NUP50_RAT
ID NUP50_RAT Reviewed; 467 AA.
AC O08587; Q4QR93;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Nuclear pore complex protein Nup50;
DE AltName: Full=50 kDa nucleoporin;
DE AltName: Full=Nuclear pore-associated protein 60 kDa-like;
DE AltName: Full=Nucleoporin Nup50;
GN Name=Nup50; Synonyms=Npap60;
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 SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=9073512; DOI=10.1006/geno.1996.4557;
RA Fan F., Liu C.-P., Korobova O., Heyting C., Offenberg H.H., Trump G.,
RA Arnheim N.;
RT "cDNA cloning and characterization of Npap60: a novel rat nuclear pore-
RT associated protein with an unusual subcellular localization during male
RT germ cell differentiation.";
RL Genomics 40:444-453(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION OF FRAMESHIFT, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley;
RX PubMed=10891499; DOI=10.1128/mcb.20.15.5619-5630.2000;
RA Guan T., Kehlenbach R.H., Schirmer E.C., Kehlenbach A., Fan F.,
RA Clurman B.E., Arnheim N., Gerace L.;
RT "Nup50, a nucleoplasmically oriented nucleoporin with a role in nuclear
RT protein export.";
RL Mol. Cell. Biol. 20:5619-5630(2000).
CC -!- FUNCTION: Component of the nuclear pore complex that has a direct role
CC in nuclear protein import. Actively displaces NLSs from importin-alpha,
CC and facilitates disassembly of the importin-alpha:beta-cargo complex
CC and importin recycling. Interacts with regulatory proteins of cell
CC cycle progression including CDKN1B. This interaction is required for
CC correct intracellular transport and degradation of CDKN1B.
CC {ECO:0000250|UniProtKB:Q9JIH2}.
CC -!- SUBUNIT: Does not interact with TPR (By similarity). Interacts with
CC Importin alpha-2, Importin beta, Importin beta-2, NUP153, Ran binding
CC protein 7, CDKN1B and itself. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10891499}. Nucleus membrane
CC {ECO:0000269|PubMed:10891499}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10891499}; Nucleoplasmic side
CC {ECO:0000269|PubMed:10891499}. Note=Dissociates from the NPC structure
CC early during prophase of mitosis (By similarity). Associates with the
CC newly formed nuclear membrane during telophase (By similarity).
CC Localizes to the nucleoplasmic fibrils of the nuclear pore complex
CC (PubMed:10891499). In the testis, the localization changes during germ
CC cell differentiation from the nuclear surface in spermatocytes to the
CC whole nucleus (interior) in spermatids and back to the nuclear surface
CC in spermatozoa (PubMed:9073512). {ECO:0000250|UniProtKB:Q9UKX7,
CC ECO:0000269|PubMed:10891499, ECO:0000269|PubMed:9073512}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, intermediate levels in
CC kidney, liver, spleen and low basal levels in somatic cells. Expression
CC in testis undergoes changes and subcellular localization during germ
CC cell differentiation.
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}.
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DR EMBL; U41845; AAC53278.2; -; mRNA.
DR EMBL; BC097337; AAH97337.1; -; mRNA.
DR RefSeq; NP_037123.1; NM_012991.1.
DR AlphaFoldDB; O08587; -.
DR SMR; O08587; -.
DR BioGRID; 247530; 1.
DR CORUM; O08587; -.
DR STRING; 10116.ENSRNOP00000018155; -.
DR iPTMnet; O08587; -.
DR PhosphoSitePlus; O08587; -.
DR jPOST; O08587; -.
DR PaxDb; O08587; -.
DR PRIDE; O08587; -.
DR GeneID; 25497; -.
DR KEGG; rno:25497; -.
DR CTD; 10762; -.
DR RGD; 3191; Nup50.
DR eggNOG; KOG2724; Eukaryota.
DR InParanoid; O08587; -.
DR OrthoDB; 793797at2759; -.
DR PhylomeDB; O08587; -.
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:O08587; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:RGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0001841; P:neural tube formation; ISO:RGD.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR015007; NUP2/50/61.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR PANTHER; PTHR23138; PTHR23138; 1.
DR Pfam; PF08911; NUP50; 1.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR PROSITE; PS50196; RANBD1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; Ubl conjugation.
FT CHAIN 1..467
FT /note="Nuclear pore complex protein Nup50"
FT /id="PRO_0000204870"
FT REPEAT 76..77
FT /note="1"
FT REPEAT 113..114
FT /note="2"
FT REPEAT 226..227
FT /note="3"
FT REPEAT 272..273
FT /note="4"
FT REPEAT 302..303
FT /note="5"
FT DOMAIN 334..467
FT /note="RanBD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..303
FT /note="5 X 2 AA repeats of F-G"
FT REGION 84..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..206
FT /note="Binding to CDKN1B"
FT /evidence="ECO:0000250"
FT REGION 201..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH2"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKX7"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKX7"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH2"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKX7"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH2"
FT MOD_RES 247
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKX7"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKX7"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKX7"
FT MOD_RES 449
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH2"
FT CROSSLNK 352
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKX7"
FT CONFLICT 211
FT /note="R -> S (in Ref. 2; AAH97337)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="V -> A (in Ref. 2; AAH97337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 49818 MW; CF213296F37F0884 CRC64;
MAKRVAEKEL TDRNWDEEDE VEEMGTFSVA SEEVMKNRAV KKAKRRNIGF ESDSGGAFKG
FKGLVVPSGG GGFSGFGGGS GGKPLEGLTN GNSTDSATPF SSAKTAAEPK AAFGSFAVNG
PTTLVDKKIS SPKCNSSNQP PSSGPASSTS CTGNTYHKQL AGLNCSVRDW IVKHVNTNPL
CDLTPIFKDY ERYLATIEKQ LENGGSSSSE RQTDRATAAM EPPSLFGSTK LQQDSPFSFH
GNKAEDTSEK LEFTAEKKSD AAQGATSASF NFGKKIESSV LGSLSSGSLT GFSFSPGNSS
LFGKDAAQSK AASSPFSAKA SESQAGGSSS ECRDGEEEES DEPPKVVVTE VKEEDAFYSK
KCKLFYKKDN EFKEKGVGTL HLKPTATQKT QLLVRADTNL GNILLNVLIP PNMPCTRTGK
NNVLIVCVPN PPLDEKQPTL PVTMLIRVKT SEDADELHKI LLQKKDV
