AHL1_ARATH
ID AHL1_ARATH Reviewed; 356 AA.
AC Q8VYJ2; Q9SZ73;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=AT-hook motif nuclear-localized protein 1 {ECO:0000303|PubMed:15604740};
GN Name=AHL1 {ECO:0000303|PubMed:15604740};
GN OrderedLocusNames=At4g12080 {ECO:0000312|Araport:AT4G12080};
GN ORFNames=F16J13_150 {ECO:0000312|EMBL:CAB40949.1};
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], GENE FAMILY, NOMENCLATURE, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF 93-GLY--PRO-95, AND FUNCTION.
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 [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 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). May
CC play a function in the positioning of chromatin fibers within the
CC nucleus. {ECO:0000269|PubMed:15604740}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:15604740}. Chromosome
CC {ECO:0000269|PubMed:15604740}. Note=Localized specifically on the
CC chromosomal surface region throughout mitotis.
CC {ECO:0000269|PubMed:15604740}.
CC -!- DOMAIN: The PPC domain mediates interactions between AHL proteins.
CC {ECO:0000269|PubMed:24218605}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB40949.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78251.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB284367; BAF37220.1; -; mRNA.
DR EMBL; AL049638; CAB40949.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161533; CAB78251.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83094.1; -; Genomic_DNA.
DR EMBL; AY070738; AAL50079.1; -; mRNA.
DR EMBL; AY149932; AAN31086.1; -; mRNA.
DR PIR; T06615; T06615.
DR RefSeq; NP_192945.2; NM_117278.4.
DR AlphaFoldDB; Q8VYJ2; -.
DR SMR; Q8VYJ2; -.
DR IntAct; Q8VYJ2; 4.
DR STRING; 3702.AT4G12080.1; -.
DR iPTMnet; Q8VYJ2; -.
DR PaxDb; Q8VYJ2; -.
DR PRIDE; Q8VYJ2; -.
DR ProteomicsDB; 244668; -.
DR EnsemblPlants; AT4G12080.1; AT4G12080.1; AT4G12080.
DR GeneID; 826816; -.
DR Gramene; AT4G12080.1; AT4G12080.1; AT4G12080.
DR KEGG; ath:AT4G12080; -.
DR Araport; AT4G12080; -.
DR TAIR; locus:2118091; AT4G12080.
DR eggNOG; ENOG502QT7J; Eukaryota.
DR HOGENOM; CLU_039808_0_0_1; -.
DR InParanoid; Q8VYJ2; -.
DR OMA; GESWSAM; -.
DR OrthoDB; 1127286at2759; -.
DR PhylomeDB; Q8VYJ2; -.
DR PRO; PR:Q8VYJ2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VYJ2; baseline and differential.
DR Genevisible; Q8VYJ2; AT.
DR GO; GO:0098687; C:chromosomal region; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR CDD; cd11378; DUF296; 1.
DR InterPro; IPR039605; AHL.
DR InterPro; IPR005175; PPC_dom.
DR PANTHER; PTHR31500; PTHR31500; 1.
DR Pfam; PF03479; PCC; 1.
DR PROSITE; PS51742; PPC; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..356
FT /note="AT-hook motif nuclear-localized protein 1"
FT /id="PRO_0000432019"
FT DOMAIN 167..309
FT /note="PPC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01078"
FT DNA_BIND 89..101
FT /note="A.T hook"
FT /evidence="ECO:0000255"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..287
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000269|PubMed:15604740"
FT MOTIF 89..97
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000303|PubMed:15604740"
FT MOTIF 295..302
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000303|PubMed:15604740"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 93..95
FT /note="GRP->AAA: Reduces DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604740"
SQ SEQUENCE 356 AA; 37312 MW; B59480020B3A5CB6 CRC64;
MVLNMESTGE AVRSTTGNDG GITVVRSDAP SDFHVAQRSE SSNQSPTSVT PPPPQPSSHH
TAPPPLQIST VTTTTTTAAM EGISGGLMKK KRGRPRKYGP DGTVVALSPK PISSAPAPSH
LPPPSSHVID FSASEKRSKV KPTNSFNRTK YHHQVENLGE WAPCSVGGNF TPHIITVNTG
EDVTMKIISF SQQGPRSICV LSANGVISSV TLRQPDSSGG TLTYEGRFEI LSLSGSFMPN
DSGGTRSRTG GMSVSLASPD GRVVGGGLAG LLVAASPVQV VVGSFLAGTD HQDQKPKKNK
HDFMLSSPTA AIPISSAADH RTIHSVSSLP VNNNTWQTSL ASDPRNKHTD INVNVT
