NUP62_DROME
ID NUP62_DROME Reviewed; 394 AA.
AC Q7JXF5;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Nuclear pore glycoprotein p62 {ECO:0000305};
DE AltName: Full=62 kDa nucleoporin {ECO:0000312|FlyBase:FBgn0034118};
GN Name=Nup62 {ECO:0000312|FlyBase:FBgn0034118};
GN ORFNames=CG6251 {ECO:0000312|FlyBase:FBgn0034118};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAM11060.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM11060.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAM11060.1};
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 [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=7641726;
RA Berrios M., Meller V.H., McConnell M., Fisher P.A.;
RT "Drosophila gp210, an invertebrate nuclear pore complex glycoprotein.";
RL Eur. J. Cell Biol. 67:1-7(1995).
RN [5] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20144760; DOI=10.1016/j.cell.2010.01.011;
RA Kalverda B., Pickersgill H., Shloma V.V., Fornerod M.;
RT "Nucleoporins directly stimulate expression of developmental and cell-cycle
RT genes inside the nucleoplasm.";
RL Cell 140:360-371(2010).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26341556; DOI=10.1101/gad.264341.115;
RA Breuer M., Ohkura H.;
RT "A negative loop within the nuclear pore complex controls global chromatin
RT organization.";
RL Genes Dev. 29:1789-1794(2015).
CC -!- FUNCTION: Essential component of the nuclear pore complex (By
CC similarity). The N-terminal is probably involved in nucleocytoplasmic
CC transport (By similarity). The C-terminal is involved in protein-
CC protein interaction probably via coiled-coil formation, promotes its
CC association with centrosomes and may function in anchorage of Nup62 to
CC the pore complex (By similarity). Binds to transcriptionally active
CC genes (PubMed:20144760). Negatively regulates chromatin attachment to
CC the nuclear envelope, probably by preventing chromatin tethering by
CC Nup154 (PubMed:26341556). {ECO:0000250|UniProtKB:P37198,
CC ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:26341556}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20144760,
CC ECO:0000269|PubMed:26341556}. Chromosome {ECO:0000269|PubMed:20144760}.
CC Nucleus envelope {ECO:0000269|PubMed:26341556}. Nucleus, nuclear pore
CC complex {ECO:0000269|PubMed:7641726}. Cytoplasm, cytoskeleton, spindle
CC pole {ECO:0000250|UniProtKB:P37198}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P37198}. Note=Central region of the nuclear
CC pore, within the transporter (By similarity). Associates with chromatin
CC (PubMed:20144760). {ECO:0000250|UniProtKB:P37198,
CC ECO:0000269|PubMed:20144760}.
CC -!- TISSUE SPECIFICITY: Expressed in adult male accessory glands (at
CC protein level). {ECO:0000269|PubMed:7641726}.
CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC karyopherins (importins, exportins) and form probably an affinity
CC gradient, guiding the transport proteins unidirectionally with their
CC cargo through the NPC. FG repeat regions are highly flexible and lack
CC ordered secondary structure. The overall conservation of FG repeats
CC regarding exact sequence, spacing, and repeat unit length is limited.
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in oocytes results in
CC increased nuclear size. RNAi-mediated knockdown in oocytes and nurse
CC cells results in irregular distribution of chromatin to the nuclear
CC periphery disrupting karyosome morphology. Simultaneous RNAi-mediated
CC knockdown of nucleoporin Nup154 restores normal karyosome formation.
CC {ECO:0000269|PubMed:26341556}.
CC -!- SIMILARITY: Belongs to the nucleoporin NSP1/NUP62 family.
CC {ECO:0000305}.
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DR EMBL; AE013599; AAF58007.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56285.1; -; Genomic_DNA.
DR EMBL; AY094707; AAM11060.1; -; mRNA.
DR RefSeq; NP_001286489.1; NM_001299560.1.
DR RefSeq; NP_611120.1; NM_137276.2.
DR AlphaFoldDB; Q7JXF5; -.
DR SMR; Q7JXF5; -.
DR IntAct; Q7JXF5; 7.
DR MINT; Q7JXF5; -.
DR STRING; 7227.FBpp0086294; -.
DR PaxDb; Q7JXF5; -.
DR PRIDE; Q7JXF5; -.
DR DNASU; 36830; -.
DR EnsemblMetazoa; FBtr0087150; FBpp0086294; FBgn0034118.
DR EnsemblMetazoa; FBtr0340060; FBpp0309066; FBgn0034118.
DR GeneID; 36830; -.
DR KEGG; dme:Dmel_CG6251; -.
DR UCSC; CG6251-RA; d. melanogaster.
DR CTD; 23636; -.
DR FlyBase; FBgn0034118; Nup62.
DR VEuPathDB; VectorBase:FBgn0034118; -.
DR eggNOG; KOG2196; Eukaryota.
DR GeneTree; ENSGT00940000167119; -.
DR HOGENOM; CLU_025936_0_0_1; -.
DR InParanoid; Q7JXF5; -.
DR OMA; EMMSKQV; -.
DR OrthoDB; 1145183at2759; -.
DR PhylomeDB; Q7JXF5; -.
DR Reactome; R-DME-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-DME-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-DME-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DME-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DME-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-DME-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DME-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR BioGRID-ORCS; 36830; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36830; -.
DR PRO; PR:Q7JXF5; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034118; Expressed in egg cell and 37 other tissues.
DR GO; GO:0000785; C:chromatin; IMP:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0044613; C:nuclear pore central transport channel; ISS:FlyBase.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0031490; F:chromatin DNA binding; IMP:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISS:FlyBase.
DR GO; GO:0097240; P:chromosome attachment to the nuclear envelope; IMP:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0030717; P:oocyte karyosome formation; IMP:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0097298; P:regulation of nucleus size; IMP:UniProtKB.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR InterPro; IPR026010; NSP1/NUP62.
DR InterPro; IPR007758; Nucleoporin_NSP1_C.
DR PANTHER; PTHR12084; PTHR12084; 1.
DR Pfam; PF05064; Nsp1_C; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; Cytoplasm; Cytoskeleton; mRNA transport;
KW Nuclear pore complex; Nucleus; Protein transport; Reference proteome;
KW Repeat; Translocation; Transport.
FT CHAIN 1..394
FT /note="Nuclear pore glycoprotein p62"
FT /id="PRO_0000439767"
FT REPEAT 22..23
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 50..51
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 75..76
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 77..78
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 116..117
FT /note="5"
FT /evidence="ECO:0000305"
FT REGION 22..117
FT /note="5 X 2 AA repeats of F-G"
FT /evidence="ECO:0000305"
FT REGION 44..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 211..341
FT /evidence="ECO:0000255"
SQ SEQUENCE 394 AA; 40684 MW; 6D3C1E3A149ECCE6 CRC64;
MVFQLPTTTA APTGGATSSF SFGLSTGTPA AAPASGAATT APATKTTFSF GTPAPTAGIG
GGDADNSKAQ APPAFGFGLG SGTASAPLTL GTQAAANPAS TTSATATGTS AAPPAFGGFT
AQPAASVVPT IATSAPNTAA TTTGLLGGSG LGAPKTTAAA STTLTAAPSA IASTQGAAPA
PTLSTGGAFA NLTTETKTTD SSAVSTASQL SYHQLEEHIN KWTLEFEEQE KVFTEQATQI
NAWDKLLISN NGKIVELNDA VKKVKTDQQV LDQELEFIAT QQKELEDSLG PLEKEFVNLP
RVDMERSQTY LMVENLDTQL KQMSEDLKEI IDNLNEANKG QDTTDPIIQI GKILNAHMNS
LQWIESQSTN ISKKLEDIGK IQDSQKRDIF RAPF
