PO210_DROME
ID PO210_DROME Reviewed; 1876 AA.
AC A1Z6H7; Q6NP18; Q9GPI0;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Nuclear pore membrane glycoprotein 210 {ECO:0000305};
DE Short=Nuclear pore protein gp210 {ECO:0000305};
DE AltName: Full=Glycoprotein 210 kDa {ECO:0000303|PubMed:7641726, ECO:0000312|FlyBase:FBgn0266580};
DE AltName: Full=Nuclear pore membrane glycoprotein gp188 {ECO:0000303|PubMed:2517292, ECO:0000312|FlyBase:FBgn0266580};
DE AltName: Full=Nucleoporin Nup210 {ECO:0000305};
DE Short=Nup210 {ECO:0000305};
DE Flags: Precursor;
GN Name=Gp210 {ECO:0000312|FlyBase:FBgn0266580};
GN Synonyms=Gp188 {ECO:0000303|PubMed:2517292,
GN ECO:0000312|FlyBase:FBgn0266580}, lyadi {ECO:0000312|FlyBase:FBgn0266580};
GN ORFNames=CG7897 {ECO:0000312|FlyBase:FBgn0266580};
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:AAR82780.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAR82780.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAR82780.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAG42828.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-1876.
RA Cohen M., Gruenbaum Y.;
RT "Drosophila melanogaster integral membrane glycoprotein gp210.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RX PubMed=3919018; DOI=10.1016/s0021-9258(18)89487-x;
RA Filson A.J., Lewis A., Blobel G., Fisher P.A.;
RT "Monoclonal antibodies prepared against the major Drosophila nuclear
RT Matrix-pore complex-lamina glycoprotein bind specifically to the nuclear
RT envelope in situ.";
RL J. Biol. Chem. 260:3164-3172(1985).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=2517292; DOI=10.1242/jcs.94.3.463;
RA Harel A., Zlotkin E., Nainudel-Epszteyn S., Feinstein N., Fisher P.A.,
RA Gruenbaum Y.;
RT "Persistence of major nuclear envelope antigens in an envelope-like
RT structure during mitosis in Drosophila melanogaster embryos.";
RL J. Cell Sci. 94:463-470(1989).
RN [7] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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 [8] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17682050; DOI=10.1083/jcb.200612135;
RA Sabri N., Roth P., Xylourgidis N., Sadeghifar F., Adler J., Samakovlis C.;
RT "Distinct functions of the Drosophila Nup153 and Nup214 FG domains in
RT nuclear protein transport.";
RL J. Cell Biol. 178:557-565(2007).
CC -!- FUNCTION: Component of the nuclear pore complex.
CC {ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:7641726}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:2517292,
CC ECO:0000269|PubMed:3919018}; Single-pass type I membrane protein
CC {ECO:0000255}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:7641726}. Cytoplasm
CC {ECO:0000269|PubMed:2517292}. Note=During mitosis diffusively localized
CC throughout the cytoplasm. {ECO:0000269|PubMed:2517292}.
CC -!- TISSUE SPECIFICITY: Expressed in adult male accessory glands (at
CC protein level). {ECO:0000269|PubMed:7641726}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos and third instar larvae (at
CC protein level) (PubMed:3919018, PubMed:2517292, PubMed:7641726). Levels
CC are highest during embryogenesis, decrease through larval stages, and
CC finally increase during pupation and adult stages (PubMed:7641726).
CC {ECO:0000269|PubMed:2517292, ECO:0000269|PubMed:3919018,
CC ECO:0000269|PubMed:7641726}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:3919018}.
CC -!- SIMILARITY: Belongs to the NUP210 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG42828.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAR82780.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF57309.2; -; Genomic_DNA.
DR EMBL; AE013599; AGB93249.1; -; Genomic_DNA.
DR EMBL; BT011113; AAR82780.1; ALT_INIT; mRNA.
DR EMBL; AF322889; AAG42828.1; ALT_INIT; mRNA.
DR RefSeq; NP_001260714.1; NM_001273785.1.
DR RefSeq; NP_610184.2; NM_136340.3.
DR AlphaFoldDB; A1Z6H7; -.
DR IntAct; A1Z6H7; 5.
DR MINT; A1Z6H7; -.
DR STRING; 7227.FBpp0085380; -.
DR GlyGen; A1Z6H7; 7 sites.
DR SwissPalm; A1Z6H7; -.
DR PaxDb; A1Z6H7; -.
DR PRIDE; A1Z6H7; -.
DR DNASU; 35512; -.
DR EnsemblMetazoa; FBtr0086044; FBpp0085380; FBgn0266580.
DR EnsemblMetazoa; FBtr0335270; FBpp0307249; FBgn0266580.
DR GeneID; 35512; -.
DR KEGG; dme:Dmel_CG7897; -.
DR UCSC; CG7897-RA; d. melanogaster.
DR CTD; 35512; -.
DR FlyBase; FBgn0266580; Gp210.
DR VEuPathDB; VectorBase:FBgn0266580; -.
DR eggNOG; KOG1833; Eukaryota.
DR GeneTree; ENSGT00390000009491; -.
DR HOGENOM; CLU_001205_1_1_1; -.
DR InParanoid; A1Z6H7; -.
DR OMA; YVCIIKV; -.
DR OrthoDB; 843414at2759; -.
DR PhylomeDB; A1Z6H7; -.
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; 35512; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 35512; -.
DR PRO; PR:A1Z6H7; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0266580; Expressed in eye disc (Drosophila) and 22 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0044611; C:nuclear pore inner ring; IDA:FlyBase.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:FlyBase.
DR GO; GO:0070762; C:nuclear pore transmembrane ring; ISS:FlyBase.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006999; P:nuclear pore organization; ISS:FlyBase.
DR GO; GO:0006606; P:protein import into nucleus; ISS:FlyBase.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR045197; NUP210-like.
DR PANTHER; PTHR23019; PTHR23019; 1.
DR SUPFAM; SSF49373; SSF49373; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycoprotein; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Protein transport; Reference proteome; Signal; Translocation;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1876
FT /note="Nuclear pore membrane glycoprotein 210"
FT /evidence="ECO:0000255"
FT /id="PRO_5015085938"
FT TOPO_DOM 21..1775
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT TRANSMEM 1776..1796
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1797..1876
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1819..1876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1819..1837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1859..1876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 183
FT /note="P -> A (in Ref. 4; AAG42828)"
FT /evidence="ECO:0000305"
FT CONFLICT 1177
FT /note="A -> G (in Ref. 4; AAG42828)"
FT /evidence="ECO:0000305"
FT CONFLICT 1379
FT /note="D -> A (in Ref. 4; AAG42828)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1876 AA; 209792 MW; 97E4D27E759A2E6F CRC64;
MDSILCMILL ILVRNHASEA ARLNHPRVLL PIFEDKAINF TLEVDEPNCY KWSSSRQDLI
SVMPIYKGFS ECAYQAVVTV RTHDRRRNTA IVFAEEVQTG ETLRSDVIVD VIASLNVRTA
TRQLYLEEAP AMFELHAFDE QGNEFFTLEG IEFDWEILEP GSKRPTAMRY LTFTDSPYHT
VPPTIEKFEA DGKKGHMILL EGINTGTAKV TIAMPQAEYK HVRPVEVYIS VLANIIIEPS
EVTIMAGDSV SFRILQLKMD RLHVIDNNQY YLEVEDSSIA YLRGNSATGA ALGRTQVFLR
DRNMADSDEV QKGPSALLTV AYPNRLSISL LPHLNWVTVQ GEHHAIALDL FAADGQKITM
GTKYSINSEV DESFFAIVDR TRNGSRLFGQ AKKEGITQVY GSYKDLSVQA ELQIFEELQL
APTKVVLPYD PNSLKPLKLQ FHASGGDNNY AWFSGNPQVI QIDTQGQATT EIRDVKSAYV
NQEVLKDGGK LTAHTTVKVA LSKNQKISRV AHIYFLPPER LQITRSNFET ALKDFVHVHV
GVYARINNSE VPYTSCDNLH FQLDFSQPIL QLEGNEGAEA AHEACHVLRL RATAVGTTSL
RVSYMYMDKV LYDIIDLYVF EPLVVLNPIE NEVVLPVGSS RNIIYANGPQ RSFTVAAEII
QSTAFDEKIL KVSKLEFDTQ NLITAFTVLC RELGETQFTY RVHNSLPTSS FALYQSEVTT
KVHCVRPRFL KLYARHNLRD SCPLEKRTSL LFLKDPENKI EIEIEVHDSN NRRLMNISSL
GLDWEFSAGE ERYQKNIIPH RQISELEFNH GVTLPSRDLL VLTLSEVATN FRIKGTVSQY
NDKLLAQHGI HAERPPFGIK NPQTGLIYTP LIENEIRLHA VNSTLLPKDY MSIFLASGYS
ERIPIAQGSG YLQLELSEAG IVQVEYNENT RILVLTPLRL GHVRLELTDR CLMNEPSHLS
ISVVGIGAIE VVSMDRLERT TRIEAIVRLF DTNDNLLLVD QSKLSAYDLS EVVADQSILS
VRLGEQENVG PGEIRYTITG NQVGETKILF QSGKGIYKVA SDPLNIQVFA PIRLFPRDST
LVVGSSIQVY FHGGPHPNTN MIISVEKEQV ATISSTVVTA HKLGTTKIVG KCLLKNPVTG
KDEVVSQDSV EVHVVALKGV QIRTPLVRIH SGAVMPATLW GLSDLSPMIL GTLQNTKISW
KVSQPQVVEI FNVFTTAGIE YQSGDLISVR VRALNPGKAT ITASVTLADG TILPPATVDL
QVFKTLELVT PNAIKMDSIL AAPRSILQLK SNMDNVVYKL DDRSNGIVSV TPDGLVHTKD
SLGRDLIIAT TADQSLPIGI EVKNVQYILV TLMPILKLRE LEHKIPRGMN FVFKVSLHDN
LGNELSHNIE DFNGLRYELG NKDDVDVQID NNLTFALNLM RETNNVIGIS LKDSTGVKHS
MDFIKLSVVE SDNLFPTKTI FSVGDIICFD SPLTLSSTWR SSNEQIVYIN KHTGIAQVLS
HRLKPGEKIE ITNGDETKRG GFLKYDLEVR ESDTILFVKS VDTFSGPEYR GQLVIRNHLQ
SEKYSNLIAQ NVSKCARELG SVPVNFFTCR LAAKDALGRN LLKMYKVDAL FEPSIGQYSC
RLQLLTGFIE LLSIVKTHDV YLELEAVVAK GVSDKMSLKL VPGIKVFPES VRVTDLKPHE
IHISGLDKAL LKVQVKPSDS KYFAVDFIEH GHGLSKYRLE LFDDLPLDEN FYILVVSPDT
KQSIEVPIIG NTMLAPKCTD RRYGGPLVYR ILENLGFVLT TTVIVIISIW VYMSCFQTQG
VTQVNFEAFK KGKSRTELMQ QSGRSSQDDT FGDSFNVRNF SPDRRRPPSN ALSESYIYGH
PRLNSSNRSE NSTSFS
