NU153_XENLA
ID NU153_XENLA Reviewed; 1605 AA.
AC Q640Z6;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Nuclear pore complex protein Nup153;
DE AltName: Full=153 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup153;
GN Name=nup153;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH KPNB1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9531546; DOI=10.1083/jcb.141.1.31;
RA Shah S., Tugendreich S., Forbes D.;
RT "Major binding sites for the nuclear import receptor are the internal
RT nucleoporin Nup153 and the adjacent nuclear filament protein Tpr.";
RL J. Cell Biol. 141:31-49(1998).
CC -!- FUNCTION: Component of the nuclear pore complex (NPC), a complex
CC required for the trafficking across the nuclear envelope. Functions as
CC a scaffolding element in the nuclear phase of the NPC essential for
CC normal nucleocytoplasmic transport of proteins and mRNAs. May be
CC involved in the retention of unspliced mRNAs in the nucleus. Probably
CC mediates tpr anchoring to the nuclear membrane at NPC. Possible DNA-
CC binding subunit of the nuclear pore complex (NPC) (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds at least 4 zinc ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts (via C-terminal domain) with the nuclear receptor
CC kpnb1; the interaction occurs in a RanGTP-dependent manner. Associates
CC with the Importin alpha/Importin beta receptor.
CC {ECO:0000269|PubMed:9531546}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:9531546}.
CC Nucleus, nuclear pore complex {ECO:0000269|PubMed:9531546}.
CC Note=Localized to the nucleoplasmic side of the nuclear pore complex
CC (NPC) core structure, forming a fibrous structure called the nuclear
CC basket. Colocalizes with tpr at the nuclear pore complex.
CC -!- TISSUE SPECIFICITY: Egg (at protein level).
CC {ECO:0000269|PubMed:9531546}.
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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NUP153 family. {ECO:0000305}.
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DR EMBL; BC082443; AAH82443.1; -; mRNA.
DR RefSeq; NP_001082284.1; NM_001088815.1.
DR AlphaFoldDB; Q640Z6; -.
DR SMR; Q640Z6; -.
DR BioGRID; 99706; 3.
DR MaxQB; Q640Z6; -.
DR GeneID; 398374; -.
DR KEGG; xla:398374; -.
DR CTD; 398374; -.
DR Xenbase; XB-GENE-6251581; nup153.L.
DR OrthoDB; 141803at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 398374; Expressed in egg cell and 19 other tissues.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0051292; P:nuclear pore complex assembly; IMP:CACAO.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR026054; Nucleoporin.
DR InterPro; IPR013913; Nup153_N.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23193; PTHR23193; 3.
DR Pfam; PF08604; Nup153; 1.
DR Pfam; PF00641; zf-RanBP; 5.
DR SMART; SM00547; ZnF_RBZ; 5.
DR SUPFAM; SSF90209; SSF90209; 4.
DR PROSITE; PS01358; ZF_RANBP2_1; 5.
DR PROSITE; PS50199; ZF_RANBP2_2; 5.
PE 1: Evidence at protein level;
KW DNA-binding; Membrane; Metal-binding; mRNA transport; Nuclear pore complex;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transport; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..1605
FT /note="Nuclear pore complex protein Nup153"
FT /id="PRO_0000422141"
FT REPEAT 249..250
FT /note="1"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 656..657
FT /note="2"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 943..944
FT /note="3"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 959..960
FT /note="4"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 988..989
FT /note="5"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1007..1008
FT /note="6"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1021..1022
FT /note="7"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1044..1045
FT /note="8"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1100..1101
FT /note="9"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1116..1117
FT /note="10"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1134..1135
FT /note="11"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1148..1149
FT /note="12"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1167..1168
FT /note="13"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1188..1189
FT /note="14"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1227..1228
FT /note="15"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1243..1244
FT /note="16"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1259..1260
FT /note="17"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1275..1276
FT /note="18"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1291..1292
FT /note="19"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1307..1308
FT /note="20"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1339..1340
FT /note="21"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1356..1357
FT /note="22"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1371..1372
FT /note="23"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1382..1383
FT /note="24"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1414..1415
FT /note="25"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1430..1431
FT /note="26"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1448..1449
FT /note="27"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1470..1471
FT /note="28"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1482..1483
FT /note="29"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1502..1503
FT /note="30"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1512..1513
FT /note="31"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1521..1522
FT /note="32"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REPEAT 1535..1536
FT /note="33"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT ZN_FING 655..684
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 720..749
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 790..819
FT /note="RanBP2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 842..871
FT /note="RanBP2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 906..935
FT /note="RanBP2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..1556
FT /note="33 X 2 AA repeats of F-G"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT REGION 332..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 661
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 664
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 675
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 678
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 726
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 729
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 740
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 743
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 796
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 799
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 810
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 813
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 848
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 851
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 862
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 865
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P49791"
SQ SEQUENCE 1605 AA; 164971 MW; 8504C80C3B635F94 CRC64;
MAAAGGGGPG GPGTGGKIRS RRYHLSSGRT PYSKSRQQQQ GIISRVTDTV KSIVPGWLQK
YFNKQEEEHD RVHSASEVIV NDTEARENNA EHHIYVVDDD DDEEGNSPTD GRVTPEPIIN
VDEEVPSTSQ SAINNTDALT RPSLHRASLN FNIFDSPALN CQPSTSSAFP IGTSGFSLIK
EIKDSTSQHD DDNISTTSGF SSRASDKDLA VSKNVSVPPL WSPEVDRSQS LSHNSSMTSK
KPTFNLSAFG SLSPSLGNAS ILNRQLGDSP FYPGKTTYQG AAAVRSSRVR ATPYQAPLRR
QVKAKPAAHS QQCGVTSSAA RRILQSLEKM SSPLADAKRI PSNSSLSHTP EKNVMDIPEN
PSKRKKVESP FPPVQRLVTP KSISVSANRS LYIKPSLTPS AVSNTNSRRI QPDKHNESRK
NNLQTTSQSH SFSYPKFSTP ASNGLSSGTG GGKMMREKGS HYSTKPANEE LDGPVLPEIP
LPLSTAALPS FQFSTLSGSA TSPISVTKPA NSTTCRLTSS SPSFTFSSPI VKSTESNAQS
PGSSVDFTFS VPAAKASSAT SDESKVSAVS RAAKTHAAVS SAKNTDDEQL GFCKPAKTLK
EGSVLDMLRS PGFSSSPSLL TSASSLNRST PTLSKTVGNT FSPANVSLGV GSKQAFGLWQ
CSACFHENMS SDSNCISCSA LKPRPTETSK KLPASPPSSN TKSTVPLSST PGLGDIFKKP
AGMWDCDTCL VQNKAEVTKC VACETPKPGT GMKATLLIPS TTKSTNPATN TLAFASCSAS
IPNEEMFKKP MGSWECTVCH MQNKTEDNTC VGCKAEKPGT VKSVPTAAPS GLLGLLDQFK
KPTGSWDCDV CLIQNKPEAN KCIACESAKP GTKAELKGTF DTVKNSVSVA PLSSGQLGLL
DQFKKSAGSW DCDVCLVENK PEATKCVACE TSKPGTKAEL KGFGTSTFSS GTAAPTFKFG
VQSSDSTAEL KSGASTSGFA KSIGNFKFGL ASASTTTEET GKKSFTFGSS TTNEVSAGFK
FGIAGSAQTK PDTLSQSTTS GFTFGSVSNT VSLAPTATSS GSTGLQVAAV IADSNLATTA
TLKSAEEKKA EAPTITPFSF GKTDQNKETA STSFVFGKKD EKTDSAPTGS SFAFGLKKDG
EESKQFLFGK PEPTKVDGSA ASAGFAFGVT NPTEKKDIEQ PGKSVFAFGA QTSITDAGAS
KQPFSFLTNV SSTAASSSTC GVSSSVFGSV TQSSTPATPS NVFGSAISAN APAPSSGVFG
NLTPSNAPAA SSTLFGNVAP SSTPSGSSGL FGTAAASSTP ATSTSLFGSA AKLSAPASSG
GVFNSAAPAA PASTASSVFG SVASSTNTSA NSANIFGSSG GAATAPGAFV FGQPASTAST
VFGNSSESKS TFVFSGQENK PVTSASTSVT PFLFGAVSAS TTPAAPGFNF GRTITSNTTG
TSSSPFIFGA GASGSASSSI TAQANPVPAF GQSSNPSTAP AFGSSTSVPV FPAGNSQQVP
AFGSSSAQPP VFGQQATQPS FGSPAAPSAG SGFPFGNNAN FNFNSTNSSG GVFTFNANSG
STTQPPPPGY MFNAAAPGFN MGTNGRTTPA STISTRKIKT ARRRK
