PAOX_MOUSE
ID PAOX_MOUSE Reviewed; 504 AA.
AC Q8C0L6; Q8K254;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Peroxisomal N(1)-acetyl-spermine/spermidine oxidase;
DE EC=1.5.3.13 {ECO:0000269|PubMed:12660232, ECO:0000269|PubMed:28029774};
DE AltName: Full=Polyamine oxidase;
GN Name=Paox; Synonyms=Pao;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, TISSUE SPECIFICITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12660232; DOI=10.1074/jbc.m302149200;
RA Wu T., Yankovskaya V., McIntire W.S.;
RT "Cloning, sequencing, and heterologous expression of the murine peroxisomal
RT flavoprotein, N(1)-acetylated polyamine oxidase.";
RL J. Biol. Chem. 278:20514-20525(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
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]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
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 [5] {ECO:0007744|PDB:5LAE, ECO:0007744|PDB:5LFO, ECO:0007744|PDB:5LGB, ECO:0007744|PDB:5MBX}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 4-504 IN COMPLEXES WITH FAD;
RP N(1)-ACETYLSPERMINE AND SYNTHETIC INHIBITOR, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, MUTAGENESIS OF ASN-313, AND PATHWAY.
RX PubMed=28029774; DOI=10.1021/acs.biochem.6b01140;
RA Sjogren T., Wassvik C.M., Snijder A., Aagaard A., Kumanomidou T.,
RA Barlind L., Kaminski T.P., Kashima A., Yokota T., Fjellstrom O.;
RT "The Structure of Murine N1-Acetylspermine Oxidase Reveals Molecular
RT Details of Vertebrate Polyamine Catabolism.";
RL Biochemistry 56:458-467(2017).
CC -!- FUNCTION: Flavoenzyme which catalyzes the oxidation of N(1)-
CC acetylspermine to spermidine and is thus involved in the polyamine
CC back-conversion (PubMed:12660232, PubMed:28029774). Can also oxidize
CC N(1)-acetylspermidine to putrescine. Substrate specificity: N(1)-
CC acetylspermine = N(1)-acetylspermidine > N(1),N(12)-diacylspermine >>
CC spermine. Does not oxidize spermidine. Plays an important role in the
CC regulation of polyamine intracellular concentration and has the
CC potential to act as a determinant of cellular sensitivity to the
CC antitumor polyamine analogs (PubMed:12660232).
CC {ECO:0000269|PubMed:12660232, ECO:0000269|PubMed:28029774}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1)-acetylspermine + O2 = 3-acetamidopropanal + H2O2 +
CC spermidine; Xref=Rhea:RHEA:25800, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:30322,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:58101; EC=1.5.3.13;
CC Evidence={ECO:0000269|PubMed:12660232, ECO:0000269|PubMed:28029774};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1)-acetylspermidine + O2 = 3-acetamidopropanal + H2O2
CC + putrescine; Xref=Rhea:RHEA:25812, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:30322,
CC ChEBI:CHEBI:58324, ChEBI:CHEBI:326268; EC=1.5.3.13;
CC Evidence={ECO:0000269|PubMed:12660232};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1),N(12)-diacetylspermine + O2 = 3-acetamidopropanal +
CC H2O2 + N(1)-acetylspermidine; Xref=Rhea:RHEA:25868,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:30322, ChEBI:CHEBI:58324, ChEBI:CHEBI:58550; EC=1.5.3.13;
CC Evidence={ECO:0000269|PubMed:12660232};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:12660232, ECO:0000269|PubMed:28029774};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:12660232,
CC ECO:0000269|PubMed:28029774};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.78 uM for N(1)-acetylspermine {ECO:0000269|PubMed:12660232};
CC KM=36.8 uM for N(1)-acetylspermidine {ECO:0000269|PubMed:12660232};
CC KM=716 uM for spermine {ECO:0000269|PubMed:12660232};
CC KM=150 uM for N(1),N(12)-diacetylspermine
CC {ECO:0000269|PubMed:12660232};
CC -!- PATHWAY: Amine and polyamine metabolism; spermine metabolism.
CC {ECO:0000269|PubMed:12660232, ECO:0000269|PubMed:28029774}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. Cytoplasm
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C0L6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C0L6-2; Sequence=VSP_011263, VSP_011264;
CC -!- TISSUE SPECIFICITY: Widely expressed at different developmental stages.
CC Expressed at high level in the liver and the stomach, expressed at
CC lower level in heart, spleen, thymus, small intestine, muscle,
CC pancreas, uterus, and breast and expressed at very low level in brain,
CC kidney, lung, testis, skin, adrenal gland and prostate gland.
CC {ECO:0000269|PubMed:12660232}.
CC -!- DEVELOPMENTAL STAGE: Expression increased during embryonic development:
CC there is a gradual increase in the tissues on going from 8.5 to 19 day
CC embryos. In the breast, expression is very low in virgin mouse and
CC quite high in pregnant mouse, but decreases in lactating and involuting
CC breasts.
CC -!- INDUCTION: By polyamine analogs.
CC -!- MISCELLANEOUS: Oxidizes N(1)-acetylated polyamines on the exo-side of
CC their N(4)-amino groups. Plant PAO oxidizes spermine on the endo-side
CC of the N(4)-nitrogen (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: N-ethylated polyamines are also good substrates for this
CC enzyme: they have been used for cancer clinical trials. They down-
CC regulate polyamine biosynthetic enzymes, but dramatically up-regulate
CC SSAT synthesis, which results in mammalian cells becoming apoptotic.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; AF226656; AAN40705.2; -; mRNA.
DR EMBL; AK030664; BAC27070.1; -; mRNA.
DR EMBL; BC033913; AAH33913.1; -; mRNA.
DR EMBL; BC082783; AAH82783.1; -; mRNA.
DR CCDS; CCDS21965.1; -. [Q8C0L6-1]
DR RefSeq; NP_722478.2; NM_153783.4. [Q8C0L6-1]
DR PDB; 5LAE; X-ray; 1.85 A; A=4-450, A=458-504.
DR PDB; 5LFO; X-ray; 1.66 A; A=4-450, A=458-504.
DR PDB; 5LGB; X-ray; 1.80 A; A=4-450, A=458-504.
DR PDB; 5MBX; X-ray; 1.40 A; A=4-504.
DR PDBsum; 5LAE; -.
DR PDBsum; 5LFO; -.
DR PDBsum; 5LGB; -.
DR PDBsum; 5MBX; -.
DR AlphaFoldDB; Q8C0L6; -.
DR SMR; Q8C0L6; -.
DR STRING; 10090.ENSMUSP00000026537; -.
DR BindingDB; Q8C0L6; -.
DR ChEMBL; CHEMBL3408; -.
DR iPTMnet; Q8C0L6; -.
DR PhosphoSitePlus; Q8C0L6; -.
DR EPD; Q8C0L6; -.
DR MaxQB; Q8C0L6; -.
DR PaxDb; Q8C0L6; -.
DR PeptideAtlas; Q8C0L6; -.
DR PRIDE; Q8C0L6; -.
DR ProteomicsDB; 288053; -. [Q8C0L6-1]
DR ProteomicsDB; 288054; -. [Q8C0L6-2]
DR DNASU; 212503; -.
DR Ensembl; ENSMUST00000026537; ENSMUSP00000026537; ENSMUSG00000025464. [Q8C0L6-1]
DR GeneID; 212503; -.
DR KEGG; mmu:212503; -.
DR UCSC; uc009kha.1; mouse. [Q8C0L6-2]
DR UCSC; uc009khb.1; mouse. [Q8C0L6-1]
DR CTD; 196743; -.
DR MGI; MGI:1916983; Paox.
DR VEuPathDB; HostDB:ENSMUSG00000025464; -.
DR eggNOG; KOG0685; Eukaryota.
DR GeneTree; ENSGT00940000158274; -.
DR HOGENOM; CLU_004498_2_3_1; -.
DR InParanoid; Q8C0L6; -.
DR OMA; LEPGNRW; -.
DR OrthoDB; 508351at2759; -.
DR PhylomeDB; Q8C0L6; -.
DR TreeFam; TF318348; -.
DR BioCyc; MetaCyc:MON-14466; -.
DR BRENDA; 1.5.3.13; 3474.
DR Reactome; R-MMU-141334; PAOs oxidise polyamines to amines.
DR Reactome; R-MMU-351200; Interconversion of polyamines.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR SABIO-RK; Q8C0L6; -.
DR UniPathway; UPA00826; -.
DR BioGRID-ORCS; 212503; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Paox; mouse.
DR PRO; PR:Q8C0L6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8C0L6; protein.
DR Bgee; ENSMUSG00000025464; Expressed in liver and 74 other tissues.
DR ExpressionAtlas; Q8C0L6; baseline and differential.
DR Genevisible; Q8C0L6; MM.
DR GO; GO:0005782; C:peroxisomal matrix; ISO:MGI.
DR GO; GO:0052899; F:N(1),N(12)-diacetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052904; F:N1-acetylspermidine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052903; F:N1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0046592; F:polyamine oxidase activity; IDA:MGI.
DR GO; GO:0052902; F:spermidine:oxygen oxidoreductase (3-aminopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0006598; P:polyamine catabolic process; IDA:MGI.
DR GO; GO:1901307; P:positive regulation of spermidine biosynthetic process; ISO:MGI.
DR GO; GO:0009446; P:putrescine biosynthetic process; ISO:MGI.
DR GO; GO:0009447; P:putrescine catabolic process; ISO:MGI.
DR GO; GO:0046203; P:spermidine catabolic process; ISO:MGI.
DR GO; GO:0046208; P:spermine catabolic process; ISO:MGI.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; FAD; Flavoprotein;
KW Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..504
FT /note="Peroxisomal N(1)-acetyl-spermine/spermidine oxidase"
FT /id="PRO_0000099876"
FT MOTIF 502..504
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28029774,
FT ECO:0007744|PDB:5LAE, ECO:0007744|PDB:5LFO,
FT ECO:0007744|PDB:5MBX"
FT BINDING 37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28029774,
FT ECO:0007744|PDB:5LAE, ECO:0007744|PDB:5LFO,
FT ECO:0007744|PDB:5MBX"
FT BINDING 45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28029774,
FT ECO:0007744|PDB:5LAE, ECO:0007744|PDB:5LFO,
FT ECO:0007744|PDB:5MBX"
FT BINDING 61..62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28029774,
FT ECO:0007744|PDB:5LAE, ECO:0007744|PDB:5LFO,
FT ECO:0007744|PDB:5MBX"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28029774,
FT ECO:0007744|PDB:5MBX"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28029774,
FT ECO:0007744|PDB:5LFO, ECO:0007744|PDB:5MBX"
FT BINDING 240
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28029774,
FT ECO:0007744|PDB:5LAE, ECO:0007744|PDB:5LFO,
FT ECO:0007744|PDB:5MBX"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28029774,
FT ECO:0007744|PDB:5LFO, ECO:0007744|PDB:5MBX"
FT BINDING 465
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28029774,
FT ECO:0007744|PDB:5LAE, ECO:0007744|PDB:5LFO,
FT ECO:0007744|PDB:5MBX"
FT BINDING 474..475
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28029774,
FT ECO:0007744|PDB:5LAE, ECO:0007744|PDB:5LFO,
FT ECO:0007744|PDB:5MBX"
FT VAR_SEQ 1..280
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011263"
FT VAR_SEQ 281..282
FT /note="PL -> ME (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011264"
FT MUTAGEN 313
FT /note="N->A,D,L,T: Decreased enzyme activity with N(1)-
FT acetylspermine."
FT /evidence="ECO:0000269|PubMed:28029774"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:5LAE"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5LFO"
FT HELIX 116..132
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 170..188
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:5MBX"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 282..292
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 313..322
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:5MBX"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 370..378
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 389..403
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:5MBX"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:5MBX"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 439..446
FT /evidence="ECO:0007829|PDB:5MBX"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:5MBX"
FT TURN 469..473
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 475..495
FT /evidence="ECO:0007829|PDB:5MBX"
FT HELIX 496..500
FT /evidence="ECO:0007829|PDB:5MBX"
SQ SEQUENCE 504 AA; 55447 MW; B40BD34C7A0B98F1 CRC64;
MAFPGPRVLV VGSGIAGLGA AQKLCSHRAA PHLRVLEATA SAGGRIRSER CFGGVVELGA
HWIHGPSQDN PVFQLAAEFG LLGEKELSEE NQLVDTGGHV ALPSMIWSSS GTSVSLELMT
EMARLFYGLI ERTREFLNES ETPMASVGEF LKKEISQQVA SWTEDDEDTR KRKLAILNTF
FNIECCVSGT HSMDLVALAP FGEYTVLPGL DCILAGGYQG LTDRILASLP KDTVAFDKPV
KTIHWNGSFQ EAAFPGETFP VLVECEDGAR LPAHHVIVTV PLGFLKEHQD TFFEPPLPAK
KAEAIKKLGF GTNNKIFLEF EEPFWEPDCQ FIQVVWEDTS PLQDTALSLQ DTWFKKLIGF
LVQPSFESSH VLCGFIAGLE SEFMETLSDE EVLLSLTQVL RRVTGNPQLP AAKSVRRSQW
HSAPYTRGSY SYVAVGSTGD DLDLMAQPLP EDGTGTQLQV LFAGEATHRT FYSTTHGALL
SGWREADRLV SLWDSQVEQS RPRL
