GLYR1_CHICK
ID GLYR1_CHICK Reviewed; 553 AA.
AC Q5ZLS7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
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;
DE AltName: Full=Putative oxidoreductase GLYR1;
GN Name=GLYR1; Synonyms=NP60; ORFNames=RCJMB04_4p18;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Cytokine-like nuclear factor with chromatin gene reader
CC activity involved in chromatin modification and regulation of gene
CC expression. Acts as a nucleosome-destabilizing factor that is recruited
CC to genes during transcriptional activation. Recognizes and binds
CC histone H3 without a preference for specific epigenetic markers and
CC also binds DNA. Interacts with KDM1B and promotes its histone
CC demethylase activity by facilitating the capture of H3 tails, they form
CC a multifunctional enzyme complex that modifies transcribed chromatin
CC and facilitates Pol II transcription through nucleosomes.
CC {ECO:0000250|UniProtKB:Q49A26}.
CC -!- SUBUNIT: Homotetramere. Binds to mononucleosomes.
CC {ECO:0000250|UniProtKB:Q49A26}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q49A26}.
CC Chromosome {ECO:0000250|UniProtKB:Q49A26}. Note=Found in actively
CC RNAPolII-transcribed gene bodies. {ECO:0000250|UniProtKB:Q49A26}.
CC -!- DOMAIN: The A.T hook DNA-binding domain is required for the interaction
CC with MAPK14. {ECO:0000250|UniProtKB:Q49A26}.
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; AJ719657; CAG31316.1; -; mRNA.
DR RefSeq; NP_001006572.1; NM_001006572.2.
DR AlphaFoldDB; Q5ZLS7; -.
DR SMR; Q5ZLS7; -.
DR STRING; 9031.ENSGALP00000002822; -.
DR PaxDb; Q5ZLS7; -.
DR GeneID; 426988; -.
DR KEGG; gga:426988; -.
DR CTD; 84656; -.
DR VEuPathDB; HostDB:geneid_426988; -.
DR eggNOG; KOG0409; Eukaryota.
DR eggNOG; KOG1904; Eukaryota.
DR InParanoid; Q5ZLS7; -.
DR OrthoDB; 885724at2759; -.
DR PhylomeDB; Q5ZLS7; -.
DR PRO; PR:Q5ZLS7; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Chromosome; DNA-binding; Nucleus; Reference proteome.
FT CHAIN 1..553
FT /note="Cytokine-like nuclear factor N-PAC"
FT /id="PRO_0000312125"
FT DOMAIN 8..66
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT DNA_BIND 168..180
FT /note="A.T hook"
FT /evidence="ECO:0000305"
FT REGION 92..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..217
FT /note="Interaction with histone H3"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT REGION 261..553
FT /note="Dehydrogenase domain"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT COMPBIAS 92..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 271..285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT BINDING 362
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT BINDING 505
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
SQ SEQUENCE 553 AA; 60601 MW; 707C3C476C82FF1A CRC64;
MAAVSLRLGD LVWGKLGRYP PWPGKIVNPP KDLKKPRGKK CFFVKFFGTE DHAWIKVEQL
KPYHLHKEEM IKINKGKRFQ QAVDAVEEFL RKTKGKDQAS SHNSSEEKNR RNSSEERGKQ
SAREEKRKAS LSEGKLKKGT GEGKKRVSSV SSERGSKSPL KRAQDQSPRK RGRPPKDEKD
LTIPESSTVK RVMTGTVAGF KWPPSVSEPV KDSDPHFHHF LLSQTEKPAV CYQAITKKLK
VCEEETGSTS IQAADSTAVN GSITPTDKKI GFLGLGLMGS GIVSNLLKMG HTVTVWNRTA
EKCDLFIQEG ARLGRTPAEV VSTCDITFAC VSDPKAAKDL VLGPSGVLQG IRPGKCYVDM
STVDADTVTE LAQVIVSRGG RFLEAPVSGN QQLSNDGMLV ILAAGDRGLY EDCSSCFQAM
GKTSFFLGEV GNAAKMMLIV NMVQGSFMAT IAEGLTLAQV TGQSQQTLLD ILNQGQLASI
FLDQKCQNIL QGNFKPDFYL KYIQKDLRLA IALGDSVNHP TPMAAAANEV YKRAKALDQS
DNDMSAVYRA YIH
