GLYR1_DROPS
ID GLYR1_DROPS Reviewed; 612 AA.
AC Q29NG1;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Cytokine-like nuclear factor N-PAC;
DE Short=NPAC;
DE AltName: Full=Glyoxylate reductase 1 homolog;
DE AltName: Full=Nuclear protein NP60 homolog;
DE AltName: Full=Putative oxidoreductase GLYR1 homolog;
GN ORFNames=GA18401;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Nucleosome-destabilizing factor that is recruited to genes
CC during transcriptional activation and colocalizes with a subset of
CC trimethylated 'Lys-36' histone H3 (H3K36me3)-enriched regions. Binds
CC DNA (in vitro). Facilitates Pol II transcription through nucleosomes.
CC Facilitates male-specific lethal (MSL) histone acetyltransferase
CC complex targeting to active genes on the X chromosome. Stimulates the
CC acetylation of 'Lys-56' of nucleosomal histone H3 (H3K56ac) by nej (By
CC similarity). {ECO:0000250|UniProtKB:Q49A26,
CC ECO:0000250|UniProtKB:Q8T079}.
CC -!- SUBUNIT: Binds to mononucleosomes. Interacts with male-specific lethal
CC (MSL) histone acetyltransferase complex at least composed of mof, msl-
CC 1, msl-2 and msl-3. {ECO:0000250|UniProtKB:Q8T079}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q8T079}.
CC Note=Localization to open chromatin depends on H3K36 trimethylation by
CC Set2. {ECO:0000250|UniProtKB:Q8T079}.
CC -!- DOMAIN: The PWWP domain is a H3 reader and strongly binds DNA.
CC {ECO:0000250|UniProtKB:Q49A26}.
CC -!- DOMAIN: In the dehydrogenase domain, the conserved NAD(P)H-binding
CC sites and sequence similarity to plant dehydrogenases suggest that this
CC protein may have oxidoreductase activity. However, since the active
CC site is not conserved, the dehydrogenase domain seems to serve as a
CC catalytically inert oligomerization module.
CC {ECO:0000250|UniProtKB:Q49A26}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. NP60 subfamily.
CC {ECO:0000305}.
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DR EMBL; CH379060; EAL33381.2; -; Genomic_DNA.
DR RefSeq; XP_001356318.2; XM_001356282.3.
DR AlphaFoldDB; Q29NG1; -.
DR SMR; Q29NG1; -.
DR STRING; 7237.FBpp0280278; -.
DR EnsemblMetazoa; FBtr0281840; FBpp0280278; FBgn0078403.
DR GeneID; 4816828; -.
DR KEGG; dpo:Dpse_GA18401; -.
DR eggNOG; KOG0409; Eukaryota.
DR HOGENOM; CLU_018075_0_0_1; -.
DR InParanoid; Q29NG1; -.
DR OMA; DNIMSKN; -.
DR Proteomes; UP000001819; Chromosome 4.
DR Bgee; FBgn0078403; Expressed in female reproductive system and 2 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd05836; N_Pac_NP60; 1.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029154; NADP-bd.
DR InterPro; IPR035501; NP60_PWWP.
DR InterPro; IPR000313; PWWP_dom.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 3: Inferred from homology;
KW Chromosome; DNA-binding; Reference proteome.
FT CHAIN 1..612
FT /note="Cytokine-like nuclear factor N-PAC"
FT /id="PRO_0000312131"
FT DOMAIN 22..81
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 168..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..279
FT /note="Interaction with histone H3"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT REGION 319..612
FT /note="Dehydrogenase domain"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT COMPBIAS 171..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 329..343
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT BINDING 421
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT BINDING 564
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
SQ SEQUENCE 612 AA; 66209 MW; ABB84781FCA292EE CRC64;
MSKNKKMSLS GGDTTEKFIY KPKDLIWAKM KGFTPWPGMI VEPPLDLLTQ QRRANTKCVF
FFGSRNFAWI EENNIKPFEG PWKEELAKVS KPAAFRHAMA DIDKYIDDPA EVDDQINESC
GVPNHATEAD FDKIRDAVDS DENAVDADAD ANNGVVVHVV GSPDVSEAVE GENNADSSAS
PTVTAATPAT AKSPAKRTPK AKPVSAVSAT KAAKASTTKS AQKRRISAHQ TPTGANTSGL
PNAKRGKRVV SGGATPGNFD GASSSSPTAR RRVEVDDLLA SLAAKRAPNA IALLDRPVVT
RPETQAIDMN SRSNTLADRD IVPSELTFGF LGLGMMGSTI VKDLIYTGHK VVVWNRTIDK
CQPFVEAGAE VKDTPMDVVE AADIIFCCVS DPKGAKDLVF GNCGVLQLKD LRNKAYVEMS
TVDPDTSLDI GEGIKQCNGR YLEAQIHGSR QEAADGMLII LAGGDRTVFE ECHSCFKTIA
KNTFFLGNVG NACKVNLILQ TIQAVSLVGL AEALALADRF SISLNDIIDI FDLTSMKSPL
LLAKGKEMAK GDFNPQQPLS HMQRDLRLVL NMAENLDQSM PVTSITNEVF KHTKRLGYSE
HDSSAVFVRS RF
