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AHL13_ARATH
ID   AHL13_ARATH             Reviewed;         439 AA.
AC   Q940I0; O49350; O49694;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=AT-hook motif nuclear-localized protein 13 {ECO:0000312|EMBL:FAA00284.1};
DE   AltName: Full=AT-hook protein 2 {ECO:0000312|EMBL:CAA11837.1};
GN   Name=AHL13 {ECO:0000303|PubMed:15604740};
GN   Synonyms=AHP2 {ECO:0000303|Ref.1};
GN   OrderedLocusNames=At4g17950 {ECO:0000312|Araport:AT4G17950};
GN   ORFNames=T6K21.130 {ECO:0000312|EMBL:CAA17138.1};
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].
RC   STRAIN=cv. Landsberg erecta;
RC   TISSUE=Flower bud {ECO:0000312|EMBL:CAA11837.1};
RA   Hofmann W.A., Saedler H., Huijser P.;
RT   "Novel AT-hook containing DNA binding protein from Arabidopsis.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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;
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   [5]
RP   IDENTIFICATION, GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=15604740; DOI=10.1007/s11103-004-3249-5;
RA   Fujimoto S., Matsunaga S., Yonemura M., Uchiyama S., Azuma T., Fukui K.;
RT   "Identification of a novel plant MAR DNA binding protein localized on
RT   chromosomal surfaces.";
RL   Plant Mol. Biol. 56:225-239(2004).
RN   [6]
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   GENE FAMILY, AND DOMAIN PPC.
RX   PubMed=24218605; DOI=10.1073/pnas.1219277110;
RA   Zhao J., Favero D.S., Peng H., Neff M.M.;
RT   "Arabidopsis thaliana AHL family modulates hypocotyl growth redundantly by
RT   interacting with each other via the PPC/DUF296 domain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:E4688-E4697(2013).
CC   -!- FUNCTION: Transcription factor that specifically binds AT-rich DNA
CC       sequences related to the nuclear matrix attachment regions (MARs).
CC       {ECO:0000250|UniProtKB:Q8VYJ2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8VYJ2}.
CC   -!- DOMAIN: The PPC domain mediates interactions between AHL proteins.
CC       {ECO:0000269|PubMed:24218605}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA17138.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78797.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ224119; CAA11837.1; -; mRNA.
DR   EMBL; AL021889; CAA17138.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161547; CAB78797.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE83971.1; -; Genomic_DNA.
DR   EMBL; AY054610; AAK96801.1; -; mRNA.
DR   EMBL; AY081495; AAM10057.1; -; mRNA.
DR   EMBL; BR000349; FAA00284.1; -; mRNA.
DR   PIR; T05081; T05081.
DR   PIR; T52291; T52291.
DR   RefSeq; NP_567546.1; NM_117905.3.
DR   AlphaFoldDB; Q940I0; -.
DR   SMR; Q940I0; -.
DR   IntAct; Q940I0; 10.
DR   STRING; 3702.AT4G17950.1; -.
DR   iPTMnet; Q940I0; -.
DR   PaxDb; Q940I0; -.
DR   PRIDE; Q940I0; -.
DR   ProteomicsDB; 244759; -.
DR   EnsemblPlants; AT4G17950.1; AT4G17950.1; AT4G17950.
DR   GeneID; 827520; -.
DR   Gramene; AT4G17950.1; AT4G17950.1; AT4G17950.
DR   KEGG; ath:AT4G17950; -.
DR   Araport; AT4G17950; -.
DR   TAIR; locus:2141045; AT4G17950.
DR   eggNOG; ENOG502R1P2; Eukaryota.
DR   HOGENOM; CLU_039808_7_2_1; -.
DR   InParanoid; Q940I0; -.
DR   OMA; ANMGWPK; -.
DR   OrthoDB; 1160056at2759; -.
DR   PhylomeDB; Q940I0; -.
DR   PRO; PR:Q940I0; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q940I0; baseline and differential.
DR   Genevisible; Q940I0; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IEA:InterPro.
DR   CDD; cd11378; DUF296; 1.
DR   InterPro; IPR039605; AHL.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   InterPro; IPR005175; PPC_dom.
DR   PANTHER; PTHR31500; PTHR31500; 1.
DR   Pfam; PF03479; PCC; 1.
DR   SMART; SM00384; AT_hook; 2.
DR   PROSITE; PS51742; PPC; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..439
FT                   /note="AT-hook motif nuclear-localized protein 13"
FT                   /id="PRO_0000432031"
FT   DOMAIN          217..359
FT                   /note="PPC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01078"
FT   DNA_BIND        131..143
FT                   /note="A.T hook 1"
FT                   /evidence="ECO:0000255"
FT   DNA_BIND        196..208
FT                   /note="A.T hook 2"
FT                   /evidence="ECO:0000255"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          69..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           131..139
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        8..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        416
FT                   /note="S -> F (in Ref. 1; CAA11837)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   439 AA;  46277 MW;  185B6862885676E2 CRC64;
     MDSREIHHQQ QQQQQQQQQQ QQQQQHLQQQ QQPPPGMLMS HHNSYNRNPN AAAAVLMGHN
     TSTSQAMHQR LPFGGSMSPH QPQQHQYHHP QPQQQIDQKT LESLGFDGSP SSVAATQQHS
     MRFGIDHQQV KKKRGRPRKY AADGGGGGGG GSNIALGLAP TSPLPSASNS YGGGNEGGGG
     GDSAGANANS SDPPAKRNRG RPPGSGKKQL DALGGTGGVG FTPHVIEVKT GEDIATKILA
     FTNQGPRAIC ILSATGAVTN VMLRQANNSN PTGTVKYEGR FEIISLSGSF LNSESNGTVT
     KTGNLSVSLA GHEGRIVGGC VDGMLVAGSQ VQVIVGSFVP DGRKQKQSAG RAQNTPEPAS
     APANMLSFGG VGGPGSPRSQ GQQHSSESSE ENESNSPLHR RSNNNNSNNH GIFGNSTPQP
     LHQIPMQMYQ NLWPGNSPQ
 
 
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