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   08-NOV-2023, entry version 144.
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 NOD
RC   {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   GlyCosmos; Q8K2I4; 10 sites, 1 glycan.
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; 10090-ENSMUSP00000029814; -.
DR   PeptideAtlas; Q8K2I4; -.
DR   ProteomicsDB; 295811; -.
DR   DNASU; 110173; -.
DR   GeneID; 110173; -.
DR   KEGG; mmu:110173; -.
DR   UCSC; uc008rlu.2; mouse.
DR   AGR; MGI:88175; -.
DR   CTD; 4126; -.
DR   MGI; MGI:88175; Manba.
DR   eggNOG; KOG2230; Eukaryota.
DR   InParanoid; Q8K2I4; -.
DR   OrthoDB; 2504097at2759; -.
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 78 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:0043202; C:lysosomal lumen; IDA:MGI.
DR   GO; GO:0005764; C:lysosome; TAS: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:0006516; P:glycoprotein catabolic process; IDA:UniProtKB.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IDA:MGI.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR   PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF17753; Ig_mannosidase; 1.
DR   Pfam; PF17786; Mannosidase_ig; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 3.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 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;
FT                   BAE24954/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;
FT                   BAE24954/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
//