PO210_RAT
ID PO210_RAT Reviewed; 1886 AA.
AC P11654;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Nuclear pore membrane glycoprotein 210;
DE Short=Nuclear pore protein gp210;
DE AltName: Full=Nuclear envelope pore membrane protein POM 210;
DE Short=POM210;
DE AltName: Full=Nucleoporin Nup210;
DE AltName: Full=Pore membrane protein of 210 kDa;
DE Flags: Precursor;
GN Name=Nup210; Synonyms=Gp210, Pom210;
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], PROTEIN SEQUENCE OF 26-49; 195-215; 211-235;
RP 282-298; 584-594; 849-868; 1163-1174; 1179-1189; 1294-1329 AND 1660-1669,
RP AND GLYCOSYLATION.
RC TISSUE=Liver;
RX PubMed=2738089; DOI=10.1083/jcb.108.6.2083;
RA Wozniak R.W., Bartnik E., Blobel G.;
RT "Primary structure analysis of an integral membrane glycoprotein of the
RT nuclear pore.";
RL J. Cell Biol. 108:2083-2092(1989).
RN [2]
RP TOPOLOGY.
RX PubMed=1281815; DOI=10.1083/jcb.119.6.1441;
RA Wozniak R.W., Blobel G.;
RT "The single transmembrane segment of gp210 is sufficient for sorting to the
RT pore membrane domain of the nuclear envelope.";
RL J. Cell Biol. 119:1441-1449(1992).
RN [3]
RP PHOSPHORYLATION AT SER-1880.
RX PubMed=8672508; DOI=10.1021/bi9600660;
RA Favreau C., Worman H.J., Wozniak R.W., Frappier T., Courvalin J.-C.;
RT "Cell cycle-dependent phosphorylation of nucleoporins and nuclear pore
RT membrane protein Gp210.";
RL Biochemistry 35:8035-8044(1996).
RN [4]
RP SUBUNIT.
RX PubMed=11453980; DOI=10.1046/j.1432-1327.2001.02290.x;
RA Favreau C., Bastos R., Cartaud J., Courvalin J.-C., Mustonen P.;
RT "Biochemical characterization of nuclear pore complex protein gp210
RT oligomers.";
RL Eur. J. Biochem. 268:3883-3889(2001).
CC -!- FUNCTION: Nucleoporin essential for nuclear pore assembly and fusion,
CC nuclear pore spacing, as well as structural integrity. {ECO:0000250}.
CC -!- SUBUNIT: Forms dimers and possibly higher-order oligomers.
CC {ECO:0000269|PubMed:11453980}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus membrane;
CC Single-pass type I membrane protein. Endoplasmic reticulum membrane;
CC Single-pass type I membrane protein.
CC -!- PTM: N-glycosylated, but not all potential glycosylation sites may be
CC used. Contains high-mannose type oligosaccharides.
CC {ECO:0000269|PubMed:2738089}.
CC -!- PTM: Phosphorylated at Ser-1880 in mitosis specifically; not
CC phosphorylated in interphase. {ECO:0000269|PubMed:8672508}.
CC -!- SIMILARITY: Belongs to the NUP210 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y00826; CAA68759.1; -; mRNA.
DR PIR; S04921; S04921.
DR RefSeq; NP_445774.1; NM_053322.2.
DR AlphaFoldDB; P11654; -.
DR CORUM; P11654; -.
DR STRING; 10116.ENSRNOP00000008888; -.
DR GlyGen; P11654; 4 sites.
DR iPTMnet; P11654; -.
DR PhosphoSitePlus; P11654; -.
DR SwissPalm; P11654; -.
DR jPOST; P11654; -.
DR PaxDb; P11654; -.
DR PRIDE; P11654; -.
DR Ensembl; ENSRNOT00000008888; ENSRNOP00000008888; ENSRNOG00000005390.
DR GeneID; 58958; -.
DR KEGG; rno:58958; -.
DR UCSC; RGD:69339; rat.
DR CTD; 23225; -.
DR RGD; 69339; Nup210.
DR eggNOG; KOG1833; Eukaryota.
DR GeneTree; ENSGT00390000009491; -.
DR HOGENOM; CLU_001205_1_1_1; -.
DR InParanoid; P11654; -.
DR OMA; AELHIRE; -.
DR OrthoDB; 843414at2759; -.
DR PhylomeDB; P11654; -.
DR TreeFam; TF313331; -.
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 PRO; PR:P11654; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000005390; Expressed in spleen and 18 other tissues.
DR Genevisible; P11654; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; NAS:RGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR045197; NUP210-like.
DR PANTHER; PTHR23019; PTHR23019; 1.
DR Pfam; PF02368; Big_2; 1.
DR SMART; SM00635; BID_2; 1.
DR SUPFAM; SSF49373; SSF49373; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Signal; Translocation;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:2738089"
FT CHAIN 26..1886
FT /note="Nuclear pore membrane glycoprotein 210"
FT /id="PRO_0000019926"
FT TOPO_DOM 26..1805
FT /note="Perinuclear space"
FT /evidence="ECO:0000305|PubMed:1281815"
FT TRANSMEM 1806..1828
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 1829..1886
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1281815"
FT DOMAIN 1078..1151
FT /note="BIG2"
FT /evidence="ECO:0000255"
FT REGION 1866..1886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1839
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY81"
FT MOD_RES 1844
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEM1"
FT MOD_RES 1873
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEM1"
FT MOD_RES 1876
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEM1"
FT MOD_RES 1880
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8672508"
FT MOD_RES 1885
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEM1"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1039
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1886 AA; 204159 MW; 6920B93C20A6C5D1 CRC64;
MARASLIQPG LWALLLLQAV GPAVAAKLNI PKVLLPFTRA TRVNFTLEAS EGCYRWSSTR
PEVASIEPLG SSEQQCSQKA VVQARLTQPA RLTSIIFAED ITTGQVLRCD AIVDLIHGIQ
IVSTTRELYL EDSPLELKIQ ALDSEGNTFS TLAGLVFDWT IVKDTEANGF SDSHNALRIL
TFLESTYIPP SYISEMEKAA KQGDTILVSG MKTGSSKLKA RIQEAVYKNV RPAEVRLLIL
ENILLNPAYD VYLLVGTSIH YKVQKIRQGK ITELSMPSDQ YELQLQNSIP DPQGDPARPV
AVLTQDTSRV TAMQMGQSNL VLGHRSIRMQ GASRLPNSTI YVVEAGYLGF TVHPGDRWVL
ETGHLYAVTI EVFDRSSNKV YPSDNIRIEA VFPAEFFEVL SSSQNGSYHH VRAIQSGQTT
ISASLTSVVD QDGGVHVLQV PVWNQQEVDI HIPITLYPSI LTFPWQPKTG AYQYTIKAHG
GSGNFTWSSS SYMVATVTVK GVMTTGGDTG LSVIRAHDVQ NPLHFGEMKV YVIEPSSMEF
APCQVEARVG HTLELPLTIS GLMPGGSSEV VTLSDCSHFD LVVEVENQGV FQPLPGRLPP
GPEHCSGVKV RADAQGSTTL LVSYTHGHVH LGAKITLAAY LPLKAVDPSS VAVVTLGSSK
EMLFEGGPRP WVLEPSKFFR NVTSEDTGSI SLSLLGPPAS RNYQQHRVLV TCQALGEQVI
ALSVGNRPSL SNPFPAVEPT VVKSVCAPPS RLTLMPVYAL PQLDLSCPLL QQNKQVVPVS
SHRNPLLDLG AYDQQGRRFD NFSSLSIQWE SFRPLLASIE VDQPMQLVSQ DDGNGQKKLH
GLQTVSVHEA SGTTAISATA TGYQQSHLSA AGVKQLRDPL VPVSASIELI LVEDVRVSPE
EVTIYNHPGV QVELHITEGS GYFFLNTSTQ DIINVAYQDT RGVAMVHPLF PGSSTVMVHD
LCLTFPAPAK ATIHVSDIQE LYVRVVDKVE IGKAVKAYVR VLDFYKKPFL AKYFTFMDLK
LRAASQIITL VTLDEALDNY TATFLVHGVA IGQTSLSASV TDKSGQRVSS TAQQIEVFPP
FRLIPRKVTL IIGAMIQITS EGGPQPQSNI LFSINNESVA AVSSAGLVRG LMVGNGSVLG
VVQAVDAETG KVIIVSQDHV EVEVLQLQAV RIRAPITRMR TGTQMPVYVT GITSNQSPFS
FGNAVPGLTF HWSVTKRDVL DLRGRHHEVS IRLSPQYNFA MNVHGRVKGR TGLRVVVKAL
DPTAGQLHGL GKELSDEIQI QVFEKLRLLN PEVEAEQILM SPNSFIKLQT NRDGAAILSY
RVLDGPEKAP IVHIDEKGFL VSGSGIGVST LEVIAQEPFG TNQTVLVAVK VSPISYLRIS
MSPVLHTQHK EVLTALPLGM TVTFTVHFHD SSGDIFHAHN SDLNFATNRD DFVQIGKGAT
NNTCIIRTVS VGLTLLHVWD VEHLGLSDFV PLPVLQAITP ELSGAVVVGD ILCLASVLIS
LGGVSGTWSS SAGNVLYVDP KTGVAIARDA GPVTVYYEIA GHLKTFKEIV VVTPQKIVAR
RLHATQTSIQ EATASKVTVS VGDRSSNLLG ECSSAQREAI EALHPESLIS CQLQFKQDVF
DFPARDIFSV EPGFDTALGQ YLCSVTMHRL TDKQLKHLNM KKTSLAVTAS MPSSRTSVEK
VGAEVPFSPG LYANQAEILL SNHYPSSEVK IFGAVEILEN LEVRSGSPAV LASVKEKSFG
LPSFITYTVG VLDPTAGSQG PLSTALTFSS PATNQAITIP VTVAFVLDRR GPGPYGASLL
SHFLDSYQVM FFTFFALLAG TAVTIIAYHT VCAPRELASP LALTPHASPQ HSPHYLASSP
TAFNTLPSDR KASPPSGLWS PAYASH
