MANBA_MOUSE
ID MANBA_MOUSE Reviewed; 879 AA.
AC Q8K2I4; Q3TDB3; Q3TLS7; Q3UQT5; Q99MS1; Q9CRH3;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Beta-mannosidase;
DE EC=3.2.1.25 {ECO:0000269|PubMed:16377659, ECO:0000305|PubMed:30552791};
DE AltName: Full=Lysosomal beta A mannosidase;
DE AltName: Full=Mannanase;
DE Short=Mannase;
DE Flags: Precursor;
GN Name=Manba {ECO:0000312|MGI:MGI:88175};
GN Synonyms=Bmn {ECO:0000303|PubMed:11892998};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK18177.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAK18177.1};
RC TISSUE=Spleen {ECO:0000269|PubMed:11892998};
RX PubMed=11892998; DOI=10.1023/a:1013286216030;
RA Beccari T., Bibi L., Stinchi S., Stirling J.L., Orlacchio A.;
RT "Mouse beta-mannosidase, cDNA cloning, expression, and chromosomal
RT localization.";
RL Biosci. Rep. 21:315-323(2001).
RN [2] {ECO:0000312|EMBL:BAB27069.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB27069.1}, and
RC NOD {ECO:0000312|EMBL:BAE41690.1};
RC TISSUE=Dendritic cell, Embryonic heart {ECO:0000312|EMBL:BAE24954.1},
RC Embryonic stem cell, and Mammary gland {ECO:0000312|EMBL:BAE38715.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|EMBL:AAH31409.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH31409.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH31409.1};
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 [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16377659; DOI=10.1093/hmg/ddi465;
RA Zhu M., Lovell K.L., Patterson J.S., Saunders T.L., Hughes E.D.,
RA Friderici K.H.;
RT "Beta-mannosidosis mice: a model for the human lysosomal storage disease.";
RL Hum. Mol. Genet. 15:493-500(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
RC Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 22-879 OF APOPROTEIN AND IN
RP COMPLEX WITH MANNOSE, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL
RP PROPERTIES, GLYCOSYLATION AT ASN-35; ASN-77; ASN-89; ASN-113; ASN-226;
RP ASN-297; ASN-302; ASN-736 AND ASN-803, AND DISULFIDE BOND.
RX PubMed=30552791; DOI=10.1111/febs.14731;
RA Gytz H., Liang J., Liang Y., Gorelik A., Illes K., Nagar B.;
RT "The structure of mammalian beta-mannosidase provides insight into beta-
RT mannosidosis and nystagmus.";
RL FEBS J. 286:1319-1331(2019).
CC -!- FUNCTION: Exoglycosidase that cleaves the single beta-linked mannose
CC residue from the non-reducing end of all N-linked glycoprotein
CC oligosaccharides. {ECO:0000269|PubMed:16377659}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues
CC in beta-D-mannosides.; EC=3.2.1.25;
CC Evidence={ECO:0000269|PubMed:16377659, ECO:0000305|PubMed:30552791};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:30552791};
CC -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC {ECO:0000269|PubMed:16377659}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:30552791}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305|PubMed:16377659}.
CC -!- TISSUE SPECIFICITY: Highest level in liver, high levels in lung,
CC testis, skin and spleen, moderate level in thymus. Activity found in
CC plasma, kidney, liver, spleen, pancreas, brain, testis, epididymis,
CC heart, lung and skeletal muscle. {ECO:0000269|PubMed:11892998,
CC ECO:0000269|PubMed:16377659}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate and
CC display no visible phenotype for at least one year. However, they
CC display vacuolation in the central nervous system and accumulation of
CC disaccharides in brain and epididymis, detectable already at four weeks
CC after birth. {ECO:0000269|PubMed:16377659}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000255}.
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DR EMBL; AF306557; AAK18177.1; -; mRNA.
DR EMBL; AK010623; BAB27069.1; -; mRNA.
DR EMBL; AK142165; BAE24954.1; -; mRNA.
DR EMBL; AK166340; BAE38715.1; -; mRNA.
DR EMBL; AK170290; BAE41690.1; -; mRNA.
DR EMBL; BC031409; AAH31409.1; -; mRNA.
DR CCDS; CCDS17857.1; -.
DR RefSeq; NP_081564.3; NM_027288.3.
DR PDB; 6DDT; X-ray; 2.10 A; A=22-879.
DR PDB; 6DDU; X-ray; 2.67 A; A=22-879.
DR PDBsum; 6DDT; -.
DR PDBsum; 6DDU; -.
DR AlphaFoldDB; Q8K2I4; -.
DR SMR; Q8K2I4; -.
DR BioGRID; 225356; 1.
DR STRING; 10090.ENSMUSP00000029814; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR GlyConnect; 2153; 1 N-Linked glycan (1 site).
DR GlyGen; Q8K2I4; 10 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8K2I4; -.
DR PhosphoSitePlus; Q8K2I4; -.
DR EPD; Q8K2I4; -.
DR MaxQB; Q8K2I4; -.
DR PaxDb; Q8K2I4; -.
DR PeptideAtlas; Q8K2I4; -.
DR PRIDE; Q8K2I4; -.
DR ProteomicsDB; 295811; -.
DR DNASU; 110173; -.
DR GeneID; 110173; -.
DR KEGG; mmu:110173; -.
DR UCSC; uc008rlu.2; mouse.
DR CTD; 4126; -.
DR MGI; MGI:88175; Manba.
DR eggNOG; KOG2230; Eukaryota.
DR InParanoid; Q8K2I4; -.
DR OrthoDB; 517710at2759; -.
DR PhylomeDB; Q8K2I4; -.
DR TreeFam; TF105723; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8853383; Lysosomal oligosaccharide catabolism.
DR UniPathway; UPA00280; -.
DR BioGRID-ORCS; 110173; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Manba; mouse.
DR PRO; PR:Q8K2I4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8K2I4; protein.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0004567; F:beta-mannosidase activity; IDA:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IDA:MGI.
DR GO; GO:0005537; F:mannose binding; ISO:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006516; P:glycoprotein catabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR041625; Beta-mannosidase_Ig.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR041447; Mannosidase_ig.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF17753; Ig_mannosidase; 1.
DR Pfam; PF17786; Mannosidase_ig; 1.
DR SUPFAM; SSF49303; SSF49303; 3.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Lysosome; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..879
FT /note="Beta-mannosidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000250613"
FT ACT_SITE 457
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:30552791"
FT ACT_SITE 554
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:30552791"
FT BINDING 190..192
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30552791,
FT ECO:0007744|PDB:6DDU"
FT BINDING 456
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30552791,
FT ECO:0007744|PDB:6DDU"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30552791,
FT ECO:0007744|PDB:6DDT"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30552791,
FT ECO:0007744|PDB:6DDT"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30552791,
FT ECO:0007744|PDB:6DDT"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30552791,
FT ECO:0007744|PDB:6DDT"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30552791,
FT ECO:0007744|PDB:6DDT"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30552791,
FT ECO:0007744|PDB:6DDT"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30552791,
FT ECO:0007744|PDB:6DDT"
FT CARBOHYD 736
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30552791,
FT ECO:0007744|PDB:6DDT"
FT CARBOHYD 803
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30552791,
FT ECO:0007744|PDB:6DDT"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 167..176
FT /evidence="ECO:0000269|PubMed:30552791,
FT ECO:0007744|PDB:6DDT"
FT DISULFID 540..629
FT /evidence="ECO:0000269|PubMed:30552791,
FT ECO:0007744|PDB:6DDT"
FT DISULFID 732..761
FT /evidence="ECO:0000269|PubMed:30552791,
FT ECO:0007744|PDB:6DDT"
FT DISULFID 764..769
FT /evidence="ECO:0000269|PubMed:30552791,
FT ECO:0007744|PDB:6DDT"
FT CONFLICT 130
FT /note="I -> V (in Ref. 1; AAK18177 and 2; BAE24954/
FT BAE38715)"
FT /evidence="ECO:0000305"
FT CONFLICT 143..145
FT /note="QFR -> RFW (in Ref. 2; BAE38715)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="C -> R (in Ref. 2; BAE38715)"
FT /evidence="ECO:0000305"
FT CONFLICT 160..162
FT /note="SYR -> RYP (in Ref. 2; BAE38715)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="K -> E (in Ref. 1; AAK18177 and 2; BAE24954/
FT BAE38715/BAE41690)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="G -> S (in Ref. 1; AAK18177 and 2; BAE24954)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="N -> H (in Ref. 2; BAE38715)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="F -> L (in Ref. 2; BAE24954)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="K -> N (in Ref. 2; BAE38715)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="M -> I (in Ref. 2; BAE38715)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="H -> Y (in Ref. 2; BAE38715)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="G -> R (in Ref. 2; BAE38715)"
FT /evidence="ECO:0000305"
FT CONFLICT 834
FT /note="S -> G (in Ref. 2; BAE38715)"
FT /evidence="ECO:0000305"
FT CONFLICT 848
FT /note="R -> Q (in Ref. 2; BAE38715)"
FT /evidence="ECO:0000305"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:6DDT"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:6DDT"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 205..225
FT /evidence="ECO:0007829|PDB:6DDT"
FT TURN 226..229
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 230..245
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 247..255
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 301..309
FT /evidence="ECO:0007829|PDB:6DDT"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:6DDU"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:6DDU"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 369..381
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 398..407
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 426..443
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 449..453
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 458..464
FT /evidence="ECO:0007829|PDB:6DDT"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:6DDT"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 474..485
FT /evidence="ECO:0007829|PDB:6DDT"
FT TURN 486..488
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 489..496
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 502..507
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 511..515
FT /evidence="ECO:0007829|PDB:6DDT"
FT TURN 516..518
FT /evidence="ECO:0007829|PDB:6DDU"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 552..555
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 563..567
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 580..585
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 591..600
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 611..639
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 653..657
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 662..665
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 679..687
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 689..698
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 701..708
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 714..724
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 734..741
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 746..753
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 754..759
FT /evidence="ECO:0007829|PDB:6DDT"
FT TURN 766..768
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 769..774
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 779..781
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 786..791
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 793..795
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 805..811
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 814..820
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 825..831
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 835..841
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 843..846
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 848..859
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 863..869
FT /evidence="ECO:0007829|PDB:6DDT"
FT STRAND 871..873
FT /evidence="ECO:0007829|PDB:6DDT"
FT HELIX 875..878
FT /evidence="ECO:0007829|PDB:6DDT"
SQ SEQUENCE 879 AA; 100831 MW; 1DE203C44557719B CRC64;
MHLHLLLILA LFRAGCVVAG PSYSLSGSWR VSNGNGSLEL PATVPGYVHS ALHQHGLIQD
PYYRFNDLNY RWISLDNWTY STEFKIPFNL SEWQKVKLIF DGVDTVAEIL FNNVTIGKTD
NMFTGYSFDI TNVVKDVNSL KLQFRSAVQY AECQSKAHTS YRVPPECPPV EQKGECHVNF
IRKAQCSFSW DWGPSFPSQG IWKDVRIEAY NIAHLDYLTF LPVYDNASQA WNIEIKASFD
VASSKSVGGQ VTVAIPQLKT QQTNDIELQQ EQRIVKLLVK IRKDVAVETW WPRGHGNQTG
YNMTILFALD GGLKIEKAAK VYFRTVQLIE EGIKGSPGLS FYFKINGLPI FLKGSNWIPA
DSFQDKVTSD RLQLLFQSVV DANMNTLRVW GGGIYEQDEF YALCDELGIM VWQDFMFASA
LYPTEPGFLA SVRKEVTYQV RRLKSHPSII IWSGNNENEV ALSVNWFHVN PRDMKTYIDD
YVTLYVKNIR KIVLSEDKSR PFIASSPTNG MKTMEEGWIS YDPYSIQYGD IHFYNYADDC
WNWKIFPKAR LVSEYGYQSW PSFSTLEKVS SQEDWAYNSR FSLHRQHHED GNHQMLHQVK
MHFKLPQGTD PLRTFKDTIY LTQVMQAQCI KTETEFYLRS RSEIVDGKGH TMGALYWQLN
DIWQAPSWAS LEYGGKWKML HYFARRFFAP LLPVGFEDEG VFYVYGVSDL HKDHHTQLTV
RLHHWSSPKP LCSLVNSSIV VKAGEAVVLF QMPVSELLKR CRGCTRETCV VSFYFSTDKE
LFSPTNYHFL SSLKDAKGLL EANITVNISQ KGNVFVFDLE TSAVAPFVWL DVGSIPGRFS
DNGFLMIRKK LSVLFYPWKP TSKSELQQAF SVTSLTDTY
