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NU124_SCHPO
ID   NU124_SCHPO             Reviewed;        1159 AA.
AC   Q09904;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Nucleoporin nup124;
DE   AltName: Full=Nuclear pore protein nup124;
GN   Name=nup124; ORFNames=SPAC30D11.04c;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10409764; DOI=10.1128/mcb.19.8.5768;
RA   Balasundaram D., Benedik M.J., Morphew M., Dang V.-D., Levin H.L.;
RT   "Nup124p is a nuclear pore factor of Schizosaccharomyces pombe that is
RT   important for nuclear import and activity of retrotransposon Tf1.";
RL   Mol. Cell. Biol. 19:5768-5784(1999).
RN   [2]
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-380; SER-465 AND
RP   SER-546, AND 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: Nucleoporins may be involved in both binding and
CC       translocation of the proteins during nucleocytoplasmic transport. In
CC       S.pombe it is required for the nuclear localization of retrotransposon
CC       tf1. {ECO:0000269|PubMed:10409764}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC       {ECO:0000269|PubMed:10409764}.
CC   -!- DOMAIN: Contains F-X-F-G repeats.
CC   -!- SIMILARITY: To yeast nucleoporins NUP1 and NUP2. {ECO:0000305}.
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DR   EMBL; AF280406; AAF90179.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA91890.1; -; Genomic_DNA.
DR   PIR; T38595; S62562.
DR   RefSeq; NP_593213.1; NM_001018609.2.
DR   AlphaFoldDB; Q09904; -.
DR   BioGRID; 278724; 70.
DR   STRING; 4896.SPAC30D11.04c.1; -.
DR   iPTMnet; Q09904; -.
DR   MaxQB; Q09904; -.
DR   PaxDb; Q09904; -.
DR   PRIDE; Q09904; -.
DR   EnsemblFungi; SPAC30D11.04c.1; SPAC30D11.04c.1:pep; SPAC30D11.04c.
DR   GeneID; 2542254; -.
DR   KEGG; spo:SPAC30D11.04c; -.
DR   PomBase; SPAC30D11.04c; nup124.
DR   VEuPathDB; FungiDB:SPAC30D11.04c; -.
DR   eggNOG; KOG4719; Eukaryota.
DR   HOGENOM; CLU_275466_0_0_1; -.
DR   InParanoid; Q09904; -.
DR   OMA; MPMGGSK; -.
DR   PhylomeDB; Q09904; -.
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:Q09904; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0140599; C:mitotic nuclear bridge midzone membrane domain; IDA:PomBase.
DR   GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR   GO; GO:0005643; C:nuclear pore; IDA:PomBase.
DR   GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR   GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006606; P:protein import into nucleus; IMP:PomBase.
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; IPR026054; Nucleoporin.
DR   InterPro; IPR013913; Nup153_N.
DR   InterPro; IPR018892; Retro-transposon_transp_CS.
DR   PANTHER; PTHR23193; PTHR23193; 1.
DR   Pfam; PF08604; Nup153; 2.
DR   Pfam; PF10599; Nup_retrotrp_bd; 1.
PE   1: Evidence at protein level;
KW   mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT   CHAIN           1..1159
FT                   /note="Nucleoporin nup124"
FT                   /id="PRO_0000204837"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          44..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          106..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..1159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..454
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..715
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        746..763
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..816
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..978
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        997..1034
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         380
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         465
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         546
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   1159 AA;  123974 MW;  852F84BA2E0619A3 CRC64;
     MPPVSKNTRT SSKTVKKPYD PPQGSSRPFF TVLKRAFSSV LHPFTSGLDE KASGTASKDR
     KSGRAGTKSL LTPELTPHYL GKSPRIIRVS NRSHVRTIDG IEEKVHTNTF EPRKPKQKQD
     YTNSPTLFKR HDELSLKSLN SLHPSSALSK KLGSTSQHQI ATPKSSASLL NILRSLHDEQ
     KNTLNISSVK QDRITEANPT CEKRKPSRSP SPMLSKKKSV ARASENEPSA KQNKSFSGND
     SHKSLTDIRD KENGETEVSA KNHVPHRSSR RRRRHQRLIP IIYETLEQMD LRKPVLVNAE
     VQTDSNPGNT MFIDKQDIYH RLSTPTSRKR QTLEKGHIKA FSAVDEDLDE IFACEDDVHY
     TALPKQNPKS ERILEPIIAS PKDNTSDKGL LTKSAPTFEE LQASITPKPV KTSPNDTALT
     LANAEDNKTF EHQPLSKDTE APKSQFSSSP TKESTTRKSE VEPPSPSKEI KSSHFSVPEF
     KFEPKTEATT DKKLNVPKFE FKPTATADVQ TNRLKENEPK PTFFAQLPSK TQETPSITEN
     KPSFFSQLSP KREETEKKDN APSAPASTSG FSFGGFAPKT LEEKEETKAP TFNFSLNNAS
     STQDTTKPTL QFNFGSSFGK PTSNIFNDKK TSENGLASST VASESKPSAP ESKPSSGFGN
     TAGSSPFSFN LTKESKEVPP TNSFSFAKKG KDEANDSLSA KASTPFSFAK PNTENVTTTA
     PQFSFNFTKP NTDAKTNLLP EKTFNEEAVK QKETEKEVPP TGPKASEIKD SVSSNNAVPS
     STFNFVSPFA AVSEKTNENN IPNDTTKTNG NATKRTLEQT EDAKPFAFSF GSTTEQANKK
     ASTSNETTKP QLDTSSKTDG VTANAPFSFA SAFNAPKPST NTADGKDSAS NLTTPSPAFS
     FGNNSGVKAS SNNNPSTNSS TAPFSFGTSN KPAFSFGSAT SKTTSEGTAP AASASAPAPT
     TSAFSFGASN SSMNKEENTP MAKDAGDTAP ASGFKSGFSF GANNSPQPAS MFGTSTPAPS
     SAFAFGNQSG TNPAAPAGFG GITNTATNNP PSTGFTFTPS NAGSTAAPMF GAGNTPNPSG
     SINNASQAFA FGSGEPSNPA SNPPSTGFSF GAATPSAFNA SASQSPAPNG IQFNLGSSNS
     QTNAPPGRKI AVPRSRRKR
 
 
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