NUP85_SCHPO
ID NUP85_SCHPO Reviewed; 675 AA.
AC Q9UUE5;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Nucleoporin nup85;
DE AltName: Full=Nuclear pore protein nup85;
GN Name=nup85; ORFNames=SPBC17G9.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP IDENTIFICATION IN NUP107-120 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=15226438; DOI=10.1128/mcb.24.14.6379-6392.2004;
RA Bai S.W., Rouquette J., Umeda M., Faigle W., Loew D., Sazer S., Doye V.;
RT "The fission yeast Nup107-120 complex functionally interacts with the small
RT GTPase Ran/Spi1 and is required for mRNA export, nuclear pore distribution,
RT and proper cell division.";
RL Mol. Cell. Biol. 24:6379-6392(2004).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15116432; DOI=10.1002/yea.1115;
RA Chen X.Q., Du X., Liu J., Balasubramanian M.K., Balasundaram D.;
RT "Identification of genes encoding putative nucleoporins and transport
RT factors in the fission yeast Schizosaccharomyces pombe: a deletion
RT analysis.";
RL Yeast 21:495-509(2004).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC).
CC NPC components, collectively referred to as nucleoporins (NUPs), can
CC play the role of both NPC structural components and of docking or
CC interaction partners for transiently associated nuclear transport
CC factors. Active directional transport is assured by both, a Phe-Gly
CC (FG) repeat affinity gradient for these transport factors across the
CC NPC and a transport cofactor concentration gradient across the nuclear
CC envelope. {ECO:0000269|PubMed:15116432}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). NPC constitutes
CC the exclusive means of nucleocytoplasmic transport. NPCs allow the
CC passive diffusion of ions and small molecules and the active, nuclear
CC transport receptor-mediated bidirectional transport of macromolecules
CC such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal
CC subunits across the nuclear envelope. Due to its 8-fold rotational
CC symmetry, all subunits are present with 8 copies or multiples thereof.
CC {ECO:0000269|PubMed:15116432}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC envelope {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole
CC body {ECO:0000269|PubMed:16823372}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:15226438}. Note=Localizes to the nuclear envelope
CC and spindle pole body. {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the nucleoporin Nup85 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB52802.1; -; Genomic_DNA.
DR PIR; T39727; T39727.
DR RefSeq; NP_595893.1; NM_001021800.2.
DR AlphaFoldDB; Q9UUE5; -.
DR SMR; Q9UUE5; -.
DR BioGRID; 276378; 12.
DR IntAct; Q9UUE5; 3.
DR STRING; 4896.SPBC17G9.04c.1; -.
DR iPTMnet; Q9UUE5; -.
DR MaxQB; Q9UUE5; -.
DR PaxDb; Q9UUE5; -.
DR PRIDE; Q9UUE5; -.
DR EnsemblFungi; SPBC17G9.04c.1; SPBC17G9.04c.1:pep; SPBC17G9.04c.
DR GeneID; 2539829; -.
DR KEGG; spo:SPBC17G9.04c; -.
DR PomBase; SPBC17G9.04c; nup85.
DR VEuPathDB; FungiDB:SPBC17G9.04c; -.
DR eggNOG; KOG2271; Eukaryota.
DR HOGENOM; CLU_019986_0_0_1; -.
DR InParanoid; Q9UUE5; -.
DR OMA; ELMEWLN; -.
DR PhylomeDB; Q9UUE5; -.
DR Reactome; R-SPO-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-SPO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-SPO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-SPO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SPO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SPO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SPO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-SPO-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-SPO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:Q9UUE5; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000791; C:euchromatin; IDA:PomBase.
DR GO; GO:0000792; C:heterochromatin; IDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0005643; C:nuclear pore; IDA:PomBase.
DR GO; GO:0031080; C:nuclear pore outer ring; IDA:PomBase.
DR GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
DR GO; GO:1990188; F:euchromatin binding; IDA:PomBase.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:PomBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006407; P:rRNA export from nucleus; ISO:PomBase.
DR InterPro; IPR011502; Nucleoporin_Nup85.
DR PANTHER; PTHR13373; PTHR13373; 1.
DR Pfam; PF07575; Nucleopor_Nup85; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; mRNA transport; Nuclear pore complex; Nucleus;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..675
FT /note="Nucleoporin nup85"
FT /id="PRO_0000290672"
SQ SEQUENCE 675 AA; 78022 MW; 799D29CB87A88FE8 CRC64;
MESSDEVDLP VYHLQNAPIE NGKLNDWRSK GRTVAFKLHP FLRKGLAYIN NKEFDENTLK
SDKFEEVESL VYEFSTPSTL IEPNYLLTAW HELWEELQDT YMTPILDSEA NLLLLTQFYG
KISSLFRSKI IQVLEELQSR INEGEKDCQP VLDSLWEVES AWRCAEAIYF PPSSPYTLST
GILDWVNAYD PQPIADDGLE IMAYRIPYQH PEFWPYVNKT AIRGLFEQTI SCLEMSGLTK
EWPVLKETVD ELIDILRYSP CTHQKRIRSV SDFERRWKLW RSRLANLRHV VKKHRDIDSE
VLDDFVVLLD ILNGNKEVIM LSCAHWQEYF SALAFLYGPL DCKNPEDISL LYQLATGEDS
KFYVNGTIEY EQICVNLCSN EPLNAIKHAY LLDLGLAVHL ADLLSKSGHL RDYITEEYPI
TLREHLILEY GQCVLESRNL WQTSFAYWKC VADSGYQRIK ACIPYVPLSD VDAKETALQL
CKQLKLRDEA QLVLTHWADE LIARNHYGEA LIALDNAANY SALNRVTWEL FDICIAEKKS
FSPDKDELLY ELFSSPKACT PTLASIISPA ATIHQYFFYL QHKKELNASE LLVGLLTMVD
FPSSRFPKLL ELLHEFLNNP LQSNSTDFKL SLVNVYDCIA VLQDQQSTVK DQQLLLSIHE
RLSSAISWYF LHLKK