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NU133_DANRE
ID   NU133_DANRE             Reviewed;        1136 AA.
AC   F1QNV4; Q7SZE9;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Nuclear pore complex protein Nup133 {ECO:0000250|UniProtKB:Q8WUM0};
DE   AltName: Full=Nucleoporin 133 {ECO:0000312|ZFIN:ZDB-GENE-040426-2941};
GN   Name=nup133 {ECO:0000312|ZFIN:ZDB-GENE-040426-2941};
GN   ORFNames=zgc:55311 {ECO:0000312|ZFIN:ZDB-GENE-040426-2941};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=30427554; DOI=10.1002/ana.25370;
RA   Fujita A., Tsukaguchi H., Koshimizu E., Nakazato H., Itoh K., Kuraoka S.,
RA   Komohara Y., Shiina M., Nakamura S., Kitajima M., Tsurusaki Y.,
RA   Miyatake S., Ogata K., Iijima K., Matsumoto N., Miyake N.;
RT   "Homozygous splicing mutation in NUP133 causes Galloway-Mowat syndrome.";
RL   Ann. Neurol. 84:814-828(2018).
RN   [4]
RP   ERRATUM OF PUBMED:30427554.
RX   PubMed=30817857; DOI=10.1002/ana.25427;
RA   Fujita A., Tsukaguchi H., Koshimizu E., Nakazato H., Itoh K., Kuraoka S.,
RA   Komohara Y., Shiina M., Nakamura S., Kitajima M., Tsurusaki Y.,
RA   Miyatake S., Ogata K., Iijima K., Matsumoto N., Miyake N.;
RL   Ann. Neurol. 85:462-463(2019).
CC   -!- FUNCTION: Involved in poly(A)+ RNA transport (By similarity). Involved
CC       in nephrogenesis (PubMed:30427554). {ECO:0000250|UniProtKB:Q8WUM0,
CC       ECO:0000269|PubMed:30427554}.
CC   -!- SUBUNIT: Forms part of the Nup160 subcomplex in the nuclear pore which
CC       is composed of NUP160, NUP133, NUP107 and Nup96. This complex plays a
CC       role in RNA export and in tethering Nup98 and NUP153 to the nucleus.
CC       {ECO:0000250|UniProtKB:Q8WUM0}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC       {ECO:0000250|UniProtKB:Q8WUM0}. Chromosome, centromere, kinetochore
CC       {ECO:0000250|UniProtKB:Q8WUM0}. Note=Located on both the cytoplasmic
CC       and nuclear sides of the nuclear pore. During mitosis, localizes to the
CC       kinetochores. {ECO:0000250|UniProtKB:Q8WUM0}.
CC   -!- TISSUE SPECIFICITY: Widely expressed in the embryo and in adult
CC       tissues. Higher expression is observed in the brain, testes, ovary,
CC       skin, and kidney. {ECO:0000269|PubMed:30427554}.
CC   -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein results in
CC       anomalies of the head, brain and kidney. Morphant embryos show
CC       decreased head sizes, reduced axonal numbers in the forebrain and
CC       midbrain, and disorganization in the hindbrain. As for the renal
CC       tissues, morphants show underdeveloped glomeruli with hypoplastic
CC       capillary vessels, and abnormal podocytes.
CC       {ECO:0000269|PubMed:30427554}.
CC   -!- SIMILARITY: Belongs to the nucleoporin Nup133 family. {ECO:0000305}.
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DR   EMBL; AL929114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU467834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC052764; AAH52764.1; -; mRNA.
DR   RefSeq; NP_998696.1; NM_213531.1.
DR   AlphaFoldDB; F1QNV4; -.
DR   SMR; F1QNV4; -.
DR   STRING; 7955.ENSDARP00000023984; -.
DR   PaxDb; F1QNV4; -.
DR   PRIDE; F1QNV4; -.
DR   Ensembl; ENSDART00000020680; ENSDARP00000023984; ENSDARG00000010078.
DR   GeneID; 406852; -.
DR   KEGG; dre:406852; -.
DR   CTD; 55746; -.
DR   ZFIN; ZDB-GENE-040426-2941; nup133.
DR   eggNOG; KOG4121; Eukaryota.
DR   GeneTree; ENSGT00390000011529; -.
DR   HOGENOM; CLU_008593_0_0_1; -.
DR   InParanoid; F1QNV4; -.
DR   OMA; RYTLHHK; -.
DR   OrthoDB; 51227at2759; -.
DR   PhylomeDB; F1QNV4; -.
DR   TreeFam; TF106141; -.
DR   Reactome; R-DRE-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-DRE-159227; Transport of the SLBP independent Mature mRNA.
DR   Reactome; R-DRE-159230; Transport of the SLBP Dependant Mature mRNA.
DR   Reactome; R-DRE-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR   Reactome; R-DRE-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-DRE-191859; snRNP Assembly.
DR   Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR   Reactome; R-DRE-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-DRE-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-DRE-3232142; SUMOylation of ubiquitinylation proteins.
DR   Reactome; R-DRE-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR   Reactome; R-DRE-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-DRE-4085377; SUMOylation of SUMOylation proteins.
DR   Reactome; R-DRE-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-DRE-4570464; SUMOylation of RNA binding proteins.
DR   Reactome; R-DRE-4615885; SUMOylation of DNA replication proteins.
DR   Reactome; R-DRE-5578749; Transcriptional regulation by small RNAs.
DR   Reactome; R-DRE-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-DRE-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR   Reactome; R-DRE-9648025; EML4 and NUDC in mitotic spindle formation.
DR   PRO; PR:F1QNV4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 1.
DR   Bgee; ENSDARG00000010078; Expressed in presomitic mesoderm and 36 other tissues.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0031080; C:nuclear pore outer ring; IBA:GO_Central.
DR   GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Centromere; Chromosome; Kinetochore; mRNA transport; Nuclear pore complex;
KW   Nucleus; Protein transport; Reference proteome; Translocation; Transport.
FT   CHAIN           1..1136
FT                   /note="Nuclear pore complex protein Nup133"
FT                   /id="PRO_0000447883"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        61
FT                   /note="D -> N (in Ref. 2; AAH52764)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="Y -> F (in Ref. 2; AAH52764)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        211
FT                   /note="L -> V (in Ref. 2; AAH52764)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        329
FT                   /note="A -> S (in Ref. 2; AAH52764)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1136 AA;  126581 MW;  42D162572BFB5646 CRC64;
     MFSPRGTPGS GRRQAPRTGG RRSVSAVQPG LLFSPRRSAV TARSTPTRVQ SHAVVESYNF
     DVQTFGSSLP VKVMEALTMA DVDDQISVKV EASGWAWMVC GERLIVWKVS QTSVAKLSVC
     KDLQLPSSEF AYSADLVSIS SSGPLDLAPI QSISVLAVSP DGLVRFWPSL AHEGSYTEIS
     LDLSGHLSNY VAAVKGGSFI VSSYRGHLLR LSADSSGKLH HRPVQQGQGM LSGIGRRVSS
     LFGIRGQPAD LSVFSVLWVK ASSCLYSLSS CGLSKWEVDE NSETQVLSWS TNQIITDSIT
     DAIWDSESNY SEIKKGVNVL YLDMQPSNAG LVVLAAAWYP GDTPCVAYFC LVTLAESIVP
     SPDLLTVEVT KYNPPFQSEE ELLKTRLVLP DPSSPAAYLY NEELVFACST GAGRGGLAEE
     KILFSSPGDR VRGGGVCADL PVFFSQNSGL VAVLARETAS LLPETMEDSL CTSVAGPGPE
     GTPLETPPKI DMVAQEDKTK LLKQAFLQFC RHDLVGAQSM VDELFPSDGE GSADLDTVVT
     QIDLDLVDDY PACDPRWAES VPDEGAGFTL TSLILLHQLE DKMKAHRCLM DFLLQTGLLD
     RLTSTKVRSC PMATRLLLCE HAEKLSAAIV LKNHHAKHPE LVNTAIQTAL KKNSTDTPTN
     LTPADVFFRE VSQISSIFEC LLDEEEKALK EHPDAARWGE VVLSVNDIIK DMLQAAAQYR
     ETKASLYRAP ENCSPEPEYI PWTASGGVGG VRSVISRQHE LILRAAYPHA DAELRSVLCE
     QLVALLDSLL SGYVAQLTSL RRGGQQERYD TLENEYTQKR SELLKPLLEL GQHQWVAALA
     EKYCDFDILV QLCERTDNQS RLQQYMVKFA DQNFADFLFR WYMEKGKRGK LLSQPMATHQ
     QLASFLQAHD HLSWLHDIHV QDYQRAHRTL YNQANMETRY FSKKKTLLAL SKLTALASDM
     PEPVHRRQLN DIVEQERFLL HQETLPKQLL EEKQLNPDSM PLLSPQNLIS LYICDENRGA
     NEYDFKKALD LLEYFEEENG IDVDALKREI FSKALKKDWK ESWSSSDDND DPLEAARDST
     FVKILQKLIQ ERVSLQTYLP DIKDLLQEDE LESLKSKPYF EFLLRANYEH YLKVQI
 
 
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