GLYR1_DANRE
ID GLYR1_DANRE Reviewed; 462 AA.
AC Q5RKN4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=zgc:103629;
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=Larva;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May have oxidoreductase activity. Regulates p38 MAP kinase
CC activity by mediating stress activation of mapk14 and specifically
CC regulating mapk14 signaling. {ECO:0000250|UniProtKB:Q49A26}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC085567; AAH85567.1; -; mRNA.
DR RefSeq; NP_001007772.1; NM_001007771.1.
DR AlphaFoldDB; Q5RKN4; -.
DR SMR; Q5RKN4; -.
DR STRING; 7955.ENSDARP00000055237; -.
DR GeneID; 493611; -.
DR KEGG; dre:493611; -.
DR CTD; 84656; -.
DR ZFIN; ZDB-GENE-041121-5; glyr1.
DR eggNOG; KOG0409; Eukaryota.
DR eggNOG; KOG1904; Eukaryota.
DR InParanoid; Q5RKN4; -.
DR OrthoDB; 885724at2759; -.
DR PhylomeDB; Q5RKN4; -.
DR PRO; PR:Q5RKN4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; Nucleus; Reference proteome.
FT CHAIN 1..462
FT /note="Cytokine-like nuclear factor N-PAC"
FT /id="PRO_0000312126"
FT DOMAIN 8..66
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 91..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..462
FT /note="Dehydrogenase domain"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT COMPBIAS 91..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT BINDING 414
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
SQ SEQUENCE 462 AA; 50601 MW; 8B5A17C1E9D270E6 CRC64;
MATVHLRIGD LVWGKLGRYP PWPGKVVSPP KDLKKPRGKK CFFVKFFGTE DHAWIKVEQL
KPYHPHKEEM IKVNKGKRFQ QAVDAVEEYL KKAKGKDQSH SDDKSKSDKG RKAAKPMKII
EEDDEDAFKG GSSDKPASSM EPITKRLKII EEDTRSTSIQ AADSTAINGS ITPTDKRIGF
LGLGLMGSGV VSNLLKMGHV VTVWNRTAEK CDLFIQEGAR LGRTPAEVVS MCDITFSCVS
DPKAARDLVL GPSGVLQGIR PGKCYVEMST VDPETITELS QVITSRGGRF LEAPVSGSQQ
LSNDGMLVIV AAGDRSVYED CSSCFQAMGK TSFFIAGEAG NAARMMLILN MVQGSFMATI
AEGLTLAQAT GQSQQTFLDI LCQGQMASTF VDQKCQNILQ GNFKPDYYLK HIQKDLRLAI
SMGDSVNHPT PMAAAANEVY KRAKALDQSD NDMSAVYRAY IH
