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HASTY_ARATH
ID   HASTY_ARATH             Reviewed;        1202 AA.
AC   Q0WP44; Q84UC4; Q9CAW7;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Protein HASTY 1;
DE   AltName: Full=Protein HASTY;
GN   Name=HST1; Synonyms=HASTY; OrderedLocusNames=At3g05040; ORFNames=T9J14.1;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, INTERACTION WITH RAN1, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP   OF 36-ASP--SER-37.
RX   PubMed=12620976; DOI=10.1242/dev.00362;
RA   Bollman K.M., Aukerman M.J., Park M.Y., Hunter C., Berardini T.Z.,
RA   Poethig R.S.;
RT   "HASTY, the Arabidopsis ortholog of exportin 5/MSN5, regulates phase change
RT   and morphogenesis.";
RL   Development 130:1493-1504(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15738428; DOI=10.1073/pnas.0405570102;
RA   Park M.Y., Wu G., Gonzalez-Sulser A., Vaucheret H., Poethig R.S.;
RT   "Nuclear processing and export of microRNAs in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3691-3696(2005).
RN   [6]
RP   FUNCTION.
RX   PubMed=16914499; DOI=10.1242/dev.02521;
RA   Wu G., Poethig R.S.;
RT   "Temporal regulation of shoot development in Arabidopsis thaliana by miR156
RT   and its target SPL3.";
RL   Development 133:3539-3547(2006).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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: Nucleocytoplasmic transporter involved in the nuclear export
CC       of microRNAs (miRNAs). Required for several miRNAs accumulation.
CC       Specifically required for miR156 accumulation which targets SPL3, SPL4
CC       and SPL5 transcription factors. Involved in plant development through
CC       its role in miRNAs processing. Required for vegetative phase change and
CC       vegetative to reproductive phase transition. Functionally dependent on
CC       RAN1 binding. Does not seem to be involved in small interfering RNAs
CC       (siRNAs) processing. {ECO:0000269|PubMed:12620976,
CC       ECO:0000269|PubMed:15738428, ECO:0000269|PubMed:16914499}.
CC   -!- SUBUNIT: Interacts with RAN1. {ECO:0000269|PubMed:12620976}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12620976}.
CC       Note=Nuclear periphery.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves and floral buds.
CC       {ECO:0000269|PubMed:12620976}.
CC   -!- DISRUPTION PHENOTYPE: Reduced size of roots and shoot lateral organs.
CC       Accelerated vegetative phase change. Increased adaxial trichome
CC       density. Disruption of phyllotaxis of the inflorescence. Reduced
CC       fertility. Reduced levels of several miRNAs and increased levels of
CC       their targeted transcripts. {ECO:0000269|PubMed:12620976,
CC       ECO:0000269|PubMed:15738428}.
CC   -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG51401.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY198396; AAO34666.1; -; mRNA.
DR   EMBL; AC009465; AAG51401.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE74179.1; -; Genomic_DNA.
DR   EMBL; AK229239; BAF01105.1; -; mRNA.
DR   RefSeq; NP_187155.2; NM_111376.4.
DR   AlphaFoldDB; Q0WP44; -.
DR   SMR; Q0WP44; -.
DR   BioGRID; 5001; 1.
DR   IntAct; Q0WP44; 1.
DR   STRING; 3702.AT3G05040.1; -.
DR   iPTMnet; Q0WP44; -.
DR   PaxDb; Q0WP44; -.
DR   ProteomicsDB; 230370; -.
DR   EnsemblPlants; AT3G05040.1; AT3G05040.1; AT3G05040.
DR   GeneID; 819666; -.
DR   Gramene; AT3G05040.1; AT3G05040.1; AT3G05040.
DR   KEGG; ath:AT3G05040; -.
DR   Araport; AT3G05040; -.
DR   TAIR; locus:2114784; AT3G05040.
DR   eggNOG; KOG2020; Eukaryota.
DR   HOGENOM; CLU_004265_0_0_1; -.
DR   InParanoid; Q0WP44; -.
DR   OMA; WPDDPDR; -.
DR   PhylomeDB; Q0WP44; -.
DR   PRO; PR:Q0WP44; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q0WP44; baseline and differential.
DR   Genevisible; Q0WP44; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0042565; C:RNA nuclear export complex; IBA:GO_Central.
DR   GO; GO:0005049; F:nuclear export signal receptor activity; IMP:TAIR.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR   GO; GO:0061716; P:miRNA export from nucleus; IMP:UniProtKB.
DR   GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR.
DR   GO; GO:0009944; P:polarity specification of adaxial/abaxial axis; IMP:TAIR.
DR   GO; GO:0006611; P:protein export from nucleus; IEA:InterPro.
DR   GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0048364; P:root development; IMP:TAIR.
DR   GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR013598; Exportin-1/Importin-b-like.
DR   InterPro; IPR045478; Exportin-5_C.
DR   InterPro; IPR045065; XPO1/5.
DR   InterPro; IPR040018; XPO5.
DR   PANTHER; PTHR11223; PTHR11223; 1.
DR   PANTHER; PTHR11223:SF3; PTHR11223:SF3; 1.
DR   Pfam; PF19273; Exportin-5; 1.
DR   Pfam; PF08389; Xpo1; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleus; Reference proteome; RNA-mediated gene silencing;
KW   Transport.
FT   CHAIN           1..1202
FT                   /note="Protein HASTY 1"
FT                   /id="PRO_0000404657"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MUTAGEN         36..37
FT                   /note="DS->A: In hst-3; loss of binding to RAN1 and miRNA
FT                   transport function."
FT                   /evidence="ECO:0000269|PubMed:12620976"
FT   CONFLICT        695
FT                   /note="Q -> H (in Ref. 1; AAO34666)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1202 AA;  133128 MW;  4D114554F8127493 CRC64;
     MEDSNSTASN VARAILAVVD FSSTSDTRKS AVQFLDSVKS GDVRVLAKTS FHLVKKEWSS
     EIRLHAFKML QHLVRLRWDE LSPPECRGLV NLSIELMSEV ANASENWPLK SQSAALVAEI
     VRREGPDRWQ EIFTLLTSLS AQGPLQAELV LMTLRWLPED ITIYNDDLEG DRRRLLLRGL
     TQSLPEILPL LYNLLERHFG AAMSEAGMQH FDLAKQHADV VIACLNAIVA YTEWAPVPDL
     ARYGILSGCS FLLSSSDFRL HACEVFKLVC SRKRPSDAST AEFDSAISNL FQILTNASRE
     FLCRSSSSSS VIDDNDYDFA VCMCESMASL GSTNLQSISS DGGVMAVYLQ QMLGFFQHFK
     LGLHFEALLF WLSLMRDLLP KPKAATYPSG GGSSTGGDDS SSQVDSEKKK TLSLINDDIS
     SAILDVSFQR MLKKEKVPTG IALSLGPLEL WSDEFEGKGD FGPYRSKLLE LIKLTASHKP
     LISSTKISER VITLIKHLLA SPAPLQHVAV MDSQQLALDC IVATLFDGSN EFAGGSSEVH
     YALRGIFEGL LQQLLSLKWN EPELMKVHVH YLDAMGPFLK YFPDAVGSLI NKLFELLTSL
     PHVVKDPATS TSRAARLQIC TSFIRIAKAA EKSVLPHMKG IADTMGYLAK EGTLLRGEHN
     ILGEAFLVMA SSAGAQQQQE VLAWLLEPLS QQWIQPEWQN NYLSDPMGLV RLCSNTSFMW
     SIYHTVTFFE KALKRSGYRK SNLNTTSATT PASHPMAHHL SWMLPPLLKL LRVLHSLWSP
     SVFQTLPPEM RAAMTMTDAE RYSLLGEANP KLSKGVSVYA DGSFEGTKEG QAEASESDIR
     NWLKGIRDCG YNVLGLSTTI GETFFKCLDA NYVAMALMEN LQSMEFRHIR LFIHTFITYI
     VKSCPADMWE SWLGVLLHPL FIHCQQALSS AWPGLLQEGR AKVPDLFGIQ SGSDMKLEVM
     EEKLLRDLTR EIATLFSTMA SPGLNTGVPV LEHSGHVGRV DMSTLTDLHA FRSNSMVGFL
     LNHKSVALPA LQICLETFTW TDGEATTKVC YFCGVVVLLA KLTNNVELRE FVSKDMFSAV
     IRGLGMESNA INSPDLVNIC REIFIYLSDR DPAPRQVLLS LPCLTPNDLH AFEEATAKTS
     SPKEQKQLMR SLLLLGTGNN LKALAAQKSQ NVITNVTART RLPASAPETI GAGVLWDEEF
     VQ
 
 
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