ALP1_ARATH
ID ALP1_ARATH Reviewed; 396 AA.
AC Q94K49; Q9M1W3;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein ANTAGONIST OF LIKE HETEROCHROMATIN PROTEIN 1 {ECO:0000303|PubMed:26642436};
DE EC=3.1.-.-;
GN Name=ALP1 {ECO:0000303|PubMed:26642436};
GN OrderedLocusNames=At3g63270 {ECO:0000312|Araport:AT3G63270};
GN ORFNames=F16M2.120 {ECO:0000312|EMBL:CAB86428.1};
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 [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 [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 FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-273.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=22837357; DOI=10.1104/pp.112.200311;
RA Hartwig B., James G.V., Konrad K., Schneeberger K., Turck F.;
RT "Fast isogenic mapping-by-sequencing of ethyl methanesulfonate-induced
RT mutant bulks.";
RL Plant Physiol. 160:591-600(2012).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, INTERACTION WITH CLF; MSI1; FIE;
RP EMF2 AND VRN2, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=26642436; DOI=10.1371/journal.pgen.1005660;
RA Liang S.C., Hartwig B., Perera P., Mora-Garcia S., de Leau E., Thornton H.,
RA de Lima Alves F., de Alves F.L., Rappsilber J., Rapsilber J., Yang S.,
RA James G.V., Schneeberger K., Finnegan E.J., Turck F., Goodrich J.;
RT "Kicking against the PRCs - A domesticated transposase antagonises
RT silencing mediated by polycomb group proteins and is an accessory component
RT of polycomb repressive complex 2.";
RL PLoS Genet. 11:E1005660-E1005660(2015).
RN [6]
RP REVIEW.
RX PubMed=27253527; DOI=10.1371/journal.pgen.1006014;
RA Ricci W.A., Zhang X.;
RT "Public service by a selfish gene: A domesticated transposase antagonizes
RT polycomb function.";
RL PLoS Genet. 12:E1006014-E1006014(2016).
CC -!- FUNCTION: Transposase-derived protein that may have nuclease activity
CC (Probable). Antagonist of polycomb-group (PcG) protein-mediated
CC chromatin silencing, probably by preventing the association of POLYCOMB
CC REPRESSIVE COMPLEX 2 (PRC2) with its accessory components. Needed for
CC full reactivation of several floral homeotic genes that are repressed
CC by PcG (PubMed:26642436). {ECO:0000269|PubMed:26642436, ECO:0000305}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q96MB7};
CC -!- SUBUNIT: Interacts with core components of POLYCOMB REPRESSIVE COMPLEX
CC 2 (PRC2), a PcG protein complex with H3K27me3 histone methyltransferase
CC activity. Associates with plant-specific PRC2 accessory components such
CC as MSI1, EMF2, VRN2, FIE and CLF. {ECO:0000269|PubMed:26642436}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:26642436}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, inflorescence stems, seedlings,
CC leaves, flower buds, inflorescences, and siliques.
CC {ECO:0000269|PubMed:26642436}.
CC -!- DISRUPTION PHENOTYPE: Suppression of PcG defects in several PRC1 and
CC PRC2 components including lhp1 (in alp1-2 and alp1-3 mutants) and clf
CC (in alp1-3 and alp1-4 mutants) phenotypes (PubMed:26642436,
CC PubMed:22837357). In alp1-4, weak downward curling and slightly late
CC flowering in short days. Increases synergistically ult1 and ult2 floral
CC organ defects in double mutants alp1-3 ult1 and alp1-3 ult2. The double
CC mutant alp1-3 efs has a stronger dwarf, branched phenotype than efs
CC single mutant (PubMed:26642436). {ECO:0000269|PubMed:22837357,
CC ECO:0000269|PubMed:26642436}.
CC -!- SIMILARITY: Belongs to the HARBI1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB86428.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL138648; CAB86428.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80459.1; -; Genomic_DNA.
DR EMBL; AF370300; AAK44115.1; -; mRNA.
DR EMBL; AY063087; AAL34261.1; -; mRNA.
DR PIR; T48116; T48116.
DR RefSeq; NP_567144.1; NM_116192.4.
DR AlphaFoldDB; Q94K49; -.
DR STRING; 3702.AT3G63270.1; -.
DR PaxDb; Q94K49; -.
DR PRIDE; Q94K49; -.
DR ProteomicsDB; 244958; -.
DR EnsemblPlants; AT3G63270.1; AT3G63270.1; AT3G63270.
DR GeneID; 825502; -.
DR Gramene; AT3G63270.1; AT3G63270.1; AT3G63270.
DR KEGG; ath:AT3G63270; -.
DR Araport; AT3G63270; -.
DR TAIR; locus:2077259; AT3G63270.
DR eggNOG; KOG4585; Eukaryota.
DR HOGENOM; CLU_018552_3_4_1; -.
DR InParanoid; Q94K49; -.
DR OMA; MFLMTYM; -.
DR OrthoDB; 822378at2759; -.
DR PhylomeDB; Q94K49; -.
DR PRO; PR:Q94K49; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94K49; baseline and differential.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0035102; C:PRC1 complex; IMP:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IPI:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR InterPro; IPR045249; HARBI1-like.
DR InterPro; IPR027806; HARBI1_dom.
DR PANTHER; PTHR22930; PTHR22930; 1.
DR Pfam; PF13359; DDE_Tnp_4; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Nuclease; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..396
FT /note="Protein ANTAGONIST OF LIKE HETEROCHROMATIN PROTEIN
FT 1"
FT /id="PRO_0000438514"
FT DOMAIN 183..348
FT /note="DDE Tnp4"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..13
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..26
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 273
FT /note="G->E: In alp1-1; suppression of lhp1 phenotype."
FT /evidence="ECO:0000269|PubMed:22837357"
SQ SEQUENCE 396 AA; 44972 MW; C2E3E01C6AA40509 CRC64;
MAPVKQKKKN KKKPLDKAKK LAKNKEKKRV NAVPLDPEAI DCDWWDTFWL RNSSPSVPSD
EDYAFKHFFR ASKTTFSYIC SLVREDLISR PPSGLINIEG RLLSVEKQVA IALRRLASGD
SQVSVGAAFG VGQSTVSQVT WRFIEALEER AKHHLRWPDS DRIEEIKSKF EEMYGLPNCC
GAIDTTHIIM TLPAVQASDD WCDQEKNYSM FLQGVFDHEM RFLNMVTGWP GGMTVSKLLK
FSGFFKLCEN AQILDGNPKT LSQGAQIREY VVGGISYPLL PWLITPHDSD HPSDSMVAFN
ERHEKVRSVA ATAFQQLKGS WRILSKVMWR PDRRKLPSII LVCCLLHNII IDCGDYLQED
VPLSGHHDSG YADRYCKQTE PLGSELRGCL TEHLLR
