NU152_CHATD
ID NU152_CHATD Reviewed; 1463 AA.
AC G0SDP9; G3EQ77;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Nucleoporin NUP152 {ECO:0000303|PubMed:21784248};
DE AltName: Full=Nuclear pore protein NUP152;
GN Name=NUP152; ORFNames=CTHT_0052560;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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 (GSP1 and GSP2 GTPases associated predominantly with GTP in
CC the nucleus, with GDP in the cytoplasm).
CC {ECO:0000250|UniProtKB:P32499}.
CC -!- SUBUNIT: The nuclear pore complex (NPC) constitutes the exclusive means
CC of nucleocytoplasmic transport. NPCs allow the passive diffusion of
CC ions and small molecules and the active, nuclear transport receptor-
CC mediated bidirectional transport of macromolecules such as proteins,
CC RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the
CC nuclear envelope. The 55-60 MDa NPC is composed of at least 28
CC different subunits: AMO1, ELYS, GLE1, GLE2, MLP1, NDC1, NIC96, NSP1,
CC NUP133, NUP145, NUP152, NUP159, NUP170, NUP188, NUP192, NUP37, NUP49,
CC NUP53, NUP56, NUP57, NUP82, NUP84, NUP85, POM152, POM33, POM34, SEC13
CC and SEH1. Due to its 8-fold rotational symmetry, all subunits are
CC present with 8 copies or multiples thereof.
CC {ECO:0000250|UniProtKB:Q9USL4, ECO:0000305|PubMed:21784248}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P32499}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P32499}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P32499}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P32499}.
CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC karyopherins (importins, exportins) and form probably an affinity
CC gradient, guiding the transport proteins unidirectionally with their
CC cargo through the NPC. FG repeat regions are highly flexible and lack
CC ordered secondary structure. The overall conservation of FG repeats
CC regarding exact sequence, spacing, and repeat unit length is limited.
CC FG repeat types and their physico-chemical environment change across
CC the NPC from the nucleoplasmic to the cytoplasmic side: FXFG repeats
CC are especially abundant in NUPs on the nucleoplasmic side (in a highly
CC charged environment and enriched in Ser and Thr).
CC {ECO:0000250|UniProtKB:P32499}.
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DR EMBL; GL988045; EGS18650.1; -; Genomic_DNA.
DR EMBL; JF276304; AEN86180.1; -; Genomic_DNA.
DR RefSeq; XP_006695595.1; XM_006695532.1.
DR AlphaFoldDB; G0SDP9; -.
DR SMR; G0SDP9; -.
DR STRING; 759272.G0SDP9; -.
DR TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR EnsemblFungi; EGS18650; EGS18650; CTHT_0052560.
DR GeneID; 18259294; -.
DR KEGG; cthr:CTHT_0052560; -.
DR eggNOG; KOG0845; Eukaryota.
DR eggNOG; KOG0866; Eukaryota.
DR HOGENOM; CLU_002780_0_0_1; -.
DR OrthoDB; 854084at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR025574; Nucleoporin_FG_rpt.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR Pfam; PF13634; Nucleoporin_FG; 5.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR PROSITE; PS50196; RANBD1; 1.
PE 3: Inferred from homology;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..1463
FT /note="Nucleoporin NUP152"
FT /id="PRO_0000433182"
FT REPEAT 729..732
FT /note="FXFG 1"
FT REPEAT 835..838
FT /note="FXFG 2"
FT REPEAT 910..913
FT /note="FXFG 3"
FT REPEAT 1074..1077
FT /note="FXFG 4"
FT REPEAT 1127..1130
FT /note="FXFG 5"
FT REPEAT 1141..1144
FT /note="FXFG 6"
FT REPEAT 1152..1155
FT /note="FXFG 7"
FT REPEAT 1173..1176
FT /note="FXFG 8"
FT REPEAT 1236..1239
FT /note="FXFG 9"
FT DOMAIN 1289..1427
FT /note="RanBD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REGION 1..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1463 AA; 152244 MW; A140158C556C80DE CRC64;
MDPPSKKRSI FGGITSLFRS STAPPEDRKG KSTNSNSVTA NAPSLPPPQP ESNGASSPFS
PAKRASEAQL SVRKIIPKPQ GPSSKLSQSV SASEIAHRPA PSTPAPAAAT PVPKRRPGDN
PHKLAASTST PALQNLPNPP APATSSKATS FSGAPSTPRP SIFRNSLYAR PAPATTYTQR
VSSHPLTQSF PPVTPGRPGR AANVDINNRI LSNTASTELF PMKIPEPPRH LTGEMLAKEV
PEDPNRAGSI YADEYLAHLC PPEFDDLQRR QFFCILDLRR LKYAADEVFL KKDWKINILN
FAKEYEKSRS LIMLRYGLYE FKTVRASEAV KREWKLKHGI PDSDDESGAP AKTNGGGKRK
AEEDLEPSSS TFTHTASPNK RARATEAPAT NKRKANDELE EESQPSKLQK PGSPSPAKTP
SATKSVFESI ANKTASPQTA PKSSLFSSST AAKPNGSIFD NAQKTPATSS NIFGHLSDAS
KDEDNESDTG SEAEAEDETP AKKKKKTTVN GASSSAPSEG GESTQSRSIF DRITRDANGQ
PVRQLPEGGL FSGESRKRSL SPVKELPANN TWNASAGIKF ATPGTSSIFG SSNPKPPATT
DTIDFAASTT KKPEEAAAPA EAPKEATPTT NLFGAQTKAT EEAPKPAATN IFGSTTNPTE
TSIPAGSLFS AKPATSTTNS LFGATTSAAG QKKDEESKPT EAAPAPAPAT STLFGAKPAT
TESPKTNLFQ FGTPNKTETA PATQPQFGGL FGKPPSTETP TEKPATTSLF GTDASKPATT
SSLFGSATTA ADKPAATNLF GSTTTPADKP TTTNLFGSTS TQATSGSDEP TAKKFAFGGT
TESKPTTSLF GSTTPAPATS TENKGGLFGA TTTSATPATN TKPLFGSTPA PAQENKPLFG
SSTTTAAPVF QFGSTPASTS TEQKPLFGAT AATDSKPLFG STSATSTEQK PLFGSSTTMT
EQKPLFGSIS TTATEQKPLF GSTSTTEAKP LFGAAPASTE QKSLFGITPS TTENNPASIF
GNSSTSTEQK PLFGSAPAST EQKPLFGSTP STTENKPAGL FGNTSTTSTS TPLFNFGSQN
TTASQPSTTG SIFGSASASF TFTAGGSDGT IKNPFASDGS YSAPTSFNFG SGDSQSSSAP
FTFGAGGGTP SFTFGASSDS SNASNNASSA PIFSFGASQP SSTPLFGQNN PPAASNIFAS
SLAPVGGTST GTSKHVPSFL ESENKASAYS SLDSPFTFGG ASSLATTPAA STPEPSAANA
AAAGEDQGAS ADADEQPQEQ ISLTDGGPGE EDESVVHEVR AKAVKLVTAA DSSADSSNGS
GEKPAEKKSN SPWKVMGVGP LRLLKHKQTG AVRMLLRAEP RGNIALNKLV LPQFTYKPDA
ATPKFIKFAA ARDDGKGLET WMIQVKTPQL AQELAAALEE HKKANEKKDG EKNEESEKKD
EKQEEKKNEE KKDEKEEKKD EKK
