HEXA_ASPOZ
ID HEXA_ASPOZ Reviewed; 600 AA.
AC Q8J2T0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Beta-hexosaminidase {ECO:0000255|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000269|PubMed:12681926, ECO:0000269|PubMed:12723619, ECO:0000269|PubMed:15494009, ECO:0000269|PubMed:17302431, ECO:0000269|PubMed:17509134, ECO:0000269|PubMed:21505251, ECO:0000269|PubMed:29239122, ECO:0000269|Ref.7};
DE AltName: Full=AoHEX {ECO:0000303|PubMed:29239122};
DE AltName: Full=Beta-N-acetylglucosaminidase {ECO:0000303|PubMed:12723619};
DE AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000303|PubMed:12681926, ECO:0000303|PubMed:15494009, ECO:0000303|PubMed:17302431, ECO:0000303|PubMed:17509134, ECO:0000303|PubMed:21505251, ECO:0000303|PubMed:29239122, ECO:0000303|Ref.7};
DE Short=Hex {ECO:0000303|PubMed:17302431, ECO:0000303|PubMed:21505251, ECO:0000303|PubMed:29239122};
DE Flags: Precursor;
GN Name=nagA {ECO:0000303|PubMed:12723619, ECO:0000312|EMBL:BAC41255.1};
GN Synonyms=hexA {ECO:0000303|PubMed:15494009, ECO:0000303|PubMed:17302431,
GN ECO:0000312|EMBL:AAM13977.1};
GN ORFNames=OAory_01008480 {ECO:0000312|EMBL:OOO13099.1};
OS Aspergillus oryzae (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5062 {ECO:0000312|EMBL:BAC41255.1};
RN [1] {ECO:0000312|EMBL:AAM13977.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND PTM.
RC STRAIN=CCF 1066 {ECO:0000303|PubMed:15494009};
RX PubMed=15494009; DOI=10.1042/bst0320764;
RA Plihal O., Sklenar J., Kmonickova J., Man P., Pompach P., Havlicek V.,
RA Kren V., Bezouska K.;
RT "N-glycosylated catalytic unit meets O-glycosylated propeptide: complex
RT protein architecture in a fungal hexosaminidase.";
RL Biochem. Soc. Trans. 32:764-765(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 19-28; 19-37;
RP 102-111; 102-131; 239-247; 397-411 AND 532-541, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBCELLULAR LOCATION, PTM, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=CCF 1066 {ECO:0000303|PubMed:17302431};
RC TISSUE=Mycelium {ECO:0000303|PubMed:17302431};
RX PubMed=17302431; DOI=10.1021/bi061828m;
RA Plihal O., Sklenar J., Hofbauerova K., Novak P., Man P., Pompach P.,
RA Kavan D., Ryslava H., Weignerova L., Charvatova-Pisvejcova A., Kren V.,
RA Bezouska K.;
RT "Large propeptides of fungal beta-N-acetylhexosaminidases are novel enzyme
RT regulators that must be intracellularly processed to control activity,
RT dimerization, and secretion into the extracellular environment.";
RL Biochemistry 46:2719-2734(2007).
RN [3] {ECO:0000312|EMBL:BAC41255.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC STRAIN=RIB 40 {ECO:0000303|PubMed:12723619};
RX PubMed=12723619; DOI=10.1271/bbb.67.646;
RA Matsuo I., Kim S., Yamamoto Y., Ajisaka K., Maruyama J.I., Nakajima H.,
RA Kitamoto K.;
RT "Cloning and overexpression of beta-N-acetylglucosaminidase encoding gene
RT nagA from Aspergillus oryzae and enzyme-catalyzed synthesis of human milk
RT oligosaccharide.";
RL Biosci. Biotechnol. Biochem. 67:646-650(2003).
RN [4] {ECO:0000312|EMBL:OOO13099.1, ECO:0000312|Proteomes:UP000190312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC7051 {ECO:0000312|EMBL:OOO13099.1,
RC ECO:0000312|Proteomes:UP000190312};
RX PubMed=28865010; DOI=10.1007/s00284-017-1350-7;
RA Thammarongtham C., Nookaew I., Vorapreeda T., Srisuk T., Land M.L.,
RA Jeennor S., Laoteng K.;
RT "Genome Characterization of Oleaginous Aspergillus oryzae BCC7051: A
RT Potential Fungal-Based Platform for Lipid Production.";
RL Curr. Microbiol. 75:57-70(2018).
RN [5]
RP PROTEIN SEQUENCE OF 19-28 AND 102-111, CRYSTALLIZATION, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND PTM.
RC STRAIN=CCF 1066 {ECO:0000303|PubMed:21505251};
RX PubMed=21505251; DOI=10.1107/s1744309111004945;
RA Vanek O., Brynda J., Hofbauerova K., Kukacka Z., Pachl P., Bezouska K.,
RA Rezacova P.;
RT "Crystallization and diffraction analysis of beta-N-acetylhexosaminidase
RT from Aspergillus oryzae.";
RL Acta Crystallogr. F 67:498-503(2011).
RN [6]
RP PROTEIN SEQUENCE OF 445-453 AND 474-488, 3D-STRUCTURE MODELING OF THE
RP CATALYTIC DOMAIN AND ITS COMPLEX WITH SUBSTRATE CHITOBIOSE, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR
RP LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT ASN-428 AND
RP ASN-500, AND DISULFIDE BONDS.
RC STRAIN=CCF 1066 {ECO:0000303|PubMed:17509134};
RX PubMed=17509134; DOI=10.1186/1472-6807-7-32;
RA Ettrich R., Kopecky V. Jr., Hofbauerova K., Baumruk V., Novak P.,
RA Pompach P., Man P., Plihal O., Kuty M., Kulik N., Sklenar J., Ryslava H.,
RA Kren V., Bezouska K.;
RT "Structure of the dimeric N-glycosylated form of fungal beta-N-
RT acetylhexosaminidase revealed by computer modeling, vibrational
RT spectroscopy, and biochemical studies.";
RL BMC Struct. Biol. 7:32-32(2007).
RN [7]
RP 3D-STRUCTURE MODELING OF THE ACTIVE CENTER IN COMPLEXES WITH DISACCHARIDES,
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, REACTION MECHANISM,
RP AND BIOTECHNOLOGY.
RC STRAIN=CCF 1066 {ECO:0000303|Ref.7};
RX DOI=10.1002/adsc.200303002;
RA Husakova L., Herkommerova-Rajnochova E., Semenuk T., Kuzma M.,
RA Rauvolfova J., Prikrylova V., Ettrich R., Plihal O., Bezouska K., Kren V.;
RT "Enzymatic discrimination of 2-acetamido-2-deoxy-D-mannopyranose-containing
RT disaccharides using beta-N-acetylhexosaminidases.";
RL Adv. Synth. Catal. 345:735-742(2003).
RN [8]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC STRAIN=CCF 1066 {ECO:0000303|PubMed:12681926};
RX PubMed=12681926; DOI=10.1016/s0008-6215(03)00044-2;
RA Weignerova L., Vavruskova P., Pisvejcova A., Thiem J., Kren V.;
RT "Fungal beta-N-acetylhexosaminidases with high beta-N-
RT acetylgalactosaminidase activity and their use for synthesis of beta-
RT GalNAc-containing oligosaccharides.";
RL Carbohydr. Res. 338:1003-1008(2003).
RN [9] {ECO:0007744|PDB:5OAR}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 19-96 AND 102-600 IN COMPLEX WITH
RP NAG-THIAZOLINE INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBUNIT, SUBCELLULAR LOCATION, PTM, IDENTIFICATION BY MASS
RP SPECTROMETRY, BIOTECHNOLOGY, ACTIVE SITES, GLYCOSYLATION AT THR-78; SER-83;
RP SER-84; ASN-318; ASN-353; ASN-387; ASN-428 AND ASN-500, AND DISULFIDE
RP BONDS.
RC STRAIN=CCF 1066 {ECO:0000303|PubMed:29239122};
RX PubMed=29239122; DOI=10.1111/febs.14360;
RA Skerlova J., Blaha J., Pachl P., Hofbauerova K., Kukacka Z., Man P.,
RA Pompach P., Novak P., Otwinowski Z., Brynda J., Vanek O., Rezacova P.;
RT "Crystal structure of native beta-N-acetylhexosaminidase isolated from
RT Aspergillusoryzae sheds light onto its substrate specificity, high
RT stability, and regulation by propeptide.";
RL FEBS J. 285:580-598(2018).
CC -!- FUNCTION: Selectively hydrolyzes GlcNAcbeta(1->4)GlcNAc (N,N'-
CC diacetylchitobiose) and Gal-NAcbeta(1->4)GlcNAc, but not their C-2
CC epimers GlcNAcbeta(1->4)ManNAc or Gal-NAcbeta(1->4)ManNAc. However,
CC hydrolyzes both GlcNAcbeta(1->6)GlcNAc and GlcNAcbeta(1->6)ManNAc
CC (Ref.7). Part of the binary chitinolytic system. Involved in
CC hydrolyzation of chitobiose and higher chito-oligomers (produced from
CC cell wall chitin by endochitinases), thus contributing to the formation
CC of germ tubes, fruit-bodies and septa during hyphenation (Probable).
CC Hydrolyzes synthetic substrate p-nitrophenyl-beta-N-acetyl-D-
CC glucosaminide (pNP-GlcNAc) (PubMed:17302431, PubMed:12723619, Ref.7).
CC Hydrolyzes synthetic substrate p-nitrophenyl-beta-N-acetyl-D-
CC galactosaminide (pNP-GalNAc) (PubMed:12723619). Hydrolyzes chromogenic
CC substrate 4-nitrophenyl-2-acetamido-2-deoxyglucopyranoside
CC (PubMed:21505251, PubMed:17509134, PubMed:29239122).
CC {ECO:0000269|PubMed:12723619, ECO:0000269|PubMed:17302431,
CC ECO:0000269|PubMed:17509134, ECO:0000269|PubMed:21505251,
CC ECO:0000269|PubMed:29239122, ECO:0000269|Ref.7, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC Evidence={ECO:0000255|PIRNR:PIRNR001093, ECO:0000269|PubMed:12681926,
CC ECO:0000269|PubMed:12723619, ECO:0000269|PubMed:15494009,
CC ECO:0000269|PubMed:17302431, ECO:0000269|PubMed:17509134,
CC ECO:0000269|PubMed:21505251, ECO:0000269|PubMed:29239122,
CC ECO:0000269|Ref.7};
CC -!- ACTIVITY REGULATION: Activated by non-covalent binding of the
CC propeptide to the catalytic domain (PubMed:15494009, PubMed:17302431,
CC PubMed:29239122). The concentration of the propeptide is regulated in
CC the endoplasmic reticulum and the propeptide thus regulates the amount
CC of the active enzyme at various stages of the growth cycle
CC (PubMed:17302431). The dimeric enzyme has about half of the maximal
CC activity in the presence of one bound propeptide, but is fully active
CC with two bound O-glycosylated propeptides (PubMed:15494009,
CC PubMed:17302431). Inhibited by N-acetylglucosamine (NAG)-thiazoline
CC (PubMed:17302431). {ECO:0000269|PubMed:15494009,
CC ECO:0000269|PubMed:17302431, ECO:0000269|PubMed:29239122}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.45 mM for 4-nitrophenyl-2-acetamido-2-deoxyglucopyranoside with
CC native glycosylated enzyme {ECO:0000269|PubMed:17509134};
CC KM=0.71 mM for 4-nitrophenyl-2-acetamido-2-deoxyglucopyranoside with
CC N-glycan deglycosylated enzyme {ECO:0000269|PubMed:17509134};
CC pH dependence:
CC Optimum pH is around 5 (PubMed:15494009, PubMed:17302431,
CC PubMed:12723619). More stable at alkaline than acidic pH
CC (PubMed:15494009, PubMed:12723619, PubMed:17509134).
CC {ECO:0000269|PubMed:12723619, ECO:0000269|PubMed:15494009,
CC ECO:0000269|PubMed:17302431, ECO:0000269|PubMed:17509134};
CC Temperature dependence:
CC Stable below 45 degrees Celsius. {ECO:0000269|PubMed:12723619};
CC -!- SUBUNIT: Homodimer (PubMed:15494009, PubMed:17302431, PubMed:21505251,
CC PubMed:17509134, PubMed:29239122). Oligosaccharide moieties may also
CC take part in the dimerization. Dimerization is a pH-dependent
CC reversible process (PubMed:17509134). The individual catalytic cores
CC dimerize and the catalytic core of one subunit in the active dimer
CC interacts with the propeptide of the second subunit (PubMed:29239122).
CC {ECO:0000269|PubMed:15494009, ECO:0000269|PubMed:17302431,
CC ECO:0000269|PubMed:17509134, ECO:0000269|PubMed:21505251,
CC ECO:0000269|PubMed:29239122}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12681926,
CC ECO:0000269|PubMed:12723619, ECO:0000269|PubMed:15494009,
CC ECO:0000269|PubMed:17302431, ECO:0000269|PubMed:17509134,
CC ECO:0000269|PubMed:21505251, ECO:0000269|PubMed:29239122}.
CC -!- PTM: The precursor of the propeptide is intracellularly processed in
CC the endoplasmic reticulum by a dibasic peptidase, different from Kex2,
CC removing Lys-97--Arg-101 from the precursor producing the activated
CC propeptide (PubMed:17302431). The propeptide binds non-covalently to
CC the catalytic domain (PubMed:15494009, PubMed:17302431,
CC PubMed:21505251, PubMed:29239122). Propeptide binding is necessary for
CC full activation of the enzyme, dimerization of the catalytic domain and
CC secretion of the active enzyme (PubMed:15494009, PubMed:17302431).
CC {ECO:0000269|PubMed:15494009, ECO:0000269|PubMed:17302431,
CC ECO:0000269|PubMed:21505251, ECO:0000269|PubMed:29239122}.
CC -!- PTM: O-glycosylated (PubMed:15494009, PubMed:17302431,
CC PubMed:29239122). O-glycosylation (O-mannosylation) at the C-terminus
CC of the propeptide is necessary for full enzyme activity
CC (PubMed:15494009). N-glycosylated (PubMed:15494009, PubMed:17302431,
CC PubMed:21505251, PubMed:17509134, PubMed:29239122). N-glycosylation of
CC the catalytic domain increases the stability and solubility of the
CC enzyme, especially at low pH (PubMed:15494009, PubMed:17509134).
CC Contains high mannose-type (M4-M11) N-glycans at the C-terminus
CC (PubMed:15494009, PubMed:17509134, PubMed:29239122). N-glycan
CC deglycosylation does not affect enzyme activity (PubMed:17509134).
CC {ECO:0000269|PubMed:15494009, ECO:0000269|PubMed:17302431,
CC ECO:0000269|PubMed:17509134, ECO:0000269|PubMed:21505251,
CC ECO:0000269|PubMed:29239122}.
CC -!- BIOTECHNOLOGY: This enzyme can be used for synthesis of lacto-N-triose
CC II (GlcNAcbeta1-3Galbeta1-4Glc), a major oligosaccharide component of
CC human breast milk, and its positional isomer (GlcNAcbeta1-6lactose)
CC from lactose and D-N-acetylglucosamine (GlcNAc) by reverse hydrolysis
CC reaction (PubMed:12723619). This enzyme can also be used for selective
CC large-scale removal of GlcNAcbeta(1->4)GlcNAc and
CC GalNAcbeta(1->4)GlcNAc from mixtures containing them and their C-2
CC epimers GlcNAcbeta(1->4)ManNAc and GalNAcbeta(1->4)ManNAc in order to
CC produce rare ManNAc-containing disaccharides that are important
CC components of microbial cell walls, and can be utilized as immunoactive
CC compounds (Ref.7). Utilized in the synthesis of beta-GalNAc-containing
CC oligosaccharides beta-D-GalpNAc-(1->4)-alpha-D-GlcpNAcOAll and beta-D-
CC GalpNAc-(1->6)-beta-D-Galp-(1->4)-alpha-D-GlcpNAcOAll
CC (PubMed:12681926). The structural features make this enzyme suitable
CC for biotechnological applications as it is very stable and has a robust
CC framework. The solved three-dimensional structure will aid in designing
CC engineered mutant enzyme variants with desired specificity and activity
CC (PubMed:29239122). {ECO:0000269|PubMed:12681926,
CC ECO:0000269|PubMed:12723619, ECO:0000305|PubMed:29239122,
CC ECO:0000305|Ref.7}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000255|PIRNR:PIRNR001093}.
CC -!- CAUTION: According to PubMed:29239122 Asn-525 is not glycosylated in
CC contrast to PubMed:17509134, which reports that all predicted N-
CC glycosylation sequences are glycosylated. {ECO:0000269|PubMed:17509134,
CC ECO:0000269|PubMed:29239122}.
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DR EMBL; AY091636; AAM13977.1; -; Genomic_DNA.
DR EMBL; AB085840; BAC41255.1; -; Genomic_DNA.
DR EMBL; MKZY01000002; OOO13099.1; -; Genomic_DNA.
DR PDB; 5OAR; X-ray; 2.30 A; A/C=19-96, B/D=102-600.
DR PDBsum; 5OAR; -.
DR AlphaFoldDB; Q8J2T0; -.
DR SMR; Q8J2T0; -.
DR STRING; 5062.CADAORAP00002577; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR CLAE; HEX20A_ASPOR; -.
DR VEuPathDB; FungiDB:AO090005000639; -.
DR eggNOG; KOG2499; Eukaryota.
DR OMA; QYWVDHA; -.
DR BRENDA; 3.2.1.52; 522.
DR Proteomes; UP000190312; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.379.10; -; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR029019; HEX_eukaryotic_N.
DR PANTHER; PTHR22600; PTHR22600; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF14845; Glycohydro_20b2; 1.
DR PIRSF; PIRSF001093; B-hxosamndse_ab_euk; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255, ECO:0000305|PubMed:17302431,
FT ECO:0000305|PubMed:21505251, ECO:0000305|PubMed:29239122"
FT PROPEP 19..96
FT /evidence="ECO:0000305|PubMed:17302431,
FT ECO:0000305|PubMed:21505251, ECO:0000305|PubMed:29239122"
FT /id="PRO_0000452799"
FT CHAIN 102..600
FT /note="Beta-hexosaminidase"
FT /evidence="ECO:0000305|PubMed:17302431,
FT ECO:0000305|PubMed:21505251, ECO:0000305|PubMed:29239122"
FT /id="PRO_5014107425"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q06GJ0,
FT ECO:0000305|PubMed:29239122, ECO:0007744|PDB:5OAR"
FT ACT_SITE 275
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q06GJ0,
FT ECO:0000305|PubMed:29239122, ECO:0007744|PDB:5OAR"
FT ACT_SITE 346
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q06GJ0,
FT ECO:0000305|PubMed:29239122, ECO:0007744|PDB:5OAR"
FT SITE 306
FT /note="Important determinant of glycosidic bond
FT specificity"
FT /evidence="ECO:0000250|UniProtKB:Q06GJ0"
FT SITE 307
FT /note="Essential for chitooligosaccharide substrate
FT binding"
FT /evidence="ECO:0000250|UniProtKB:Q06GJ0"
FT SITE 482
FT /note="Essential for chitooligosaccharide substrate
FT binding"
FT /evidence="ECO:0000250|UniProtKB:Q06GJ0"
FT SITE 525
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:29239122"
FT CARBOHYD 78
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:29239122,
FT ECO:0007744|PDB:5OAR"
FT CARBOHYD 83
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:29239122,
FT ECO:0007744|PDB:5OAR"
FT CARBOHYD 84
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:29239122,
FT ECO:0007744|PDB:5OAR"
FT CARBOHYD 318
FT /note="N-linked (HexNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:29239122"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:29239122, ECO:0007744|PDB:5OAR"
FT CARBOHYD 387
FT /note="N-linked (HexNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:29239122"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:17509134, ECO:0000269|PubMed:29239122,
FT ECO:0007744|PDB:5OAR"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:17509134, ECO:0000269|PubMed:29239122,
FT ECO:0007744|PDB:5OAR"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 290..351
FT /evidence="ECO:0000269|PubMed:29239122,
FT ECO:0007744|PDB:5OAR"
FT DISULFID 448..483
FT /evidence="ECO:0000269|PubMed:17509134,
FT ECO:0000269|PubMed:29239122, ECO:0007744|PDB:5OAR"
FT DISULFID 583..590
FT /evidence="ECO:0000269|PubMed:29239122,
FT ECO:0007744|PDB:5OAR"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 56..71
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 106..116
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 198..211
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 265..275
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 320..334
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 349..354
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 356..363
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 370..386
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 423..431
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:5OAR"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:5OAR"
FT TURN 446..449
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 489..493
FT /evidence="ECO:0007829|PDB:5OAR"
FT TURN 497..500
FT /evidence="ECO:0007829|PDB:5OAR"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:5OAR"
FT STRAND 509..516
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 523..530
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 533..542
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 554..570
FT /evidence="ECO:0007829|PDB:5OAR"
FT HELIX 581..585
FT /evidence="ECO:0007829|PDB:5OAR"
FT TURN 587..590
FT /evidence="ECO:0007829|PDB:5OAR"
SQ SEQUENCE 600 AA; 67525 MW; 30399ADCEEF5851B CRC64;
MRISQICTVL STVTSAVAVG VNPLPAPREI SWGSSGPKSI AGELQLRTDS DSADGIVADA
WNRAWETIVA LRWVPAATEA PISSFEPFPT PTAGASKKSK RASNSLQYVN VQVKDIEADL
QHGVDESYTL DVEEDSDTIT INAETVWGAL HAFTTLQQLV ISDGHGGLII EEPVNIKDSP
LYPYRGIMLD TGRNFVSLPK IFEQLEGMSL SKLNVLHWHI DDAQSWPIWV DVYPEMVKDA
YSPHEIYSRN DVRNIVNYAR ARGIRVIPEI DMPSHSSSGW KQVDPEMVTC TDSWWSNDDW
PLHTAVEPNP GQLDIIYNKT YEVVGNVYKE LSDIFPDHWF HVGGDEIQPN CFNFSTHVTK
WFAEDPSRTY HDLAQYWVDH AVPIFQNYSQ ERRLVMWEDI ALSADNAHDV PKNIVMQSWN
NGLEYISNLT ARGYDVIVSS SDFLYLDCGH GGFVTNDPRY NVMANPDANT PNFNYGGNGG
SWCAPYKTWQ RIYDYDFTLN LTETQAKHII GATAPLWGEQ VDDINVSSMF WPRAAALAEL
VWSGNRDANG NKRTTEMTQR ILNFREYLVA NGVQAQALVP KYCLQHPHAC DLYRNQAAIQ
