NU50A_ARATH
ID NU50A_ARATH Reviewed; 440 AA.
AC Q9C829; Q8L6Y2;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Nuclear pore complex protein NUP50A {ECO:0000303|PubMed:21189294};
DE AltName: Full=Nucleoporin 50A;
GN Name=NUP50A {ECO:0000303|PubMed:21189294};
GN OrderedLocusNames=At1g52380 {ECO:0000312|Araport:AT1G52380};
GN ORFNames=F19K6.4 {ECO:0000312|EMBL:AAG51549.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-430 AND SER-434, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; THR-430 AND SER-434, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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 -!- DOMAIN: Contains FG repeats mediating the translocation through the NPC
CC by interacting with transport factors. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM98235.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC037424; AAG51549.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32797.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59970.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59971.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59972.1; -; Genomic_DNA.
DR EMBL; AY037180; AAK59765.1; -; mRNA.
DR EMBL; AY059149; AAL15374.1; -; mRNA.
DR EMBL; AY140094; AAM98235.1; ALT_INIT; mRNA.
DR PIR; A96564; A96564.
DR RefSeq; NP_001322286.1; NM_001333543.1.
DR RefSeq; NP_001322287.1; NM_001333541.1.
DR RefSeq; NP_001322288.1; NM_001333542.1.
DR RefSeq; NP_564606.1; NM_104116.4.
DR AlphaFoldDB; Q9C829; -.
DR SMR; Q9C829; -.
DR BioGRID; 26893; 59.
DR IntAct; Q9C829; 1.
DR STRING; 3702.AT1G52380.1; -.
DR iPTMnet; Q9C829; -.
DR PaxDb; Q9C829; -.
DR PRIDE; Q9C829; -.
DR ProteomicsDB; 250524; -.
DR EnsemblPlants; AT1G52380.1; AT1G52380.1; AT1G52380.
DR EnsemblPlants; AT1G52380.2; AT1G52380.2; AT1G52380.
DR EnsemblPlants; AT1G52380.3; AT1G52380.3; AT1G52380.
DR EnsemblPlants; AT1G52380.4; AT1G52380.4; AT1G52380.
DR GeneID; 841668; -.
DR Gramene; AT1G52380.1; AT1G52380.1; AT1G52380.
DR Gramene; AT1G52380.2; AT1G52380.2; AT1G52380.
DR Gramene; AT1G52380.3; AT1G52380.3; AT1G52380.
DR Gramene; AT1G52380.4; AT1G52380.4; AT1G52380.
DR KEGG; ath:AT1G52380; -.
DR Araport; AT1G52380; -.
DR TAIR; locus:2018204; AT1G52380.
DR eggNOG; KOG0864; Eukaryota.
DR HOGENOM; CLU_050764_1_0_1; -.
DR InParanoid; Q9C829; -.
DR OMA; EFRVAID; -.
DR OrthoDB; 1322172at2759; -.
DR PhylomeDB; Q9C829; -.
DR PRO; PR:Q9C829; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C829; baseline and differential.
DR Genevisible; Q9C829; 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:0007744|PubMed:22223895"
FT CHAIN 2..440
FT /note="Nuclear pore complex protein NUP50A"
FT /id="PRO_0000431080"
FT REPEAT 245..246
FT /note="1"
FT REPEAT 260..261
FT /note="2"
FT REPEAT 262..263
FT /note="3"
FT REPEAT 273..274
FT /note="4"
FT DOMAIN 291..410
FT /note="RanBD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..274
FT /note="4 X 2 AA repeats of F-G"
FT REGION 283..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 430
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
SQ SEQUENCE 440 AA; 46592 MW; 6CCC7FA29C17B809 CRC64;
MGDSENVQQP SKKRGALKQL SRDNPGLDDD DDSAELESGT FKKASDEVLA SRRIVRVKRK
EPSAAPVAAS NPFAGIQLVP TTAPASTPVG TNAPLAESKL APAEAVVEDN QKASDIEEGD
EVDSKKVDVK DAVGEETEKT KDKDDNHCGK SADVQVAATE VAQMVSCDTN VCNNAVEGTD
QTDFPLEKDS GGDQAEKKEK EGNGIEEADK NGDNGAFSSF QQHSSNKNAF TGLASTEASG
SSFSFGLVSQ DGSTGTGSLF GFGLPSSNSS SIFGATGSSI IKKSEGSGFP PKQEVSTETG
EENEKVAFSA DSIMFEYLDG GWKERGKGEL KVNVSSNDGK ARLVMRAKGN YRLILNASLY
PEMKLANMDK KGITFACVNS VSEGKEGLST FALKFKDPTI VEEFRVAIDK HKDSKPMEKA
AEKSALPLKT PENSPTATDT
