FGGY_HUMAN
ID FGGY_HUMAN Reviewed; 551 AA.
AC Q96C11; B1AK92; B1AK93; B1AK94; B2RDR8; D3DQ56; Q9HA63; Q9NV20;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=FGGY carbohydrate kinase domain-containing protein;
DE AltName: Full=D-ribulokinase FGGY {ECO:0000303|PubMed:27909055};
DE EC=2.7.1.47 {ECO:0000269|PubMed:27909055};
GN Name=FGGY {ECO:0000303|PubMed:27909055};
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 [LARGE SCALE MRNA] (ISOFORMS 2; 3; 5 AND 6).
RC TISSUE=Cerebellum, Mammary gland, Placenta, and Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=27909055; DOI=10.1074/jbc.m116.760744;
RA Singh C., Glaab E., Linster C.L.;
RT "Molecular Identification of d-Ribulokinase in Budding Yeast and Mammals.";
RL J. Biol. Chem. 292:1005-1028(2017).
RN [6]
RP INVOLVEMENT IN SPORADIC AMYOTROPHIC LATERAL SCLEROSIS, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=17671248; DOI=10.1056/nejmoa070174;
RA Dunckley T., Huentelman M.J., Craig D.W., Pearson J.V., Szelinger S.,
RA Joshipura K., Halperin R.F., Stamper C., Jensen K.R., Letizia D.,
RA Hesterlee S.E., Pestronk A., Levine T., Bertorini T., Graves M.C.,
RA Mozaffar T., Jackson C.E., Bosch P., McVey A., Dick A., Barohn R.,
RA Lomen-Hoerth C., Rosenfeld J., O'connor D.T., Zhang K., Crook R.,
RA Ryberg H., Hutton M., Katz J., Simpson E.P., Mitsumoto H., Bowser R.,
RA Miller R.G., Appel S.H., Stephan D.A.;
RT "Whole-genome analysis of sporadic amyotrophic lateral sclerosis.";
RL N. Engl. J. Med. 357:775-788(2007).
CC -!- FUNCTION: Catalyzes ATP-dependent phosphorylation of D-ribulose at C-5
CC to form D-ribulose 5-phosphate. Postulated to function in a metabolite
CC repair mechanism by preventing toxic accumulation of free D-ribulose
CC formed by non-specific phosphatase activities. Alternatively, may play
CC a role in regulating D-ribulose 5-phosphate recycling in the pentose
CC phosphate pathway. Can phosphorylate ribitol with low efficiency.
CC {ECO:0000269|PubMed:27909055}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:17601, ChEBI:CHEBI:15378, ChEBI:CHEBI:17173,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58121, ChEBI:CHEBI:456216;
CC EC=2.7.1.47; Evidence={ECO:0000269|PubMed:27909055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17602;
CC Evidence={ECO:0000305|PubMed:27909055};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=97 uM for D-ribulose {ECO:0000269|PubMed:27909055};
CC KM=1468 uM for ribitol {ECO:0000269|PubMed:27909055};
CC Vmax=5.6 umol/min/mg enzyme toward D-ribulose
CC {ECO:0000269|PubMed:27909055};
CC Vmax=2.4 umol/min/mg enzyme toward ribitol
CC {ECO:0000269|PubMed:27909055};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000305|PubMed:27909055}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q96C11-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96C11-2; Sequence=VSP_032658, VSP_032659;
CC Name=3;
CC IsoId=Q96C11-4; Sequence=VSP_032658;
CC Name=4;
CC IsoId=Q96C11-3; Sequence=VSP_033424;
CC Name=5;
CC IsoId=Q96C11-5; Sequence=VSP_045338;
CC Name=6;
CC IsoId=Q96C11-6; Sequence=VSP_054533;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, lung and small intestine and
CC to a lower extent in liver and detected in cerebrospinal fluid (at
CC protein level). {ECO:0000269|PubMed:17671248}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain (at protein level).
CC {ECO:0000269|PubMed:17671248}.
CC -!- DISEASE: Amyotrophic lateral sclerosis (ALS) [MIM:105400]: A
CC neurodegenerative disorder affecting upper motor neurons in the brain
CC and lower motor neurons in the brain stem and spinal cord, resulting in
CC fatal paralysis. Sensory abnormalities are absent. The pathologic
CC hallmarks of the disease include pallor of the corticospinal tract due
CC to loss of motor neurons, presence of ubiquitin-positive inclusions
CC within surviving motor neurons, and deposition of pathologic
CC aggregates. The etiology of amyotrophic lateral sclerosis is likely to
CC be multifactorial, involving both genetic and environmental factors.
CC The disease is inherited in 5-10% of the cases.
CC {ECO:0000269|PubMed:17671248}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH14947.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK001848; BAA91940.1; -; mRNA.
DR EMBL; AK022237; BAB13993.1; -; mRNA.
DR EMBL; AK054842; BAG51432.1; -; mRNA.
DR EMBL; AK315649; BAG38015.1; -; mRNA.
DR EMBL; AL954338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL713859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX119322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06619.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06621.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06622.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06623.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06624.1; -; Genomic_DNA.
DR EMBL; BC014947; AAH14947.1; ALT_INIT; mRNA.
DR CCDS; CCDS44155.1; -. [Q96C11-3]
DR CCDS; CCDS58003.1; -. [Q96C11-5]
DR CCDS; CCDS60155.1; -. [Q96C11-6]
DR CCDS; CCDS611.2; -. [Q96C11-1]
DR RefSeq; NP_001106882.1; NM_001113411.1. [Q96C11-3]
DR RefSeq; NP_001231643.1; NM_001244714.1. [Q96C11-5]
DR RefSeq; NP_001265153.1; NM_001278224.1. [Q96C11-6]
DR RefSeq; NP_060761.3; NM_018291.3. [Q96C11-1]
DR RefSeq; XP_011540032.1; XM_011541730.1. [Q96C11-3]
DR RefSeq; XP_011540033.1; XM_011541731.1. [Q96C11-3]
DR RefSeq; XP_011540034.1; XM_011541732.1.
DR RefSeq; XP_011540035.1; XM_011541733.1.
DR RefSeq; XP_011540037.1; XM_011541735.1.
DR RefSeq; XP_016857132.1; XM_017001643.1. [Q96C11-3]
DR RefSeq; XP_016857133.1; XM_017001644.1.
DR RefSeq; XP_016857134.1; XM_017001645.1. [Q96C11-1]
DR RefSeq; XP_016857135.1; XM_017001646.1. [Q96C11-1]
DR RefSeq; XP_016857136.1; XM_017001647.1.
DR RefSeq; XP_016857155.1; XM_017001666.1.
DR RefSeq; XP_016857156.1; XM_017001667.1.
DR RefSeq; XP_016857161.1; XM_017001672.1.
DR RefSeq; XP_016857162.1; XM_017001673.1. [Q96C11-4]
DR AlphaFoldDB; Q96C11; -.
DR SMR; Q96C11; -.
DR BioGRID; 120565; 4.
DR IntAct; Q96C11; 3.
DR STRING; 9606.ENSP00000360262; -.
DR iPTMnet; Q96C11; -.
DR PhosphoSitePlus; Q96C11; -.
DR BioMuta; FGGY; -.
DR DMDM; 172045850; -.
DR EPD; Q96C11; -.
DR MassIVE; Q96C11; -.
DR MaxQB; Q96C11; -.
DR PaxDb; Q96C11; -.
DR PeptideAtlas; Q96C11; -.
DR PRIDE; Q96C11; -.
DR ProteomicsDB; 3030; -.
DR ProteomicsDB; 76142; -. [Q96C11-1]
DR ProteomicsDB; 76143; -. [Q96C11-2]
DR ProteomicsDB; 76144; -. [Q96C11-3]
DR ProteomicsDB; 76145; -. [Q96C11-4]
DR ProteomicsDB; 82738; -.
DR Antibodypedia; 33269; 122 antibodies from 22 providers.
DR DNASU; 55277; -.
DR Ensembl; ENST00000303721.12; ENSP00000305922.8; ENSG00000172456.18. [Q96C11-1]
DR Ensembl; ENST00000371210.1; ENSP00000360254.1; ENSG00000172456.18. [Q96C11-6]
DR Ensembl; ENST00000371212.5; ENSP00000360256.1; ENSG00000172456.18. [Q96C11-5]
DR Ensembl; ENST00000371218.8; ENSP00000360262.4; ENSG00000172456.18. [Q96C11-3]
DR Ensembl; ENST00000635156.1; ENSP00000489417.1; ENSG00000172456.18. [Q96C11-5]
DR GeneID; 55277; -.
DR KEGG; hsa:55277; -.
DR MANE-Select; ENST00000303721.12; ENSP00000305922.8; NM_018291.5; NP_060761.3.
DR UCSC; uc001czi.6; human. [Q96C11-1]
DR CTD; 55277; -.
DR DisGeNET; 55277; -.
DR GeneCards; FGGY; -.
DR HGNC; HGNC:25610; FGGY.
DR HPA; ENSG00000172456; Tissue enhanced (liver).
DR MIM; 105400; phenotype.
DR MIM; 611370; gene.
DR neXtProt; NX_Q96C11; -.
DR OpenTargets; ENSG00000172456; -.
DR PharmGKB; PA162388453; -.
DR VEuPathDB; HostDB:ENSG00000172456; -.
DR eggNOG; KOG2517; Eukaryota.
DR GeneTree; ENSGT01000000214434; -.
DR HOGENOM; CLU_009281_10_0_1; -.
DR InParanoid; Q96C11; -.
DR OMA; GHKAMWH; -.
DR OrthoDB; 1252682at2759; -.
DR PhylomeDB; Q96C11; -.
DR TreeFam; TF300904; -.
DR BioCyc; MetaCyc:ENSG00000172456-MON; -.
DR BRENDA; 2.7.1.47; 2681.
DR PathwayCommons; Q96C11; -.
DR SignaLink; Q96C11; -.
DR UniPathway; UPA00246; -.
DR BioGRID-ORCS; 55277; 6 hits in 1076 CRISPR screens.
DR ChiTaRS; FGGY; human.
DR GenomeRNAi; 55277; -.
DR Pharos; Q96C11; Tbio.
DR PRO; PR:Q96C11; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96C11; protein.
DR Bgee; ENSG00000172456; Expressed in right lobe of liver and 128 other tissues.
DR ExpressionAtlas; Q96C11; baseline and differential.
DR Genevisible; Q96C11; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019150; F:D-ribulokinase activity; IDA:SGD.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IDA:UniProtKB.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:UniProtKB.
DR GO; GO:0019321; P:pentose metabolic process; IDA:SGD.
DR CDD; cd07782; FGGY_YpCarbK_like; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR006003; FGGY_RbtK-like.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01315; 5C_CHO_kinase; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amyotrophic lateral sclerosis; Kinase;
KW Neurodegeneration; Reference proteome; Transferase.
FT CHAIN 1..551
FT /note="FGGY carbohydrate kinase domain-containing protein"
FT /id="PRO_0000326452"
FT VAR_SEQ 1..299
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054533"
FT VAR_SEQ 1..112
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032658"
FT VAR_SEQ 68..155
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045338"
FT VAR_SEQ 359..551
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032659"
FT VAR_SEQ 407
FT /note="M -> MRTTGYLYIPALAALHSPSSLLSPQ (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_033424"
FT VARIANT 43
FT /note="N -> K (in dbSNP:rs835409)"
FT /id="VAR_059193"
FT VARIANT 134
FT /note="L -> V (in dbSNP:rs11207463)"
FT /id="VAR_040072"
FT VARIANT 246
FT /note="L -> V (in dbSNP:rs11207463)"
FT /id="VAR_059194"
SQ SEQUENCE 551 AA; 59993 MW; 938946C33E6DC78F CRC64;
MSGGEQKPER YYVGVDVGTG SVRAALVDQS GVLLAFADQP IKNWEPQFNH HEQSSEDIWA
ACCVVTKKVV QGIDLNQIRG LGFDATCSLV VLDKQFHPLP VNQEGDSHRN VIMWLDHRAV
SQVNRINETK HSVLQYVGGV MSVEMQAPKL LWLKENLREI CWDKAGHFFD LPDFLSWKAT
GVTARSLCSL VCKWTYSAEK GWDDSFWKMI GLEDFVADNY SKIGNQVLPP GASLGNGLTP
EAARDLGLLP GIAVAASLID AHAGGLGVIG ADVRGHGLIC EGQPVTSRLA VICGTSSCHM
GISKDPIFVP GVWGPYFSAM VPGFWLNEGG QSVTGKLIDH MVQGHAAFPE LQVKATARCQ
SIYAYLNSHL DLIKKAQPVG FLTVDLHVWP DFHGNRSPLA DLTLKGMVTG LKLSQDLDDL
AILYLATVQA IALGTRFIIE AMEAAGHSIS TLFLCGGLSK NPLFVQMHAD ITGMPVVLSQ
EVESVLVGAA VLGACASGDF ASVQEAMAKM SKVGKVVFPR LQDKKYYDKK YQVFLKLVEH
QKEYLAIMND D
