ID   CBR3_HUMAN              Reviewed;         277 AA.
AC   O75828; Q6FHP2;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 198.
DE   RecName: Full=Carbonyl reductase [NADPH] 3 {ECO:0000305};
DE            EC=1.1.1.184 {ECO:0000269|PubMed:18493841};
DE   AltName: Full=NADPH-dependent carbonyl reductase 3;
DE   AltName: Full=Quinone reductase CBR3 {ECO:0000305};
DE            EC=1.6.5.10 {ECO:0000269|PubMed:15537833, ECO:0000269|PubMed:19841672};
DE   AltName: Full=Short chain dehydrogenase/reductase family 21C member 2;
GN   Name=CBR3 {ECO:0000312|HGNC:HGNC:1549};
GN   Synonyms=SDR21C2 {ECO:0000312|HGNC:HGNC:1549};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=9740676; DOI=10.1006/geno.1998.5380;
RA   Watanabe K., Sugawara C., Ono A., Fukuzumi Y., Itakura S., Yamazaki M.,
RA   Tashiro H., Osoegawa K., Soeda E., Nomura T.;
RT   "Mapping of a novel human carbonyl reductase, CBR3, and ribosomal
RT   pseudogenes to human chromosome 21q22.2.";
RL   Genomics 52:95-100(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fetal kidney;
RA   Shimizu N., Kudoh J., Shibuya K.;
RT   "Homo sapiens mRNA for NADPH-dependent carbonyl reductase 3, complete
RT   cds.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fetal brain;
RA   Terada T., Mizobuchi H.;
RT   "Human fetal brain carbonyl reductases.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TYR-4; VAL-84; SER-131;
RP   LEU-235 AND MET-244.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA   Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA   Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA   Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA   Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA   Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA   Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA   Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA   Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA   Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA   Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANT MET-244, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=15537833; DOI=10.1124/dmd.104.002006;
RA   Lakhman S.S., Ghosh D., Blanco J.G.;
RT   "Functional significance of a natural allelic variant of human carbonyl
RT   reductase 3 (CBR3).";
RL   Drug Metab. Dispos. 33:254-257(2005).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND CATALYTIC ACTIVITY.
RX   PubMed=18493841; DOI=10.1007/s11010-008-9794-5;
RA   Miura T., Nishinaka T., Terada T.;
RT   "Different functions between human monomeric carbonyl reductase 3 and
RT   carbonyl reductase 1.";
RL   Mol. Cell. Biochem. 315:113-121(2008).
RN   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND MUTAGENESIS OF GLN-142; PRO-230 AND ASP-236.
RX   PubMed=19841672; DOI=10.1371/journal.pone.0007113;
RA   Pilka E.S., Niesen F.H., Lee W.H., El-Hawari Y., Dunford J.E., Kochan G.,
RA   Wsol V., Martin H.J., Maser E., Oppermann U.;
RT   "Structural basis for substrate specificity in human monomeric carbonyl
RT   reductases.";
RL   PLoS ONE 4:e7113-e7113(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 6-276 IN COMPLEX WITH NADP.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of human carbonyl reductase 3, complexed with NADP+.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of carbonyl compounds
CC       to their corresponding alcohols (PubMed:18493841). Has low NADPH-
CC       dependent oxidoreductase activity. Acts on several orthoquinones, acts
CC       as well on non-quinone compounds, such as isatin or on the anticancer
CC       drug oracin (PubMed:18493841, PubMed:15537833, PubMed:19841672). Best
CC       substrates for CBR3 is 1,2- naphthoquinone, hence could play a role in
CC       protection against cytotoxicity of exogenous quinones
CC       (PubMed:19841672). Exerts activity toward ortho-quinones but not
CC       paraquinones. No endogenous substrate for CBR3 except isatin has been
CC       identified (PubMed:19841672). {ECO:0000269|PubMed:15537833,
CC       ECO:0000269|PubMed:18493841, ECO:0000269|PubMed:19841672}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:19257, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.184; Evidence={ECO:0000269|PubMed:18493841};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19259;
CC         Evidence={ECO:0000305|PubMed:18493841};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC         Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124;
CC         EC=1.6.5.10; Evidence={ECO:0000269|PubMed:15537833,
CC         ECO:0000269|PubMed:18493841, ECO:0000269|PubMed:19841672};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46165;
CC         Evidence={ECO:0000305|PubMed:19841672};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=25 uM for menadione {ECO:0000269|PubMed:15537833};
CC         KM=43 uM for menadione {ECO:0000269|PubMed:18493841};
CC         KM=300 uM for 4-benzoylpyridine {ECO:0000269|PubMed:18493841};
CC         KM=130 uM for 4-nitorobenzaldehyde {ECO:0000269|PubMed:18493841};
CC         KM=420 uM for 1,2-naphthoquinone {ECO:0000269|PubMed:19841672};
CC         KM=14630 uM for isatin {ECO:0000269|PubMed:19841672};
CC         KM=140 uM for oracin {ECO:0000269|PubMed:19841672};
CC         KM=90 uM for NADPH {ECO:0000269|PubMed:15537833};
CC         KM=38 uM for NADPH {ECO:0000269|PubMed:18493841};
CC         Vmax=6 umol/min/mg enzyme with 1,2-naphthoquinone as substrate
CC         {ECO:0000269|PubMed:19841672};
CC         Vmax=0.1 umol/min/mg enzyme with oracin as substrate
CC         {ECO:0000269|PubMed:19841672};
CC         Vmax=15 umol/min/mg enzyme with isatin as substrate
CC         {ECO:0000269|PubMed:19841672};
CC         Note=kcat is 0.55 min(-1) with menadione as substrate
CC         (PubMed:18493841). kcat is 0.70 min(-1) with 4-benzoylpyridine as
CC         substrate (PubMed:18493841). kcat is 0.59 min(-1) with
CC         4-nitorobenzaldehyde as substrate (PubMed:18493841).
CC         {ECO:0000269|PubMed:18493841};
CC       pH dependence:
CC         Optimum pH is 5.5-7. {ECO:0000269|PubMed:15537833,
CC         ECO:0000269|PubMed:18493841};
CC   -!- INTERACTION:
CC       O75828; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-714504, EBI-11975051;
CC       O75828; O00560: SDCBP; NbExp=8; IntAct=EBI-714504, EBI-727004;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18493841}.
CC   -!- TISSUE SPECIFICITY: Detected in ovary, pancreas, intestine, colon,
CC       kidney, brain, thymus, lung, heart, liver, spleen, leukocyte, prostate
CC       and testis. {ECO:0000269|PubMed:18493841}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   -!- CAUTION: There are conflicting results on the ability of CBR3 to
CC       metabolize menadione. Although menadione was originally reported as a
CC       good substrate of CBR3 (PubMed:15537833), results of later studies
CC       showed that CBR3 possesses very low or no activity toward menadione
CC       (PubMed:19841672, PubMed:18493841). {ECO:0000269|PubMed:15537833,
CC       ECO:0000269|PubMed:18493841, ECO:0000269|PubMed:19841672}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/cbr3/";
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DR   EMBL; AB004854; BAA33500.1; -; mRNA.
DR   EMBL; AB003151; BAA34207.1; -; Genomic_DNA.
DR   EMBL; AB041012; BAD74062.1; -; mRNA.
DR   EMBL; AB124847; BAE45939.1; -; mRNA.
DR   EMBL; CR541709; CAG46510.1; -; mRNA.
DR   EMBL; EF462915; ABO43035.1; -; Genomic_DNA.
DR   EMBL; AP000689; BAA89425.1; -; Genomic_DNA.
DR   EMBL; AP001725; BAA95547.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09747.1; -; Genomic_DNA.
DR   EMBL; BC002812; AAH02812.1; -; mRNA.
DR   CCDS; CCDS13642.1; -.
DR   RefSeq; NP_001227.1; NM_001236.3.
DR   PDB; 2HRB; X-ray; 1.90 A; A=6-277.
DR   PDBsum; 2HRB; -.
DR   AlphaFoldDB; O75828; -.
DR   SMR; O75828; -.
DR   BioGRID; 107320; 41.
DR   IntAct; O75828; 22.
DR   MINT; O75828; -.
DR   STRING; 9606.ENSP00000290354; -.
DR   ChEMBL; CHEMBL6008; -.
DR   DrugBank; DB00694; Daunorubicin.
DR   DrugBank; DB12161; Deutetrabenazine.
DR   DrugBank; DB00997; Doxorubicin.
DR   DrugBank; DB00776; Oxcarbazepine.
DR   iPTMnet; O75828; -.
DR   PhosphoSitePlus; O75828; -.
DR   SwissPalm; O75828; -.
DR   BioMuta; CBR3; -.
DR   REPRODUCTION-2DPAGE; IPI00290462; -.
DR   EPD; O75828; -.
DR   jPOST; O75828; -.
DR   MassIVE; O75828; -.
DR   PaxDb; 9606-ENSP00000290354; -.
DR   PeptideAtlas; O75828; -.
DR   ProteomicsDB; 50216; -.
DR   Pumba; O75828; -.
DR   Antibodypedia; 8258; 353 antibodies from 35 providers.
DR   DNASU; 874; -.
DR   Ensembl; ENST00000290354.6; ENSP00000290354.5; ENSG00000159231.6.
DR   GeneID; 874; -.
DR   KEGG; hsa:874; -.
DR   MANE-Select; ENST00000290354.6; ENSP00000290354.5; NM_001236.4; NP_001227.1.
DR   AGR; HGNC:1549; -.
DR   DisGeNET; 874; -.
DR   GeneCards; CBR3; -.
DR   HGNC; HGNC:1549; CBR3.
DR   HPA; ENSG00000159231; Tissue enhanced (esophagus, salivary gland).
DR   MIM; 603608; gene.
DR   neXtProt; NX_O75828; -.
DR   OpenTargets; ENSG00000159231; -.
DR   PharmGKB; PA26122; -.
DR   VEuPathDB; HostDB:ENSG00000159231; -.
DR   eggNOG; KOG1208; Eukaryota.
DR   GeneTree; ENSGT00940000162541; -.
DR   HOGENOM; CLU_010194_9_0_1; -.
DR   InParanoid; O75828; -.
DR   OMA; YWANDSV; -.
DR   OrthoDB; 3346557at2759; -.
DR   PhylomeDB; O75828; -.
DR   TreeFam; TF329359; -.
DR   BRENDA; 1.1.1.184; 2681.
DR   PathwayCommons; O75828; -.
DR   Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR   SABIO-RK; O75828; -.
DR   SignaLink; O75828; -.
DR   BioGRID-ORCS; 874; 9 hits in 1147 CRISPR screens.
DR   ChiTaRS; CBR3; human.
DR   EvolutionaryTrace; O75828; -.
DR   GeneWiki; CBR3; -.
DR   GenomeRNAi; 874; -.
DR   Pharos; O75828; Tbio.
DR   PRO; PR:O75828; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; O75828; Protein.
DR   Bgee; ENSG00000159231; Expressed in gingival epithelium and 162 other cell types or tissues.
DR   ExpressionAtlas; O75828; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0000253; F:3-keto sterol reductase activity; IEA:Ensembl.
DR   GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:UniProtKB.
DR   GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR   GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IDA:UniProtKB.
DR   GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR   GO; GO:0042376; P:phylloquinone catabolic process; IEA:Ensembl.
DR   GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR   CDD; cd05324; carb_red_PTCR-like_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR045313; CBR1-like.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43963; CARBONYL REDUCTASE 1-RELATED; 1.
DR   PANTHER; PTHR43963:SF3; CARBONYL REDUCTASE [NADPH] 3; 1.
DR   Pfam; PF00106; adh_short; 2.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
DR   Genevisible; O75828; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; NADP; Oxidoreductase; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P16152"
FT   CHAIN           2..277
FT                   /note="Carbonyl reductase [NADPH] 3"
FT                   /id="PRO_0000054608"
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         10..34
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|Ref.13"
FT   BINDING         38..42
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|Ref.13"
FT   BINDING         63..64
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|Ref.13"
FT   BINDING         90
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|Ref.13"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         194..198
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|Ref.13"
FT   BINDING         239
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|Ref.13"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16152"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48758"
FT   VARIANT         4
FT                   /note="C -> Y (in dbSNP:rs8133052)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_033868"
FT   VARIANT         84
FT                   /note="L -> V (in dbSNP:rs9282628)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_033869"
FT   VARIANT         93
FT                   /note="V -> I (in dbSNP:rs2835285)"
FT                   /id="VAR_033870"
FT   VARIANT         131
FT                   /note="P -> S (in dbSNP:rs16993929)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_033871"
FT   VARIANT         235
FT                   /note="M -> L (in dbSNP:rs4987121)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_033872"
FT   VARIANT         244
FT                   /note="V -> M (increased carbonyl reductase (NADPH)
FT                   activity; exhibits a 2-fold higher Vmax with menadione;
FT                   higher Vmax with NADP(H); does not affect Km for menadione;
FT                   dbSNP:rs1056892)"
FT                   /evidence="ECO:0000269|PubMed:15537833, ECO:0000269|Ref.5"
FT                   /id="VAR_033873"
FT   MUTAGEN         142
FT                   /note="Q->M: Modest increase in carbonyl reductase (NADPH)
FT                   activity toward 1,2-naphthoquinone."
FT                   /evidence="ECO:0000269|PubMed:19841672"
FT   MUTAGEN         230
FT                   /note="P->F,W: Decreased carbonyl reductase (NADPH)
FT                   activity toward 1,2-naphthoquinone and isatin."
FT                   /evidence="ECO:0000269|PubMed:19841672"
FT   MUTAGEN         236
FT                   /note="D->A: Significant decreased of the Km value for
FT                   isatin."
FT                   /evidence="ECO:0000269|PubMed:19841672"
FT   STRAND          7..12
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   HELIX           16..28
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   STRAND          30..39
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   HELIX           40..52
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   HELIX           67..81
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   STRAND          82..89
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   HELIX           103..114
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   HELIX           116..125
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   STRAND          129..138
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   HELIX           142..149
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   HELIX           152..159
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   HELIX           165..180
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   TURN            184..188
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   HELIX           193..215
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   HELIX           217..219
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   STRAND          222..227
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   HELIX           241..247
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   HELIX           249..255
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   STRAND          268..270
FT                   /evidence="ECO:0007829|PDB:2HRB"
FT   STRAND          273..275
FT                   /evidence="ECO:0007829|PDB:2HRB"
SQ   SEQUENCE   277 AA;  30850 MW;  8D39D6B99CFE5389 CRC64;
     MSSCSRVALV TGANRGIGLA IARELCRQFS GDVVLTARDV ARGQAAVQQL QAEGLSPRFH
     QLDIDDLQSI RALRDFLRKE YGGLNVLVNN AAVAFKSDDP MPFDIKAEMT LKTNFFATRN
     MCNELLPIMK PHGRVVNISS LQCLRAFENC SEDLQERFHS ETLTEGDLVD LMKKFVEDTK
     NEVHEREGWP NSPYGVSKLG VTVLSRILAR RLDEKRKADR ILVNACCPGP VKTDMDGKDS
     IRTVEEGAET PVYLALLPPD ATEPQGQLVH DKVVQNW
//