ID   PYRD2_RAT               Reviewed;         581 AA.
AC   Q68FT3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000305};
DE            EC=1.-.-.-;
GN   Name=Pyroxd2 {ECO:0000312|RGD:1303232};
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=Kidney;
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).
CC   -!- FUNCTION: Probable oxidoreductase that may play a role as regulator of
CC       mitochondrial function. {ECO:0000250|UniProtKB:Q8N2H3}.
CC   -!- SUBUNIT: Interacts with COX5B; this interaction may contribute to
CC       localize PYROXD2 to the inner face of the inner mitochondrial membrane.
CC       {ECO:0000250|UniProtKB:Q8N2H3}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q8N2H3}. Note=The import into mitochondria is
CC       dependent on TOMM40 and TIMM23. {ECO:0000250|UniProtKB:Q8N2H3}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; BC079368; AAH79368.1; -; mRNA.
DR   RefSeq; NP_001004261.1; NM_001004261.1.
DR   AlphaFoldDB; Q68FT3; -.
DR   SMR; Q68FT3; -.
DR   STRING; 10116.ENSRNOP00000021257; -.
DR   iPTMnet; Q68FT3; -.
DR   PhosphoSitePlus; Q68FT3; -.
DR   PaxDb; Q68FT3; -.
DR   PRIDE; Q68FT3; -.
DR   GeneID; 309381; -.
DR   KEGG; rno:309381; -.
DR   UCSC; RGD:1303232; rat.
DR   CTD; 84795; -.
DR   RGD; 1303232; Pyroxd2.
DR   VEuPathDB; HostDB:ENSRNOG00000015807; -.
DR   eggNOG; KOG4254; Eukaryota.
DR   HOGENOM; CLU_019327_0_0_1; -.
DR   InParanoid; Q68FT3; -.
DR   OMA; GMQGAWG; -.
DR   OrthoDB; 392025at2759; -.
DR   PhylomeDB; Q68FT3; -.
DR   TreeFam; TF315188; -.
DR   PRO; PR:Q68FT3; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000015807; Expressed in adult mammalian kidney and 18 other tissues.
DR   Genevisible; Q68FT3; RN.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome.
FT   CHAIN           1..581
FT                   /note="Pyridine nucleotide-disulfide oxidoreductase domain-
FT                   containing protein 2"
FT                   /id="PRO_0000244074"
FT   BINDING         38..71
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   581 AA;  62879 MW;  954B2E8C38C6E2BF CRC64;
     MAASGRGLSR ALHSTPCPAW KRVQSGANGC LKPEYDAVVI GAGHNGLVAA AYLQRLGVNT
     AVFERRHVIG GAAVTEEIIP GFKFSRASYL LSLLRPQIYT DLELKKHGLK LHLRNPYSFT
     PMLEEGTLSK PPRSLLLGTD VAENQKQISQ FSRKDAQAFP RYEEFMKRLV LAIDPLLDAA
     PVDIAALQHG SLLQRLRALS TLRPLLKAGR TLGAQLPQYY EVLTAPISKV LDQWFESEPL
     KATLATDAVI GAMTSPHTPG SGYVLLHHVM GSLEGMQGAW SYVQGGMGAL SDAIASSATA
     HGASIFTEKT VAKVQVNSEG RVQGVVLQGG EEVRSRVVLS CASPQVTFLE LTPQEWLPGA
     FVKRISQLDT QSPVTKINVA VDRLPNFQAA PNAPGDQPQA HHQCSIHLNC EDTLLLHQAF
     EDAKGGLPSQ RPMIELCIPS SLDPTLAPTG CHVVSLFTQY TPYTLAGGKV WDEQKKNTYA
     DKVFDCIEAY APGFKRSVLG RDILTPQDLE RIFGLPGGNI FHGAMSLDQL YFARPVPQHS
     DYRCPVQGLY LCGSGAHPGG GVMGAAGRNA AHIVFRDLKN M