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Quinone oxidoreductase PIG3 (EC 1.-.-.-) (Tumor protein p53-inducible protein 3) (p53-induced gene 3 protein)

 QORX_HUMAN              Reviewed;         332 AA.
Q53FA7; D6W533; O14679; O14685; Q38G78; Q6JLE7; Q9BWB8;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
27-SEP-2005, sequence version 2.
05-DEC-2018, entry version 125.
RecName: Full=Quinone oxidoreductase PIG3;
EC=1.-.-.-;
AltName: Full=Tumor protein p53-inducible protein 3;
AltName: Full=p53-induced gene 3 protein;
Name=TP53I3; Synonyms=PIG3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND INDUCTION BY
TP53.
TISSUE=Colon cancer;
PubMed=9305847; DOI=10.1038/38525;
Polyak K., Xia Y., Zweier J.L., Kinzler K.W., Vogelstein B.;
"A model for p53-induced apoptosis.";
Nature 389:300-306(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Mammary tumor;
PubMed=15067011; DOI=10.1074/jbc.M401049200;
Nicholls C.D., Shields M.A., Lee P.W.K., Robbins S.M., Beattie T.L.;
"UV-dependent alternative splicing uncouples p53 activity and PIG3
gene function through rapid proteolytic degradation.";
J. Biol. Chem. 279:24171-24178(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Gastric mucosa;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 1-33; 163-176; 184-203; 259-267; 297-303 AND
326-332, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Lung carcinoma;
Bienvenut W.V., Vousden K.H., Lukashchuk N.;
Submitted (MAR-2008) to UniProtKB.
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NADP, FUNCTION,
SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF TYR-51 AND SER-151.
PubMed=19349281; DOI=10.1074/jbc.M109.001800;
Porte S., Valencia E., Yakovtseva E.A., Borras E., Shafqat N.,
Debreczeny J.E., Pike A.C.W., Oppermann U., Farres J., Fita I.,
Pares X.;
"Three-dimensional structure and enzymatic function of proapoptotic
human p53-inducible quinone oxidoreductase PIG3.";
J. Biol. Chem. 284:17194-17205(2009).
[12]
VARIANT LYS-180.
PubMed=17224074; DOI=10.1186/bcr1637;
Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A.,
Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S.,
Kristensen V., Perou C.M., Boerresen-Dale A.-L.;
"Somatic sequence alterations in twenty-one genes selected by
expression profile analysis of breast carcinomas.";
Breast Cancer Res. 9:R5-R5(2007).
-!- FUNCTION: May be involved in the generation of reactive oxygen
species (ROS). Has low NADPH-dependent beta-naphthoquinone
reductase activity, with a preference for 1,2-beta-naphthoquinone
over 1,4-beta-naphthoquinone. Has low NADPH-dependent diamine
reductase activity (in vitro). {ECO:0000269|PubMed:19349281}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=215 uM for 1,2-naphthoquinone {ECO:0000269|PubMed:19349281};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19349281}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=UV radiation favors the production of isoform 2.;
Name=1;
IsoId=Q53FA7-1; Sequence=Displayed;
Note=Major isoform under normal light conditions.;
Name=2; Synonyms=PIG3AS;
IsoId=Q53FA7-2; Sequence=VSP_015783, VSP_015784;
Note=Major isoform under UV light exposure. Undergoes rapid
proteolytic degradation by the proteasome.;
-!- INDUCTION: Isoform 1 and isoform 2 are both activated by p53/TP53,
doxorubicin, etoposide and ionizing radiation. Isoform 2 is highly
activated by UV radiation. {ECO:0000269|PubMed:9305847}.
-!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
family. Quinone oxidoreductase subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC39535.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tp53i3/";
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EMBL; AF010309; AAC39528.1; -; mRNA.
EMBL; AF010317; AAC39535.1; ALT_SEQ; Genomic_DNA.
EMBL; AY371700; AAQ90166.1; -; mRNA.
EMBL; BT007149; AAP35813.1; -; mRNA.
EMBL; AK223382; BAD97102.1; -; mRNA.
EMBL; DQ232851; ABB02183.1; -; Genomic_DNA.
EMBL; AC008073; AAY14665.1; -; Genomic_DNA.
EMBL; CH471053; EAX00762.1; -; Genomic_DNA.
EMBL; CH471053; EAX00763.1; -; Genomic_DNA.
EMBL; CH471053; EAX00766.1; -; Genomic_DNA.
EMBL; BC000474; AAH00474.1; -; mRNA.
CCDS; CCDS1708.1; -. [Q53FA7-1]
CCDS; CCDS56112.1; -. [Q53FA7-2]
RefSeq; NP_001193731.1; NM_001206802.2. [Q53FA7-2]
RefSeq; NP_004872.2; NM_004881.4. [Q53FA7-1]
RefSeq; NP_671713.1; NM_147184.3. [Q53FA7-1]
RefSeq; XP_006712213.1; XM_006712150.2. [Q53FA7-2]
UniGene; Hs.50649; -.
UniGene; Hs.733381; -.
PDB; 2J8Z; X-ray; 2.50 A; A=1-332.
PDB; 2OBY; X-ray; 3.00 A; A/B/C/D/E=1-332.
PDBsum; 2J8Z; -.
PDBsum; 2OBY; -.
ProteinModelPortal; Q53FA7; -.
SMR; Q53FA7; -.
BioGrid; 114915; 11.
IntAct; Q53FA7; 4.
STRING; 9606.ENSP00000238721; -.
iPTMnet; Q53FA7; -.
PhosphoSitePlus; Q53FA7; -.
BioMuta; TP53I3; -.
DMDM; 76789665; -.
EPD; Q53FA7; -.
MaxQB; Q53FA7; -.
PaxDb; Q53FA7; -.
PeptideAtlas; Q53FA7; -.
PRIDE; Q53FA7; -.
ProteomicsDB; 62462; -.
ProteomicsDB; 62463; -. [Q53FA7-2]
DNASU; 9540; -.
Ensembl; ENST00000238721; ENSP00000238721; ENSG00000115129. [Q53FA7-1]
Ensembl; ENST00000335934; ENSP00000337834; ENSG00000115129. [Q53FA7-1]
Ensembl; ENST00000407482; ENSP00000384414; ENSG00000115129. [Q53FA7-2]
GeneID; 9540; -.
KEGG; hsa:9540; -.
UCSC; uc002rex.3; human. [Q53FA7-1]
CTD; 9540; -.
DisGeNET; 9540; -.
EuPathDB; HostDB:ENSG00000115129.13; -.
GeneCards; TP53I3; -.
HGNC; HGNC:19373; TP53I3.
HPA; CAB017479; -.
HPA; HPA022012; -.
HPA; HPA028742; -.
MIM; 605171; gene.
neXtProt; NX_Q53FA7; -.
OpenTargets; ENSG00000115129; -.
PharmGKB; PA134923704; -.
eggNOG; KOG1198; Eukaryota.
eggNOG; COG0604; LUCA.
GeneTree; ENSGT00940000161217; -.
HOGENOM; HOG000294672; -.
HOVERGEN; HBG097584; -.
InParanoid; Q53FA7; -.
KO; K10133; -.
OMA; MVGGDYI; -.
OrthoDB; EOG091G0JZF; -.
PhylomeDB; Q53FA7; -.
TreeFam; TF300079; -.
Reactome; R-HSA-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
EvolutionaryTrace; Q53FA7; -.
GeneWiki; TP53I3; -.
GenomeRNAi; 9540; -.
PRO; PR:Q53FA7; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115129; Expressed in 184 organ(s), highest expression level in lower esophagus mucosa.
CleanEx; HS_TP53I3; -.
ExpressionAtlas; Q53FA7; baseline and differential.
Genevisible; Q53FA7; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
GO; GO:0003960; F:NADPH:quinone reductase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0048038; F:quinone binding; IDA:UniProtKB.
GO; GO:0006739; P:NADP metabolic process; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
CDD; cd05276; p53_inducible_oxidoreductase; 1.
InterPro; IPR013149; ADH_C.
InterPro; IPR013154; ADH_N.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020843; PKS_ER.
InterPro; IPR014189; Quinone_OxRdtase_PIG3.
Pfam; PF08240; ADH_N; 1.
Pfam; PF00107; ADH_zinc_N; 1.
SMART; SM00829; PKS_ER; 1.
SUPFAM; SSF50129; SSF50129; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR02824; quinone_pig3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; NADP; Oxidoreductase; Polymorphism;
Reference proteome.
CHAIN 1 332 Quinone oxidoreductase PIG3.
/FTId=PRO_0000160917.
NP_BIND 148 154 NADP. {ECO:0000269|PubMed:19349281}.
NP_BIND 173 177 NADP. {ECO:0000269|PubMed:19349281}.
NP_BIND 264 266 NADP. {ECO:0000269|PubMed:19349281}.
BINDING 41 41 NADP. {ECO:0000269|PubMed:19349281}.
BINDING 192 192 NADP. {ECO:0000269|PubMed:19349281}.
BINDING 322 322 NADP. {ECO:0000269|PubMed:19349281}.
MOD_RES 1 1 N-acetylmethionine. {ECO:0000269|Ref.9}.
VAR_SEQ 207 248 GAGVNLILDCIGGSYWEKNVNCLALDGRWVLYGLMGGGDIN
G -> VQANAGECFHGANSASLLHGGPPTSAAGSGQNLPSD
RNPGGP (in isoform 2).
{ECO:0000303|PubMed:15067011}.
/FTId=VSP_015783.
VAR_SEQ 249 332 Missing (in isoform 2).
{ECO:0000303|PubMed:15067011}.
/FTId=VSP_015784.
VARIANT 180 180 M -> K (in a breast cancer sample;
somatic mutation; dbSNP:rs899619458).
{ECO:0000269|PubMed:17224074}.
/FTId=VAR_033032.
VARIANT 223 223 E -> K (in dbSNP:rs35176319).
/FTId=VAR_048201.
MUTAGEN 51 51 Y->A: Loss of enzyme activity.
{ECO:0000269|PubMed:19349281}.
MUTAGEN 51 51 Y->F: Increased enzyme activity.
{ECO:0000269|PubMed:19349281}.
MUTAGEN 151 151 S->V: Loss of enzyme activity.
{ECO:0000269|PubMed:19349281}.
CONFLICT 36 36 A -> AA (in Ref. 1; AAC39535).
{ECO:0000305}.
CONFLICT 263 263 T -> A (in Ref. 4; BAD97102).
{ECO:0000305}.
CONFLICT 315 332 KYMEANKNIGKIVLELPQ -> STWRPTRT (in Ref.
1; AAC39528). {ECO:0000305}.
STRAND 1 8 {ECO:0000244|PDB:2J8Z}.
HELIX 12 14 {ECO:0000244|PDB:2J8Z}.
STRAND 15 21 {ECO:0000244|PDB:2J8Z}.
STRAND 29 38 {ECO:0000244|PDB:2J8Z}.
HELIX 41 47 {ECO:0000244|PDB:2J8Z}.
STRAND 59 61 {ECO:0000244|PDB:2J8Z}.
STRAND 63 72 {ECO:0000244|PDB:2J8Z}.
STRAND 78 80 {ECO:0000244|PDB:2OBY}.
STRAND 85 89 {ECO:0000244|PDB:2J8Z}.
STRAND 95 102 {ECO:0000244|PDB:2J8Z}.
HELIX 103 105 {ECO:0000244|PDB:2J8Z}.
STRAND 106 108 {ECO:0000244|PDB:2J8Z}.
HELIX 115 118 {ECO:0000244|PDB:2J8Z}.
HELIX 122 132 {ECO:0000244|PDB:2J8Z}.
TURN 133 135 {ECO:0000244|PDB:2J8Z}.
STRAND 143 148 {ECO:0000244|PDB:2J8Z}.
HELIX 152 163 {ECO:0000244|PDB:2J8Z}.
STRAND 167 173 {ECO:0000244|PDB:2J8Z}.
HELIX 175 184 {ECO:0000244|PDB:2J8Z}.
STRAND 187 191 {ECO:0000244|PDB:2J8Z}.
TURN 192 194 {ECO:0000244|PDB:2J8Z}.
HELIX 197 204 {ECO:0000244|PDB:2J8Z}.
TURN 205 207 {ECO:0000244|PDB:2J8Z}.
STRAND 210 217 {ECO:0000244|PDB:2J8Z}.
HELIX 219 221 {ECO:0000244|PDB:2J8Z}.
HELIX 222 228 {ECO:0000244|PDB:2J8Z}.
STRAND 229 237 {ECO:0000244|PDB:2J8Z}.
STRAND 246 248 {ECO:0000244|PDB:2OBY}.
HELIX 250 256 {ECO:0000244|PDB:2J8Z}.
STRAND 260 263 {ECO:0000244|PDB:2J8Z}.
HELIX 271 284 {ECO:0000244|PDB:2J8Z}.
HELIX 286 289 {ECO:0000244|PDB:2J8Z}.
STRAND 301 306 {ECO:0000244|PDB:2J8Z}.
HELIX 307 309 {ECO:0000244|PDB:2J8Z}.
HELIX 310 318 {ECO:0000244|PDB:2J8Z}.
STRAND 323 329 {ECO:0000244|PDB:2J8Z}.
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


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