NAGA_HUMAN
ID NAGA_HUMAN Reviewed; 409 AA.
AC Q9Y303; B4DL77; Q8WV54;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000305|PubMed:22692205};
DE Short=GlcNAc 6-P deacetylase {ECO:0000305};
DE EC=3.5.1.25 {ECO:0000269|PubMed:22692205};
DE AltName: Full=Amidohydrolase domain-containing protein 2 {ECO:0000305};
GN Name=AMDHD2; ORFNames=CGI-14;
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] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Tongue;
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 [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 2).
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 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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=22692205; DOI=10.1074/jbc.m112.363549;
RA Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.;
RT "Metabolism of vertebrate amino sugars with N-glycolyl groups: elucidating
RT the intracellular fate of the non-human sialic acid N-glycolylneuraminic
RT acid.";
RL J. Biol. Chem. 287:28865-28881(2012).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-294.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Hydrolyzes the N-glycolyl group from N-glycolylglucosamine 6-
CC phosphate (GlcNGc-6-P) in the N-glycolylneuraminic acid (Neu5Gc)
CC degradation pathway. Although human is not able to catalyze formation
CC of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food
CC and must be degraded. {ECO:0000269|PubMed:22692205}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-
CC glucosamine 6-phosphate; Xref=Rhea:RHEA:22936, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=3.5.1.25;
CC Evidence={ECO:0000269|PubMed:22692205};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P0AF18};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000250|UniProtKB:P0AF18};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC {ECO:0000269|PubMed:22692205}.
CC -!- INTERACTION:
CC Q9Y303; Q8TDQ7: GNPDA2; NbExp=4; IntAct=EBI-2798672, EBI-10275006;
CC Q9Y303; Q15645: TRIP13; NbExp=3; IntAct=EBI-2798672, EBI-358993;
CC Q9Y303-2; P55212: CASP6; NbExp=3; IntAct=EBI-12323557, EBI-718729;
CC Q9Y303-2; Q8TDQ7-2: GNPDA2; NbExp=3; IntAct=EBI-12323557, EBI-12197555;
CC Q9Y303-2; O00291: HIP1; NbExp=3; IntAct=EBI-12323557, EBI-473886;
CC Q9Y303-2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-12323557, EBI-21591415;
CC Q9Y303-2; P62826: RAN; NbExp=3; IntAct=EBI-12323557, EBI-286642;
CC Q9Y303-2; Q15645: TRIP13; NbExp=3; IntAct=EBI-12323557, EBI-358993;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y303-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y303-2; Sequence=VSP_030698;
CC Name=3;
CC IsoId=Q9Y303-3; Sequence=VSP_030698, VSP_038782;
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC NagA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27723.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF132948; AAD27723.1; ALT_FRAME; mRNA.
DR EMBL; AK296877; BAG59439.1; -; mRNA.
DR EMBL; CH471112; EAW85500.1; -; Genomic_DNA.
DR EMBL; BC018734; AAH18734.1; -; mRNA.
DR CCDS; CCDS10471.1; -. [Q9Y303-2]
DR CCDS; CCDS53984.1; -. [Q9Y303-3]
DR CCDS; CCDS81936.1; -. [Q9Y303-1]
DR RefSeq; NP_001139287.1; NM_001145815.1. [Q9Y303-3]
DR RefSeq; NP_001317378.1; NM_001330449.1. [Q9Y303-1]
DR RefSeq; NP_057028.2; NM_015944.3. [Q9Y303-2]
DR PDB; 7NUT; X-ray; 1.90 A; A/B=1-409.
DR PDB; 7NUU; X-ray; 1.84 A; A/B=1-409.
DR PDBsum; 7NUT; -.
DR PDBsum; 7NUU; -.
DR AlphaFoldDB; Q9Y303; -.
DR SMR; Q9Y303; -.
DR BioGRID; 119213; 4.
DR IntAct; Q9Y303; 8.
DR STRING; 9606.ENSP00000391596; -.
DR ChEMBL; CHEMBL3217376; -.
DR MEROPS; M38.979; -.
DR iPTMnet; Q9Y303; -.
DR PhosphoSitePlus; Q9Y303; -.
DR BioMuta; AMDHD2; -.
DR DMDM; 166233266; -.
DR EPD; Q9Y303; -.
DR jPOST; Q9Y303; -.
DR MassIVE; Q9Y303; -.
DR MaxQB; Q9Y303; -.
DR PaxDb; Q9Y303; -.
DR PeptideAtlas; Q9Y303; -.
DR PRIDE; Q9Y303; -.
DR ProteomicsDB; 85950; -. [Q9Y303-1]
DR ProteomicsDB; 85951; -. [Q9Y303-2]
DR ProteomicsDB; 85952; -. [Q9Y303-3]
DR Antibodypedia; 23813; 109 antibodies from 15 providers.
DR DNASU; 51005; -.
DR Ensembl; ENST00000293971.11; ENSP00000293971.6; ENSG00000162066.16. [Q9Y303-1]
DR Ensembl; ENST00000302956.8; ENSP00000307481.4; ENSG00000162066.16. [Q9Y303-2]
DR Ensembl; ENST00000413459.7; ENSP00000391596.3; ENSG00000162066.16. [Q9Y303-3]
DR GeneID; 51005; -.
DR KEGG; hsa:51005; -.
DR MANE-Select; ENST00000293971.11; ENSP00000293971.6; NM_001330449.2; NP_001317378.1.
DR UCSC; uc002cqp.4; human. [Q9Y303-1]
DR CTD; 51005; -.
DR DisGeNET; 51005; -.
DR GeneCards; AMDHD2; -.
DR HGNC; HGNC:24262; AMDHD2.
DR HPA; ENSG00000162066; Low tissue specificity.
DR neXtProt; NX_Q9Y303; -.
DR OpenTargets; ENSG00000162066; -.
DR PharmGKB; PA143485298; -.
DR VEuPathDB; HostDB:ENSG00000162066; -.
DR eggNOG; KOG3892; Eukaryota.
DR GeneTree; ENSGT00390000012605; -.
DR InParanoid; Q9Y303; -.
DR OMA; HAFNAMP; -.
DR OrthoDB; 1066877at2759; -.
DR PhylomeDB; Q9Y303; -.
DR TreeFam; TF315036; -.
DR PathwayCommons; Q9Y303; -.
DR Reactome; R-HSA-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR SignaLink; Q9Y303; -.
DR UniPathway; UPA00629; -.
DR BioGRID-ORCS; 51005; 16 hits in 1071 CRISPR screens.
DR ChiTaRS; AMDHD2; human.
DR GenomeRNAi; 51005; -.
DR Pharos; Q9Y303; Tchem.
DR PRO; PR:Q9Y303; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9Y303; protein.
DR Bgee; ENSG00000162066; Expressed in left testis and 100 other tissues.
DR ExpressionAtlas; Q9Y303; baseline and differential.
DR Genevisible; Q9Y303; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047419; F:N-acetylgalactosamine-6-phosphate deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; TAS:UniProtKB.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; TAS:Reactome.
DR CDD; cd00854; NagA; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR003764; GlcNAc_6-P_deAcase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11113:SF14; PTHR11113:SF14; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF038994; NagA; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR00221; nagA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Carbohydrate metabolism; Hydrolase;
KW Metal-binding; Reference proteome.
FT CHAIN 1..409
FT /note="N-acetylglucosamine-6-phosphate deacetylase"
FT /id="PRO_0000315776"
FT ACT_SITE 294
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 143
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 154..155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 211
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 232
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 235..236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 269..272
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 328..330
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT VAR_SEQ 323
FT /note="A -> AGERPDPLGPRSQPACQVAHDPPRACPLCSQ (in isoform 2
FT and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030698"
FT VAR_SEQ 399..409
FT /note="ELVWQADAARQ -> PVLAGCGDPAWCWRAVWEAPVCPAHPISVILPSSVSP
FT WPWHTPMWQTRAVRLPEQLRGGWASGALLALRTATVGSDVRDWCSPTSGVIVLTFSPFE
FT FWGGWLPSPLLTGAVLGTGGTRLALPLFSSLCCKAQLRKCLQVQRDRMVWAPPVGREQP
FT GKNHLPGQGLA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038782"
FT VARIANT 294
FT /note="D -> N (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1220386463)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_038301"
FT CONFLICT 97
FT /note="R -> E (in Ref. 1; AAD27723)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="A -> Q (in Ref. 1; AAD27723)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="A -> T (in Ref. 1; AAD27723)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="I -> L (in Ref. 1; AAD27723)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="Missing (in Ref. 1; AAD27723)"
FT /evidence="ECO:0000305"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:7NUT"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:7NUU"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:7NUU"
FT HELIX 87..97
FT /evidence="ECO:0007829|PDB:7NUU"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:7NUU"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:7NUU"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:7NUU"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:7NUU"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:7NUU"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:7NUU"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:7NUU"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:7NUU"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:7NUU"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:7NUU"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:7NUU"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:7NUU"
FT TURN 297..301
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:7NUT"
FT HELIX 335..346
FT /evidence="ECO:0007829|PDB:7NUU"
FT HELIX 350..356
FT /evidence="ECO:0007829|PDB:7NUU"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:7NUU"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:7NUU"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:7NUU"
SQ SEQUENCE 409 AA; 43748 MW; E647E8F384BBC1D6 CRC64;
MRGEQGAAGA RVLQFTNCRI LRGGKLLRED LWVRGGRILD PEKLFFEERR VADERRDCGG
RILAPGFIDV QINGGFGVDF SQATEDVGSG VALVARRILS HGVTSFCPTL VTSPPEVYHK
VVPQIPVKSG GPHGAGVLGL HLEGPFISRE KRGAHPEAHL RSFEADAFQD LLATYGPLDN
VRIVTLAPEL GRSHEVIRAL TARGICVSLG HSVADLRAAE DAVWSGATFI THLFNAMLPF
HHRDPGIVGL LTSDRLPAGR CIFYGMIADG THTNPAALRI AHRAHPQGLV LVTDAIPALG
LGNGRHTLGQ QEVEVDGLTA YVAGTKTLSG SIAPMDVCVR HFLQATGCSM ESALEAASLH
PAQLLGLEKS KGTLDFGADA DFVVLDDSLH VQATYISGEL VWQADAARQ
