NAA15_ARATH
ID NAA15_ARATH Reviewed; 897 AA.
AC Q8VZM1; Q9M8L0;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=N-terminal acetyltransferase A complex auxiliary subunit NAA15 {ECO:0000303|PubMed:25966763};
DE Short=AtNAA15 {ECO:0000303|PubMed:25966763};
DE AltName: Full=Protein OMISHA {ECO:0000303|PubMed:17915010};
GN Name=NAA15 {ECO:0000303|PubMed:25966763};
GN Synonyms=EMB2753 {ECO:0000303|PubMed:15266054},
GN MUSE6 {ECO:0000303|PubMed:25966763}, OMA {ECO:0000303|PubMed:17915010};
GN OrderedLocusNames=At1g80410 {ECO:0000312|Araport:AT1G80410};
GN ORFNames=T21F11.26 {ECO:0000312|EMBL:AAF27136.1};
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 {ECO:0000312|EMBL:AAL36371.1};
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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP FUNCTION.
RX PubMed=15266054; DOI=10.1104/pp.104.045179;
RA Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R., Hutchens S.,
RA Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT "Identification of genes required for embryo development in Arabidopsis.";
RL Plant Physiol. 135:1206-1220(2004).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=17915010; DOI=10.1186/gb-2007-8-10-r204;
RA Johnston A.J., Meier P., Gheyselinck J., Wuest S.E.J., Federer M.,
RA Schlagenhauf E., Becker J.D., Grossniklaus U.;
RT "Genetic subtraction profiling identifies genes essential for Arabidopsis
RT reproduction and reveals interaction between the female gametophyte and the
RT maternal sporophyte.";
RL Genome Biol. 8:R204.1-R204.21(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH NAA10, AND INDUCTION BY
RP ABSCISIC ACID.
RC STRAIN=cv. Columbia;
RX PubMed=26184543; DOI=10.1038/ncomms8640;
RA Linster E., Stephan I., Bienvenut W.V., Maple-Groedem J., Myklebust L.M.,
RA Huber M., Reichelt M., Sticht C., Moeller S.G., Meinnel T., Arnesen T.,
RA Giglione C., Hell R., Wirtz M.;
RT "Downregulation of N-terminal acetylation triggers ABA-mediated drought
RT responses in Arabidopsis.";
RL Nat. Commun. 6:7640-7640(2015).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25966763; DOI=10.1105/tpc.15.00173;
RA Xu F., Huang Y., Li L., Gannon P., Linster E., Huber M., Kapos P.,
RA Bienvenut W., Polevoda B., Meinnel T., Hell R., Giglione C., Zhang Y.,
RA Wirtz M., Chen S., Li X.;
RT "Two N-terminal acetyltransferases antagonistically regulate the stability
RT of a nod-like receptor in Arabidopsis.";
RL Plant Cell 27:1547-1562(2015).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH NAA10.
RC STRAIN=cv. Columbia;
RX PubMed=27385766; DOI=10.1093/jxb/erw257;
RA Feng J., Li R., Yu J., Ma S., Wu C., Li Y., Cao Y., Ma L.;
RT "Protein N-terminal acetylation is required for embryogenesis in
RT Arabidopsis.";
RL J. Exp. Bot. 67:4779-4789(2016).
RN [11]
RP FUNCTION.
RX PubMed=27610925; DOI=10.1080/15592324.2016.1231293;
RA Feng J., Ma L.;
RT "NatA is required for suspensor development in Arabidopsis.";
RL Plant Signal. Behav. 11:E1231293-E1231293(2016).
CC -!- FUNCTION: Auxiliary subunit of the NatA N-alpha-acetyltransferase
CC complex. Required for male gametocyte development, embryogenesis,
CC suspensor development and the formation of the quiescent center (QC) in
CC the root meristem (PubMed:27385766, PubMed:27610925). Involved in plant
CC immunity through the regulation of SNC1 stability (PubMed:25966763).
CC Required for embryo development (PubMed:15266054).
CC {ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:25966763,
CC ECO:0000269|PubMed:27385766, ECO:0000269|PubMed:27610925}.
CC -!- SUBUNIT: Part of the NatA complex. Associates with ribosomes. Interacts
CC with NAA10. {ECO:0000269|PubMed:26184543, ECO:0000269|PubMed:27385766}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q8VZM1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, shoots and flowers.
CC {ECO:0000269|PubMed:26184543}.
CC -!- INDUCTION: Down-regulated upon abscisic acid treatment.
CC {ECO:0000269|PubMed:26184543}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethal when homozygous.
CC {ECO:0000269|PubMed:17915010, ECO:0000269|PubMed:25966763,
CC ECO:0000269|PubMed:27385766}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF27136.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC018849; AAF27136.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36399.1; -; Genomic_DNA.
DR EMBL; AY064015; AAL36371.1; -; mRNA.
DR EMBL; AY091419; AAM14358.1; -; mRNA.
DR EMBL; AK118131; BAC42757.1; -; mRNA.
DR PIR; H96835; H96835.
DR RefSeq; NP_178157.2; NM_106690.6. [Q8VZM1-1]
DR AlphaFoldDB; Q8VZM1; -.
DR SMR; Q8VZM1; -.
DR IntAct; Q8VZM1; 6.
DR STRING; 3702.AT1G80410.2; -.
DR iPTMnet; Q8VZM1; -.
DR PRIDE; Q8VZM1; -.
DR EnsemblPlants; AT1G80410.1; AT1G80410.1; AT1G80410. [Q8VZM1-1]
DR GeneID; 844381; -.
DR Gramene; AT1G80410.1; AT1G80410.1; AT1G80410. [Q8VZM1-1]
DR KEGG; ath:AT1G80410; -.
DR Araport; AT1G80410; -.
DR eggNOG; KOG1156; Eukaryota.
DR HOGENOM; CLU_006686_0_0_1; -.
DR PhylomeDB; Q8VZM1; -.
DR PRO; PR:Q8VZM1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VZM1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IBA:GO_Central.
DR InterPro; IPR021183; NatA_aux_su.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF12569; NARP1; 1.
DR Pfam; PF00515; TPR_1; 1.
DR PIRSF; PIRSF000422; N-terminal-AcTrfase-A_aux_su; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..897
FT /note="N-terminal acetyltransferase A complex auxiliary
FT subunit NAA15"
FT /id="PRO_0000439079"
FT REPEAT 77..110
FT /note="TPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 111..144
FT /note="TPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 189..222
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 223..256
FT /note="TPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 298..331
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 380..413
FT /note="TPR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 488..523
FT /note="TPR 7"
FT /evidence="ECO:0000255"
FT REGION 578..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 102147 MW; 4B577F578BD35100 CRC64;
MGASLPPKEA NLFKLIVKSY ETKQYKKGLK AADAILKKFP DHGETLSMKG LTLNCMDRKT
EAYELVRLGV KNDIKSHVCW HVLGLLYRSD REYREAIKCY RNALRIDPDN LEILRDLSLL
QAQMRDLSGF VETRQQLLTL KPNHRMNWIG FAVSQHLNAN ASKAVEILEA YEGTLEDDYP
PENELIEHTE MILYKVSLLE ESGSFDKALE ELHKKEPKIV DKLSYKEQEV SLLSKVGRLE
EANKLYRVLL SMNPDNYRYH EGLQKCLGLY SESGQYSSDQ IEKLNALYQS LSEQYTRSSA
VKRIPLDFLQ DENFKEAVAK YIKPLLTKGV PSLFSDLSSL YDHPRKPDIL EQLVVEMKHS
IGTTGSFPGS DVKEPPSTLL WTLFFLAQHY DRRGQYDVAL CKIDEAIAHT PTVIDLYSVK
SRIMKHAGDL TAAAALADEA RGMDLADRYI NSECVKRMLQ ADQVPLAEKT AVLFTKEGDQ
LNNLHDMQCM WYDLASGDSY FRQGDLGRAL KKFLAVEKHY ADISEDQFDF HSYCLRKMTL
RSYVDMLKFQ DRLHSFPYFH KAAIRAIRCY LKLHDSPKST AGEDEMSKLA PAQKKKIKKQ
KKAEARAKKE AESKSEESTA SGASKSGKRN VKPVDPDPHG QKLIQVEEPM AEASKYLRLL
QKHSPNSLET HLLSFEVNMR KQKFLLAFQA VKQLLKLGAE NPDSHRSLVK FFLMTESISA
PTTEAEKLRW RVLEAERPSI SQLQNKSLME ANKEFLGRHE DSLVHRAAYA EMLYILDPSK
KTEAIKIIED STNKVVQTNE ALGQAREWKL KDCIAVHTLL DTVLLDSQAA SRWKSRCAEY
FPCSTHFEGK HCSLMPDSVY NSSRKSNENG DTPNHPMGQT ELSDGQLEAF KSLSVAT
