CBR3_HUMAN
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 03-AUG-2022, entry version 189.
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 4-
CC 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; 37.
DR IntAct; O75828; 19.
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; O75828; -.
DR PeptideAtlas; O75828; -.
DR PRIDE; O75828; -.
DR ProteomicsDB; 50216; -.
DR Antibodypedia; 8258; 319 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 CTD; 874; -.
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; QKKFRCE; -.
DR OrthoDB; 1259665at2759; -.
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; 8 hits in 1066 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 tissues.
DR ExpressionAtlas; O75828; baseline and differential.
DR Genevisible; O75828; HS.
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: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:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR CDD; cd05324; carb_red_PTCR-like_SDR_c; 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 Pfam; PF00106; adh_short; 2.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
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
