QORX_HUMAN
ID QORX_HUMAN Reviewed; 332 AA.
AC Q53FA7; D6W533; O14679; O14685; Q38G78; Q6JLE7; Q9BWB8;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Quinone oxidoreductase PIG3 {ECO:0000303|PubMed:19349281};
DE EC=1.6.5.5 {ECO:0000269|PubMed:19349281};
DE AltName: Full=NADPH:quinone reductase PIG3 {ECO:0000303|PubMed:19349281};
DE AltName: Full=Tumor protein p53-inducible protein 3 {ECO:0000303|PubMed:19349281};
DE Short=Protein PIG3 {ECO:0000303|PubMed:19349281};
DE AltName: Full=p53-induced gene 3 protein {ECO:0000303|PubMed:19349281};
GN Name=TP53I3 {ECO:0000312|HGNC:HGNC:19373}; Synonyms=PIG3;
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] (ISOFORM 1), AND INDUCTION BY
RP TP53.
RC TISSUE=Colon cancer;
RX PubMed=9305847; DOI=10.1038/38525;
RA Polyak K., Xia Y., Zweier J.L., Kinzler K.W., Vogelstein B.;
RT "A model for p53-induced apoptosis.";
RL Nature 389:300-306(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Mammary tumor;
RX PubMed=15067011; DOI=10.1074/jbc.m401049200;
RA Nicholls C.D., Shields M.A., Lee P.W.K., Robbins S.M., Beattie T.L.;
RT "UV-dependent alternative splicing uncouples p53 activity and PIG3 gene
RT function through rapid proteolytic degradation.";
RL J. Biol. Chem. 279:24171-24178(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Gastric mucosa;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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] (ISOFORM 1).
RC TISSUE=Muscle;
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 PROTEIN SEQUENCE OF 1-33; 163-176; 184-203; 259-267; 297-303 AND 326-332,
RP ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NADP, FUNCTION,
RP SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS
RP OF TYR-51 AND SER-151.
RX PubMed=19349281; DOI=10.1074/jbc.m109.001800;
RA Porte S., Valencia E., Yakovtseva E.A., Borras E., Shafqat N.,
RA Debreczeny J.E., Pike A.C.W., Oppermann U., Farres J., Fita I., Pares X.;
RT "Three-dimensional structure and enzymatic function of proapoptotic human
RT p53-inducible quinone oxidoreductase PIG3.";
RL J. Biol. Chem. 284:17194-17205(2009).
RN [12]
RP VARIANT LYS-180.
RX PubMed=17224074; DOI=10.1186/bcr1637;
RA Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A., Presswalla S.,
RA Kaaresen R., Strausberg R.L., Gerhard D.S., Kristensen V., Perou C.M.,
RA Boerresen-Dale A.-L.;
RT "Somatic sequence alterations in twenty-one genes selected by expression
RT profile analysis of breast carcinomas.";
RL Breast Cancer Res. 9:R5-R5(2007).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of quinones
CC (PubMed:19349281). Exhibits a low enzymatic activity with beta-
CC naphthoquinones, with a strong preference for the ortho-quinone isomer
CC (1,2-beta-naphthoquinone) over the para isomer (1,4-beta-
CC naphthoquinone). Also displays a low reductase activity for non-quinone
CC compounds such as diamine and 2,6-dichloroindophenol (in vitro)
CC (PubMed:19349281). Involved in the generation of reactive oxygen
CC species (ROS) (PubMed:19349281). {ECO:0000269|PubMed:19349281}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a quinone + H(+) + NADPH = 2 a 1,4-benzosemiquinone +
CC NADP(+); Xref=Rhea:RHEA:14269, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225;
CC EC=1.6.5.5; Evidence={ECO:0000269|PubMed:19349281};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14270;
CC Evidence={ECO:0000305|PubMed:19349281};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=215 uM for 1,2-naphthoquinone {ECO:0000269|PubMed:19349281};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19349281}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=UV radiation favors the production of isoform 2.;
CC Name=1;
CC IsoId=Q53FA7-1; Sequence=Displayed;
CC Name=2; Synonyms=PIG3AS;
CC IsoId=Q53FA7-2; Sequence=VSP_015783, VSP_015784;
CC -!- INDUCTION: Isoform 1 and isoform 2 are both activated by p53/TP53,
CC doxorubicin, etoposide and ionizing radiation. Isoform 2 is highly
CC activated by UV radiation. {ECO:0000269|PubMed:9305847}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform under normal light
CC conditions.
CC -!- MISCELLANEOUS: [Isoform 2]: Major isoform under UV light exposure.
CC Undergoes rapid proteolytic degradation by the proteasome.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39535.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/tp53i3/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF010309; AAC39528.1; -; mRNA.
DR EMBL; AF010317; AAC39535.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY371700; AAQ90166.1; -; mRNA.
DR EMBL; BT007149; AAP35813.1; -; mRNA.
DR EMBL; AK223382; BAD97102.1; -; mRNA.
DR EMBL; DQ232851; ABB02183.1; -; Genomic_DNA.
DR EMBL; AC008073; AAY14665.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00762.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00763.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00766.1; -; Genomic_DNA.
DR EMBL; BC000474; AAH00474.1; -; mRNA.
DR CCDS; CCDS1708.1; -. [Q53FA7-1]
DR CCDS; CCDS56112.1; -. [Q53FA7-2]
DR RefSeq; NP_001193731.1; NM_001206802.2. [Q53FA7-2]
DR RefSeq; NP_004872.2; NM_004881.4. [Q53FA7-1]
DR RefSeq; NP_671713.1; NM_147184.3. [Q53FA7-1]
DR RefSeq; XP_006712213.1; XM_006712150.2. [Q53FA7-2]
DR PDB; 2J8Z; X-ray; 2.50 A; A=1-332.
DR PDB; 2OBY; X-ray; 3.00 A; A/B/C/D/E=1-332.
DR PDBsum; 2J8Z; -.
DR PDBsum; 2OBY; -.
DR AlphaFoldDB; Q53FA7; -.
DR SMR; Q53FA7; -.
DR BioGRID; 114915; 12.
DR IntAct; Q53FA7; 5.
DR STRING; 9606.ENSP00000238721; -.
DR iPTMnet; Q53FA7; -.
DR MetOSite; Q53FA7; -.
DR PhosphoSitePlus; Q53FA7; -.
DR BioMuta; TP53I3; -.
DR DMDM; 76789665; -.
DR EPD; Q53FA7; -.
DR jPOST; Q53FA7; -.
DR MassIVE; Q53FA7; -.
DR MaxQB; Q53FA7; -.
DR PaxDb; Q53FA7; -.
DR PeptideAtlas; Q53FA7; -.
DR PRIDE; Q53FA7; -.
DR ProteomicsDB; 62462; -. [Q53FA7-1]
DR ProteomicsDB; 62463; -. [Q53FA7-2]
DR Antibodypedia; 13084; 428 antibodies from 33 providers.
DR DNASU; 9540; -.
DR Ensembl; ENST00000238721.9; ENSP00000238721.4; ENSG00000115129.14. [Q53FA7-1]
DR Ensembl; ENST00000335934.8; ENSP00000337834.4; ENSG00000115129.14. [Q53FA7-1]
DR Ensembl; ENST00000407482.5; ENSP00000384414.1; ENSG00000115129.14. [Q53FA7-2]
DR GeneID; 9540; -.
DR KEGG; hsa:9540; -.
DR MANE-Select; ENST00000238721.9; ENSP00000238721.4; NM_004881.5; NP_004872.2.
DR UCSC; uc002rex.3; human. [Q53FA7-1]
DR CTD; 9540; -.
DR DisGeNET; 9540; -.
DR GeneCards; TP53I3; -.
DR HGNC; HGNC:19373; TP53I3.
DR HPA; ENSG00000115129; Tissue enhanced (esophagus).
DR MIM; 605171; gene.
DR neXtProt; NX_Q53FA7; -.
DR OpenTargets; ENSG00000115129; -.
DR PharmGKB; PA134923704; -.
DR VEuPathDB; HostDB:ENSG00000115129; -.
DR eggNOG; KOG1198; Eukaryota.
DR GeneTree; ENSGT00940000161217; -.
DR HOGENOM; CLU_026673_3_4_1; -.
DR InParanoid; Q53FA7; -.
DR OMA; VWSNVFM; -.
DR OrthoDB; 1085436at2759; -.
DR PhylomeDB; Q53FA7; -.
DR TreeFam; TF300079; -.
DR PathwayCommons; Q53FA7; -.
DR Reactome; R-HSA-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
DR SignaLink; Q53FA7; -.
DR SIGNOR; Q53FA7; -.
DR BioGRID-ORCS; 9540; 16 hits in 1077 CRISPR screens.
DR ChiTaRS; TP53I3; human.
DR EvolutionaryTrace; Q53FA7; -.
DR GeneWiki; TP53I3; -.
DR GenomeRNAi; 9540; -.
DR Pharos; Q53FA7; Tbio.
DR PRO; PR:Q53FA7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q53FA7; protein.
DR Bgee; ENSG00000115129; Expressed in lower esophagus mucosa and 157 other tissues.
DR ExpressionAtlas; Q53FA7; baseline and differential.
DR Genevisible; Q53FA7; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; IDA:UniProtKB.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0048038; F:quinone binding; IDA:UniProtKB.
DR GO; GO:0006739; P:NADP metabolic process; IDA:UniProtKB.
DR CDD; cd05276; p53_inducible_oxidoreductase; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR014189; Quinone_OxRdtase_PIG3.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR02824; quinone_pig3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..332
FT /note="Quinone oxidoreductase PIG3"
FT /id="PRO_0000160917"
FT BINDING 41
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19349281"
FT BINDING 148..154
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19349281"
FT BINDING 173..177
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19349281"
FT BINDING 192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19349281"
FT BINDING 264..266
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19349281"
FT BINDING 322
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19349281"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.9"
FT VAR_SEQ 207..248
FT /note="GAGVNLILDCIGGSYWEKNVNCLALDGRWVLYGLMGGGDING -> VQANAG
FT ECFHGANSASLLHGGPPTSAAGSGQNLPSDRNPGGP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15067011"
FT /id="VSP_015783"
FT VAR_SEQ 249..332
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15067011"
FT /id="VSP_015784"
FT VARIANT 180
FT /note="M -> K (in a breast cancer sample; somatic mutation;
FT dbSNP:rs899619458)"
FT /evidence="ECO:0000269|PubMed:17224074"
FT /id="VAR_033032"
FT VARIANT 223
FT /note="E -> K (in dbSNP:rs35176319)"
FT /id="VAR_048201"
FT MUTAGEN 51
FT /note="Y->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:19349281"
FT MUTAGEN 51
FT /note="Y->F: Increased enzyme activity."
FT /evidence="ECO:0000269|PubMed:19349281"
FT MUTAGEN 151
FT /note="S->V: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:19349281"
FT CONFLICT 36
FT /note="A -> AA (in Ref. 1; AAC39535)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="T -> A (in Ref. 4; BAD97102)"
FT /evidence="ECO:0000305"
FT CONFLICT 315..332
FT /note="KYMEANKNIGKIVLELPQ -> STWRPTRT (in Ref. 1;
FT AAC39528)"
FT /evidence="ECO:0000305"
FT STRAND 1..8
FT /evidence="ECO:0007829|PDB:2J8Z"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:2J8Z"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2OBY"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:2J8Z"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2J8Z"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:2J8Z"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:2J8Z"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:2J8Z"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:2J8Z"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:2J8Z"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:2J8Z"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:2J8Z"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:2J8Z"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:2J8Z"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2OBY"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:2J8Z"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:2J8Z"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:2J8Z"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:2J8Z"
FT HELIX 310..318
FT /evidence="ECO:0007829|PDB:2J8Z"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:2J8Z"
SQ SEQUENCE 332 AA; 35536 MW; C5A33C46B3F96473 CRC64;
MLAVHFDKPG GPENLYVKEV AKPSPGEGEV LLKVAASALN RADLMQRQGQ YDPPPGASNI
LGLEASGHVA ELGPGCQGHW KIGDTAMALL PGGGQAQYVT VPEGLLMPIP EGLTLTQAAA
IPEAWLTAFQ LLHLVGNVQA GDYVLIHAGL SGVGTAAIQL TRMAGAIPLV TAGSQKKLQM
AEKLGAAAGF NYKKEDFSEA TLKFTKGAGV NLILDCIGGS YWEKNVNCLA LDGRWVLYGL
MGGGDINGPL FSKLLFKRGS LITSLLRSRD NKYKQMLVNA FTEQILPHFS TEGPQRLLPV
LDRIYPVTEI QEAHKYMEAN KNIGKIVLEL PQ
