PYRD2_BOVIN
ID PYRD2_BOVIN Reviewed; 581 AA.
AC Q3MHH6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000250|UniProtKB:Q8N2H3};
DE EC=1.-.-.-;
GN Name=PYROXD2 {ECO:0000250|UniProtKB:Q8N2H3};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; BC105235; AAI05236.1; -; mRNA.
DR RefSeq; NP_001029704.1; NM_001034532.2.
DR AlphaFoldDB; Q3MHH6; -.
DR SMR; Q3MHH6; -.
DR STRING; 9913.ENSBTAP00000032879; -.
DR PaxDb; Q3MHH6; -.
DR PRIDE; Q3MHH6; -.
DR Ensembl; ENSBTAT00000081264; ENSBTAP00000072106; ENSBTAG00000014313.
DR GeneID; 519120; -.
DR KEGG; bta:519120; -.
DR CTD; 84795; -.
DR VEuPathDB; HostDB:ENSBTAG00000014313; -.
DR VGNC; VGNC:33594; PYROXD2.
DR eggNOG; KOG4254; Eukaryota.
DR GeneTree; ENSGT00390000011684; -.
DR InParanoid; Q3MHH6; -.
DR OMA; GMQGAWG; -.
DR OrthoDB; 392025at2759; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000014313; Expressed in cortex of kidney and 99 other tissues.
DR ExpressionAtlas; Q3MHH6; baseline and differential.
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_0000244070"
FT BINDING 38..71
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 581 AA; 62987 MW; 7CBE660429F49E95 CRC64;
MTICGRGLRR AVGASPRPTW RRALSDTRGR LKPEYDAVVV GAGHNGLVAA AYLQRFGVNT
AVFERRHVIG GAAVTEEIVP GFKFSRASYL LSLLRPQIYS ELELKKHGLR LHLRNPYSFT
PMLEEGTGGK VPRSLLLGTD MVENQKQIAQ FSKKDAQAFP KYEAFMDRLA LAIDPLLDSA
PVDLEAFQRG SLLQRLKSLS TLKPLWQAGC ILGAQLPQYY QVLTAPAAKV LDQWFESEPL
KATLATDAVI GAMTNPYIPG SGYVLLHHVM GSLEGVRGAW GYVQGGMGAL SDAIASSATA
HGVSIFTEKT VAKVQVSSGG RVQGVVLQDG SEVRSKVVLS NASPQITFLK LTPQEWLPEE
FVARIAQLDT KSPVTKINVA VNRLPDFLAA PNTPGDQPLP HHQCSIHLNC EDTLLVHQAF
EDTLDGLPSK RPLIELCIPS SLDPTLAPPG CHVVSLFTQY TPYTLAGGKA WDEQQRNTYA
DRVFDCIEAY APGFKGSVVG RDILTPPDLE RVFGLPGGNI FHCAMSLDQL YFARPVPLHS
SYCSPLRGLY LCGSGAHPGG GVMGAAGRNA AHVVFRDLRS M