NSP1_SCHPO
ID NSP1_SCHPO Reviewed; 598 AA.
AC Q10168;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Nucleoporin nsp1;
DE AltName: Full=Nuclear pore protein nsp1;
DE AltName: Full=Nucleoskeletal-like protein;
GN Name=nsp1; ORFNames=SPAC26A3.15c;
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 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 [3]
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489 AND SER-490, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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. Appears to have a role in the formation of the septum.
CC {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:0000250|UniProtKB:P14907}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:15116432}. Nucleus membrane
CC {ECO:0000269|PubMed:16823372}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16823372}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P14907}. Nucleus membrane
CC {ECO:0000269|PubMed:16823372}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16823372}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P14907}.
CC -!- DOMAIN: Contains X-F-X-F-G repeats.
CC -!- SIMILARITY: Belongs to the nucleoporin NSP1/NUP62 family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA93238.1; -; Genomic_DNA.
DR PIR; T38403; T38403.
DR RefSeq; NP_594158.1; NM_001019582.2.
DR AlphaFoldDB; Q10168; -.
DR SMR; Q10168; -.
DR BioGRID; 279121; 5.
DR STRING; 4896.SPAC26A3.15c.1; -.
DR iPTMnet; Q10168; -.
DR MaxQB; Q10168; -.
DR PaxDb; Q10168; -.
DR PRIDE; Q10168; -.
DR EnsemblFungi; SPAC26A3.15c.1; SPAC26A3.15c.1:pep; SPAC26A3.15c.
DR GeneID; 2542668; -.
DR KEGG; spo:SPAC26A3.15c; -.
DR PomBase; SPAC26A3.15c; nsp1.
DR VEuPathDB; FungiDB:SPAC26A3.15c; -.
DR eggNOG; KOG2196; Eukaryota.
DR HOGENOM; CLU_488480_0_0_1; -.
DR InParanoid; Q10168; -.
DR OMA; EMMSKQV; -.
DR PhylomeDB; Q10168; -.
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 PRO; PR:Q10168; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0005643; C:nuclear pore; IDA:PomBase.
DR GO; GO:0044613; C:nuclear pore central transport channel; ISO:PomBase.
DR GO; GO:0044615; C:nuclear pore nuclear basket; ISO:PomBase.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; ISO:PomBase.
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 Cell cycle; Cell division; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Septation;
KW Translocation; Transport.
FT CHAIN 1..598
FT /note="Nucleoporin nsp1"
FT /id="PRO_0000204921"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 598 AA; 60730 MW; 0BE7E551EC296D94 CRC64;
MSFNPGNNQN SGFSFGKPAQ PNSAAQGAAT PAATGLFGNT NNNTSSTAPS GGLFGSNNAS
NTSAPSTFSF GKAATTGNST NASTSSPFSF GSTNTNNTAG AKPLFGGLGS TGSANSTGDK
SKNTASSATG AATTNPSGST FNFGSSNNSF NFGKPASTTN TTTPAAASTG SLFGKPAATG
TTSNAPPASS TSTTPATGSG GFSFGKPASL GSTNNASTST TANSGFSFGK PATTSAPGSN
TTVTPSSSIT GTNDSKPAAS NTGSAPTTGF SFGKPAGQAA STATDKGTTT TSSAGTGFSF
GKPATTEDTN KPTAPNSAFT KPATSTGDNK PTFSFGNTSK PTENTSTTAT SAPPLSNNTK
PAEGANQTSS GFSFGKPATD TTTSTSKTGP LFGNKPADPS AKPGATASTT PSEPPPSSIK
HKTLQEILNK WSTDLTTQTE VFNKLCDQVS DWDRTLVDNG ALISKLYTET VEAEQMSNRI
DDGLEYVSSS QQELFKLLDS YETQLETFDG RATSALNVER ERAFGVADDI LSRLDRLGED
LGTVINQMND FSKPDDSISE IVKVLNAQLA SLGWVENRIF QMEEKLDTIK KKNSDVLF
