ALFL7_ARATH
ID ALFL7_ARATH Reviewed; 252 AA.
AC Q8LA16; Q9M9R2; Q9MA31;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=PHD finger protein ALFIN-LIKE 7;
DE Short=Protein AL7;
GN Name=AL7; OrderedLocusNames=At1g14510; ORFNames=F14L17.29, T5E21.1;
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=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 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, SUBCELLULAR LOCATION, INTERACTION WITH HISTONES H3K4ME3 AND
RP H3K4ME2, DOMAIN PHD-TYPE ZINC-FINGER, TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF TYR-205; TRP-211; ASP-215 AND GLU-218.
RX PubMed=19154204; DOI=10.1111/j.1365-313x.2009.03795.x;
RA Lee W.Y., Lee D., Chung W.I., Kwon C.S.;
RT "Arabidopsis ING and Alfin1-like protein families localize to the nucleus
RT and bind to H3K4me3/2 via plant homeodomain fingers.";
RL Plant J. 58:511-524(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Histone-binding component that specifically recognizes H3
CC tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription
CC start sites of virtually all active genes. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2.
CC {ECO:0000269|PubMed:19154204}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19154204}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:19154204}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000269|PubMed:19154204}.
CC -!- SIMILARITY: Belongs to the Alfin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF43952.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF63181.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010657; AAF63181.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC012188; AAF43952.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29173.1; -; Genomic_DNA.
DR EMBL; BT006199; AAP12848.1; -; mRNA.
DR EMBL; AK228067; BAF00027.1; -; mRNA.
DR EMBL; AY088087; AAM65633.1; -; mRNA.
DR PIR; A86280; A86280.
DR RefSeq; NP_172903.1; NM_101318.4.
DR PDB; 5XVJ; X-ray; 1.40 A; A/B=9-141.
DR PDBsum; 5XVJ; -.
DR AlphaFoldDB; Q8LA16; -.
DR SMR; Q8LA16; -.
DR BioGRID; 23253; 13.
DR IntAct; Q8LA16; 5.
DR STRING; 3702.AT1G14510.1; -.
DR iPTMnet; Q8LA16; -.
DR PaxDb; Q8LA16; -.
DR PRIDE; Q8LA16; -.
DR ProteomicsDB; 244980; -.
DR EnsemblPlants; AT1G14510.1; AT1G14510.1; AT1G14510.
DR GeneID; 838013; -.
DR Gramene; AT1G14510.1; AT1G14510.1; AT1G14510.
DR KEGG; ath:AT1G14510; -.
DR Araport; AT1G14510; -.
DR TAIR; locus:2012577; AT1G14510.
DR eggNOG; KOG1632; Eukaryota.
DR HOGENOM; CLU_058315_1_0_1; -.
DR InParanoid; Q8LA16; -.
DR OMA; KFYHQCD; -.
DR OrthoDB; 1180726at2759; -.
DR PhylomeDB; Q8LA16; -.
DR PRO; PR:Q8LA16; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LA16; baseline and differential.
DR Genevisible; Q8LA16; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd15613; PHD_AL_plant; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045104; Alfin.
DR InterPro; IPR021998; Alfin_N.
DR InterPro; IPR044104; PHD_AL_plant.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12321; PTHR12321; 1.
DR Pfam; PF12165; Alfin; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..252
FT /note="PHD finger protein ALFIN-LIKE 7"
FT /id="PRO_0000412934"
FT ZN_FING 195..247
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 141..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 205
FT /note="Histone H3K4me3 binding"
FT SITE 211
FT /note="Histone H3K4me3 binding"
FT SITE 215
FT /note="Histone H3K4me3 binding"
FT SITE 220
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MUTAGEN 205
FT /note="Y->L: Slightly affects binding to H3K4me2/3."
FT /evidence="ECO:0000269|PubMed:19154204"
FT MUTAGEN 211
FT /note="W->M: Abolishes binding to H3K4me2/3."
FT /evidence="ECO:0000269|PubMed:19154204"
FT MUTAGEN 215
FT /note="D->N: Abolishes binding to H3K4me2/3."
FT /evidence="ECO:0000269|PubMed:19154204"
FT MUTAGEN 218
FT /note="E->Q: Does not affect binding to H3K4me2/3."
FT /evidence="ECO:0000269|PubMed:19154204"
FT HELIX 10..30
FT /evidence="ECO:0007829|PDB:5XVJ"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:5XVJ"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:5XVJ"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:5XVJ"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:5XVJ"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:5XVJ"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:5XVJ"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:5XVJ"
FT HELIX 87..112
FT /evidence="ECO:0007829|PDB:5XVJ"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:5XVJ"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:5XVJ"
SQ SEQUENCE 252 AA; 28286 MW; 09D4D4F3D531E5E4 CRC64;
MEGIQHPIPR TVEEVFSDFR GRRAGLIKAL STDVQKFYHQ CDPEKENLCL YGLPNETWEV
NLPVEEVPPE LPEPALGINF ARDGMQEKDW ISLVAVHSDS WLISVAFYFG ARFGFGKNER
KRLFQMINDL PTIFEVVTGN AKQSKDQSAN HNSSRSKSSG GKPRHSESHT KASKMSPPPR
KEDESGDEDE DDEQGAVCGA CGDNYGGDEF WICCDACEKW FHGKCVKITP AKAEHIKHYK
CPSCTTSKKM KA
