
FT MUTAGEN 138
FT /note="R->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17868694"
FT MUTAGEN 139
FT /note="K->A,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17868694"
FT MUTAGEN 161
FT /note="R->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:17868694"
FT MUTAGEN 161
FT /note="R->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17868694"
FT MUTAGEN 171
FT /note="K->A,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17868694"
FT CONFLICT 53
FT /note="V -> I (in Ref. 2; AAP35895 and 3; AAH05060)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="V -> L (in Ref. 1; BAA11242)"
FT /evidence="ECO:0000305"
FT CONFLICT 177..178
FT /note="AA -> PP (in Ref. 1; BAA11242)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="A -> V (in Ref. 1; BAA11242)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="V -> A (in Ref. 1; BAA11242)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="A -> V (in Ref. 1; BAA11242)"
FT /evidence="ECO:0000305"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:2JBM"
FT HELIX 12..26
FT /evidence="ECO:0007829|PDB:2JBM"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:2JBM"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:2JBM"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:5AYX"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:2JBM"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:2JBM"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:2JBM"
FT HELIX 94..127
FT /evidence="ECO:0007829|PDB:2JBM"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:2JBM"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:2JBM"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:5AYX"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:2JBM"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:2JBM"
FT HELIX 181..192
FT /evidence="ECO:0007829|PDB:2JBM"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:2JBM"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:2JBM"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:2JBM"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:2JBM"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:2JBM"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:2JBM"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:2JBM"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:2JBM"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:2JBM"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:2JBM"
FT STRAND 281..288
FT /evidence="ECO:0007829|PDB:2JBM"
SQ SEQUENCE 297 AA; 30846 MW; E3199814DB9FA0D5 CRC64;
MDAEGLALLL PPVTLAALVD SWLREDCPGL NYAALVSGAG PSQAALWAKS PGVLAGQPFF
DAIFTQLNCQ VSWFLPEGSK LVPVARVAEV RGPAHCLLLG ERVALNTLAR CSGIASAAAA
AVEAARGAGW TGHVAGTRKT TPGFRLVEKY GLLVGGAASH RYDLGGLVMV KDNHVVAAGG
VEKAVRAARQ AADFTLKVEV ECSSLQEAVQ AAEAGADLVL LDNFKPEELH PTATVLKAQF
PSVAVEASGG ITLDNLPQFC GPHIDVISMG MLTQAAPALD FSLKLFAKEV APVPKIH
