NU155_MOUSE
ID NU155_MOUSE Reviewed; 1391 AA.
AC Q99P88;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Nuclear pore complex protein Nup155;
DE AltName: Full=155 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup155;
GN Name=Nup155;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang X., Li Z., Yang H., Bolund L.;
RT "The genomic organization, alternative splicing and comparative analysis of
RT the human nucleoporin 155 (NUP155) gene.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19070573; DOI=10.1016/j.cell.2008.10.022;
RA Zhang X., Chen S., Yoo S., Chakrabarti S., Zhang T., Ke T., Oberti C.,
RA Yong S.L., Fang F., Li L., de la Fuente R., Wang L., Chen Q., Wang Q.K.;
RT "Mutation in nuclear pore component NUP155 leads to atrial fibrillation and
RT early sudden cardiac death.";
RL Cell 135:1017-1027(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP DISULFIDE BOND.
RX PubMed=23641069; DOI=10.1242/jcs.124172;
RA Yoshimura S.H., Otsuka S., Kumeta M., Taga M., Takeyasu K.;
RT "Intermolecular disulfide bonds between nucleoporins regulate karyopherin-
RT dependent nuclear transport.";
RL J. Cell Sci. 126:3141-3150(2013).
CC -!- FUNCTION: Essential component of nuclear pore complex. Could be
CC essessential for embryogenesis. Nucleoporins may be involved both in
CC binding and translocating proteins during nucleocytoplasmic transport.
CC {ECO:0000250|UniProtKB:P37199, ECO:0000269|PubMed:19070573}.
CC -!- SUBUNIT: Interacts with GLE1 and NUP35/NUP53. Able to form a
CC heterotrimer with GLE1 and NUP42 in vitro (By similarity). Forms a
CC complex with NUP35, NUP93, NUP205 and lamin B (By similarity).
CC {ECO:0000250|UniProtKB:O75694}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P37199}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P37199}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P37199}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P37199}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P37199}. Note=In mitosis, assumes a diffuse
CC cytoplasmic distribution probably as a monomer, before reversing back
CC into a punctate nuclear surface localization at the end of mitosis.
CC {ECO:0000250|UniProtKB:P37199}.
CC -!- PTM: Phosphorylated. Phosphorylation and dephosphorylation may be
CC important for the function of NUP155 and may play a role in the
CC reversible disassembly of the nuclear pore complex during mitosis (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Disulfide-linked to NUP62. The inner channel of the NPC has a
CC different redox environment from the cytoplasm and allows the formation
CC of interchain disulfide bonds between some nucleoporins, the
CC significant increase of these linkages upon oxidative stress reduces
CC the permeability of the NPC.
CC -!- DISRUPTION PHENOTYPE: Homozygous null mice die before embryonic day
CC 8.5. {ECO:0000269|PubMed:19070573}.
CC -!- SIMILARITY: Belongs to the non-repetitive/WGA-negative nucleoporin
CC family. {ECO:0000305}.
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DR EMBL; AF322375; AAK11317.1; -; mRNA.
DR CCDS; CCDS37034.1; -.
DR RefSeq; NP_573490.3; NM_133227.3.
DR AlphaFoldDB; Q99P88; -.
DR SMR; Q99P88; -.
DR BioGRID; 228424; 30.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; Q99P88; 24.
DR MINT; Q99P88; -.
DR STRING; 10090.ENSMUSP00000128819; -.
DR CarbonylDB; Q99P88; -.
DR GlyGen; Q99P88; 1 site.
DR iPTMnet; Q99P88; -.
DR PhosphoSitePlus; Q99P88; -.
DR SwissPalm; Q99P88; -.
DR EPD; Q99P88; -.
DR jPOST; Q99P88; -.
DR MaxQB; Q99P88; -.
DR PaxDb; Q99P88; -.
DR PRIDE; Q99P88; -.
DR ProteomicsDB; 287841; -.
DR Antibodypedia; 22985; 161 antibodies from 30 providers.
DR DNASU; 170762; -.
DR Ensembl; ENSMUST00000163765; ENSMUSP00000128819; ENSMUSG00000022142.
DR GeneID; 170762; -.
DR KEGG; mmu:170762; -.
DR UCSC; uc007vei.1; mouse.
DR CTD; 9631; -.
DR MGI; MGI:2181182; Nup155.
DR VEuPathDB; HostDB:ENSMUSG00000022142; -.
DR eggNOG; KOG1900; Eukaryota.
DR GeneTree; ENSGT00390000016532; -.
DR HOGENOM; CLU_000429_0_0_1; -.
DR InParanoid; Q99P88; -.
DR OMA; EYYSRMI; -.
DR OrthoDB; 140051at2759; -.
DR PhylomeDB; Q99P88; -.
DR TreeFam; TF105951; -.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR BioGRID-ORCS; 170762; 22 hits in 76 CRISPR screens.
DR ChiTaRS; Nup155; mouse.
DR PRO; PR:Q99P88; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q99P88; protein.
DR Bgee; ENSMUSG00000022142; Expressed in indifferent gonad and 246 other tissues.
DR ExpressionAtlas; Q99P88; baseline and differential.
DR Genevisible; Q99P88; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; IC:ComplexPortal.
DR GO; GO:0044611; C:nuclear pore inner ring; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0086014; P:atrial cardiac muscle cell action potential; IMP:MGI.
DR GO; GO:0035196; P:miRNA processing; IMP:MGI.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:MGI.
DR GO; GO:0006998; P:nuclear envelope organization; ISO:MGI.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR GO; GO:0036228; P:protein localization to nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:MGI.
DR GO; GO:0006405; P:RNA export from 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; 1.20.120.1880; -; 1.
DR Gene3D; 1.25.40.440; -; 1.
DR Gene3D; 1.25.40.450; -; 1.
DR InterPro; IPR007187; Nucleoporin_Nup133/Nup155_C.
DR InterPro; IPR014908; Nucleoporin_Nup133/Nup155_N.
DR InterPro; IPR004870; Nucleoporin_Nup155.
DR InterPro; IPR042533; Nucleoporin_Nup155_C_1.
DR InterPro; IPR042537; Nucleoporin_Nup155_C_2.
DR InterPro; IPR042538; Nucleoporin_Nup155_C_3.
DR PANTHER; PTHR10350; PTHR10350; 1.
DR Pfam; PF03177; Nucleoporin_C; 1.
DR Pfam; PF08801; Nucleoporin_N; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Translocation; Transport.
FT CHAIN 1..1391
FT /note="Nuclear pore complex protein Nup155"
FT /id="PRO_0000204845"
FT REGION 604..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1057
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75694"
FT CARBOHYD 526
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1391 AA; 155118 MW; A8F9BE2E25653F32 CRC64;
MPSVLGSMMV ASTSAAASLQ EALENAGRLI DRQLQEDRMY PDLSELLMVS APNSPTVSGM
SDMDYPLQGP GLLSVPSLPE ISTIRRVPLP PELVEQFGHM QCNCMMGVFP PISRAWLTID
SDIFMWNYED GGDLAYFDGL SETILAVGLV KPKAGIFQPH VRHLLVLATP VDIVILGLSY
ANVQTGSGIL NDSMCGGMQL LPDPLYSLPT DNTYLLTITS TDNGRIFLAG KDGCLYEVAY
QAEAGWFSQR CRKINHSKSS LSFLVPSLLQ FTFSEDDPIV QIEIDNSRNI LYTRSEKGVI
QVYDLGHDGQ GMSRVASVSQ NAIVSAAGNI ARTIDRSVFK PIVQIAVIES SESLDCQLLA
VTHAGVRLYF STCPFRQPLA RPNTLTLVHV RLPPGFSASS TVEKPSKVHK ALYSKGILLM
TASENEDNDI LWCVNHDTFP FQKPMMETQM TTRVDGHSWA LSAIDELKVD KIITPLNKDH
IPITDSPVVV QQHMLPPKKF VLLSAQGSLM FHKLRPVDQL RHLLVSNVGG DGEEIERFFK
LHQEDQACAT CLILACSTAA CDREVSAWAT RAFFRYGGEA QMRFPATLPT PSNVGPILGS
PMYSSSPVPS GSPYPNPSSL GTPSHGAQPP TMSTPMCAVG SPAMQAASMS GLTGPEIVYS
GKHNGICIYF SRIMGNIWDA SLVVERVFKS SNREITAIES SVPVQLLESV LQELKGLQEF
LDRNSQFSGG PLGNPNTTAR VQQRLVGFMR PENGNTQQMQ QELQRKFQEA QLSEKISLQA
IQQLVRKSYQ ALALWKLLCE HQFSVIVGEL QKEFQEQLKI TTFKDLVIRD KEVTGALIAS
LINCYIRDNA AVDGISLHLQ DTCPLLYSTD DAVCSKANEL LQRSRQVQSK TERERMLRES
LKEYQKISNQ VDLPSVCAQY RQVRFYEGVV ELSLTAAEKK DPQGLGLHFY KHGEPEEDVV
GLQTFQERLN SYKCITDTLQ ELVNQSKAAP QSPSVPKKPG PPVLSSDPNM LSNEEAGHHF
EQMLKLAQRS KDELFSIALY NWLIQADLAD KLLQIASPFL EPHLVRMARV DQNRVRYMDL
LWRYYEKNRS FSSAARVLSK LADMHSTEIS LQQRLEYIAR AILSAKSSTA ISSIAADGEF
LHELEEKMEV ARIQLQIQET LQRQYSHHSS VQDAISQLDS ELMDITKLYG EFADPFKLAE
CKLAVIHCAG YSDPILVHTL WQDIIEKELN DSVALSSSDR MHALSLKLVL LGKIYAGTPR
FFPLDFIVQF LEQQVCTLNW DVGFVIQTMN EIGVPLPRLL EVYDQLFKSR DPFWNRVKSP
LHLLDCIHVL LTRYVENPSL VLNCERRRFT NLCLDAVCGY LVELQSMSSS VAVQAITGNF
KSLQAKLERL H
