ID   NU50B_ARATH             Reviewed;         465 AA.
AC   Q9LW88; Q8GXC8; Q8LG62;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=Nuclear pore complex protein NUP50B {ECO:0000303|PubMed:21189294};
DE   AltName: Full=Nucleoporin 50B;
GN   Name=NUP50B {ECO:0000303|PubMed:21189294};
GN   OrderedLocusNames=At3g15970 {ECO:0000312|Araport:AT3G15970};
GN   ORFNames=MSL1.1 {ECO:0000312|EMBL:BAB02663.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 392-465.
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
RP   IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, SUBCELLULAR LOCATION, FUNCTION,
RP   AND NOMENCLATURE.
RX   PubMed=21189294; DOI=10.1105/tpc.110.079947;
RA   Tamura K., Fukao Y., Iwamoto M., Haraguchi T., Hara-Nishimura I.;
RT   "Identification and characterization of nuclear pore complex components in
RT   Arabidopsis thaliana.";
RL   Plant Cell 22:4084-4097(2010).
CC   -!- FUNCTION: Probably involved in nucleocytoplasmic transport via its
CC       interactions with importins and Ran, rather than by forming part of the
CC       nuclear pore complex (NPC) scaffolding. {ECO:0000305|PubMed:21189294}.
CC   -!- SUBUNIT: Part of the nuclear pore complex (NPC). The NPC has an eight-
CC       fold symmetrical structure comprising a central transport channel and
CC       two rings, the cytoplasmic and nuclear rings, to which eight filaments
CC       are attached. The cytoplasmic filaments have loose ends, while the
CC       nuclear filaments are joined in a distal ring, forming a nuclear
CC       basket. NPCs are highly dynamic in configuration and composition, and
CC       can be devided in 3 subcomplexes, the NUP62 subcomplex, the NUP107-160
CC       subcomplex and the NUP93 subcomplex, containing approximately 30
CC       different nucleoporin proteins. {ECO:0000305|PubMed:21189294}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex
CC       {ECO:0000305|PubMed:21189294}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC42920.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB012247; BAB02663.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75754.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM64912.1; -; Genomic_DNA.
DR   EMBL; AY084443; AAM61016.1; -; mRNA.
DR   EMBL; AK118302; BAC42920.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001326913.1; NM_001338194.1.
DR   RefSeq; NP_566532.1; NM_112467.3.
DR   AlphaFoldDB; Q9LW88; -.
DR   SMR; Q9LW88; -.
DR   BioGRID; 6175; 2.
DR   IntAct; Q9LW88; 1.
DR   STRING; 3702.AT3G15970.1; -.
DR   iPTMnet; Q9LW88; -.
DR   PaxDb; Q9LW88; -.
DR   PRIDE; Q9LW88; -.
DR   ProteomicsDB; 248662; -.
DR   EnsemblPlants; AT3G15970.1; AT3G15970.1; AT3G15970.
DR   EnsemblPlants; AT3G15970.2; AT3G15970.2; AT3G15970.
DR   GeneID; 820841; -.
DR   Gramene; AT3G15970.1; AT3G15970.1; AT3G15970.
DR   Gramene; AT3G15970.2; AT3G15970.2; AT3G15970.
DR   KEGG; ath:AT3G15970; -.
DR   Araport; AT3G15970; -.
DR   TAIR; locus:2093372; AT3G15970.
DR   eggNOG; KOG0864; Eukaryota.
DR   HOGENOM; CLU_050764_1_0_1; -.
DR   InParanoid; Q9LW88; -.
DR   OMA; VMFEYLE; -.
DR   OrthoDB; 1322172at2759; -.
DR   PhylomeDB; Q9LW88; -.
DR   PRO; PR:Q9LW88; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LW88; baseline and differential.
DR   Genevisible; Q9LW88; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR   CDD; cd13169; RanBD_NUP50_plant; 1.
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; IPR045207; RanBD_NUP50_plant.
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   1: Evidence at protein level;
KW   Acetylation; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C829"
FT   CHAIN           2..465
FT                   /note="Nuclear pore complex protein NUP50B"
FT                   /id="PRO_0000431081"
FT   REPEAT          266..267
FT                   /note="1"
FT   REPEAT          286..287
FT                   /note="2"
FT   REPEAT          297..298
FT                   /note="3"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          59..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..298
FT                   /note="3 X 2 AA repeats of F-G"
FT   REGION          308..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C829"
FT   MOD_RES         125
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C829"
FT   MOD_RES         455
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C829"
FT   MOD_RES         459
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C829"
FT   CONFLICT        223
FT                   /note="G -> C (in Ref. 3; AAM61016)"
FT   CONFLICT        382
FT                   /note="T -> I (in Ref. 3; AAM61016)"
SQ   SEQUENCE   465 AA;  49108 MW;  FC3CA51234EE9CAC CRC64;
     MGDSDNAIPF SRKRTALKEL SRDNPGLDDD DEDTSALESG TFNTASKEVL ASRRIIRVRR
     TDRSATAPPA SNPFTGIRLV PFTAPAPSTA AAETTKPLSA GKQETLADGR SDATKETDGD
     SKEKSDAIDA VGKQETQGDE ISAKTKDIID GGEKEMSEAV NSVEGGGAVN KNEDEIKTTM
     VTEVAAGEET VKDDNNNSNT VEGSDCVVKD TGGNQTEKEG KEGDGNEDTE KNGDSGALSS
     FHQHSSSKNA FTGLASTGFS ASSFSFGLVP QEGSTGSGSE QSSFSFGQAN NGNSSLFGAS
     VATSITTKST ETTTAFPSKQ DVSVETGEEN EKAAFTADSV MFEYLEGGWK ERGKGELKVN
     ISTTENRKAR LVMRSKGNYR LTLNASLYPE MKLAKMDKKG ITFACVNSVS DAKDGLSTLA
     LKFKDPTVVE EFRAVIEEHK DSKPSVAEAA APLKTPENSP SAEDA