GLYR1_XENTR
ID GLYR1_XENTR Reviewed; 534 AA.
AC Q562D5;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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; BC092548; AAH92548.1; -; mRNA.
DR RefSeq; NP_001025665.1; NM_001030494.1.
DR AlphaFoldDB; Q562D5; -.
DR SMR; Q562D5; -.
DR STRING; 8364.ENSXETP00000006808; -.
DR DNASU; 595057; -.
DR GeneID; 595057; -.
DR KEGG; xtr:595057; -.
DR CTD; 84656; -.
DR Xenbase; XB-GENE-958848; glyr1.
DR InParanoid; Q562D5; -.
DR OrthoDB; 885724at2759; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
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; NAD; Nucleus; Reference proteome.
FT CHAIN 1..534
FT /note="Cytokine-like nuclear factor N-PAC"
FT /id="PRO_0000312127"
FT DOMAIN 8..66
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT DNA_BIND 144..156
FT /note="A.T hook"
FT /evidence="ECO:0000305"
FT REGION 93..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..193
FT /note="Interaction with histone H3"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT REGION 242..534
FT /note="Dehydrogenase domain"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT COMPBIAS 93..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 252..266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT BINDING 343
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT BINDING 486
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
SQ SEQUENCE 534 AA; 58475 MW; 69D3609740288A51 CRC64;
MAAVSLRQGD LVWGKLGRYP PWPGKIVNPP KDLKKPRGKK CLFVKFFGTE DHAWIKVEQL
KPYHAHKEEM IKANKGKRFQ QAVDAVEEFL KKAKAKEHAK EHNSSDEKGK KGEGKGKKQT
GEKRRKSSES SSHSPQKRSR DQSPRKRGRP PKDDKDSPSP QPSSLKKLAM KTVSRFSWPP
PSTEDDLGSD SWLIHGHRTL GTEMILKKPS VTYQAITKRL KISEEDSGST SIQAADSTAI
NGNIIPTDKK IGFLGLGLMG SGIVSNLLKM GHTVTVWNRT AEKCDLFIQE GAHMGRTPAE
VVSTCDITFA CVADPKAAKD LVLGPSGVLQ GIRPGKCYVD MSTVDPETVA ELAQVIVSRG
GRFLEAPVSG NQQLSNDGML VILAAGDQGV YEDCSSCFLA MGKTSFFLGE VGNAARMMLI
LNMVQGSFMA TIAEGMTLAQ VTGQSQQTLL DILNQGQLAS IFLDQKCQNI LQGNFKPDFY
LKYIQKDLRL AIALGDSVNH PTPMAAAANE VYKRAKALDQ SDNDMSAVYR AYIH
