ID   PIR_RAT                 Reviewed;         291 AA.
AC   Q5M827;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Pirin;
DE            EC=1.13.11.24;
DE   AltName: Full=Probable quercetin 2,3-dioxygenase PIR;
DE            Short=Probable quercetinase;
GN   Name=Pir;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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   [2]
RP   PROTEIN SEQUENCE OF 35-46 AND 145-160, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA   Lubec G., Diao W.;
RL   Submitted (APR-2007) to UniProtKB.
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) (By similarity). {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- PATHWAY: Flavonoid metabolism; quercetin degradation.
CC   -!- SUBUNIT: May interact with NF1/CTF1. Interacts with BCL3. Identified in
CC       a complex comprised of PIR, BLC3, NFKB1 and target DNA (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Predominantly localized in dot-like subnuclear structures.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pirin family. {ECO:0000305}.
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DR   EMBL; BC088290; AAH88290.1; -; mRNA.
DR   RefSeq; NP_001009474.1; NM_001009474.1.
DR   AlphaFoldDB; Q5M827; -.
DR   SMR; Q5M827; -.
DR   STRING; 10116.ENSRNOP00000004884; -.
DR   iPTMnet; Q5M827; -.
DR   PhosphoSitePlus; Q5M827; -.
DR   jPOST; Q5M827; -.
DR   PaxDb; Q5M827; -.
DR   PRIDE; Q5M827; -.
DR   Ensembl; ENSRNOT00000004884; ENSRNOP00000004884; ENSRNOG00000003674.
DR   GeneID; 363465; -.
DR   KEGG; rno:363465; -.
DR   UCSC; RGD:1359212; rat.
DR   CTD; 8544; -.
DR   RGD; 1359212; Pir.
DR   eggNOG; ENOG502QQ5A; Eukaryota.
DR   GeneTree; ENSGT00390000008044; -.
DR   HOGENOM; CLU_045717_0_1_1; -.
DR   InParanoid; Q5M827; -.
DR   OMA; TPWHPHR; -.
DR   OrthoDB; 1328043at2759; -.
DR   PhylomeDB; Q5M827; -.
DR   TreeFam; TF300002; -.
DR   Reactome; R-RNO-8935690; Digestion.
DR   UniPathway; UPA00724; -.
DR   PRO; PR:Q5M827; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000003674; Expressed in esophagus and 19 other tissues.
DR   Genevisible; Q5M827; RN.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; ISS:UniProtKB.
DR   GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR   GO; GO:0030224; P:monocyte differentiation; ISO:RGD.
DR   GO; GO:0030099; P:myeloid cell differentiation; ISO:RGD.
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; Direct protein sequencing; Iron; Metal-binding;
KW   Nucleus; Oxidoreductase; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..291
FT                   /note="Pirin"
FT                   /id="PRO_0000288474"
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"
SQ   SEQUENCE   291 AA;  32179 MW;  E2DD54C259D831F3 CRC64;
     MASSKKVTLS VLSREQSEGV GARVRRSIGG PELKMLDPFL LFDEFKGGRP GGFPDHPHRG
     FETVSYLLEG GSMAHEDFCG HVGKMNPGDL QWMTAGRGIL HAEMPCSEEP AHGLQLWVNL
     KRSEKMVEPQ YQELKSEEIP KPSKDGVTVA VISGEALGIK SKVYTRTPTL YLDFKLDQGA
     KHSQPIPKGW TSFIYTISGD VYIGPDDAQQ KIEPHRTAVL GEGDTVQLEN KDPKRSHFVL
     IAGEPLREPV VQHGPFVMNT NEEISEAILD FRNAKNGFEG AKTWKSKIGN Q