GLYR1_ANOGA
ID GLYR1_ANOGA Reviewed; 566 AA.
AC Q7Q161;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 5.
DT 03-AUG-2022, entry version 105.
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=AGAP009949;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
CC -!- FUNCTION: May have oxidoreductase activity.
CC {ECO:0000250|UniProtKB:Q49A26}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA14020.4; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAAB01008980; EAA14020.4; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_319082.4; XM_319082.4.
DR AlphaFoldDB; Q7Q161; -.
DR SMR; Q7Q161; -.
DR STRING; 7165.AGAP009949-PA; -.
DR PaxDb; Q7Q161; -.
DR GeneID; 1279367; -.
DR KEGG; aga:AgaP_AGAP009949; -.
DR CTD; 1279367; -.
DR VEuPathDB; VectorBase:AGAP009949; -.
DR eggNOG; KOG0409; Eukaryota.
DR HOGENOM; CLU_018075_0_0_1; -.
DR InParanoid; Q7Q161; -.
DR OrthoDB; 885724at2759; -.
DR Proteomes; UP000007062; Chromosome 3R.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
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; 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; Reference proteome.
FT CHAIN 1..566
FT /note="Cytokine-like nuclear factor N-PAC"
FT /id="PRO_0000312129"
FT DOMAIN 9..70
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 127..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..566
FT /note="Dehydrogenase domain"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT BINDING 284..298
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT BINDING 518
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
SQ SEQUENCE 566 AA; 61543 MW; 3F3FFD60DEFB74FD CRC64;
MSDSTGYAVN DLVWAKMKGF SPWPGRISVP PAELRKIAVK KNNPVKCIFF FGSNNYAWIE
ETQIKPYLQF KDTHLNSSKS AQFKEALKQI EEFRVNPEKF QPLFVGENEA ANRPDPDEEF
NRLREGVASG TEESGAEDGA SVNNTTTPAV LESVDEATST PMVKKSAKKK VRASLPIKLN
VDKVVCESII TFQCSPRSVG NKAKAMLDDG VSGAPSPKRK KKLLNDSGEL SSLDASPVRR
NAPVTHLLNR PVTVTRPETP EIDMSSVSNA VQSRNIKASQ LKFGFLGLGV MGCGIVKNLI
KSGHSVVVWN RSAHKCRKFQ EVGAEVADTP SDVVEMTDVT YSCVSDPQVA KDMVFGNCGV
MSANLAGKGY VEMTGVDPET SNDINEAIIS KGGRYLEAQI QGSKNQAEEG TLIILASGDR
LLFEECQSCF EAISRNSFYL GDVGNATKMN LILQMISGIT LAGVAEAMAL ADRAGLQQKD
VLEVLELTNM SSEMMLQKGN AIIKGEFPTH HALKHMQKDL KLALSLADGL EQSLPITAAS
NEVYKHAKRL GYGSHDASAV YVRARF
