PUR4_HUMAN
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 03-AUG-2022, entry version 201.
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; 138.
DR IntAct; O15067; 15.
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 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; O15067; -.
DR PeptideAtlas; O15067; -.
DR PRIDE; O15067; -.
DR ProteomicsDB; 48417; -.
DR Antibodypedia; 12486; 138 antibodies from 23 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 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; 38224at2759; -.
DR PhylomeDB; O15067; -.
DR TreeFam; TF106371; -.
DR BioCyc; MetaCyc:HS11329-MON; -.
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; 228 hits in 1091 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 178 other tissues.
DR ExpressionAtlas; O15067; baseline and differential.
DR Genevisible; O15067; HS.
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:0009168; P:purine ribonucleoside monophosphate biosynthetic process; TAS:Reactome.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR Gene3D; 3.30.1330.10; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.650.10; -; 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 Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF55326; SSF55326; 2.
DR SUPFAM; SSF56042; SSF56042; 2.
DR SUPFAM; SSF82697; SSF82697; 1.
DR TIGRFAMs; TIGR01735; FGAM_synt; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
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; AAI46769/
FT 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
