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Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase (EC 3.2.1.113) (ER alpha-1,2-mannosidase) (ER mannosidase 1) (ERMan1) (Man9GlcNAc2-specific-processing alpha-mannosidase) (Mannosidase alpha class 1B member 1)

 MA1B1_HUMAN             Reviewed;         699 AA.
Q9UKM7; Q5VSG3; Q9BRS9; Q9Y5K7;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 2.
22-NOV-2017, entry version 175.
RecName: Full=Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase;
EC=3.2.1.113 {ECO:0000269|PubMed:10409699, ECO:0000269|PubMed:12090241, ECO:0000269|PubMed:15713668};
AltName: Full=ER alpha-1,2-mannosidase;
AltName: Full=ER mannosidase 1;
Short=ERMan1;
AltName: Full=Man9GlcNAc2-specific-processing alpha-mannosidase;
AltName: Full=Mannosidase alpha class 1B member 1;
Name=MAN1B1; ORFNames=UNQ747/PRO1477;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
SPECIFICITY, AND VARIANT SER-59.
TISSUE=Fetal brain, Liver, Placenta, and Testis;
PubMed=10521544; DOI=10.1093/glycob/9.10.1073;
Tremblay L.O., Herscovics A.;
"Cloning and expression of a specific human alpha1,2-mannosidase that
trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan
biosynthesis.";
Glycobiology 9:1073-1078(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 37-699, TISSUE SPECIFICITY, ENZYME
ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, AND VARIANT SER-59.
PubMed=10409699; DOI=10.1074/jbc.274.30.21375;
Gonzalez D.S., Karaveg K., Vandersall-Nairn A.S., Lal A.,
Moremen K.W.;
"Identification, expression, and characterization of a cDNA encoding
human endoplasmic reticulum mannosidase I, the enzyme that catalyzes
the first mannose trimming step in mammalian Asn-linked
oligosaccharide biosynthesis.";
J. Biol. Chem. 274:21375-21386(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-59.
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-59.
TISSUE=Lung, and 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).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
PubMed=12090241;
Herscovics A., Romero P.A., Tremblay L.O.;
"The specificity of the yeast and human class I ER alpha 1,2-
mannosidases involved in ER quality control is not as strict
previously reported.";
Glycobiology 12:14G-15G(2002).
[7]
FUNCTION.
PubMed=18003979; DOI=10.1091/mbc.E07-05-0505;
Avezov E., Frenkel Z., Ehrlich M., Herscovics A., Lederkremer G.Z.;
"Endoplasmic reticulum (ER) mannosidase I is compartmentalized and
required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-
associated degradation.";
Mol. Biol. Cell 19:216-225(2008).
[8]
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).
[9]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 243-699, AND DISULFIDE BOND.
PubMed=10995765; DOI=10.1074/jbc.M006927200;
Vallee F., Karaveg K., Herscovics A., Moremen K.W., Howell P.L.;
"Structural basis for catalysis and inhibition of N-glycan processing
class I alpha 1,2-mannosidases.";
J. Biol. Chem. 275:41287-41298(2000).
[10]
X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 172-699 IN COMPLEX WITH A
THIO-DISACCHARIDE SUBSTRATE ANALOG, ENZYME ACTIVITY, AND MUTAGENESIS
OF GLU-330; ASP-463; HIS-524 AND GLU-599.
PubMed=15713668; DOI=10.1074/jbc.M500119200;
Karaveg K., Siriwardena A., Tempel W., Liu Z.J., Glushka J.,
Wang B.C., Moremen K.W.;
"Mechanism of class 1 (glycosylhydrolase family 47) {alpha}-
mannosidases involved in N-glycan processing and endoplasmic reticulum
quality control.";
J. Biol. Chem. 280:16197-16207(2005).
[11]
VARIANTS MRT15 CYS-334 AND LYS-397, AND CHARACTERIZATION OF VARIANTS
MRT15 CYS-334 AND LYS-397.
PubMed=21763484; DOI=10.1016/j.ajhg.2011.06.006;
Rafiq M.A., Kuss A.W., Puettmann L., Noor A., Ramiah A., Ali G.,
Hu H., Kerio N.A., Xiang Y., Garshasbi M., Khan M.A., Ishak G.E.,
Weksberg R., Ullmann R., Tzschach A., Kahrizi K., Mahmood K.,
Naeem F., Ayub M., Moremen K.W., Vincent J.B., Ropers H.H., Ansar M.,
Najmabadi H.;
"Mutations in the alpha 1,2-mannosidase gene, MAN1B1, cause autosomal-
recessive intellectual disability.";
Am. J. Hum. Genet. 89:176-182(2011).
-!- FUNCTION: Involved in glycoprotein quality control targeting of
misfolded glycoproteins for degradation. It primarily trims a
single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to
produce Man(8)GlcNAc(2), but at high enzyme concentrations, as
found in the ER quality control compartment (ERQC), it further
trims the carbohydrates to Man(5-6)GlcNAc(2).
{ECO:0000269|PubMed:12090241, ECO:0000269|PubMed:18003979}.
-!- CATALYTIC ACTIVITY: Hydrolysis of the terminal (1->2)-linked
alpha-D-mannose residues in the oligo-mannose oligosaccharide
Man(9)(GlcNAc)(2). {ECO:0000269|PubMed:10409699,
ECO:0000269|PubMed:12090241, ECO:0000269|PubMed:15713668}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000250|UniProtKB:P45700};
-!- ENZYME REGULATION: Inhibited by both 1-deoxymannojirimycin (dMNJ)
and kifunensine. {ECO:0000269|PubMed:10409699}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.4 mM for Man9GlcNAc2 {ECO:0000269|PubMed:10521544};
pH dependence:
Optimum pH is between 6.5 and 6.9.
{ECO:0000269|PubMed:10521544};
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000250|UniProtKB:P32906}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:10409699}; Single-pass type II membrane
protein {ECO:0000269|PubMed:10409699}.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:10409699, ECO:0000269|PubMed:10521544}.
-!- DISEASE: Mental retardation, autosomal recessive 15 (MRT15)
[MIM:614202]: A disorder characterized by significantly below
average general intellectual functioning associated with
impairments in adaptive behavior and manifested during the
developmental period. {ECO:0000269|PubMed:21763484}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-37 is the initiator.
{ECO:0000305}.
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EMBL; AF148509; AAF03215.1; -; mRNA.
EMBL; AF145732; AAD45504.1; -; mRNA.
EMBL; AY358465; AAQ88830.1; -; mRNA.
EMBL; AL929554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL807752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002953; AAH02953.1; -; mRNA.
EMBL; BC006079; AAH06079.1; -; mRNA.
CCDS; CCDS7029.1; -.
RefSeq; NP_057303.2; NM_016219.4.
UniGene; Hs.279881; -.
PDB; 1FMI; X-ray; 1.90 A; A=243-697.
PDB; 1FO2; X-ray; 2.38 A; A=243-699.
PDB; 1FO3; X-ray; 1.75 A; A=243-699.
PDB; 1X9D; X-ray; 1.41 A; A=172-699.
PDB; 5KIJ; X-ray; 1.65 A; A=245-696.
PDB; 5KK7; X-ray; 1.73 A; A/B=245-699.
PDBsum; 1FMI; -.
PDBsum; 1FO2; -.
PDBsum; 1FO3; -.
PDBsum; 1X9D; -.
PDBsum; 5KIJ; -.
PDBsum; 5KK7; -.
ProteinModelPortal; Q9UKM7; -.
SMR; Q9UKM7; -.
BioGrid; 116414; 7.
IntAct; Q9UKM7; 4.
MINT; MINT-6610355; -.
STRING; 9606.ENSP00000360645; -.
BindingDB; Q9UKM7; -.
ChEMBL; CHEMBL2308; -.
DrugBank; DB03206; Duvoglustat.
DrugBank; DB02742; Kifunensine.
DrugBank; DB02422; Methyl-2-S-(Alpha-D-Mannopyranosyl)-2-Thio-Alpha-D-Mannopyranoside.
CAZy; GH47; Glycoside Hydrolase Family 47.
iPTMnet; Q9UKM7; -.
PhosphoSitePlus; Q9UKM7; -.
SwissPalm; Q9UKM7; -.
BioMuta; MAN1B1; -.
DMDM; 93195043; -.
EPD; Q9UKM7; -.
MaxQB; Q9UKM7; -.
PaxDb; Q9UKM7; -.
PeptideAtlas; Q9UKM7; -.
PRIDE; Q9UKM7; -.
DNASU; 11253; -.
Ensembl; ENST00000371589; ENSP00000360645; ENSG00000177239.
GeneID; 11253; -.
KEGG; hsa:11253; -.
UCSC; uc004cld.3; human.
CTD; 11253; -.
DisGeNET; 11253; -.
EuPathDB; HostDB:ENSG00000177239.14; -.
GeneCards; MAN1B1; -.
H-InvDB; HIX0035043; -.
HGNC; HGNC:6823; MAN1B1.
HPA; HPA051516; -.
MalaCards; MAN1B1; -.
MIM; 604346; gene.
MIM; 614202; phenotype.
neXtProt; NX_Q9UKM7; -.
OpenTargets; ENSG00000177239; -.
Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
Orphanet; 397941; MAN1B1-CDG.
PharmGKB; PA30572; -.
eggNOG; KOG2431; Eukaryota.
eggNOG; ENOG410XP04; LUCA.
GeneTree; ENSGT00390000016529; -.
HOGENOM; HOG000181987; -.
HOVERGEN; HBG052389; -.
InParanoid; Q9UKM7; -.
KO; K01230; -.
OMA; DHLTCYL; -.
OrthoDB; EOG091G0342; -.
PhylomeDB; Q9UKM7; -.
TreeFam; TF354274; -.
BRENDA; 3.2.1.113; 2681.
Reactome; R-HSA-4793950; Defective MAN1B1 causes MRT15.
Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
SABIO-RK; Q9UKM7; -.
UniPathway; UPA00378; -.
ChiTaRS; MAN1B1; human.
EvolutionaryTrace; Q9UKM7; -.
GeneWiki; MAN1B1; -.
GenomeRNAi; 11253; -.
PRO; PR:Q9UKM7; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000177239; -.
CleanEx; HS_MAN1B1; -.
ExpressionAtlas; Q9UKM7; baseline and differential.
Genevisible; Q9UKM7; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IDA:ParkinsonsUK-UCL.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; TAS:ParkinsonsUK-UCL.
GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IDA:UniProtKB.
GO; GO:1904380; P:endoplasmic reticulum mannose trimming; IMP:ParkinsonsUK-UCL.
GO; GO:1904382; P:mannose trimming involved in glycoprotein ERAD pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
GO; GO:0009311; P:oligosaccharide metabolic process; TAS:ProtInc.
GO; GO:0036508; P:protein alpha-1,2-demannosylation; IDA:ParkinsonsUK-UCL.
GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
GO; GO:0036511; P:trimming of first mannose on A branch; TAS:Reactome.
GO; GO:0036512; P:trimming of second mannose on A branch; TAS:Reactome.
GO; GO:0036509; P:trimming of terminal mannose on B branch; IDA:ParkinsonsUK-UCL.
GO; GO:0036510; P:trimming of terminal mannose on C branch; TAS:Reactome.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
InterPro; IPR001382; Glyco_hydro_47.
InterPro; IPR036026; Seven-hairpin_glycosidases.
Pfam; PF01532; Glyco_hydro_47; 1.
PRINTS; PR00747; GLYHDRLASE47.
SUPFAM; SSF48225; SSF48225; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Disease mutation;
Disulfide bond; Endoplasmic reticulum; Glycosidase; Hydrolase;
Membrane; Mental retardation; Metal-binding; Polymorphism;
Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 699 Endoplasmic reticulum mannosyl-
oligosaccharide 1,2-alpha-mannosidase.
/FTId=PRO_0000210314.
TOPO_DOM 1 84 Cytoplasmic. {ECO:0000255}.
TRANSMEM 85 105 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 106 699 Lumenal. {ECO:0000255}.
COMPBIAS 39 45 Poly-Pro.
ACT_SITE 330 330 Proton donor. {ECO:0000305}.
ACT_SITE 463 463 {ECO:0000305}.
ACT_SITE 570 570 Proton donor.
{ECO:0000250|UniProtKB:P31723}.
ACT_SITE 599 599 {ECO:0000305}.
METAL 688 688 Calcium. {ECO:0000250|UniProtKB:P32906}.
DISULFID 527 556 {ECO:0000269|PubMed:10995765}.
VARIANT 59 59 N -> S (in dbSNP:rs968733).
{ECO:0000269|PubMed:10409699,
ECO:0000269|PubMed:10521544,
ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_055841.
VARIANT 334 334 R -> C (in MRT15; results in about 1300-
fold decrease in activity;
dbSNP:rs387906886).
{ECO:0000269|PubMed:21763484}.
/FTId=VAR_066592.
VARIANT 397 397 E -> K (in MRT15; disrupts stable protein
expression; dbSNP:rs387906885).
{ECO:0000269|PubMed:21763484}.
/FTId=VAR_066593.
MUTAGEN 330 330 E->Q: About 44-fold reduction in K(cat),
slight reduction in K(m), about 100-fold
increase in binding affinity for
Man(9)GlcnAc(2) but no change in binding
affinity for the inhibitor, dMNJ. Even
further greater reduction in K(cat) and
increase in K(m); when associated with Q-
599. {ECO:0000269|PubMed:15713668}.
MUTAGEN 463 463 D->N: Some reduction in K(cat) but no
change in K(m), abolishes almost all
binding to Man(9)GlcnAc(2) but reduced
binding to the inhibitor dMNJ by about
73-fold. Further reduction in K(m) but
slight increase in K(m); when associated
with Q-599.
{ECO:0000269|PubMed:15713668}.
MUTAGEN 524 524 H->A: About 4-fold reduction in K(cat).
{ECO:0000269|PubMed:15713668}.
MUTAGEN 599 599 E->Q: Very significant reduction in
K(cat), 4-fold weaker binding affinity
for Man(9)GlcnAc(2) but about 1000-fold
reduction in binding affinity for the
inhibitor, dMNJ. Significant reductions
in K(cat) and slight increase in K(m);
when associated with E-330 or N-463.
{ECO:0000269|PubMed:15713668}.
CONFLICT 204 204 T -> A (in Ref. 2; AAD45504).
{ECO:0000305}.
CONFLICT 223 223 S -> P (in Ref. 2; AAD45504).
{ECO:0000305}.
STRAND 244 246 {ECO:0000244|PDB:1FO3}.
HELIX 248 267 {ECO:0000244|PDB:1X9D}.
STRAND 271 275 {ECO:0000244|PDB:1X9D}.
TURN 276 279 {ECO:0000244|PDB:1X9D}.
STRAND 280 282 {ECO:0000244|PDB:1X9D}.
STRAND 284 287 {ECO:0000244|PDB:1X9D}.
HELIX 289 300 {ECO:0000244|PDB:1X9D}.
HELIX 304 317 {ECO:0000244|PDB:1X9D}.
STRAND 325 327 {ECO:0000244|PDB:1X9D}.
HELIX 328 346 {ECO:0000244|PDB:1X9D}.
HELIX 349 362 {ECO:0000244|PDB:1X9D}.
HELIX 363 366 {ECO:0000244|PDB:1X9D}.
STRAND 368 370 {ECO:0000244|PDB:1FO3}.
STRAND 375 378 {ECO:0000244|PDB:1X9D}.
TURN 379 381 {ECO:0000244|PDB:1X9D}.
STRAND 391 394 {ECO:0000244|PDB:1X9D}.
HELIX 395 399 {ECO:0000244|PDB:1X9D}.
HELIX 402 412 {ECO:0000244|PDB:1X9D}.
HELIX 416 429 {ECO:0000244|PDB:1X9D}.
STRAND 441 444 {ECO:0000244|PDB:1X9D}.
TURN 445 447 {ECO:0000244|PDB:1X9D}.
STRAND 450 452 {ECO:0000244|PDB:1X9D}.
TURN 460 462 {ECO:0000244|PDB:1X9D}.
HELIX 463 475 {ECO:0000244|PDB:1X9D}.
HELIX 481 497 {ECO:0000244|PDB:1X9D}.
STRAND 499 501 {ECO:0000244|PDB:1X9D}.
TURN 503 505 {ECO:0000244|PDB:1X9D}.
STRAND 508 510 {ECO:0000244|PDB:1X9D}.
STRAND 512 514 {ECO:0000244|PDB:1X9D}.
STRAND 517 519 {ECO:0000244|PDB:1X9D}.
STRAND 521 523 {ECO:0000244|PDB:1X9D}.
HELIX 524 527 {ECO:0000244|PDB:1X9D}.
HELIX 528 538 {ECO:0000244|PDB:1X9D}.
HELIX 543 561 {ECO:0000244|PDB:1X9D}.
STRAND 563 566 {ECO:0000244|PDB:1FO2}.
STRAND 570 573 {ECO:0000244|PDB:1X9D}.
STRAND 584 586 {ECO:0000244|PDB:5KIJ}.
HELIX 589 591 {ECO:0000244|PDB:1X9D}.
HELIX 599 611 {ECO:0000244|PDB:1X9D}.
HELIX 615 630 {ECO:0000244|PDB:1X9D}.
HELIX 659 662 {ECO:0000244|PDB:1X9D}.
HELIX 664 672 {ECO:0000244|PDB:1X9D}.
TURN 676 679 {ECO:0000244|PDB:5KIJ}.
TURN 681 683 {ECO:0000244|PDB:1X9D}.
STRAND 684 686 {ECO:0000244|PDB:1X9D}.
STRAND 692 694 {ECO:0000244|PDB:1X9D}.
SEQUENCE 699 AA; 79580 MW; B8BF3BE333D90261 CRC64;
MAACEGRRSG ALGSSQSDFL TPPVGGAPWA VATTVVMYPP PPPPPHRDFI SVTLSFGENY
DNSKSWRRRS CWRKWKQLSR LQRNMILFLL AFLLFCGLLF YINLADHWKA LAFRLEEEQK
MRPEIAGLKP ANPPVLPAPQ KADTDPENLP EISSQKTQRH IQRGPPHLQI RPPSQDLKDG
TQEEATKRQE APVDPRPEGD PQRTVISWRG AVIEPEQGTE LPSRRAEVPT KPPLPPARTQ
GTPVHLNYRQ KGVIDVFLHA WKGYRKFAWG HDELKPVSRS FSEWFGLGLT LIDALDTMWI
LGLRKEFEEA RKWVSKKLHF EKDVDVNLFE STIRILGGLL SAYHLSGDSL FLRKAEDFGN
RLMPAFRTPS KIPYSDVNIG TGVAHPPRWT SDSTVAEVTS IQLEFRELSR LTGDKKFQEA
VEKVTQHIHG LSGKKDGLVP MFINTHSGLF THLGVFTLGA RADSYYEYLL KQWIQGGKQE
TQLLEDYVEA IEGVRTHLLR HSEPSKLTFV GELAHGRFSA KMDHLVCFLP GTLALGVYHG
LPASHMELAQ ELMETCYQMN RQMETGLSPE IVHFNLYPQP GRRDVEVKPA DRHNLLRPET
VESLFYLYRV TGDRKYQDWG WEILQSFSRF TRVPSGGYSS INNVQDPQKP EPRDKMESFF
LGETLKYLFL LFSDDPNLLS LDAYVFNTEA HPLPIWTPA


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