PYRD1_MOUSE
ID PYRD1_MOUSE Reviewed; 498 AA.
AC Q3TMV7; Q3UFM2; Q8R2X5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1;
DE EC=1.8.1.-;
GN Name=Pyroxd1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP SUBCELLULAR LOCATION.
RX PubMed=30345904; DOI=10.1152/physiolgenomics.00036.2018;
RA Saha M., Reddy H.M., Salih M., Estrella E., Jones M.D., Mitsuhashi S.,
RA Cho K.A., Suzuki-Hatano S., Rizzo S.A., Hamad M.H., Mukhtar M.M.,
RA Hamed A.A., Elseed M.A., Lek M., Valkanas E., MacArthur D.G., Kunkel L.M.,
RA Pacak C.A., Draper I., Kang P.B.;
RT "The impact of PYROXD1 deficiency on cellular respiration and correlations
RT with genetic analyses of limb-girdle muscular dystrophy in Saudi Arabia and
RT Sudan.";
RL Physiol. Genomics 50:929-939(2018).
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:0000269|PubMed:30345904}. Cytoplasm
CC {ECO:0000269|PubMed:30345904}. 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}.
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DR EMBL; AK148411; BAE28538.1; -; mRNA.
DR EMBL; AK165677; BAE38333.1; -; mRNA.
DR EMBL; BC027061; AAH27061.1; -; mRNA.
DR CCDS; CCDS20681.1; -.
DR RefSeq; NP_898988.2; NM_183165.3.
DR AlphaFoldDB; Q3TMV7; -.
DR SMR; Q3TMV7; -.
DR STRING; 10090.ENSMUSP00000036394; -.
DR PhosphoSitePlus; Q3TMV7; -.
DR EPD; Q3TMV7; -.
DR MaxQB; Q3TMV7; -.
DR PaxDb; Q3TMV7; -.
DR PeptideAtlas; Q3TMV7; -.
DR PRIDE; Q3TMV7; -.
DR ProteomicsDB; 301956; -.
DR Antibodypedia; 49414; 69 antibodies from 21 providers.
DR DNASU; 232491; -.
DR Ensembl; ENSMUST00000041852; ENSMUSP00000036394; ENSMUSG00000041671.
DR GeneID; 232491; -.
DR KEGG; mmu:232491; -.
DR UCSC; uc009epc.1; mouse.
DR CTD; 79912; -.
DR MGI; MGI:2676395; Pyroxd1.
DR VEuPathDB; HostDB:ENSMUSG00000041671; -.
DR eggNOG; KOG2755; Eukaryota.
DR GeneTree; ENSGT00390000014894; -.
DR HOGENOM; CLU_026335_0_0_1; -.
DR InParanoid; Q3TMV7; -.
DR OMA; MCENLIL; -.
DR OrthoDB; 1463391at2759; -.
DR PhylomeDB; Q3TMV7; -.
DR TreeFam; TF105963; -.
DR BioGRID-ORCS; 232491; 22 hits in 73 CRISPR screens.
DR ChiTaRS; Pyroxd1; mouse.
DR PRO; PR:Q3TMV7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q3TMV7; protein.
DR Bgee; ENSMUSG00000041671; Expressed in embryonic post-anal tail and 171 other tissues.
DR Genevisible; Q3TMV7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA: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_0000327420"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8WU10"
FT CONFLICT 68
FT /note="T -> I (in Ref. 1; BAE28538 and 2; AAH27061)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="I -> T (in Ref. 1; BAE28538 and 2; AAH27061)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="L -> F (in Ref. 1; BAE28538)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="T -> K (in Ref. 1; BAE28538 and 2; AAH27061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 55592 MW; ABD67D55D64F82F5 CRC64;
MEAPRPAGTF VVVGGGIAGV TCAEQLAVSF PEEDILLVTA SPVIKAVTNF RQVSKVLEEF
DVEEQPGTML ESRFPNIKVI ESGVKQLKSE DHCIFTEDGR EFVYKKLCLC AGAKPKLIYE
GNPRVLGIRD TDSAQEFQKE LAKARRIMIV GNGGIALELA YEIEGCEVVW AIKDNAIGNT
FFDAGAAEFL TSKLMSEKSE AKIAHKRTIY TVEEAKKETR TKSKADYVGS ALGPDWHGGL
ALKGTEEFSH SVHIETRCEV KKIYLEEEFK IMKKKSLAFP KDHHKSVTAD KEMWPVYVEL
TNGTIYGCDF LVSATGVTPN VHPFLHRNNF ALGEDGGLRV DDQMRTSLPD IYAAGDICTA
CWQPSPVWQQ MRLWTQARQM GYYAAKCMAA ASMGHPIDMD FSFELFAHVT KFFNYKVVLL
GKYNAQGLGA DHELMLRCTR GQEYVKVVMQ NGRMMGAVLI GETDLEETFE NLILNQMDLS
SYGEDLLDPN IDIEDYFD
