ID   PUR4_HUMAN              Reviewed;        1338 AA.
AC   O15067; A6H8V8;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 4.
DT   27-MAR-2024, entry version 210.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase;
DE            Short=FGAM synthase;
DE            Short=FGAMS;
DE            EC=6.3.5.3 {ECO:0000305|PubMed:10548741};
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase;
DE            Short=FGAR amidotransferase;
DE            Short=FGAR-AT {ECO:0000303|PubMed:10548741};
DE   AltName: Full=Formylglycinamide ribotide amidotransferase;
DE   AltName: Full=Phosphoribosylformylglycineamide amidotransferase {ECO:0000303|PubMed:10548741};
GN   Name=PFAS; Synonyms=KIAA0361;
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], VARIANTS SER-19; LEU-367 AND PRO-621, FUNCTION,
RP   AND CATALYTIC ACTIVITY.
RX   PubMed=10548741; DOI=10.1016/s0378-1119(99)00378-9;
RA   Patterson D., Bleskan J., Gardiner K., Bowersox J.;
RT   "Human phosphoribosylformylglycinamide amidotransferase (FGARAT): regional
RT   mapping, complete coding sequence, isolation of a functional genomic clone,
RT   and DNA sequence analysis.";
RL   Gene 239:381-391(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-19; LEU-367 AND
RP   PRO-621.
RC   TISSUE=Brain;
RX   PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA   Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VII. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 4:141-150(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-19; LEU-367 AND
RP   PRO-621.
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-619 AND THR-623, VARIANT
RP   [LARGE SCALE ANALYSIS] PRO-621, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569 AND THR-619, VARIANT
RP   [LARGE SCALE ANALYSIS] PRO-621, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [8]
RP   IDENTIFICATION BY MASS 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).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, VARIANT [LARGE SCALE
RP   ANALYSIS] PRO-621, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND SER-569, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
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   [12]
RP   VARIANT [LARGE SCALE ANALYSIS] PRO-621, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
CC   -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the
CC       purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of
CC       formylglycinamide ribonucleotide (FGAR) and glutamine to yield
CC       formylglycinamidine ribonucleotide (FGAM) and glutamate.
CC       {ECO:0000305|PubMed:10548741}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC         ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC         ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC         ChEBI:CHEBI:456216; EC=6.3.5.3;
CC         Evidence={ECO:0000305|PubMed:10548741};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17130;
CC         Evidence={ECO:0000305|PubMed:10548741};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC       phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000305|PubMed:10548741}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA20816.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB002359; BAA20816.1; ALT_INIT; mRNA.
DR   EMBL; AC135178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC146768; AAI46769.1; -; mRNA.
DR   EMBL; BC167158; AAI67158.1; -; mRNA.
DR   CCDS; CCDS11136.1; -.
DR   RefSeq; NP_036525.1; NM_012393.2.
DR   AlphaFoldDB; O15067; -.
DR   SMR; O15067; -.
DR   BioGRID; 111221; 171.
DR   IntAct; O15067; 17.
DR   MINT; O15067; -.
DR   STRING; 9606.ENSP00000313490; -.
DR   ChEMBL; CHEMBL4295655; -.
DR   DrugBank; DB00142; Glutamic acid.
DR   DrugBank; DB00130; L-Glutamine.
DR   MEROPS; C56.972; -.
DR   GlyCosmos; O15067; 1 site, 1 glycan.
DR   GlyGen; O15067; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O15067; -.
DR   MetOSite; O15067; -.
DR   PhosphoSitePlus; O15067; -.
DR   SwissPalm; O15067; -.
DR   BioMuta; PFAS; -.
DR   EPD; O15067; -.
DR   jPOST; O15067; -.
DR   MassIVE; O15067; -.
DR   MaxQB; O15067; -.
DR   PaxDb; 9606-ENSP00000313490; -.
DR   PeptideAtlas; O15067; -.
DR   ProteomicsDB; 48417; -.
DR   Pumba; O15067; -.
DR   Antibodypedia; 12486; 171 antibodies from 25 providers.
DR   DNASU; 5198; -.
DR   Ensembl; ENST00000314666.11; ENSP00000313490.6; ENSG00000178921.14.
DR   GeneID; 5198; -.
DR   KEGG; hsa:5198; -.
DR   MANE-Select; ENST00000314666.11; ENSP00000313490.6; NM_012393.3; NP_036525.1.
DR   UCSC; uc002gkr.4; human.
DR   AGR; HGNC:8863; -.
DR   CTD; 5198; -.
DR   DisGeNET; 5198; -.
DR   GeneCards; PFAS; -.
DR   HGNC; HGNC:8863; PFAS.
DR   HPA; ENSG00000178921; Low tissue specificity.
DR   MalaCards; PFAS; -.
DR   MIM; 602133; gene.
DR   neXtProt; NX_O15067; -.
DR   OpenTargets; ENSG00000178921; -.
DR   VEuPathDB; HostDB:ENSG00000178921; -.
DR   eggNOG; KOG1907; Eukaryota.
DR   GeneTree; ENSGT00390000007600; -.
DR   HOGENOM; CLU_001031_0_0_1; -.
DR   InParanoid; O15067; -.
DR   OMA; LSANWMW; -.
DR   OrthoDB; 2891567at2759; -.
DR   PhylomeDB; O15067; -.
DR   TreeFam; TF106371; -.
DR   BioCyc; MetaCyc:HS11329-MONOMER; -.
DR   BRENDA; 6.3.5.3; 2681.
DR   PathwayCommons; O15067; -.
DR   Reactome; R-HSA-73817; Purine ribonucleoside monophosphate biosynthesis.
DR   SignaLink; O15067; -.
DR   SIGNOR; O15067; -.
DR   UniPathway; UPA00074; UER00128.
DR   BioGRID-ORCS; 5198; 256 hits in 1169 CRISPR screens.
DR   ChiTaRS; PFAS; human.
DR   GenomeRNAi; 5198; -.
DR   Pharos; O15067; Tbio.
DR   PRO; PR:O15067; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; O15067; Protein.
DR   Bgee; ENSG00000178921; Expressed in ventricular zone and 179 other cell types or tissues.
DR   ExpressionAtlas; O15067; baseline and differential.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IDA:UniProtKB.
DR   GO; GO:0044208; P:'de novo' AMP biosynthetic process; IDA:MGI.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IDA:MGI.
DR   GO; GO:0097294; P:'de novo' XMP biosynthetic process; IDA:MGI.
DR   GO; GO:0097065; P:anterior head development; IEA:Ensembl.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; IDA:MGI.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; TAS:Reactome.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   CDD; cd01740; GATase1_FGAR_AT; 1.
DR   CDD; cd02203; PurL_repeat1; 1.
DR   CDD; cd02204; PurL_repeat2; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR   HAMAP; MF_00419; PurL_1; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR040707; FGAR-AT_N.
DR   InterPro; IPR010073; PurL_large.
DR   InterPro; IPR041609; PurL_linker.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   InterPro; IPR036604; PurS-like_sf.
DR   NCBIfam; TIGR01735; FGAM_synt; 1.
DR   PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   Pfam; PF02769; AIRS_C; 2.
DR   Pfam; PF18072; FGAR-AT_linker; 1.
DR   Pfam; PF18076; FGAR-AT_N; 1.
DR   Pfam; PF13507; GATase_5; 1.
DR   SMART; SM01211; GATase_5; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF109736; FGAM synthase PurL, linker domain; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR   SUPFAM; SSF82697; PurS-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   Genevisible; O15067; HS.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Glutamine amidotransferase; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..1338
FT                   /note="Phosphoribosylformylglycinamidine synthase"
FT                   /id="PRO_0000100401"
FT   DOMAIN          1064..1302
FT                   /note="Glutamine amidotransferase type-1"
FT   ACT_SITE        1158
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1297
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1299
FT                   /evidence="ECO:0000250"
FT   BINDING         322..333
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         402..404
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         706
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         707
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         746
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         750
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         909
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         911
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         215
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         569
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         619
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         623
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   VARIANT         19
FT                   /note="P -> S (in dbSNP:rs9891699)"
FT                   /evidence="ECO:0000269|PubMed:10548741,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9205841"
FT                   /id="VAR_055008"
FT   VARIANT         367
FT                   /note="P -> L (in dbSNP:rs4791641)"
FT                   /evidence="ECO:0000269|PubMed:10548741,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9205841"
FT                   /id="VAR_055009"
FT   VARIANT         481
FT                   /note="F -> Y (in dbSNP:rs35217368)"
FT                   /id="VAR_055010"
FT   VARIANT         621
FT                   /note="L -> P (in dbSNP:rs11078738)"
FT                   /evidence="ECO:0000269|PubMed:10548741,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9205841,
FT                   ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT                   /id="VAR_055011"
FT   CONFLICT        1326
FT                   /note="F -> S (in Ref. 1, 2; BAA20816 and 4;
FT                   AAI46769/AAI67158)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1338 AA;  144734 MW;  273405025B701DAF CRC64;
     MSPVLHFYVR PSGHEGAAPG HTRRKLQGKL PELQGVETEL CYNVNWTAEA LPSAEETKKL
     MWLFGCPLLL DDVARESWLL PGSNDLLLEV GPRLNFSTPT STNIVSVCRA TGLGPVDRVE
     TTRRYRLSFA HPPSAEVEAI ALATLHDRMT EQHFPHPIQS FSPESMPEPL NGPINILGEG
     RLALEKANQE LGLALDSWDL DFYTKRFQEL QRNPSTVEAF DLAQSNSEHS RHWFFKGQLH
     VDGQKLVHSL FESIMSTQES SNPNNVLKFC DNSSAIQGKE VRFLRPEDPT RPSRFQQQQG
     LRHVVFTAET HNFPTGVCPF SGATTGTGGR IRDVQCTGRG AHVVAGTAGY CFGNLHIPGY
     NLPWEDPSFQ YPGNFARPLE VAIEASNGAS DYGNKFGEPV LAGFARSLGL QLPDGQRREW
     IKPIMFSGGI GSMEADHISK EAPEPGMEVV KVGGPVYRIG VGGGAASSVQ VQGDNTSDLD
     FGAVQRGDPE MEQKMNRVIR ACVEAPKGNP ICSLHDQGAG GNGNVLKELS DPAGAIIYTS
     RFQLGDPTLN ALEIWGAEYQ ESNALLLRSP NRDFLTHVSA RERCPACFVG TITGDRRIVL
     VDDRECPVRR NGQGDAPPTP LPTPVDLELE WVLGKMPRKE FFLQRKPPML QPLALPPGLS
     VHQALERVLR LPAVASKRYL TNKVDRSVGG LVAQQQCVGP LQTPLADVAV VALSHEELIG
     AATALGEQPV KSLLDPKVAA RLAVAEALTN LVFALVTDLR DVKCSGNWMW AAKLPGEGAA
     LADACEAMVA VMAALGVAVD GGKDSLSMAA RVGTETVRAP GSLVISAYAV CPDITATVTP
     DLKHPEGRGH LLYVALSPGQ HRLGGTALAQ CFSQLGEHPP DLDLPENLVR AFSITQGLLK
     DRLLCSGHDV SDGGLVTCLL EMAFAGNCGL QVDVPVPRVD VLSVLFAEEP GLVLEVQEPD
     LAQVLKRYRD AGLHCLELGH TGEAGPHAMV RVSVNGAVVL EEPVGELRAL WEETSFQLDR
     LQAEPRCVAE EERGLRERMG PSYCLPPTFP KASVPREPGG PSPRVAILRE EGSNGDREMA
     DAFHLAGFEV WDVTMQDLCS GAIGLDTFRG VAFVGGFSYA DVLGSAKGWA AAVTFHPRAG
     AELRRFRKRP DTFSLGVCNG CQLLALLGWV GGDPNEDAAE MGPDSQPARP GLLLRHNLSG
     RYESRWASVR VGPGPALMLR GMEGAVLPVW SAHGEGYVAF SSPELQAQIE ARGLAPLHWA
     DDDGNPTEQY PLNPNGSPGG VAGICSCDGR HLAVMPHPER AVRPWQWAWR PPPFDTLTTS
     PWLQLFINAR NWTLEGSC
//