BAH1_ARATH
ID BAH1_ARATH Reviewed; 335 AA.
AC Q9SRX9; B3H5D0; Q8L8T3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=E3 ubiquitin-protein ligase BAH1;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=Protein BENZOIC ACID HYPERSENSITIVE 1;
DE AltName: Full=Protein NITROGEN LIMITATION ADAPTATION;
DE AltName: Full=RING-type E3 ubiquitin transferase BAH1 {ECO:0000305};
GN Name=BAH1; Synonyms=NLA; OrderedLocusNames=At1g02860; ORFNames=F22D16.14;
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 [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, MUTANT NLA, TISSUE SPECIFICITY, INTERACTION WITH UBC8, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17355433; DOI=10.1111/j.1365-313x.2007.03050.x;
RA Peng M., Hannam C., Gu H., Bi Y.-M., Rothstein S.J.;
RT "A mutation in NLA, which encodes a RING-type ubiquitin ligase, disrupts
RT the adaptability of Arabidopsis to nitrogen limitation.";
RL Plant J. 50:320-337(2007).
RN [8]
RP FUNCTION.
RX PubMed=18552353; DOI=10.1093/jxb/ern148;
RA Peng M., Hudson D., Schofield A., Tsao R., Yang R., Gu H., Bi Y.-M.,
RA Rothstein S.J.;
RT "Adaptation of Arabidopsis to nitrogen limitation involves induction of
RT anthocyanin synthesis which is controlled by the NLA gene.";
RL J. Exp. Bot. 59:2933-2944(2008).
RN [9]
RP FUNCTION, MUTAGENESIS OF SER-55; GLU-74; VAL-156; ARG-160; GLU-162 AND
RP GLU-181, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=18753285; DOI=10.1104/pp.108.124529;
RA Yaeno T., Iba K.;
RT "BAH1/NLA, a RING-type ubiquitin E3 ligase, regulates the accumulation of
RT salicylic acid and immune responses to pseudomonas syringae DC3000.";
RL Plant Physiol. 148:1032-1041(2008).
CC -!- FUNCTION: Mediates E2-dependent protein ubiquitination. Plays a role in
CC salicylic acid-mediated negative feedback regulation of salicylic acid
CC (SA) accumulation. May be involved in the overall regulation of SA,
CC benzoic acid and phenylpropanoid biosynthesis. Controls the
CC adaptability to nitrogen limitation by channeling the phenylpropanoid
CC metabolic flux to the induced anthocyanin synthesis.
CC {ECO:0000269|PubMed:17355433, ECO:0000269|PubMed:18552353,
CC ECO:0000269|PubMed:18753285}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with UBC8. {ECO:0000269|PubMed:17355433}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:17355433}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SRX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SRX9-2; Sequence=VSP_035909;
CC -!- TISSUE SPECIFICITY: High expression in roots and stems, medium in
CC seedlings, flowers, rosette and cauline leaves, and very low in
CC siliques. Detected in cotyledons, hypocotyls, pedicel, receptacle,
CC pistil, sepal, filament of stamen and at the two ends of developing
CC siliques. {ECO:0000269|PubMed:17355433}.
CC -!- INDUCTION: By salicylic acid and benzoic acid.
CC {ECO:0000269|PubMed:18753285}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme.
CC -!- DISRUPTION PHENOTYPE: Plants show a low-nitrogen-induced early
CC senescence phenotype and an excessive accumulation of salicylic acid
CC after pathogen infection or application of benzoic acid.
CC {ECO:0000269|PubMed:18753285}.
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DR EMBL; DQ059096; AAY57582.1; -; mRNA.
DR EMBL; AC009525; AAF02879.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27485.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27486.1; -; Genomic_DNA.
DR EMBL; AK229396; BAF01258.1; -; mRNA.
DR EMBL; AY088823; AAM67132.1; -; mRNA.
DR EMBL; BT044616; ACI31316.1; -; mRNA.
DR PIR; H86158; H86158.
DR RefSeq; NP_001117218.1; NM_001123746.1. [Q9SRX9-2]
DR RefSeq; NP_563667.1; NM_100167.3. [Q9SRX9-1]
DR AlphaFoldDB; Q9SRX9; -.
DR SMR; Q9SRX9; -.
DR STRING; 3702.AT1G02860.1; -.
DR PaxDb; Q9SRX9; -.
DR PRIDE; Q9SRX9; -.
DR ProteomicsDB; 240968; -. [Q9SRX9-1]
DR EnsemblPlants; AT1G02860.1; AT1G02860.1; AT1G02860. [Q9SRX9-1]
DR EnsemblPlants; AT1G02860.2; AT1G02860.2; AT1G02860. [Q9SRX9-2]
DR GeneID; 839559; -.
DR Gramene; AT1G02860.1; AT1G02860.1; AT1G02860. [Q9SRX9-1]
DR Gramene; AT1G02860.2; AT1G02860.2; AT1G02860. [Q9SRX9-2]
DR KEGG; ath:AT1G02860; -.
DR Araport; AT1G02860; -.
DR TAIR; locus:2024675; AT1G02860.
DR eggNOG; ENOG502QQHB; Eukaryota.
DR HOGENOM; CLU_058131_0_0_1; -.
DR InParanoid; Q9SRX9; -.
DR OMA; RRCPEYW; -.
DR PhylomeDB; Q9SRX9; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SRX9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SRX9; baseline and differential.
DR Genevisible; Q9SRX9; AT.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
DR GO; GO:0010337; P:regulation of salicylic acid metabolic process; IMP:TAIR.
DR GO; GO:0080021; P:response to benzoic acid; IMP:TAIR.
DR GO; GO:0010167; P:response to nitrate; IMP:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR GO; GO:0009697; P:salicylic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0009627; P:systemic acquired resistance; IMP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR033326; BAH1.
DR InterPro; IPR004331; SPX_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46764; PTHR46764; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS51382; SPX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Nucleus; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..335
FT /note="E3 ubiquitin-protein ligase BAH1"
FT /id="PRO_0000355543"
FT DOMAIN 1..154
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT ZN_FING 231..280
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT VAR_SEQ 301..302
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035909"
FT MUTAGEN 55
FT /note="S->F: In bah1-2; loss of activity."
FT /evidence="ECO:0000269|PubMed:18753285"
FT MUTAGEN 74
FT /note="E->K: In bah1-4; loss of activity."
FT /evidence="ECO:0000269|PubMed:18753285"
FT MUTAGEN 156
FT /note="V->I: In bah1-5; loss of activity."
FT /evidence="ECO:0000269|PubMed:18753285"
FT MUTAGEN 160
FT /note="R->Q: In bah1-6; loss of activity."
FT /evidence="ECO:0000269|PubMed:18753285"
FT MUTAGEN 162
FT /note="E->K: In bah1-7; loss of activity."
FT /evidence="ECO:0000269|PubMed:18753285"
FT MUTAGEN 181
FT /note="E->K: In bah1-9; loss of activity."
FT /evidence="ECO:0000269|PubMed:18753285"
FT MUTAGEN 236..281
FT /note="Missing: In nla; loss of activity."
FT CONFLICT 292
FT /note="D -> Y (in Ref. 5; AAM67132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 38409 MW; 8073DB557199BF1A CRC64;
MKFCKKYEEY MQGQKEKKNL PGVGFKKLKK ILKRCRRNHV PSRISFTDAI NHNCSRECPV
CDGTFFPELL KEMEDVVGWF NEHAQKLLEL HLASGFTKCL TWLRGNSRKK DHHGLIQEGK
DLVNYALINA VAIRKILKKY DKIHESRQGQ AFKTQVQKMR IEILQSPWLC ELMAFHINLK
ESKKESGATI TSPPPPVHAL FDGCALTFDD GKPLLSCELS DSVKVDIDLT CSICLDTVFD
PISLTCGHIY CYMCACSAAS VNVVDGLKTA EATEKCPLCR EDGVYKGAVH LDELNILLKR
SCRDYWEERR KTERAERLQQ AKEYWDYQCR SFTGI
