ID   PYRD1_DANRE             Reviewed;         490 AA.
AC   Q6PBT5;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1;
DE            EC=1.8.1.-;
GN   Name=pyroxd1; ORFNames=zgc:73254;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27745833; DOI=10.1016/j.ajhg.2016.09.005;
RA   O'Grady G.L., Best H.A., Sztal T.E., Schartner V., Sanjuan-Vazquez M.,
RA   Donkervoort S., Abath Neto O., Sutton R.B., Ilkovski B., Romero N.B.,
RA   Stojkovic T., Dastgir J., Waddell L.B., Boland A., Hu Y., Williams C.,
RA   Ruparelia A.A., Maisonobe T., Peduto A.J., Reddel S.W., Lek M.,
RA   Tukiainen T., Cummings B.B., Joshi H., Nectoux J., Brammah S.,
RA   Deleuze J.F., Ing V.O., Ramm G., Ardicli D., Nowak K.J., Talim B.,
RA   Topaloglu H., Laing N.G., North K.N., MacArthur D.G., Friant S.,
RA   Clarke N.F., Bryson-Richardson R.J., Boennemann C.G., Laporte J.,
RA   Cooper S.T.;
RT   "Variants in the oxidoreductase PYROXD1 cause early-onset myopathy with
RT   internalized nuclei and myofibrillar disorganization.";
RL   Am. J. Hum. Genet. 99:1086-1105(2016).
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 (PubMed:27745833).
CC       {ECO:0000250|UniProtKB:Q8WU10, ECO:0000269|PubMed:27745833}.
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:0000269|PubMed:27745833}. Cytoplasm
CC       {ECO:0000269|PubMed:27745833}. Cytoplasm, myofibril, sarcomere
CC       {ECO:0000269|PubMed:27745833}.
CC   -!- DISRUPTION PHENOTYPE: Morpholino-injected embryos show severe
CC       disruption of the musculature with fragmentation of the muscle fibers,
CC       altered sarcomeric structure, loss of fiber integrity and accumulation
CC       of actin at the myosepta (PubMed:27745833). Disintegration of the
CC       myofibrils with mitochondrial infiltration of the resulting space, loss
CC       of Z-disk structures, and electron dense, nemaline-like bodies are
CC       observed by electron microscopy (PubMed:27745833).
CC       {ECO:0000269|PubMed:27745833}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. PYROXD1 subfamily. {ECO:0000305}.
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DR   EMBL; BC059591; AAH59591.1; -; mRNA.
DR   RefSeq; NP_957057.1; NM_200763.1.
DR   AlphaFoldDB; Q6PBT5; -.
DR   SMR; Q6PBT5; -.
DR   STRING; 7955.ENSDARP00000042662; -.
DR   PaxDb; Q6PBT5; -.
DR   PRIDE; Q6PBT5; -.
DR   GeneID; 393736; -.
DR   KEGG; dre:393736; -.
DR   CTD; 79912; -.
DR   ZFIN; ZDB-GENE-040426-1732; pyroxd1.
DR   eggNOG; KOG2755; Eukaryota.
DR   InParanoid; Q6PBT5; -.
DR   OrthoDB; 1463391at2759; -.
DR   PhylomeDB; Q6PBT5; -.
DR   PRO; PR:Q6PBT5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; FAD; Flavoprotein; NADP; Nucleus; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..490
FT                   /note="Pyridine nucleotide-disulfide oxidoreductase domain-
FT                   containing protein 1"
FT                   /id="PRO_0000327423"
SQ   SEQUENCE   490 AA;  54257 MW;  BFCD52CF088C3E24 CRC64;
     MCGSSMASEK QVKFVIVGGG IAGVTCAEQI ASQFPSDEVC LLTASPLVKK VTNFRQVSKT
     LEEFDIEEQP SRVLEEKYPN LKVLQSAVRL LKAREHLLET EDGQRFFYRK LCLCSGGRPK
     LLSKDNPHVL GIRDTDSAQE FQKRLSTAKR IVVIGNGGIA LELVYEVEGC EVIWAVKDKA
     IGNTFFDAGA AQFLIPSLEA DRREASSVCK RARYTTDSSA AGHSGSSSEL GSALGPDWHE
     GIELRGAKQS VRGVHIEYEC EVEQIYTQQE LLQSEHGTKT AELGVWPAYV QLTNGKIYGC
     DFIVSATGVV PNTDPFLPGN NFDVAADLGL LVDDHMRTSE ADVFAAGDVC SAGWEPSSIW
     QQMRLWTQAR QMGWYAARCM AADVLDEPIE LDFCFELFSH ITKFFNYKVV LLGKFNAQGL
     GQDHELLVRC TKGQEYVKVV LSGGRMVGAV LIGETDLEET FENLILNQMD LTRYGEELLN
     PNIDIEDYFD