PYRD2_HUMAN
ID PYRD2_HUMAN Reviewed; 581 AA.
AC Q8N2H3; D3DR61; Q5TAA9; Q9BRQ1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000305};
DE EC=1.-.-.-;
GN Name=PYROXD2 {ECO:0000312|HGNC:HGNC:23517}; Synonyms=C10orf33;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-461 AND THR-533.
RC TISSUE=Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-428 AND THR-461.
RC TISSUE=Uterus;
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 [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH COX5B, AND FUNCTION.
RX PubMed=31170524; DOI=10.1016/j.mito.2019.05.007;
RA Wang T., Xie X., Liu H., Chen F., Du J., Wang X., Jiang X., Yu F., Fan H.;
RT "Pyridine nucleotide-disulphide oxidoreductase domain 2 (PYROXD2): Role in
RT mitochondrial function.";
RL Mitochondrion 47:114-124(2019).
CC -!- FUNCTION: Probable oxidoreductase that may play a role as regulator of
CC mitochondrial function. {ECO:0000269|PubMed:31170524}.
CC -!- SUBUNIT: Interacts with COX5B; this interaction may contribute to
CC localize PYROXD2 to the inner face of the inner mitochondrial membrane.
CC {ECO:0000269|PubMed:31170524}.
CC -!- INTERACTION:
CC Q8N2H3; Q92624: APPBP2; NbExp=3; IntAct=EBI-3919450, EBI-743771;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:31170524}. Note=The import into mitochondria is
CC dependent on TOMM40 and TIMM23. {ECO:0000269|PubMed:31170524}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AK075265; BAC11507.1; -; mRNA.
DR EMBL; AL139243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49884.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49885.1; -; Genomic_DNA.
DR EMBL; BC006131; AAH06131.1; -; mRNA.
DR CCDS; CCDS7474.1; -.
DR RefSeq; NP_116098.2; NM_032709.2.
DR AlphaFoldDB; Q8N2H3; -.
DR SMR; Q8N2H3; -.
DR BioGRID; 124263; 24.
DR IntAct; Q8N2H3; 5.
DR MINT; Q8N2H3; -.
DR STRING; 9606.ENSP00000359607; -.
DR iPTMnet; Q8N2H3; -.
DR PhosphoSitePlus; Q8N2H3; -.
DR BioMuta; PYROXD2; -.
DR DMDM; 109820933; -.
DR jPOST; Q8N2H3; -.
DR MassIVE; Q8N2H3; -.
DR MaxQB; Q8N2H3; -.
DR PaxDb; Q8N2H3; -.
DR PeptideAtlas; Q8N2H3; -.
DR PRIDE; Q8N2H3; -.
DR ProteomicsDB; 71699; -.
DR Antibodypedia; 31034; 99 antibodies from 19 providers.
DR DNASU; 84795; -.
DR Ensembl; ENST00000370575.5; ENSP00000359607.4; ENSG00000119943.13.
DR GeneID; 84795; -.
DR KEGG; hsa:84795; -.
DR MANE-Select; ENST00000370575.5; ENSP00000359607.4; NM_032709.3; NP_116098.2.
DR UCSC; uc001kpc.4; human.
DR CTD; 84795; -.
DR DisGeNET; 84795; -.
DR GeneCards; PYROXD2; -.
DR HGNC; HGNC:23517; PYROXD2.
DR HPA; ENSG00000119943; Low tissue specificity.
DR MIM; 617889; gene.
DR neXtProt; NX_Q8N2H3; -.
DR OpenTargets; ENSG00000119943; -.
DR PharmGKB; PA165549043; -.
DR VEuPathDB; HostDB:ENSG00000119943; -.
DR eggNOG; KOG4254; Eukaryota.
DR GeneTree; ENSGT00390000011684; -.
DR HOGENOM; CLU_019327_0_0_1; -.
DR InParanoid; Q8N2H3; -.
DR OMA; GMQGAWG; -.
DR OrthoDB; 392025at2759; -.
DR PhylomeDB; Q8N2H3; -.
DR TreeFam; TF315188; -.
DR PathwayCommons; Q8N2H3; -.
DR SignaLink; Q8N2H3; -.
DR BioGRID-ORCS; 84795; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; PYROXD2; human.
DR GenomeRNAi; 84795; -.
DR Pharos; Q8N2H3; Tbio.
DR PRO; PR:Q8N2H3; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8N2H3; protein.
DR Bgee; ENSG00000119943; Expressed in right uterine tube and 169 other tissues.
DR Genevisible; Q8N2H3; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IMP:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0007005; P:mitochondrion organization; IMP: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 1: Evidence at protein 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_0000244071"
FT BINDING 38..71
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT VARIANT 428
FT /note="P -> S (in dbSNP:rs17856170)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026877"
FT VARIANT 461
FT /note="M -> T (in dbSNP:rs2147896)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_026878"
FT VARIANT 533
FT /note="A -> T (in dbSNP:rs2296441)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_026879"
SQ SEQUENCE 581 AA; 63068 MW; 64A9FB0B283939EE CRC64;
MAASGRGLCK AVAASPFPAW RRDNTEARGG LKPEYDAVVI GAGHNGLVAA AYLQRLGVNT
AVFERRHVIG GAAVTEEIIP GFKFSRASYL LSLLRPQIYT DLELKKHGLR LHLRNPYSFT
PMLEEGAGSK VPRCLLLGTD MAENQKQIAQ FSQKDAQVFP KYEEFMHRLA LAIDPLLDAA
PVDMAAFQHG SLLQRMRSLS TLKPLLKAGR ILGAQLPRYY EVLTAPITKV LDQWFESEPL
KATLATDAVI GAMTSPHTPG SGYVLLHHVM GGLEGMQGAW GYVQGGMGAL SDAIASSATT
HGASIFTEKT VAKVQVNSEG CVQGVVLEDG TEVRSKMVLS NTSPQITFLK LTPQEWLPEE
FLERISQLDT RSPVTKINVA VDRLPSFLAA PNAPRGQPLP HHQCSIHLNC EDTLLLHQAF
EDAMDGLPSH RPVIELCIPS SLDPTLAPPG CHVVSLFTQY MPYTLAGGKA WDEQERDAYA
DRVFDCIEVY APGFKDSVVG RDILTPPDLE RIFGLPGGNI FHCAMSLDQL YFARPVPLHS
GYRCPLQGLY LCGSGAHPGG GVMGAAGRNA AHVAFRDLKS M
