NU132_SCHPO
ID NU132_SCHPO Reviewed; 1162 AA.
AC Q9UTH0; Q9UU23;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Nucleoporin nup132;
DE AltName: Full=Nuclear pore protein nup132;
GN Name=nup132; Synonyms=nup133b; ORFNames=SPAC1805.04;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 909-1055, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
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 [4]
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 [5]
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 Q9UTH0; Q10331: nup107; NbExp=2; IntAct=EBI-295780, EBI-295788;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:15226438,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the nucleoporin Nup133 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA87164.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CU329670; CAB55845.1; -; Genomic_DNA.
DR EMBL; AB027860; BAA87164.1; ALT_FRAME; Genomic_DNA.
DR PIR; T37889; T37889.
DR RefSeq; NP_593915.1; NM_001019344.2.
DR AlphaFoldDB; Q9UTH0; -.
DR SMR; Q9UTH0; -.
DR BioGRID; 278842; 126.
DR IntAct; Q9UTH0; 1.
DR STRING; 4896.SPAC1805.04.1; -.
DR iPTMnet; Q9UTH0; -.
DR MaxQB; Q9UTH0; -.
DR PaxDb; Q9UTH0; -.
DR PRIDE; Q9UTH0; -.
DR EnsemblFungi; SPAC1805.04.1; SPAC1805.04.1:pep; SPAC1805.04.
DR GeneID; 2542378; -.
DR KEGG; spo:SPAC1805.04; -.
DR PomBase; SPAC1805.04; nup132.
DR VEuPathDB; FungiDB:SPAC1805.04; -.
DR eggNOG; KOG4121; Eukaryota.
DR HOGENOM; CLU_274527_0_0_1; -.
DR InParanoid; Q9UTH0; -.
DR OMA; EHIIPWI; -.
DR PhylomeDB; Q9UTH0; -.
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:Q9UTH0; -.
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:0031965; C:nuclear membrane; 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:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IMP:PomBase.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:PomBase.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0090234; P:regulation of kinetochore assembly; EXP:PomBase.
DR GO; GO:0031297; P:replication fork processing; IMP:PomBase.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR007187; Nucleoporin_Nup133/Nup155_C.
DR InterPro; IPR014908; Nucleoporin_Nup133/Nup155_N.
DR InterPro; IPR037624; Nup133-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13405; PTHR13405; 1.
DR Pfam; PF03177; Nucleoporin_C; 1.
DR Pfam; PF08801; Nucleoporin_N; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Transport.
FT CHAIN 1..1162
FT /note="Nucleoporin nup132"
FT /id="PRO_0000290669"
SQ SEQUENCE 1162 AA; 132071 MW; 9788EC634E2019E3 CRC64;
MSSILGKRKN EEVVSFSPLK RISVEKSLLD STAYNNSLDW LRSKNFKVSC LLKHFNSKII
NDHPLSGSCY TDIGYALINS RKACFILSYR QSLGTAEPPT ITFPLPEEDS NGFSGQNALT
AFVPSDASDK EPGLLIVMPI SGRIAYWTSI GNALAQSYIC PQGMESLIKL LPKEKCEHLC
CSNPMKFIIS TNFGRLFSVQ LRDPAGQPDV SVQLFASDIS TFSTILQKMK IFNYPSIHII
ALKSPPLFSP YQHLLYVAEA SGLLEIYDLK LENKLVSGMN LSPIFKQVLR EGCPDASGLE
VLDLTICPTN GNLVSFLVCW KNSINYRYMI ISLDFSDISS PSVMNIHPLY SFSSKSLESS
KLHYSSSGNS LFVVLTDAVI IVHVQEDDKD IVSRTSWEEV IRMNTNVSGG IFMSTCYKYV
LGKYSIPTES CFIATPYSGI AEIEVHSLEH PANNESLVKS KLEEAVFYSF LPGNPIDFSC
NYLRSIKKPE LERIIVDLGM DILNSRSTHL PPLFASLMQH LSCRLNSLNN LVRYIRSMSL
DVDRQVLYKL RVMGEKCNSV RYLWNTIDTE FSTVSHSLIF QRIIYRLTQS ASSDNALREW
FLHNIESIDQ LIAQAHEFCI DSGSRVQELP LEVLDVIMEA NEVILAIQSS ALAYRRESQK
IYKLSIDTFG EEVPWTSTPE TLVLLCRQFE LTRSALVQSH QGTSDVENTF KIKDKGVLRN
VVSNLEVQLV ALTEVCFDAY SERIRWIEQR CGKDASEIQD VKEAFAVNRR FWVQTLSDIG
KGSSAIRIAE KYSDYRSLVE LCYQLYEDNE LTDALNNYLD LFGIKFAFIL YDYFVENGMA
LELLNSDRFN KSYLKQFFKS RDYNQISWMH DMRLGDYDAA SHRLLQLATK QEKLVDKKES
ELSLSKLFLY AVPSNSGNIR DLVLVEQKLE QLHIQKMVSK SVMPVVERLR SQGKKYQLVE
AVVDDLIGAK VAPVIARQVM QRVVKKFIAG QVVEATELLE YLSFSLYRRE DLVEGEVTDY
YLALRLLLTT RLTDDAKRFY ENTIWRRAVL HDNWIQVLDT QGKNDAIIET QFRMSALYRT
LEAVTINGLF HEGLIRPGSL SSCKFEGYDP QNLISIYPPA RFGDVTEVTK VLNRESVKLD
HYLTKTNLNT CYISMCLSCD TI