NLP_DROME
ID NLP_DROME Reviewed; 152 AA.
AC Q27415; Q24565; Q540W3; Q9VAC3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Nucleoplasmin-like protein;
DE AltName: Full=Chromatin decondensation protein 1;
DE AltName: Full=dNLP;
GN Name=Nlp; Synonyms=CRP1; ORFNames=CG7917;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PARTIAL PROTEIN SEQUENCE,
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8798787; DOI=10.1074/jbc.271.40.25041;
RA Ito T., Tyler J.K., Bulger M., Kobayashi R., Kadonaga J.T.;
RT "ATP-facilitated chromatin assembly with a nucleoplasmin-like protein from
RT Drosophila melanogaster.";
RL J. Biol. Chem. 271:25041-25048(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 116-148,
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=9087911; DOI=10.1006/jsbi.1996.3836;
RA Crevel G.L., Huikeshoven H., Cotterill S., Simon M., Wall J., Philpott A.,
RA Laskey R.A., McConnell M., Fisher P.A., Berrios M.;
RT "Molecular and cellular characterization of CRP1, a Drosophila chromatin
RT decondensation protein.";
RL J. Struct. Biol. 118:9-22(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-108, AND SUBUNIT.
RX PubMed=12575937; DOI=10.1016/s0969-2126(03)00007-8;
RA Namboodiri V.M., Dutta S., Akey I.V., Head J.F., Akey C.W.;
RT "The crystal structure of Drosophila NLP-core provides insight into
RT pentamer formation and histone binding.";
RL Structure 11:175-186(2003).
CC -!- FUNCTION: Binds to core histones and functions in the ATP-facilitated
CC assembly of approximately regularly spaced nucleosomal arrays. May
CC participate in parallel with other histone-binding proteins such as
CC NAP-1.
CC -!- FUNCTION: [Isoform 2]: Inactive for chromatin assembly. In vitro it
CC appears to form a high molecular mass aggregate with the core histones.
CC -!- SUBUNIT: Decamer formed by two pentameric rings associated in a head-
CC to-head fashion. {ECO:0000269|PubMed:12575937}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8798787,
CC ECO:0000269|PubMed:9087911}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long, DNLP;
CC IsoId=Q27415-1; Sequence=Displayed;
CC Name=2; Synonyms=Short, DNLP-S;
CC IsoId=Q27415-2; Sequence=VSP_003618;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically, present
CC throughout development. Highest levels are found during oogenesis and
CC in early embryos. {ECO:0000269|PubMed:8798787,
CC ECO:0000269|PubMed:9087911}.
CC -!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
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DR EMBL; U59497; AAC47294.1; -; mRNA.
DR EMBL; U59498; AAC47295.1; -; mRNA.
DR EMBL; X99293; CAA67679.1; -; mRNA.
DR EMBL; AE014297; AAF56988.1; -; Genomic_DNA.
DR EMBL; AY119592; AAM50246.1; -; mRNA.
DR RefSeq; NP_001263094.1; NM_001276165.1. [Q27415-1]
DR RefSeq; NP_524557.1; NM_079833.2. [Q27415-1]
DR PDB; 1NLQ; X-ray; 1.50 A; A/B/C/D/E=1-108.
DR PDBsum; 1NLQ; -.
DR AlphaFoldDB; Q27415; -.
DR SMR; Q27415; -.
DR BioGRID; 68416; 91.
DR DIP; DIP-21663N; -.
DR IntAct; Q27415; 7.
DR STRING; 7227.FBpp0084918; -.
DR iPTMnet; Q27415; -.
DR PaxDb; Q27415; -.
DR PRIDE; Q27415; -.
DR DNASU; 43560; -.
DR EnsemblMetazoa; FBtr0085552; FBpp0084918; FBgn0016685. [Q27415-1]
DR EnsemblMetazoa; FBtr0334701; FBpp0306756; FBgn0016685. [Q27415-1]
DR GeneID; 43560; -.
DR KEGG; dme:Dmel_CG7917; -.
DR CTD; 43560; -.
DR FlyBase; FBgn0016685; Nlp.
DR VEuPathDB; VectorBase:FBgn0016685; -.
DR eggNOG; ENOG502S1E6; Eukaryota.
DR GeneTree; ENSGT00730000113508; -.
DR HOGENOM; CLU_097031_1_0_1; -.
DR InParanoid; Q27415; -.
DR OMA; TEDYFWG; -.
DR PhylomeDB; Q27415; -.
DR Reactome; R-DME-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-DME-8869496; TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation.
DR BioGRID-ORCS; 43560; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Nlp; fly.
DR EvolutionaryTrace; Q27415; -.
DR GenomeRNAi; 43560; -.
DR PRO; PR:Q27415; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0016685; Expressed in eye disc (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q27415; baseline and differential.
DR Genevisible; Q27415; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IDA:FlyBase.
DR GO; GO:0035041; P:sperm DNA decondensation; IDA:FlyBase.
DR InterPro; IPR004301; Nucleoplasmin.
DR InterPro; IPR024057; Nucleoplasmin_core_dom.
DR InterPro; IPR036824; Nucleoplasmin_core_dom_sf.
DR PANTHER; PTHR22747; PTHR22747; 1.
DR Pfam; PF03066; Nucleoplasmin; 1.
DR SUPFAM; SSF69203; SSF69203; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing; Nucleus;
KW Reference proteome.
FT CHAIN 1..152
FT /note="Nucleoplasmin-like protein"
FT /id="PRO_0000219493"
FT REGION 109..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..126
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 45
FT /note="Interaction between pentamers"
FT /evidence="ECO:0000305"
FT SITE 68
FT /note="Interaction between pentamers"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..32
FT /note="MAEESFYGVTLTAESDSVTWDVDEDYARGQKL -> M (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:8798787"
FT /id="VSP_003618"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:1NLQ"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1NLQ"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:1NLQ"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1NLQ"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1NLQ"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:1NLQ"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1NLQ"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1NLQ"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:1NLQ"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1NLQ"
SQ SEQUENCE 152 AA; 16996 MW; 324CF99C17AF3CDE CRC64;
MAEESFYGVT LTAESDSVTW DVDEDYARGQ KLVIKQILLG AEAKENEFNV VEVNTPKDSV
QIPIAVLKAG ETRAVNPDVE FYESKVTFKL IKGSGPVYIH GHNIKDDVEV VDMEEDDEED
DVAEDEEDEH PKKRAKIENA ADGKNAKNNK KK
