NU155_RAT
ID NU155_RAT Reviewed; 1390 AA.
AC P37199;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Nuclear pore complex protein Nup155;
DE AltName: Full=155 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup155;
DE AltName: Full=P140;
GN Name=Nup155;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8458861; DOI=10.1083/jcb.121.1.1;
RA Radu A., Blobel G., Wozniak R.W.;
RT "Nup155 is a novel nuclear pore complex protein that contains neither
RT repetitive sequence motifs nor reacts with WGA.";
RL J. Cell Biol. 121:1-9(1993).
RN [2]
RP GLYCOSYLATION AT SER-525.
RX PubMed=12438562; DOI=10.1074/mcp.m200048-mcp200;
RA Wells L., Vosseller K., Cole R.N., Cronshaw J.M., Matunis M.J., Hart G.W.;
RT "Mapping sites of O-GlcNAc modification using affinity tags for serine and
RT threonine post-translational modifications.";
RL Mol. Cell. Proteomics 1:791-804(2002).
RN [3]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH LAMIN B; NUP35;
RP NUP93 AND NUP155.
RX PubMed=15703211; DOI=10.1091/mbc.e04-10-0857;
RA Hawryluk-Gara L.A., Shibuya E.K., Wozniak R.W.;
RT "Vertebrate Nup53 interacts with the nuclear lamina and is required for the
RT assembly of a Nup93-containing complex.";
RL Mol. Biol. Cell 16:2382-2394(2005).
CC -!- FUNCTION: Essential component of nuclear pore complex. Could be
CC essessential for embryogenesis (By similarity). Nucleoporins may be
CC involved both in binding and translocating proteins during
CC nucleocytoplasmic transport. {ECO:0000250|UniProtKB:Q99P88}.
CC -!- SUBUNIT: Interacts with GLE1. Able to form a heterotrimer with GLE1 and
CC NUP42 in vitro (By similarity). Forms a complex with NUP35, NUP93,
CC NUP205 and lamin B. {ECO:0000250, ECO:0000269|PubMed:15703211}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:15703211}. Nucleus membrane
CC {ECO:0000269|PubMed:15703211}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15703211}; Cytoplasmic side
CC {ECO:0000269|PubMed:15703211}. Nucleus membrane
CC {ECO:0000269|PubMed:15703211}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15703211}; Nucleoplasmic side
CC {ECO:0000269|PubMed:15703211}. 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 -!- 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.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the non-repetitive/WGA-negative nucleoporin
CC family. {ECO:0000305}.
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DR EMBL; Z21780; CAA79848.1; -; mRNA.
DR PIR; A45455; A45455.
DR RefSeq; NP_446404.1; NM_053952.1.
DR AlphaFoldDB; P37199; -.
DR SMR; P37199; -.
DR BioGRID; 250622; 1.
DR CORUM; P37199; -.
DR STRING; 10116.ENSRNOP00000042749; -.
DR GlyGen; P37199; 1 site.
DR iPTMnet; P37199; -.
DR PhosphoSitePlus; P37199; -.
DR jPOST; P37199; -.
DR PaxDb; P37199; -.
DR PRIDE; P37199; -.
DR GeneID; 117021; -.
DR KEGG; rno:117021; -.
DR CTD; 9631; -.
DR RGD; 621199; Nup155.
DR eggNOG; KOG1900; Eukaryota.
DR InParanoid; P37199; -.
DR OrthoDB; 140051at2759; -.
DR PhylomeDB; P37199; -.
DR Reactome; R-RNO-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-RNO-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-RNO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-RNO-191859; snRNP Assembly.
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-RNO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-RNO-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-RNO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-RNO-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-RNO-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-RNO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:P37199; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
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; ISO:RGD.
DR GO; GO:0035196; P:miRNA processing; ISO:RGD.
DR GO; GO:0006406; P:mRNA export from nucleus; ISO:RGD.
DR GO; GO:0006998; P:nuclear envelope organization; ISO:RGD.
DR GO; GO:0006606; P:protein import into nucleus; ISO:RGD.
DR GO; GO:0036228; P:protein localization to nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0034504; P:protein localization to nucleus; ISO:RGD.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Isopeptide bond;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport;
KW Ubl conjugation.
FT CHAIN 1..1390
FT /note="Nuclear pore complex protein Nup155"
FT /id="PRO_0000204846"
FT REGION 598..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1056
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75694"
FT CARBOHYD 525
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:12438562"
FT CROSSLNK 739
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75694"
SQ SEQUENCE 1390 AA; 155003 MW; 1B51716043BF9CCF CRC64;
MPSMLGSMMV ASTSAPSLQE ALENAGRLID RQLQEDRMYP DLSELLMVSA PNSPTVSGMS
DMDYPLQGPG LLSVPSLPEI STIRRVPLRL SWLNSLDTCS VTAMMGVFPP ISRAWLTIDS
DIFMWNYEDG GDLAYFDGLS ETILAVGLVK PKAGIFQPHV RHLLVLATPV DIVILGLSYA
NVQTGSGILN DSVCGGLQLL PDPLYSLPTD NTYLLTITST DNGRIFLAGK DGCLYEVAYQ
AEAGWFSQRC RKINHSKSSL SFLVPSLLQF TFSEDDPIVQ IEIDNSRNIL YTRSEKGVIQ
VYDLGHDGQG MSRVASVSQN AIVCAAGNIA RTIDRSVFKP IVQIAVIENS ESLDCQLLAV
THAGVRLYFS TCPFRQPLAR PNTLTLVHVR LPPGFSASST VEKPSKVHKA LYSKGILLMT
ASENEDNDIL WCVNHDTFPF QKPMMETQMT TRVDGHSWAL SAIDELKVDK IITPLNKDHI
PITDSPVVVQ QHMLPPKKFV LLSAQGSLMF HKLRPVDQLR HLLVSNVGGD GEEIERFFKL
HQEDQACATC LILACSTAAC DREVSAWATR AFFRYGGEAQ MRFPATLPTP SNVGPILGSP
MYSSSPVPTG SPYPNPSSLG TPSHGAQPPT MSTPMSAVGN PAMQAASLSG LTGPEIVYSG
KHNGICIYFS RIMGNIWDAS LVVERVFKSS NREITAIESS VPIQLLESVL QELKGLQEFL
DRNSQFSGGP LGNPNTTAKV QQRLLGVMRP ENGNTQQMQQ ELQRKFHEAQ LSEKISLQAI
QQLVRKSYQA LALWKLLCEH QFTVIVGELQ KEFQEQLKIT TFKDLVIREK EVTGALIASL
INCYIRDNAA VDGISLHLQD TCPLLYSTDD AVCSKANELL QRSRQVQSKS ERERMLRESL
KEYQKISNQV DLPSVCAQYR QVRFYEGVVE LSLTAAEKKD PQGLGLHFYK HGEPEEDVVG
LQTFQERLNS YKCITDTLQE LVNQSKAAPQ SPSVPKKPGP PVLSSDPNML SNEEAGHHFE
QMLKLAQRSK DELFSIALYN WLIQADLADK LLQIASPFLE PHLVRMAKVD QNRVRYMDLL
WRYYEKNRSF SSAARVLSKL ADMHSTEISL QQRLEYIARA ILSAKSSTAI SSIAADGEFL
HELEEKMEVA RIQLQIQETL QRQYSHHSSV QDAISQLDSE LMDITKLYGE FADPFKLAEC
KLAIIHCAGY SDPILVHTLW QDIIEKELSD SVTLSSSDRM HALSLKLVLL GKIYAGTPRF
FPLDFIVQFL EQQVCTLNWD VGFVIQTMNE IGVPLPRLLE VYDQLFKSRD PFWNRVKSPL
HLLDCIHVLL TRYVENPSLV LNCERRRFTN LCLDAVCGYL VELQSMSSSV AVQAITGNFK
SLQAKLERLH
