PIR_MOUSE
ID PIR_MOUSE Reviewed; 290 AA.
AC Q9D711; A2AIH9; Q3UAN0; Q8CIE9;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Pirin;
DE EC=1.13.11.24 {ECO:0000250|UniProtKB:O00625};
DE AltName: Full=Probable quercetin 2,3-dioxygenase PIR;
DE Short=Probable quercetinase;
GN Name=Pir;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Hypothalamus, and Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 255-290.
RC STRAIN=ICR;
RA Teng X., Li D., Johns R.A.;
RT "Hypoxia upregulates VEGF-D promoter in pulmonary vascular smooth muscle
RT cells.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, and Spleen;
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=129/SvEv;
RX PubMed=20010624; DOI=10.1038/leu.2009.247;
RA Licciulli S., Cambiaghi V., Scafetta G., Gruszka A.M., Alcalay M.;
RT "Pirin downregulation is a feature of AML and leads to impairment of
RT terminal myeloid differentiation.";
RL Leukemia 24:429-437(2010).
CC -!- FUNCTION: Transcriptional coregulator of NF-kappa-B which facilitates
CC binding of NF-kappa-B proteins to target kappa-B genes in a redox-
CC state-dependent manner. May be required for efficient terminal myeloid
CC maturation of hematopoietic cells. Has quercetin 2,3-dioxygenase
CC activity (in vitro). {ECO:0000250|UniProtKB:O00625}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + quercetin = 2-(3,4-dihydroxybenzoyloxy)-4,6-
CC dihydroxybenzoate + CO; Xref=Rhea:RHEA:15381, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17245, ChEBI:CHEBI:57628, ChEBI:CHEBI:57694;
CC EC=1.13.11.24; Evidence={ECO:0000250|UniProtKB:O00625};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:O00625};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:O00625};
CC -!- PATHWAY: Flavonoid metabolism; quercetin degradation.
CC {ECO:0000250|UniProtKB:O00625}.
CC -!- SUBUNIT: May interact with NF1/CTF1. Interacts with BCL3. Identified in
CC a complex comprised of PIR, BLC3, NFKB1 and target DNA.
CC {ECO:0000250|UniProtKB:O00625}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00625}. Cytoplasm
CC {ECO:0000250|UniProtKB:O00625}. Note=Predominantly localized in dot-
CC like subnuclear structures. {ECO:0000250|UniProtKB:O00625}.
CC -!- TISSUE SPECIFICITY: Weakly expressed in bone marrow.
CC {ECO:0000269|PubMed:20010624}.
CC -!- INDUCTION: Down-regulated in mice with acute myeloid leukemias induced
CC by either PML-RAR or AML1-ETO fusion oncoproteins.
CC {ECO:0000269|PubMed:20010624}.
CC -!- MISCELLANEOUS: Quercetin is a flavonoid compound synthesized by a
CC variety of plants, including foods for human consumption.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the pirin family. {ECO:0000305}.
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DR EMBL; AK009757; BAB26481.1; -; mRNA.
DR EMBL; AK138314; BAE23621.1; -; mRNA.
DR EMBL; AK151301; BAE30284.1; -; mRNA.
DR EMBL; AL671706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466571; EDL40759.1; -; Genomic_DNA.
DR EMBL; BC024062; AAH24062.1; -; mRNA.
DR EMBL; AF345635; AAK54068.1; -; Genomic_DNA.
DR CCDS; CCDS30520.1; -.
DR RefSeq; NP_081429.1; NM_027153.3.
DR RefSeq; XP_006529040.1; XM_006528977.3.
DR AlphaFoldDB; Q9D711; -.
DR SMR; Q9D711; -.
DR STRING; 10090.ENSMUSP00000033749; -.
DR iPTMnet; Q9D711; -.
DR PhosphoSitePlus; Q9D711; -.
DR MaxQB; Q9D711; -.
DR PaxDb; Q9D711; -.
DR PRIDE; Q9D711; -.
DR ProteomicsDB; 289579; -.
DR Antibodypedia; 358; 214 antibodies from 31 providers.
DR DNASU; 69656; -.
DR Ensembl; ENSMUST00000033749; ENSMUSP00000033749; ENSMUSG00000031379.
DR GeneID; 69656; -.
DR KEGG; mmu:69656; -.
DR UCSC; uc009uvl.2; mouse.
DR CTD; 8544; -.
DR MGI; MGI:1916906; Pir.
DR VEuPathDB; HostDB:ENSMUSG00000031379; -.
DR eggNOG; ENOG502QQ5A; Eukaryota.
DR GeneTree; ENSGT00390000008044; -.
DR HOGENOM; CLU_045717_0_1_1; -.
DR InParanoid; Q9D711; -.
DR OMA; TPWHPHR; -.
DR OrthoDB; 1328043at2759; -.
DR PhylomeDB; Q9D711; -.
DR TreeFam; TF300002; -.
DR Reactome; R-MMU-8935690; Digestion.
DR UniPathway; UPA00724; -.
DR BioGRID-ORCS; 69656; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Pir; mouse.
DR PRO; PR:Q9D711; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9D711; protein.
DR Bgee; ENSMUSG00000031379; Expressed in esophagus and 190 other tissues.
DR ExpressionAtlas; Q9D711; baseline and differential.
DR Genevisible; Q9D711; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0008127; F:quercetin 2,3-dioxygenase activity; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR GO; GO:0030224; P:monocyte differentiation; ISO:MGI.
DR GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR012093; Pirin.
DR InterPro; IPR008778; Pirin_C_dom.
DR InterPro; IPR003829; Pirin_N_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR13903; PTHR13903; 1.
DR Pfam; PF02678; Pirin; 1.
DR Pfam; PF05726; Pirin_C; 1.
DR PIRSF; PIRSF006232; Pirin; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..290
FT /note="Pirin"
FT /id="PRO_0000214052"
FT BINDING 56
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 49
FT /note="K -> R (in Ref. 2; AAH24062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 32066 MW; B95915522F62EC5F CRC64;
MASSKKVTLS VLSREQSEGV GARVRRSIGR PELKNLDPFL LFDEFKGGKP GGFPDHPHRG
FETVSYLLEG GSMAHEDFCG HVGKMNPGDL QWMTAGRGIL HAEMPCSEEP AHGLQLWVNL
RRSEKMVAPQ YQELKSEEIP KPTKDGVTVA VISGEALGIK SKVYTRTPTL YLDFKLDQGA
KHSQPIPKGW TSFIYTISGD VYIGPDDAQQ KIEPHHTAVL GEGDAVQLEN KDPKRSHFVL
IAGEPLREPV VQHGPFVMNT NEEISQAILD FRNAKNGFEG ARTWKSKIGN
