TAP1_SOYBN
ID TAP1_SOYBN Reviewed; 231 AA.
AC K7MTW9;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Histone acetyltransferase TAP1 {ECO:0000305};
DE Short=GmTAP1 {ECO:0000303|PubMed:30346270};
DE EC=2.3.1.48 {ECO:0000269|PubMed:30346270};
GN Name=TAP1 {ECO:0000303|PubMed:30346270};
GN ORFNames=GLYMA_18G216900 {ECO:0000312|EMBL:KRH00502.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PHYTOPHTORA SOJAE AVH52, AND
RP SUBCELLULAR LOCATION.
RX PubMed=30346270; DOI=10.7554/elife.40039;
RA Li H., Wang H., Jing M., Zhu J., Guo B., Wang Y., Lin Y., Chen H., Kong L.,
RA Ma Z., Wang Y., Ye W., Dong S., Tyler B., Wang Y.;
RT "A Phytophthora effector recruits a host cytoplasmic transacetylase into
RT nuclear speckles to enhance plant susceptibility.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Acetylates histones H2A and H3 in vitro.
CC {ECO:0000269|PubMed:30346270}.
CC -!- FUNCTION: (Microbial infection) Acts as negative regulator of immunity
CC when hijacked and relocated to the nucleus by the effector Avh52 from
CC the pathogen Phytophtora sojae (PubMed:30346270). Acts as a
CC susceptibility factor that is hijacked by Avh52 in order to promote
CC acetylation of histones H2A and H3 during early infection by
CC Phytophtora sojae (PubMed:30346270). These epigenetic modifications may
CC up-regulate the expression of potential plant susceptibility genes,
CC thereby promoting susceptibility to Phytophtora sojae
CC (PubMed:30346270). {ECO:0000269|PubMed:30346270}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:30346270};
CC -!- SUBUNIT: Interacts with the effector Avh52 from the pathogen
CC Phytophtora sojae. {ECO:0000269|PubMed:30346270}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30346270}. Nucleus
CC {ECO:0000269|PubMed:30346270}. Note=Localizes to the cytoplasm, but is
CC relocated to the nucleus when interacting with the effector Avh52 from
CC the pathogen Phytophtora sojae. {ECO:0000269|PubMed:30346270}.
CC -!- MISCELLANEOUS: Plants silencing TAP1 exhibit decreased susceptibility
CC to the pathogen Phytophtora sojae. {ECO:0000269|PubMed:30346270}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; CM000851; KRH00502.1; -; Genomic_DNA.
DR RefSeq; XP_003551622.2; XM_003551574.3.
DR AlphaFoldDB; K7MTW9; -.
DR SMR; K7MTW9; -.
DR STRING; 3847.GLYMA18G44940.2; -.
DR EnsemblPlants; KRH00502; KRH00502; GLYMA_18G216900.
DR GeneID; 100799333; -.
DR Gramene; KRH00502; KRH00502; GLYMA_18G216900.
DR eggNOG; ENOG502QSCQ; Eukaryota.
DR InParanoid; K7MTW9; -.
DR OrthoDB; 1429454at2759; -.
DR Proteomes; UP000008827; Chromosome 18.
DR ExpressionAtlas; K7MTW9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043998; F:H2A histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR045039; NSI-like.
DR PANTHER; PTHR43626; PTHR43626; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Nucleus; Plant defense; Reference proteome;
KW Transferase.
FT CHAIN 1..231
FT /note="Histone acetyltransferase TAP1"
FT /id="PRO_0000446672"
FT DOMAIN 88..231
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 231 AA; 25952 MW; 8A9C796FE89FDE60 CRC64;
MSMLSLLRSQ LFNFMPIIHC LLKLNSTRKF KSFQLKAGFW ESIKSGLMKN NSMQVIDPPS
TDEENVEPLS QDFVLVEKTE PDGTIEQIIF SSGGDVDVYD LQALCDKVGW PRRPLSKLAA
ALKNSYIVAS LHSIRKSHGS EGNEQKRLIG MARATSDHAF NATIWDVLVD PGYQGQGLGK
ALIEKLIRTL LQRDIGNITL FADSQVVEFY RNLGFEADPE GIKGMFWYPN H
