NHL6_ARATH
ID NHL6_ARATH Reviewed; 252 AA.
AC Q8LD98; Q9SHY5;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=NDR1/HIN1-like protein 6 {ECO:0000303|PubMed:26849212};
GN Name=NHL6 {ECO:0000303|PubMed:26849212};
GN OrderedLocusNames=At1g65690 {ECO:0000312|Araport:AT1G65690};
GN ORFNames=F1E22.7 {ECO:0000312|EMBL:AAF23842.1};
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].
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 [4]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=26849212; DOI=10.1371/journal.pone.0148572;
RA Bao Y., Song W.M., Pan J., Jiang C.M., Srivastava R., Li B., Zhu L.Y.,
RA Su H.Y., Gao X.S., Liu H., Yu X., Yang L., Cheng X.H., Zhang H.X.;
RT "Overexpression of the NDR1/HIN1-like gene NHL6 modifies seed germination
RT in response to abscisic acid and abiotic stresses in Arabidopsis.";
RL PLoS ONE 11:E0148572-E0148572(2016).
CC -!- FUNCTION: Plays an important role in the abiotic stresses-induced
CC abscisic acid (ABA) signaling and biosynthesis. Acts as positive
CC regulator of ABA-mediated seed germination inhibition. Functions
CC downstream of ABF2/AREB1, ABF4/AREB2 and ABF3.
CC {ECO:0000269|PubMed:26849212}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26849212}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26849212};
CC Single-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:26849212}. Note=Moves from plasma membrane to
CC cytosol under abiotic stress. {ECO:0000269|PubMed:26849212}.
CC -!- TISSUE SPECIFICITY: Highly expressed in seeds and at lower level in
CC roots and senescing leaves. Expressed in leaves and flowers.
CC {ECO:0000269|PubMed:26849212}.
CC -!- INDUCTION: Induced by abscisic acid (ABA), osmotic shock and drought
CC stress. Slightly induced by salt stress. {ECO:0000269|PubMed:26849212}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seeds show decreased sensitivity to abscisic
CC acid (ABA) during germination. {ECO:0000269|PubMed:26849212}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF23842.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AC007234; AAF23842.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34412.1; -; Genomic_DNA.
DR EMBL; AY086125; AAM63331.1; -; mRNA.
DR RefSeq; NP_564862.1; NM_105243.4.
DR AlphaFoldDB; Q8LD98; -.
DR IntAct; Q8LD98; 136.
DR STRING; 3702.AT1G65690.1; -.
DR SwissPalm; Q8LD98; -.
DR PaxDb; Q8LD98; -.
DR PRIDE; Q8LD98; -.
DR ProteomicsDB; 250510; -.
DR EnsemblPlants; AT1G65690.1; AT1G65690.1; AT1G65690.
DR GeneID; 842880; -.
DR Gramene; AT1G65690.1; AT1G65690.1; AT1G65690.
DR KEGG; ath:AT1G65690; -.
DR Araport; AT1G65690; -.
DR TAIR; locus:2018531; AT1G65690.
DR eggNOG; ENOG502QVVS; Eukaryota.
DR HOGENOM; CLU_051752_0_2_1; -.
DR InParanoid; Q8LD98; -.
DR OMA; RSCLCKC; -.
DR OrthoDB; 1324259at2759; -.
DR PhylomeDB; Q8LD98; -.
DR PRO; PR:Q8LD98; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LD98; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010116; P:positive regulation of abscisic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:1902074; P:response to salt; IMP:TAIR.
DR InterPro; IPR004864; LEA_2.
DR Pfam; PF03168; LEA_2; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Cell membrane; Cytoplasm; Glycoprotein;
KW Membrane; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..252
FT /note="NDR1/HIN1-like protein 6"
FT /id="PRO_0000439592"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 252 AA; 28574 MW; E5BA9E4AE23D1753 CRC64;
MSQHQKIYPV QDPEAATARP TAPLVPRGSS RSEHGDPSKV PLNQRPQRFV PLAPPKKRRS
CCCRCFCYTF CFLLLLVVAV GASIGILYLV FKPKLPDYSI DRLQLTRFAL NQDSSLTTAF
NVTITAKNPN EKIGIYYEDG SKITVWYMEH QLSNGSLPKF YQGHENTTVI YVEMTGQTQN
ASGLRTTLEE QQQRTGNIPL RIRVNQPVRV KFGKLKLFEV RFLVRCGVFV DSLATNNVIK
IQSSSCKFRL RL
