NU120_SCHPO
ID NU120_SCHPO Reviewed; 1136 AA.
AC O43044;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Nucleoporin nup120;
DE AltName: Full=Nuclear pore protein nup120;
GN Name=nup120; ORFNames=SPBC3B9.16c;
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, INTERACTION WITH NUP107, AND
RP 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 npc107-120 complex which consists of nup85,
CC nup107, nup120, nup131, nup132 and seh1. Interacts with nup107.
CC {ECO:0000269|PubMed:15226438}.
CC -!- INTERACTION:
CC O43044; O36030: SPAC4F10.18; NbExp=3; IntAct=EBI-1563733, EBI-16014622;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15116432,
CC ECO:0000269|PubMed:15226438, ECO:0000269|PubMed:16823372}. Note=Nuclear
CC rim.
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DR EMBL; CU329671; CAA17796.1; -; Genomic_DNA.
DR PIR; T40355; T40355.
DR RefSeq; NP_596674.1; NM_001022596.2.
DR PDB; 4FHM; X-ray; 4.34 A; B=1-961.
DR PDB; 4FHN; X-ray; 6.99 A; B/D=1-1136.
DR PDB; 4GQ2; X-ray; 2.40 A; M=1-949.
DR PDBsum; 4FHM; -.
DR PDBsum; 4FHN; -.
DR PDBsum; 4GQ2; -.
DR AlphaFoldDB; O43044; -.
DR SMR; O43044; -.
DR BioGRID; 277033; 6.
DR DIP; DIP-38661N; -.
DR IntAct; O43044; 3.
DR STRING; 4896.SPBC3B9.16c.1; -.
DR SwissPalm; O43044; -.
DR MaxQB; O43044; -.
DR PaxDb; O43044; -.
DR EnsemblFungi; SPBC3B9.16c.1; SPBC3B9.16c.1:pep; SPBC3B9.16c.
DR GeneID; 2540505; -.
DR KEGG; spo:SPBC3B9.16c; -.
DR PomBase; SPBC3B9.16c; nup120.
DR VEuPathDB; FungiDB:SPBC3B9.16c; -.
DR eggNOG; ENOG502QQWQ; Eukaryota.
DR HOGENOM; CLU_277873_0_0_1; -.
DR InParanoid; O43044; -.
DR OMA; NEWERFA; -.
DR PhylomeDB; O43044; -.
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:O43044; -.
DR Proteomes; UP000002485; Chromosome II.
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:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:PomBase.
DR InterPro; IPR021717; Nucleoporin_Nup160.
DR PANTHER; PTHR21286; PTHR21286; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Transport.
FT CHAIN 1..1136
FT /note="Nucleoporin nup120"
FT /id="PRO_0000290667"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:4GQ2"
FT TURN 13..17
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:4GQ2"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 110..120
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:4GQ2"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:4GQ2"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:4GQ2"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 308..316
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 345..353
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 358..369
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 372..381
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 418..427
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 433..442
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 452..458
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 463..477
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 484..489
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 491..514
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 519..524
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 531..543
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 547..552
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 556..560
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 570..584
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 589..604
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 611..622
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 624..626
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 629..640
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 642..644
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 645..657
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 671..702
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 708..712
FT /evidence="ECO:0007829|PDB:4GQ2"
FT TURN 713..717
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 718..738
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 762..764
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 769..776
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 785..787
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 789..802
FT /evidence="ECO:0007829|PDB:4GQ2"
FT STRAND 806..808
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 811..821
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 825..831
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 832..834
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 839..851
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 855..863
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 877..879
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 880..888
FT /evidence="ECO:0007829|PDB:4GQ2"
FT TURN 889..891
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 894..908
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 912..924
FT /evidence="ECO:0007829|PDB:4GQ2"
FT HELIX 931..948
FT /evidence="ECO:0007829|PDB:4GQ2"
SQ SEQUENCE 1136 AA; 129783 MW; 0D8E7A0839FA6FFE CRC64;
MNELKHAVVP IDLQSFCLEG TLALWVPALE NDSEDDSEAI ETADDNEKLF KKECVAYDAG
VYTSNKSKGS QTLRWSIFQN RTLTIFDVSL NSKKEPLSKF NVKIHFPSNV MKDGVAFSFS
EHSDTTIIYA ITHARVLYYI RLSKTWFQLP DARLDDDWCL CYRPISFLNQ KPDLMAAIST
SEICVSFFNG GLTKIILNPK DASHYEQHID DSSYLFSLKK YLSLQAFKAD YRSPNTIISM
IFLSTYNVLV MLSLDYKLKV LDLSTNQCVE TIELSQTILP LQSFPYLTSD HTTNSFIALY
YPDNSHGSFS IYKLNANAHS FKLNVVIEKG IIPPSLPDDE FIPWMLSDFQ LISSEGSQSK
FLLIIAWKSN LNTVIQKCNL SLDQDESFSC VWSHSLDSFS LIEKTFFDVP TNMSSGDISE
IWLQHIFAHN TSIESIQVAL LSFQNSSSQV SKNKLDKFGA LTISELKNAV LSSIVSTIQI
EPNSDLTGYD YYEYKRLLYN EWERFAKLVA YLDHFGDEIL SINFDPSNAV TYINYANKVA
FIRDPYLIES FDEEPLTKLI SSLETDDPSL IEGYQILDLG RSLHSCMSFS TLSEIRYSLR
ELVQDLPSYS LFDTLWVFYD KHIYPNVDPD YISTLIDTLV SLENPMRDID SLIQRLRSFD
IYNHSAQSPS LFLCASVARV LDSILKKFQV SIEGFIFLLS LITSQQDYEL QSKFAGCDKL
FLSLLEDWRL VSFLLENSAL LLEKFEEEDV DSTNCNLNTM EALASVNTAL QFFSALNYSE
CFSESQISPL HATVISSLSA IFIRDDTEND LVTELVEKLF LFKQYNACMQ LIGWLNSDPI
AVYLKALIYL KSKEAVKAVR CFKTTSLVLY SHTSQFAVLR EFQEIAEKYH HQNLLSCYYL
HLSKKLFEES AYIDALEFSL LADASKETDD EDLSIAITHE TLKTACAAGK FDAAHVALMV
LSTTPLKKSC LLDFVNQLTK QGKINQLLNY SMPTLRQDVD NLLERKAFQM INVESQPCWY
NILFSWRYKH QNYRDAAAII YEKLSRYIST TELIGKKERT FIIEHYLIVL NTLELLPKED
TWILVTDMSV DKEPDPNFLP QKLLTLDAIV AEYHLQLKDV AVQVTAEMSS AMNIDL
