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Alpha-N-acetylgalactosaminidase (EC 3.2.1.49) (Alpha-galactosidase B)

 NAGAB_HUMAN             Reviewed;         411 AA.
P17050;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 2.
20-JUN-2018, entry version 190.
RecName: Full=Alpha-N-acetylgalactosaminidase;
EC=3.2.1.49;
AltName: Full=Alpha-galactosidase B;
Flags: Precursor;
Name=NAGA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Lung;
PubMed=2174888;
Wang A.M., Bishop D.F., Desnick R.J.;
"Human alpha-N-acetylgalactosaminidase-molecular cloning, nucleotide
sequence, and expression of a full-length cDNA. Homology with human
alpha-galactosidase A suggests evolution from a common ancestral
gene.";
J. Biol. Chem. 265:21859-21866(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1646157; DOI=10.1016/0888-7543(91)90493-X;
Wang A.M., Desnick R.J.;
"Structural organization and complete sequence of the human alpha-N-
acetylgalactosaminidase gene: homology with the alpha-galactosidase A
gene provides evidence for evolution from a common ancestral gene.";
Genomics 10:133-142(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=2551294; DOI=10.1016/0006-291X(89)91149-2;
Tsuji S., Yamauchi T., Hiraiwa M., Isobe T., Okuyama T., Sakimura K.,
Takahashi Y., Nishizawa M., Uda Y., Miyatake T.;
"Molecular cloning of a full-length cDNA for human alpha-N-
acetylgalactosaminidase (alpha-galactosidase B).";
Biochem. Biophys. Res. Commun. 163:1498-1504(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2372288; DOI=10.1016/0006-291X(90)91264-S;
Yamauchi T., Hiraiwa M., Kobayashi H., Uda Y., Miyatake T., Tsuji S.;
"Molecular cloning of two species of cDNAs for human alpha-N-
acetylgalactosaminidase and expression in mammalian cells.";
Biochem. Biophys. Res. Commun. 170:231-237(1990).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 18-37.
TISSUE=Placenta;
PubMed=2256909; DOI=10.1016/S0006-291X(05)81014-9;
Warner T.G., Louie A., Potier M.;
"Photolabeling of the alpha-neuraminidase/beta-galactosidase complex
from human placenta with a photoreactive neuraminidase inhibitor.";
Biochem. Biophys. Res. Commun. 173:13-19(1990).
[9]
FUNCTION.
PubMed=9741689;
Asfaw B., Schindler D., Ledvinova J., Cerny B., Smid F.,
Conzelmann E.;
"Degradation of blood group A glycolipid A-6-2 by normal and mutant
human skin fibroblasts.";
J. Lipid Res. 39:1768-1780(1998).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322 AND SER-332, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
network: indicating the involvement of ribonucleoside-diphosphate
reductase M2 subunit phosphorylation at residue serine 20 in canonical
Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-177 AND ASN-201.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 18-411 IN COMPLEXES WITH
N-ACETYLGALACTOSAMINE AND GALACTOSE, DISULFIDE BONDS, GLYCOSYLATION AT
ASN-124; ASN-177 AND ASN-385, SUBUNIT, CATALYTIC ACTIVITY, AND
MUTAGENESIS OF ASN-201.
PubMed=19683538; DOI=10.1016/j.jmb.2009.08.021;
Clark N.E., Garman S.C.;
"The 1.9 A structure of human alpha-N-acetylgalactosaminidase: the
molecular basis of Schindler and Kanzaki diseases.";
J. Mol. Biol. 393:435-447(2009).
[14]
VARIANT SCHIND LYS-325.
PubMed=2243144; DOI=10.1172/JCI114901;
Wang A.M., Schindler D., Desnick R.J.;
"Schindler disease: the molecular lesion in the alpha-N-
acetylgalactosaminidase gene that causes an infantile neuroaxonal
dystrophy.";
J. Clin. Invest. 86:1752-1756(1990).
[15]
VARIANT KANZD TRP-329, AND CHARACTERIZATION OF VARIANT KANZD TRP-329.
PubMed=8040340; DOI=10.1172/JCI117404;
Wang A.M., Kanzaki T., Desnick R.J.;
"The molecular lesion in the alpha-N-acetylgalactosaminidase gene that
causes angiokeratoma corporis diffusum with glycopeptiduria.";
J. Clin. Invest. 94:839-845(1994).
[16]
VARIANTS SCHIND CYS-160 AND LYS-325.
PubMed=8782044; DOI=10.1136/jmg.33.6.458;
Keulemans J.L.M., Reuser A.J.J., Kroos M.A., Willemsen R.,
Hermans M.M.P., van den Ouweland A.M.W., de Jong J.G.N., Wevers R.A.,
Renier W.O., Schindler D., Coll M.J., Chabas A., Sakuraba H.,
Suzuki Y., van Diggelen O.P.;
"Human alpha-N-acetylgalactosaminidase (alpha-NAGA) deficiency: new
mutations and the paradox between genotype and phenotype.";
J. Med. Genet. 33:458-464(1996).
[17]
VARIANT KANZD GLN-329.
PubMed=11251574; DOI=10.1046/j.1365-2133.2001.04028.x;
Kodama K., Kobayashi H., Abe R., Ohkawara A., Yoshii N., Yotsumoto S.,
Fukushige T., Nagatsuka Y., Hirabayashi Y., Kanzaki T.;
"A new case of alpha-N-acetylgalactosaminidase deficiency with
angiokeratoma corporis diffusum, with Meniere's syndrome and without
mental retardation.";
Br. J. Dermatol. 144:363-368(2001).
-!- FUNCTION: Removes terminal alpha-N-acetylgalactosamine residues
from glycolipids and glycopeptides. Required for the breakdown of
glycolipids. {ECO:0000269|PubMed:9741689}.
-!- CATALYTIC ACTIVITY: Cleavage of non-reducing alpha-(1->3)-N-
acetylgalactosamine residues from human blood group A and AB mucin
glycoproteins, Forssman hapten and blood group A lacto series
glycolipids. {ECO:0000269|PubMed:19683538}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19683538}.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- DISEASE: Schindler disease (SCHIND) [MIM:609241]: Form of NAGA
deficiency characterized by early-onset neuroaxonal dystrophy and
neurological signs (convulsion during fever, epilepsy, psychomotor
retardation and hypotonia). NAGA deficiency is typically
classified in three main phenotypes: NAGA deficiency type I
(Schindler disease or Schindler disease type I) with severe
manifestations; NAGA deficiency type II (Kanzazi disease or
Schindler disease type II) which is mild; NAGA deficiency type III
(Schindler disease type III) characterized by mild-to-moderate
neurologic manifestations. NAGA deficiency results in the
increased urinary excretion of glycopeptides and oligosaccharides
containing alpha-N-acetylgalactosaminyl moieties. Inheritance is
autosomal recessive. {ECO:0000269|PubMed:2243144,
ECO:0000269|PubMed:8782044}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Kanzaki disease (KANZD) [MIM:609242]: Autosomal recessive
disorder characterized by late-onset, angiokeratoma corporis
diffusum and mild intellectual impairment.
{ECO:0000269|PubMed:11251574, ECO:0000269|PubMed:8040340}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Alpha-galactosidase B was first found to be an
isoenzyme of alpha-galactosidases, but apparently it differs from
alpha-galactosidase A in substrate specificity and is alpha-N-
acetylgalactosaminidase.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA59902.1; Type=Frameshift; Positions=320; Evidence={ECO:0000305};
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EMBL; M62783; AAA51677.1; -; mRNA.
EMBL; M59199; AAB06718.1; -; Genomic_DNA.
EMBL; M29276; AAA59902.1; ALT_FRAME; mRNA.
EMBL; M38083; AAA36351.1; -; mRNA.
EMBL; CR456527; CAG30413.1; -; mRNA.
EMBL; Z99716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000095; AAH00095.1; -; mRNA.
CCDS; CCDS14030.1; -.
PIR; A33265; A33265.
PIR; A36530; A35485.
RefSeq; NP_000253.1; NM_000262.2.
RefSeq; XP_005261672.1; XM_005261615.4.
RefSeq; XP_005261673.1; XM_005261616.4.
UniGene; Hs.75372; -.
PDB; 3H53; X-ray; 2.01 A; A/B=18-411.
PDB; 3H54; X-ray; 2.20 A; A/B=18-411.
PDB; 3H55; X-ray; 1.91 A; A/B=18-411.
PDB; 3IGU; X-ray; 2.15 A; A/B=18-411.
PDB; 4DO4; X-ray; 1.40 A; A/B=18-411.
PDB; 4DO5; X-ray; 1.51 A; A/B=18-411.
PDB; 4DO6; X-ray; 1.60 A; A/B=18-411.
PDBsum; 3H53; -.
PDBsum; 3H54; -.
PDBsum; 3H55; -.
PDBsum; 3IGU; -.
PDBsum; 4DO4; -.
PDBsum; 4DO5; -.
PDBsum; 4DO6; -.
ProteinModelPortal; P17050; -.
SMR; P17050; -.
BioGrid; 110749; 5.
STRING; 9606.ENSP00000379680; -.
ChEMBL; CHEMBL3132; -.
DrugBank; DB04077; Glycerol.
SwissLipids; SLP:000001402; -.
CAZy; GH27; Glycoside Hydrolase Family 27.
GlyConnect; 45; -.
iPTMnet; P17050; -.
PhosphoSitePlus; P17050; -.
UniCarbKB; P17050; -.
BioMuta; NAGA; -.
DMDM; 127801; -.
EPD; P17050; -.
MaxQB; P17050; -.
PaxDb; P17050; -.
PeptideAtlas; P17050; -.
PRIDE; P17050; -.
ProteomicsDB; 53450; -.
DNASU; 4668; -.
Ensembl; ENST00000396398; ENSP00000379680; ENSG00000198951.
Ensembl; ENST00000402937; ENSP00000384603; ENSG00000198951.
Ensembl; ENST00000403363; ENSP00000385283; ENSG00000198951.
GeneID; 4668; -.
KEGG; hsa:4668; -.
UCSC; uc003bbw.5; human.
CTD; 4668; -.
DisGeNET; 4668; -.
EuPathDB; HostDB:ENSG00000198951.11; -.
GeneCards; NAGA; -.
HGNC; HGNC:7631; NAGA.
HPA; HPA000649; -.
MalaCards; NAGA; -.
MIM; 104170; gene.
MIM; 609241; phenotype.
MIM; 609242; phenotype.
neXtProt; NX_P17050; -.
OpenTargets; ENSG00000198951; -.
Orphanet; 79279; Alpha-N-acetylgalactosaminidase deficiency type 1.
Orphanet; 79280; Alpha-N-acetylgalactosaminidase deficiency type 2.
Orphanet; 79281; Alpha-N-acetylgalactosaminidase deficiency type 3.
PharmGKB; PA31435; -.
eggNOG; KOG2366; Eukaryota.
eggNOG; ENOG410XPF1; LUCA.
GeneTree; ENSGT00390000008751; -.
HOGENOM; HOG000161224; -.
HOVERGEN; HBG001989; -.
InParanoid; P17050; -.
KO; K01204; -.
OMA; DDLWDRW; -.
OrthoDB; EOG091G0BGV; -.
PhylomeDB; P17050; -.
TreeFam; TF312909; -.
BioCyc; MetaCyc:HS01993-MONOMER; -.
BRENDA; 3.2.1.49; 2681.
SABIO-RK; P17050; -.
ChiTaRS; NAGA; human.
EvolutionaryTrace; P17050; -.
GeneWiki; NAGA_(gene); -.
GenomeRNAi; 4668; -.
PRO; PR:P17050; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000198951; -.
CleanEx; HS_NAGA; -.
ExpressionAtlas; P17050; baseline and differential.
Genevisible; P17050; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
GO; GO:0004557; F:alpha-galactosidase activity; IBA:GO_Central.
GO; GO:0008456; F:alpha-N-acetylgalactosaminidase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0016052; P:carbohydrate catabolic process; IDA:UniProtKB.
GO; GO:0019377; P:glycolipid catabolic process; IMP:UniProtKB.
GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central.
GO; GO:0046477; P:glycosylceramide catabolic process; IBA:GO_Central.
GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
CDD; cd14792; GH27; 1.
Gene3D; 2.60.40.1180; -; 1.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR002241; Glyco_hydro_27.
InterPro; IPR000111; Glyco_hydro_27/36_CS.
InterPro; IPR013780; Glyco_hydro_b.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR035373; Melibiase/NAGA_C.
Pfam; PF16499; Melibiase_2; 1.
Pfam; PF17450; Melibiase_2_C; 1.
PRINTS; PR00740; GLHYDRLASE27.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Epilepsy; Glycoprotein; Glycosidase;
Hydrolase; Lysosome; Phosphoprotein; Reference proteome; Signal.
SIGNAL 1 17 {ECO:0000269|PubMed:2256909}.
CHAIN 18 411 Alpha-N-acetylgalactosaminidase.
/FTId=PRO_0000001018.
REGION 78 79 Substrate binding.
ACT_SITE 156 156 Nucleophile.
ACT_SITE 217 217 Proton donor.
BINDING 154 154 Substrate.
BINDING 188 188 Substrate.
BINDING 213 213 Substrate.
BINDING 217 217 Substrate.
MOD_RES 322 322 Phosphoserine.
{ECO:0000244|PubMed:17693683}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000244|PubMed:17693683}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19683538}.
CARBOHYD 177 177 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19683538}.
CARBOHYD 201 201 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 359 359 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 385 385 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19683538}.
DISULFID 38 80 {ECO:0000269|PubMed:19683538}.
DISULFID 42 49 {ECO:0000269|PubMed:19683538}.
DISULFID 127 158 {ECO:0000269|PubMed:19683538}.
DISULFID 187 209 {ECO:0000269|PubMed:19683538}.
VARIANT 160 160 S -> C (in SCHIND; type III;
dbSNP:rs121434532).
{ECO:0000269|PubMed:8782044}.
/FTId=VAR_000496.
VARIANT 325 325 E -> K (in SCHIND; type I and type III;
dbSNP:rs121434529).
{ECO:0000269|PubMed:2243144,
ECO:0000269|PubMed:8782044}.
/FTId=VAR_000497.
VARIANT 329 329 R -> Q (in KANZD; dbSNP:rs121434533).
{ECO:0000269|PubMed:11251574}.
/FTId=VAR_022525.
VARIANT 329 329 R -> W (in KANZD; loss of activity;
dbSNP:rs121434530).
{ECO:0000269|PubMed:8040340}.
/FTId=VAR_000498.
MUTAGEN 201 201 N->Q: Loss of glycosylation site; no
effect on enzyme activity and stability.
{ECO:0000269|PubMed:19683538}.
CONFLICT 24 24 Q -> N (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 165 165 R -> A (in Ref. 2; AAA59902).
{ECO:0000305}.
CONFLICT 175 175 A -> G (in Ref. 2; AAA59902).
{ECO:0000305}.
CONFLICT 205 205 L -> Q (in Ref. 2; AAA59902).
{ECO:0000305}.
STRAND 28 32 {ECO:0000244|PDB:4DO4}.
HELIX 33 36 {ECO:0000244|PDB:4DO4}.
TURN 42 44 {ECO:0000244|PDB:4DO4}.
TURN 46 48 {ECO:0000244|PDB:4DO4}.
STRAND 49 51 {ECO:0000244|PDB:4DO4}.
HELIX 52 64 {ECO:0000244|PDB:4DO4}.
HELIX 67 70 {ECO:0000244|PDB:4DO4}.
STRAND 74 76 {ECO:0000244|PDB:4DO4}.
STRAND 82 85 {ECO:0000244|PDB:4DO4}.
STRAND 91 93 {ECO:0000244|PDB:4DO4}.
TURN 95 97 {ECO:0000244|PDB:4DO4}.
HELIX 102 111 {ECO:0000244|PDB:4DO4}.
STRAND 115 125 {ECO:0000244|PDB:4DO4}.
HELIX 135 137 {ECO:0000244|PDB:4DO4}.
HELIX 138 147 {ECO:0000244|PDB:4DO4}.
STRAND 152 156 {ECO:0000244|PDB:4DO4}.
HELIX 162 178 {ECO:0000244|PDB:4DO4}.
STRAND 184 187 {ECO:0000244|PDB:4DO4}.
HELIX 189 192 {ECO:0000244|PDB:4DO4}.
TURN 197 199 {ECO:0000244|PDB:4DO4}.
HELIX 202 208 {ECO:0000244|PDB:4DO4}.
STRAND 210 213 {ECO:0000244|PDB:4DO4}.
HELIX 222 234 {ECO:0000244|PDB:4DO4}.
HELIX 236 239 {ECO:0000244|PDB:4DO4}.
HELIX 240 242 {ECO:0000244|PDB:4DO4}.
STRAND 247 250 {ECO:0000244|PDB:4DO4}.
STRAND 258 260 {ECO:0000244|PDB:4DO4}.
HELIX 263 275 {ECO:0000244|PDB:4DO4}.
STRAND 280 282 {ECO:0000244|PDB:4DO4}.
TURN 286 288 {ECO:0000244|PDB:4DO4}.
HELIX 291 297 {ECO:0000244|PDB:4DO4}.
HELIX 300 306 {ECO:0000244|PDB:4DO4}.
STRAND 315 319 {ECO:0000244|PDB:4DO4}.
STRAND 323 330 {ECO:0000244|PDB:4DO4}.
HELIX 332 334 {ECO:0000244|PDB:4DO4}.
STRAND 336 342 {ECO:0000244|PDB:4DO4}.
STRAND 345 347 {ECO:0000244|PDB:4DO4}.
STRAND 349 354 {ECO:0000244|PDB:4DO4}.
HELIX 355 358 {ECO:0000244|PDB:4DO4}.
STRAND 365 370 {ECO:0000244|PDB:4DO4}.
TURN 371 373 {ECO:0000244|PDB:4DO4}.
STRAND 376 380 {ECO:0000244|PDB:4DO4}.
STRAND 385 390 {ECO:0000244|PDB:4DO4}.
STRAND 395 403 {ECO:0000244|PDB:4DO4}.
HELIX 405 408 {ECO:0000244|PDB:4DO4}.
SEQUENCE 411 AA; 46565 MW; 781A0728C0B29CD9 CRC64;
MLLKTVLLLG HVAQVLMLDN GLLQTPPMGW LAWERFRCNI NCDEDPKNCI SEQLFMEMAD
RMAQDGWRDM GYTYLNIDDC WIGGRDASGR LMPDPKRFPH GIPFLADYVH SLGLKLGIYA
DMGNFTCMGY PGTTLDKVVQ DAQTFAEWKV DMLKLDGCFS TPEERAQGYP KMAAALNATG
RPIAFSCSWP AYEGGLPPRV NYSLLADICN LWRNYDDIQD SWWSVLSILN WFVEHQDILQ
PVAGPGHWND PDMLLIGNFG LSLEQSRAQM ALWTVLAAPL LMSTDLRTIS AQNMDILQNP
LMIKINQDPL GIQGRRIHKE KSLIEVYMRP LSNKASALVF FSCRTDMPYR YHSSLGQLNF
TGSVIYEAQD VYSGDIISGL RDETNFTVII NPSGVVMWYL YPIKNLEMSQ Q


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