HMGYA_MAIZE
ID HMGYA_MAIZE Reviewed; 193 AA.
AC Q9FYS5;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=HMG-Y-related protein A;
DE Short=ZmHMGA;
DE AltName: Full=High mobility group A protein;
GN Name=HMGIY2 {ECO:0000303|PubMed:11278346};
GN ORFNames=GRMZM2G106133 {ECO:0000305}, Zm.66288;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND MISCELLANEOUS.
RC STRAIN=cv. AMO406;
RX PubMed=11278346; DOI=10.1074/jbc.m007462200;
RA Forzani C., Loulergue C., Lobreaux S., Briat J.-F., Lebrun M.;
RT "Nickel resistance and chromatin condensation in Saccharomyces cerevisiae
RT expressing a maize high mobility group I/Y protein.";
RL J. Biol. Chem. 276:16731-16738(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=10864924; DOI=10.1074/jbc.m001711200;
RA Zhao J., Grafi G.;
RT "The high mobility group I/Y protein is hypophosphorylated in
RT endoreduplicating maize endosperm cells and is involved in alleviating
RT histone H1-mediated transcriptional repression.";
RL J. Biol. Chem. 275:27494-27499(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, ACETYLATION, PHOSPHORYLATION, AND
RP MUTAGENESIS OF 155-SER--PRO-160 AND 170-THR--LYS-173.
RX PubMed=19781672; DOI=10.1016/j.bbagrm.2009.09.004;
RA Zhao J., Paul L.K., Grafi G.;
RT "The maize HMGA protein is localized to the nucleolus and can be acetylated
RT in vitro at its globular domain, and phosphorylation by CDK reduces its
RT binding activity to AT-rich DNA.";
RL Biochim. Biophys. Acta 1789:751-757(2009).
CC -!- FUNCTION: Binds A/T-rich DNA (e.g. present in the storage gamma-zein
CC gene promoter) with a highly dynamic distribution into the nucleus
CC (PubMed:19781672, PubMed:10864924). Probably involved in endosperm
CC development, during cells shift from a mitotic cycle to
CC endoreduplication leading to massive synthesis of storage proteins
CC (zeins) and starch (PubMed:10864924). {ECO:0000269|PubMed:10864924,
CC ECO:0000269|PubMed:19781672}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|PROSITE-
CC ProRule:PRU00837, ECO:0000269|PubMed:11278346,
CC ECO:0000269|PubMed:19781672}. Note=Follows a highly dynamic speckled
CC distribution pattern throughout the chromatin of interphase nuclei.
CC {ECO:0000250|UniProtKB:Q43386}.
CC -!- PTM: Phosphorylated by CDK, this phosphorylation prevents DNA-binding
CC (PubMed:19781672, PubMed:10864924). Motility is increased when
CC hypophosphorylated (PubMed:10864924). {ECO:0000269|PubMed:10864924,
CC ECO:0000269|PubMed:19781672}.
CC -!- PTM: Acetylated. {ECO:0000269|PubMed:19781672}.
CC -!- MISCELLANEOUS: Confers resistance to nickel NiSO(4) when expressed in
CC yeast (e.g. S.cerevisiae) by counterbalancing nickel impact on cell
CC cycle associated with an increased chromatin condensation.
CC {ECO:0000269|PubMed:11278346}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF291748; AAG00601.1; -; mRNA.
DR EMBL; CM007647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EU952311; ACG24429.1; -; mRNA.
DR RefSeq; NP_001105009.1; NM_001111539.2.
DR AlphaFoldDB; Q9FYS5; -.
DR SMR; Q9FYS5; -.
DR STRING; 4577.GRMZM2G106133_P02; -.
DR iPTMnet; Q9FYS5; -.
DR PaxDb; Q9FYS5; -.
DR PRIDE; Q9FYS5; -.
DR EnsemblPlants; Zm00001eb041850_T001; Zm00001eb041850_P001; Zm00001eb041850.
DR GeneID; 541871; -.
DR Gramene; Zm00001eb041850_T001; Zm00001eb041850_P001; Zm00001eb041850.
DR KEGG; zma:541871; -.
DR eggNOG; ENOG502RXFH; Eukaryota.
DR HOGENOM; CLU_078915_0_0_1; -.
DR OMA; QSGQIVM; -.
DR OrthoDB; 1565299at2759; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; Q9FYS5; baseline and differential.
DR Genevisible; Q9FYS5; ZM.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:2000014; P:regulation of endosperm development; IEP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR000116; HMGA.
DR InterPro; IPR031059; HMGA_plant.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11467:SF103; PTHR11467:SF103; 1.
DR Pfam; PF02178; AT_hook; 4.
DR Pfam; PF00538; Linker_histone; 1.
DR PRINTS; PR00929; ATHOOK.
DR PRINTS; PR00930; HIGHMOBLTYIY.
DR SMART; SM00384; AT_hook; 4.
DR SMART; SM00526; H15; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51504; H15; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..193
FT /note="HMG-Y-related protein A"
FT /id="PRO_0000434726"
FT DOMAIN 11..81
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DNA_BIND 87..98
FT /note="A.T hook 1"
FT /evidence="ECO:0000255"
FT DNA_BIND 113..124
FT /note="A.T hook 2"
FT /evidence="ECO:0000255"
FT DNA_BIND 138..149
FT /note="A.T hook 3"
FT /evidence="ECO:0000255"
FT DNA_BIND 173..184
FT /note="A.T hook 4"
FT /evidence="ECO:0000255"
FT REGION 75..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 86..92
FT /note="Nuclear localization signal 1 (NLS)"
FT /evidence="ECO:0000250|UniProtKB:Q43386"
FT MOTIF 145..149
FT /note="Nuclear localization signal 2 (NLS)"
FT /evidence="ECO:0000250|UniProtKB:Q43386"
FT MUTAGEN 155..160
FT /note="Missing: Impaired phosphorylation."
FT /evidence="ECO:0000269|PubMed:19781672"
FT MUTAGEN 170..173
FT /note="Missing: Impaired phosphorylation."
FT /evidence="ECO:0000269|PubMed:19781672"
SQ SEQUENCE 193 AA; 19825 MW; 1AC4FBA24F5569E4 CRC64;
MATDEATKPS PIPPYPEMIL AAIEGLDDKS GSNKSAISKY IEGKYGSLPP AHASLLTAHL
ARMKESGELV FLKNNYFRAG APDAPPKRGR GRPPKARDPN APAPAPKSPS STGRGRGRPP
KAKSPLEAAV KQATAGMPKP RGRPPKKAKT DGAASPSPSP APAPAGDGST PGKRGRGRPP
KVRPAVPSET AAA
