GNPI2_HUMAN
ID GNPI2_HUMAN Reviewed; 276 AA.
AC Q8TDQ7; B4DJF3; Q2VYF1; Q59EA7; Q8NCZ8; Q96BJ4; Q96NC6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Glucosamine-6-phosphate isomerase 2;
DE EC=3.5.99.6 {ECO:0000269|PubMed:12616532};
DE AltName: Full=Glucosamine-6-phosphate deaminase 2;
DE Short=GNPDA 2;
DE Short=GlcN6P deaminase 2;
DE AltName: Full=Glucosamine-6-phosphate isomerase SB52;
GN Name=GNPDA2 {ECO:0000303|PubMed:26887390}; Synonyms=GNP2;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=12616532; DOI=10.1002/jcb.10444;
RA Zhang J., Zhang W., Zou D., Chen G., Wan T., Li N., Cao X.;
RT "Cloning and functional characterization of GNPI2, a novel human homolog of
RT glucosamine-6-phosphate isomerase/oscillin.";
RL J. Cell. Biochem. 88:932-940(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RA Xu J., Xie Y., Mao Y.;
RT "Characterization of a novel putative glucosamine-6-phosphate isomerase.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Subthalamic nucleus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Aortic endothelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-182.
RC TISSUE=Uterus;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-276 (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP SUBUNIT.
RX PubMed=12965206; DOI=10.1016/s0014-5793(03)00896-2;
RA Arreola R., Valderrama B., Morante M.L., Horjales E.;
RT "Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic
RT study.";
RL FEBS Lett. 551:63-70(2003).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=26887390; DOI=10.1093/glycob/cww019;
RA Oikari S., Makkonen K., Deen A.J., Tyni I., Kaernae R., Tammi R.H.,
RA Tammi M.I.;
RT "Hexosamine biosynthesis in keratinocytes: roles of GFAT and GNPDA enzymes
RT in the maintenance of UDP-GlcNAc content and hyaluronan synthesis.";
RL Glycobiology 26:710-722(2016).
CC -!- FUNCTION: Catalyzes the reversible conversion of alpha-D-glucosamine 6-
CC phosphate (GlcN-6P) into beta-D-fructose 6-phosphate (Fru-6P) and
CC ammonium ion, a regulatory reaction step in de novo uridine
CC diphosphate-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc) biosynthesis via
CC hexosamine pathway. Deamination is coupled to aldo-keto isomerization
CC mediating the metabolic flux from UDP-GlcNAc toward Fru-6P. At high
CC ammonium level can drive amination and isomerization of Fru-6P toward
CC hexosamines and UDP-GlcNAc synthesis. Has a role in fine tuning the
CC metabolic fluctuations of cytosolic UDP-GlcNAc and their effects on
CC hyaluronan synthesis that occur during tissue remodeling.
CC {ECO:0000269|PubMed:12616532, ECO:0000269|PubMed:26887390}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-
CC phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6;
CC Evidence={ECO:0000269|PubMed:12616532};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12173;
CC Evidence={ECO:0000305|PubMed:12616532, ECO:0000305|PubMed:26887390};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12174;
CC Evidence={ECO:0000305|PubMed:26887390};
CC -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine-6-
CC phosphate (GlcNAc6P). {ECO:0000269|PubMed:12616532}.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-
CC fructose 6-phosphate: step 1/1. {ECO:0000305|PubMed:26887390}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8TDQ7; Q9Y303: AMDHD2; NbExp=4; IntAct=EBI-10275006, EBI-2798672;
CC Q8TDQ7; P14373: TRIM27; NbExp=4; IntAct=EBI-10275006, EBI-719493;
CC Q8TDQ7-2; Q9Y303-2: AMDHD2; NbExp=3; IntAct=EBI-12197555, EBI-12323557;
CC Q8TDQ7-2; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-12197555, EBI-746778;
CC Q8TDQ7-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12197555, EBI-741158;
CC Q8TDQ7-2; P14373: TRIM27; NbExp=3; IntAct=EBI-12197555, EBI-719493;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8TDQ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TDQ7-2; Sequence=VSP_034579;
CC Name=3;
CC IsoId=Q8TDQ7-3; Sequence=VSP_034580;
CC Name=4;
CC IsoId=Q8TDQ7-4; Sequence=VSP_047033;
CC Name=5;
CC IsoId=Q8TDQ7-5; Sequence=VSP_047034;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression detected in
CC testis, ovary, placenta, and heart. {ECO:0000269|PubMed:12616532}.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93141.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF247786; AAL95691.1; -; mRNA.
DR EMBL; AY173948; AAO49718.1; -; mRNA.
DR EMBL; AK055639; BAB70977.1; -; mRNA.
DR EMBL; AK296051; BAG58815.1; -; mRNA.
DR EMBL; AB209904; BAD93141.1; ALT_INIT; mRNA.
DR EMBL; AC096586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471069; EAW93019.1; -; Genomic_DNA.
DR EMBL; BC015532; AAH15532.1; -; mRNA.
DR EMBL; AL834506; CAD39163.1; -; mRNA.
DR CCDS; CCDS3469.1; -. [Q8TDQ7-1]
DR CCDS; CCDS59472.1; -. [Q8TDQ7-4]
DR CCDS; CCDS59473.1; -. [Q8TDQ7-5]
DR RefSeq; NP_001257809.1; NM_001270880.1. [Q8TDQ7-5]
DR RefSeq; NP_001257810.1; NM_001270881.1. [Q8TDQ7-4]
DR RefSeq; NP_612208.1; NM_138335.2. [Q8TDQ7-1]
DR AlphaFoldDB; Q8TDQ7; -.
DR SMR; Q8TDQ7; -.
DR BioGRID; 126335; 41.
DR DIP; DIP-62122N; -.
DR IntAct; Q8TDQ7; 6.
DR STRING; 9606.ENSP00000295448; -.
DR iPTMnet; Q8TDQ7; -.
DR MetOSite; Q8TDQ7; -.
DR PhosphoSitePlus; Q8TDQ7; -.
DR BioMuta; GNPDA2; -.
DR DMDM; 74723936; -.
DR EPD; Q8TDQ7; -.
DR jPOST; Q8TDQ7; -.
DR MassIVE; Q8TDQ7; -.
DR MaxQB; Q8TDQ7; -.
DR PaxDb; Q8TDQ7; -.
DR PeptideAtlas; Q8TDQ7; -.
DR PRIDE; Q8TDQ7; -.
DR ProteomicsDB; 4374; -.
DR ProteomicsDB; 61529; -.
DR ProteomicsDB; 74327; -. [Q8TDQ7-1]
DR ProteomicsDB; 74328; -. [Q8TDQ7-2]
DR ProteomicsDB; 74329; -. [Q8TDQ7-3]
DR TopDownProteomics; Q8TDQ7-2; -. [Q8TDQ7-2]
DR Antibodypedia; 23728; 133 antibodies from 28 providers.
DR DNASU; 132789; -.
DR Ensembl; ENST00000295448.8; ENSP00000295448.3; ENSG00000163281.12. [Q8TDQ7-1]
DR Ensembl; ENST00000507534.5; ENSP00000427423.1; ENSG00000163281.12. [Q8TDQ7-4]
DR Ensembl; ENST00000507917.5; ENSP00000425868.1; ENSG00000163281.12. [Q8TDQ7-5]
DR Ensembl; ENST00000509756.1; ENSP00000424061.1; ENSG00000163281.12. [Q8TDQ7-3]
DR GeneID; 132789; -.
DR KEGG; hsa:132789; -.
DR MANE-Select; ENST00000295448.8; ENSP00000295448.3; NM_138335.3; NP_612208.1.
DR UCSC; uc003gwy.5; human. [Q8TDQ7-1]
DR CTD; 132789; -.
DR DisGeNET; 132789; -.
DR GeneCards; GNPDA2; -.
DR HGNC; HGNC:21526; GNPDA2.
DR HPA; ENSG00000163281; Low tissue specificity.
DR MIM; 613222; gene.
DR neXtProt; NX_Q8TDQ7; -.
DR OpenTargets; ENSG00000163281; -.
DR PharmGKB; PA134939177; -.
DR VEuPathDB; HostDB:ENSG00000163281; -.
DR eggNOG; KOG3148; Eukaryota.
DR GeneTree; ENSGT00390000014316; -.
DR HOGENOM; CLU_049611_0_1_1; -.
DR InParanoid; Q8TDQ7; -.
DR OMA; NSYRYYM; -.
DR PhylomeDB; Q8TDQ7; -.
DR TreeFam; TF300841; -.
DR BRENDA; 3.5.99.6; 2681.
DR PathwayCommons; Q8TDQ7; -.
DR Reactome; R-HSA-70171; Glycolysis.
DR SignaLink; Q8TDQ7; -.
DR UniPathway; UPA00113; UER00528.
DR BioGRID-ORCS; 132789; 17 hits in 1075 CRISPR screens.
DR ChiTaRS; GNPDA2; human.
DR GeneWiki; GNPDA2; -.
DR GenomeRNAi; 132789; -.
DR Pharos; Q8TDQ7; Tbio.
DR PRO; PR:Q8TDQ7; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8TDQ7; protein.
DR Bgee; ENSG00000163281; Expressed in secondary oocyte and 145 other tissues.
DR ExpressionAtlas; Q8TDQ7; baseline and differential.
DR Genevisible; Q8TDQ7; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006043; P:glucosamine catabolic process; IBA:GO_Central.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IMP:UniProtKB.
DR CDD; cd01399; GlcN6P_deaminase; 1.
DR HAMAP; MF_01241; GlcN6P_deamin; 1.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR InterPro; IPR004547; Glucosamine6P_isomerase.
DR InterPro; IPR018321; Glucosamine6P_isomerase_CS.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR11280; PTHR11280; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00502; nagB; 1.
DR PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Carbohydrate metabolism; Coiled coil; Cytoplasm;
KW Hydrolase; Isomerase; Phosphoprotein; Reference proteome.
FT CHAIN 1..276
FT /note="Glucosamine-6-phosphate isomerase 2"
FT /id="PRO_0000343205"
FT COILED 105..130
FT /evidence="ECO:0000255"
FT ACT_SITE 72
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000250"
FT ACT_SITE 141
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 143
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 148
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88958"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047033"
FT VAR_SEQ 43..76
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_047034"
FT VAR_SEQ 217
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034579"
FT VAR_SEQ 258..276
FT /note="LMHVHNKLVDPLFSMKDGN -> EH (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_034580"
FT VARIANT 182
FT /note="P -> S (in dbSNP:rs17851302)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_044348"
FT CONFLICT 37
FT /note="L -> P (in Ref. 3; BAB70977)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 276 AA; 31085 MW; 2BCFD72F734639D0 CRC64;
MRLVILDNYD LASEWAAKYI CNRIIQFKPG QDRYFTLGLP TGSTPLGCYK KLIEYHKNGH
LSFKYVKTFN MDEYVGLPRN HPESYHSYMW NNFFKHIDID PNNAHILDGN AADLQAECDA
FENKIKEAGG IDLFVGGIGP DGHIAFNEPG SSLVSRTRLK TLAMDTILAN AKYFDGDLSK
VPTMALTVGV GTVMDAREVM ILITGAHKAF ALYKAIEEGV NHMWTVSAFQ QHPRTIFVCD
EDATLELRVK TVKYFKGLMH VHNKLVDPLF SMKDGN
