PYRD1_RAT
ID PYRD1_RAT Reviewed; 498 AA.
AC Q68FS6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1;
DE EC=1.8.1.-;
GN Name=Pyroxd1;
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 FAD-dependent oxidoreductase; involved in the
CC cellular oxidative stress response (By similarity). Required for normal
CC sarcomere structure and muscle fiber integrity (By similarity).
CC {ECO:0000250|UniProtKB:Q6PBT5, ECO:0000250|UniProtKB:Q8WU10}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:O52582};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O52582};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WU10}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q3TMV7}. Cytoplasm, myofibril, sarcomere
CC {ECO:0000250|UniProtKB:Q8WU10}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. PYROXD1 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC079377; AAH79377.1; -; mRNA.
DR RefSeq; NP_001004234.1; NM_001004234.1.
DR AlphaFoldDB; Q68FS6; -.
DR SMR; Q68FS6; -.
DR STRING; 10116.ENSRNOP00000016794; -.
DR iPTMnet; Q68FS6; -.
DR PhosphoSitePlus; Q68FS6; -.
DR PaxDb; Q68FS6; -.
DR GeneID; 297708; -.
DR KEGG; rno:297708; -.
DR UCSC; RGD:1303253; rat.
DR CTD; 79912; -.
DR RGD; 1303253; Pyroxd1.
DR eggNOG; KOG2755; Eukaryota.
DR InParanoid; Q68FS6; -.
DR OrthoDB; 1463391at2759; -.
DR PhylomeDB; Q68FS6; -.
DR PRO; PR:Q68FS6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030017; C:sarcomere; ISS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 3.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR041575; Rubredoxin_C.
DR Pfam; PF07992; Pyr_redox_2; 2.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; FAD; Flavoprotein; NADP; Nucleus; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..498
FT /note="Pyridine nucleotide-disulfide oxidoreductase domain-
FT containing protein 1"
FT /id="PRO_0000327422"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8WU10"
SQ SEQUENCE 498 AA; 55490 MW; 320BDA30A6675AB6 CRC64;
MEAARPAGTF VVVGGGIAGV TCAEQLAINF PAEDILLVTA SPVIKAVTNF KQVSKVLEEF
DVEEQPSTML ENRFPNIKVI ESGVKQLKSD KHCIFTEDGR EYVYKKLCLC AGAKPKLICE
GNPYVLGIRD TDSAQEFQKQ LTKARRIMIV GNGGIALELA YEVEVCEVIW AIKDKAIGNT
FFDAGAAEFL TSRLLSEKSE AKLAHKRTIY TVEEAKKETS TKSKADYVGS ALGPDWHGGL
ALKGTEEFSH SIHIETKCEV KKIYLQEEFK IMKKKSLAFP KDHHKSVTVD KEMWPVYVEL
TNGSIYGCDF LVSATGVTPN VQPFLHGNDF DLGEDGGLRV DEQMRTSLPD IYAAGDICTA
CWPPSPVWQQ MRLWTQARQM GCYAAKCMAA ATMGHPIDMD FSFELFAHVT KFFNYKVVLL
GKYNAQGLGV DHELMLRCTR GQEYIKVVMH NGRMMGAVLI GETDLEETFE NLILNQMDLS
SYGEDLLNPD IDIEDYFD