NU160_DROME
ID NU160_DROME Reviewed; 1411 AA.
AC Q9VKJ3; C0KG65; C0KG66; C0KG67; C0KG68; C0KG69; C0KG70; C0KG71; C0KG74;
AC C0KG75; Q6AWI7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Nuclear pore complex protein Nup160 homolog;
DE AltName: Full=Nuclear pore protein 160;
GN Name=Nup160; ORFNames=CG4738;
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 [GENOMIC DNA], FUNCTION, IDENTIFICATION IN THE NUCLEAR
RP PORE COMPLEX, INTERACTION WITH NUP98, SUBCELLULAR LOCATION, AND VARIANTS
RP LYS-57; LEU-86; LEU-127; SER-137; ALA-165; GLN-202; ALA-204; ALA-281;
RP ILE-730 AND GLU-1408.
RC STRAIN=s125, s131, s145, s159, s178, s189, s191, s196, s81, s82, s84, and
RC s95;
RX PubMed=19197064; DOI=10.1126/science.1169123;
RA Tang S., Presgraves D.C.;
RT "Evolution of the Drosophila nuclear pore complex results in multiple
RT hybrid incompatibilities.";
RL Science 323:779-782(2009).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=20547758; DOI=10.1128/mcb.00124-10;
RA Chen X., Xu L.;
RT "Specific nucleoporin requirement for Smad nuclear translocation.";
RL Mol. Cell. Biol. 30:4022-4034(2010).
RN [6]
RP FUNCTION.
RX PubMed=26502056; DOI=10.1038/ncb3258;
RA Ryu T., Spatola B., Delabaere L., Bowlin K., Hopp H., Kunitake R.,
RA Karpen G.H., Chiolo I.;
RT "Heterochromatic breaks move to the nuclear periphery to continue
RT recombinational repair.";
RL Nat. Cell Biol. 17:1401-1411(2015).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30910934; DOI=10.1681/asn.2018080786;
RA Zhao F., Zhu J.Y., Richman A., Fu Y., Huang W., Chen N., Pan X., Yi C.,
RA Ding X., Wang S., Wang P., Nie X., Huang J., Yang Y., Yu Z., Han Z.;
RT "Mutations in NUP160 Are Implicated in Steroid-Resistant Nephrotic
RT Syndrome.";
RL J. Am. Soc. Nephrol. 30:840-853(2019).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC)
CC (PubMed:19197064). Involved in poly(A)+ RNA transport (By similarity).
CC Required for nuclear import of Mad (PubMed:20547758). May play a role
CC in double strand break DNA repair (PubMed:26502056). Essential for
CC nephrocyte development (PubMed:30910934).
CC {ECO:0000250|UniProtKB:Q12769, ECO:0000269|PubMed:19197064,
CC ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:26502056,
CC ECO:0000269|PubMed:30910934}.
CC -!- SUBUNIT: Part of the nuclear pore complex (PubMed:19197064). Interacts
CC with Nup98 (PubMed:19197064). {ECO:0000269|PubMed:19197064}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:19197064}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in nephrocytes alters
CC their cell morphology and function (PubMed:30910934). Reduces total
CC number of nephrocytes starting from larval stage and results in
CC shortened lifespan (PubMed:30910934). {ECO:0000269|PubMed:30910934}.
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DR EMBL; FJ600378; ACM79337.1; -; Genomic_DNA.
DR EMBL; FJ600379; ACM79338.1; -; Genomic_DNA.
DR EMBL; FJ600380; ACM79339.1; -; Genomic_DNA.
DR EMBL; FJ600381; ACM79340.1; -; Genomic_DNA.
DR EMBL; FJ600382; ACM79341.1; -; Genomic_DNA.
DR EMBL; FJ600383; ACM79342.1; -; Genomic_DNA.
DR EMBL; FJ600384; ACM79343.1; -; Genomic_DNA.
DR EMBL; FJ600385; ACM79344.1; -; Genomic_DNA.
DR EMBL; FJ600386; ACM79345.1; -; Genomic_DNA.
DR EMBL; FJ600387; ACM79346.1; -; Genomic_DNA.
DR EMBL; FJ600388; ACM79347.1; -; Genomic_DNA.
DR EMBL; FJ600389; ACM79348.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53075.1; -; Genomic_DNA.
DR EMBL; BT015261; AAT94490.1; -; mRNA.
DR RefSeq; NP_001285832.1; NM_001298903.1.
DR RefSeq; NP_609493.1; NM_135649.2.
DR AlphaFoldDB; Q9VKJ3; -.
DR SMR; Q9VKJ3; -.
DR BioGRID; 60611; 2.
DR IntAct; Q9VKJ3; 1.
DR STRING; 7227.FBpp0079788; -.
DR PaxDb; Q9VKJ3; -.
DR PRIDE; Q9VKJ3; -.
DR DNASU; 34549; -.
DR EnsemblMetazoa; FBtr0080199; FBpp0079788; FBgn0262647.
DR EnsemblMetazoa; FBtr0343613; FBpp0310208; FBgn0262647.
DR GeneID; 34549; -.
DR KEGG; dme:Dmel_CG4738; -.
DR UCSC; CG4738-RA; d. melanogaster.
DR CTD; 23279; -.
DR FlyBase; FBgn0262647; Nup160.
DR VEuPathDB; VectorBase:FBgn0262647; -.
DR eggNOG; KOG4521; Eukaryota.
DR HOGENOM; CLU_005083_0_0_1; -.
DR InParanoid; Q9VKJ3; -.
DR OMA; CQFDQAY; -.
DR OrthoDB; 284127at2759; -.
DR PhylomeDB; Q9VKJ3; -.
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 Reactome; R-DME-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR SignaLink; Q9VKJ3; -.
DR BioGRID-ORCS; 34549; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 34549; -.
DR PRO; PR:Q9VKJ3; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0262647; Expressed in oviduct (Drosophila) and 18 other tissues.
DR ExpressionAtlas; Q9VKJ3; baseline and differential.
DR Genevisible; Q9VKJ3; DM.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0031080; C:nuclear pore outer ring; ISS:FlyBase.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISS:FlyBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:FlyBase.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:FlyBase.
DR GO; GO:0006606; P:protein import into nucleus; IMP:FlyBase.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:FlyBase.
DR InterPro; IPR021717; Nucleoporin_Nup160.
DR PANTHER; PTHR21286; PTHR21286; 1.
PE 1: Evidence at protein level;
KW DNA damage; mRNA transport; Nuclear pore complex; Nucleus;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..1411
FT /note="Nuclear pore complex protein Nup160 homolog"
FT /id="PRO_0000204850"
FT VARIANT 57
FT /note="N -> K (in strain: s81 and s196)"
FT /evidence="ECO:0000269|PubMed:19197064"
FT VARIANT 86
FT /note="Q -> L (in strain: s82 and s84)"
FT /evidence="ECO:0000269|PubMed:19197064"
FT VARIANT 127
FT /note="P -> L (in strain: s82)"
FT /evidence="ECO:0000269|PubMed:19197064"
FT VARIANT 137
FT /note="A -> S (in strain: s131)"
FT /evidence="ECO:0000269|PubMed:19197064"
FT VARIANT 165
FT /note="T -> A (in strain: s95)"
FT /evidence="ECO:0000269|PubMed:19197064"
FT VARIANT 202
FT /note="K -> Q (in strain: s95)"
FT /evidence="ECO:0000269|PubMed:19197064"
FT VARIANT 204
FT /note="S -> A (in strain: s81, s95, s125, s131 and s196)"
FT /evidence="ECO:0000269|PubMed:19197064"
FT VARIANT 281
FT /note="T -> A (in strain: s81 and s196)"
FT /evidence="ECO:0000269|PubMed:19197064"
FT VARIANT 730
FT /note="T -> I (in strain: s189)"
FT /evidence="ECO:0000269|PubMed:19197064"
FT VARIANT 1408
FT /note="Q -> E (in strain: s191)"
FT /evidence="ECO:0000269|PubMed:19197064"
SQ SEQUENCE 1411 AA; 160276 MW; AB0C312222691848 CRC64;
MPTSKLQANM SYREVIPRNL SPAEWIEVKI NTGTQSTLQD LKTFETSGGY CYKNTKNVQT
RNRFIYWRTY QDVLELSEVS LDISLQRNHL RLRFTDSAVL NVSLTEQGTS VTLLVVTVSS
VHRYVFPLKV AGQEGGAASP EDLLSQSIFY DVNDKINDPS TYYVTDGFGT MPNAAVSYLT
QDSQSAYFAV AYQSKLLLHV MKCSTGHTIT HEIKEPKLMP WFLSNLKGAL TGRSETLEAA
TSMAFSEIGG EIFILVLYRN NELRLWSVDN LQTVASINCS TELGQDSAAQ GPQNSQLRKI
SDQNFCLFLS HNSRAEFICV SIMPDADDAS VINLVQNMVP APQTDLVDFD ATSSHIWALW
SNAEGDFHVS AAYFASNNAI KWVSAALEPP PDRYCLTMEQ GVDPRETYCS YIFHPGRFDR
NVIAKALYMF RRVNLQFDVK QLSMSVLKEQ VCQAVEDEIQ NELKDFVVTD EEYLEISTRL
WDRFYSCCEQ YHIKLSEPTG LAVLGGMDAV CLVRRQSFAL LRPCEVLEHL LLIGEHNDEV
ATYVAPLFRN DPEMAKGFVE LMNVVTLLDK LISEDIKIEL DKQLYQRESP VEVISKLVAR
ISMIDDNGPI LPSNCVRQIQ QKLQNIPNLE PALEMLLDVL CMIDPDEPPH DYSLSTRFLQ
SSGALMGSEY GLSILSETVK QMAMIRFSVC RNLLVLQYMA YGQNEMESEN VLTNLNYLNS
YYTLVWIAET PISSSTPAGF EASIQRLSRA QLFSGYNRPY SSHLKHNGND QTTLLRLFLE
SKGLFSALTM LLKHDSLSLD SEQLNLRQSL LQLVGYINKM LWPGSPIYVF PEWLFGTCHH
IIVQDYVRIL SNWCSVQKHA RRFMLAVSLL DCGEAHKAVH LFHEAESGIV EDDFLFEHVL
KNTPLYGKLQ NSVSRGDTIS PEDTKLAIVH YYLKVIQLFE QHSALDYIIQ LADMAIRVLQ
PDDPQLPMFQ SIVFNNHLQL GHYVEAYTAL VNNADISRRK DCLRQLVITL FQNKCLPLLM
QFSYIGLQDE FESIVESRAR SMSIDQNEVY NFLYAFHTNK GNMRKASTVM YEQAMRFQVD
SDAPNALEKR CSSLLICLNC LHLVDSRYRW IAKPVLGDEQ VITIDQDNDD GEPKCDEDKR
GQEVVVLELA DIRRELVHAE ALRELSFYRK DTAAYERATP EELSYLLASS GLYTAALKLS
RGHSFSVLPI FESLTSACVA ATEDKSSDAW NWLQNNDMAD LPHRSNAADM AWTLLQKLVV
DNEAKDSTLI RKSVVQRLLG LNAFLPQWLI NSYKLSHSRE LLHLLVKHNR LLEAADLGCE
IIAGMLGAGS EYFEFKHAVN IANPQLCFPI STIDLLLHGL KINGKDDLDY EMAYFKLEEE
VQRYIETIKR TTDDKMSMAV LQMRTDLQEE R
