NPL4_DROME
ID NPL4_DROME Reviewed; 652 AA.
AC Q9VBP9; C9QPJ1; E1JIX5; H8F4R9; Q8IMS6; Q95U63;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Nuclear protein localization protein 4 homolog;
GN Name=Npl4; ORFNames=CG4673;
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 [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 [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Booth B., Carlson J.W., Frise E., Kapadia B., Park S.,
RA Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION.
RX PubMed=15899868; DOI=10.1128/mcb.25.11.4662-4675.2005;
RA Lundgren J., Masson P., Mirzaei Z., Young P.;
RT "Identification and characterization of a Drosophila proteasome regulatory
RT network.";
RL Mol. Cell. Biol. 25:4662-4675(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115 AND SER-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-114; SER-115 AND THR-117, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 35-105 IN COMPLEX WITH TER94, AND
RP INTERACTION WITH TER94.
RX PubMed=26471729; DOI=10.15252/embj.201591888;
RA Hao Q., Jiao S., Shi Z., Li C., Meng X., Zhang Z., Wang Y., Song X.,
RA Wang W., Zhang R., Zhao Y., Wong C.C., Zhou Z.;
RT "A non-canonical role of the p97 complex in RIG-I antiviral signaling.";
RL EMBO J. 34:2903-2920(2015).
CC -!- FUNCTION: May be part of a complex that binds ubiquitinated proteins
CC and that is necessary for the export of misfolded proteins from the ER
CC to the cytoplasm, where they are degraded by the proteasome.
CC {ECO:0000250}.
CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway.
CC -!- SUBUNIT: Interacts with TER94. {ECO:0000269|PubMed:26471729}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9VBP9-1; Sequence=Displayed;
CC Name=B; Synonyms=D;
CC IsoId=Q9VBP9-2; Sequence=VSP_037209;
CC -!- SIMILARITY: Belongs to the NPL4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACX70078.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AFD10756.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF56480.3; -; Genomic_DNA.
DR EMBL; AE014297; AAN14058.2; -; Genomic_DNA.
DR EMBL; AE014297; ACZ95025.1; -; Genomic_DNA.
DR EMBL; AY058286; AAL13515.1; -; mRNA.
DR EMBL; BT100105; ACX70078.1; ALT_INIT; mRNA.
DR EMBL; BT133309; AFD10756.1; ALT_INIT; mRNA.
DR RefSeq; NP_001163731.1; NM_001170260.2. [Q9VBP9-2]
DR RefSeq; NP_651407.3; NM_143150.4. [Q9VBP9-1]
DR RefSeq; NP_733110.2; NM_170231.3. [Q9VBP9-2]
DR PDB; 4RV0; X-ray; 2.00 A; B/D/F/H=35-105.
DR PDBsum; 4RV0; -.
DR AlphaFoldDB; Q9VBP9; -.
DR SMR; Q9VBP9; -.
DR BioGRID; 68004; 24.
DR IntAct; Q9VBP9; 21.
DR STRING; 7227.FBpp0084267; -.
DR iPTMnet; Q9VBP9; -.
DR PaxDb; Q9VBP9; -.
DR PRIDE; Q9VBP9; -.
DR DNASU; 43091; -.
DR EnsemblMetazoa; FBtr0084892; FBpp0084266; FBgn0039348. [Q9VBP9-2]
DR EnsemblMetazoa; FBtr0084893; FBpp0084267; FBgn0039348. [Q9VBP9-1]
DR EnsemblMetazoa; FBtr0300730; FBpp0289954; FBgn0039348. [Q9VBP9-2]
DR GeneID; 43091; -.
DR KEGG; dme:Dmel_CG4673; -.
DR UCSC; CG4673-RA; d. melanogaster. [Q9VBP9-1]
DR UCSC; CG4673-RB; d. melanogaster.
DR CTD; 43091; -.
DR FlyBase; FBgn0039348; Npl4.
DR VEuPathDB; VectorBase:FBgn0039348; -.
DR eggNOG; KOG2834; Eukaryota.
DR GeneTree; ENSGT00390000018731; -.
DR InParanoid; Q9VBP9; -.
DR OMA; KWSRTGR; -.
DR PhylomeDB; Q9VBP9; -.
DR Reactome; R-DME-110320; Translesion Synthesis by POLH.
DR Reactome; R-DME-8951664; Neddylation.
DR Reactome; R-DME-9755511; KEAP1-NFE2L2 pathway.
DR SignaLink; Q9VBP9; -.
DR UniPathway; UPA00144; -.
DR BioGRID-ORCS; 43091; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 43091; -.
DR PRO; PR:Q9VBP9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039348; Expressed in adult organism and 26 other tissues.
DR Genevisible; Q9VBP9; DM.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0071795; F:K11-linked polyubiquitin modification-dependent protein binding; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0098586; P:cellular response to virus; IMP:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR CDD; cd08061; MPN_NPL4; 1.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR016563; Npl4.
DR InterPro; IPR007717; NPL4_C.
DR InterPro; IPR024682; Npl4_Ub-like_dom.
DR InterPro; IPR007716; NPL4_Zn-bd_put.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR12710; PTHR12710; 1.
DR Pfam; PF05021; NPL4; 1.
DR Pfam; PF11543; UN_NPL4; 1.
DR Pfam; PF05020; zf-NPL4; 1.
DR PIRSF; PIRSF010052; Polyub_prc_Npl4; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS50249; MPN; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Metal-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..652
FT /note="Nuclear protein localization protein 4 homolog"
FT /id="PRO_0000372853"
FT DOMAIN 260..397
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT ZN_FING 625..652
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT MOD_RES 114
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT VAR_SEQ 1..34
FT /note="MACAPLLLEQFIYKKRNFAYAFVRHRLFVLCKQS -> MPNDKI (in
FT isoform B)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_037209"
FT CONFLICT 465
FT /note="L -> R (in Ref. 3; ACX70078)"
FT /evidence="ECO:0000305"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:4RV0"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:4RV0"
FT HELIX 55..65
FT /evidence="ECO:0007829|PDB:4RV0"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:4RV0"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:4RV0"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:4RV0"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:4RV0"
SQ SEQUENCE 652 AA; 73361 MW; B8D3B986EE19786A CRC64;
MACAPLLLEQ FIYKKRNFAY AFVRHRLFVL CKQSLIRVQS AEGIKRIEIS PKSNLKHLYD
SVQNALKVDG FGLFKERNFL TELQASGSQL VGTSLRHGDM VYLKQMAGTS SRRTSTTVLD
SQAFKTSTIS NPNSARPSFN VIEDDVDQAL SKADGTIKRE RDSKLCHHNA NGRCVHCSAL
EPYDESYLKE HNIKHLSFHS YIRKQTSGMD QGKYFVFDDI NCRIKPGCRE HPPWPKGICS
KCQPSAITLN RQTYRHVDNV MFENTKIVER FLNYWRTTGH QRMGYLYGTY EQHTDVPLGI
RAKVAAIYEP PQESTRDSIN IQPDEFADDV DAVASALGLK KIGWIFTDLI TDDASIGTVK
QIRGIESHFI TAQECITAGE LQNRHPNPCK YASNGVFGSK FVTICVTGDK TKQVHMEGYA
VSAQCMALVR DNCLIPTKDA PELGYVREST DKQYVPDVFY KEKDLYGNEV QRLARPLPVE
YLLVDVPAST PLQPIYTFTE YDKRQPFPIE NRYIDGHLQD FNALSCYLSA WGEEEFLEAI
SDFHLLVYLY KMDMLPLRQH MGPLLEAVRT KNPNQAAQFK VVDVWKLLES LIQASSGGSG
GTTSYPSGGA SASAGASGSE AMDLDANTWT CNHCTFINRG ELTSCEICSL PR
