NAC14_ARATH
ID NAC14_ARATH Reviewed; 652 AA.
AC B5X570; Q9MAN7;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=NAC domain-containing protein 14 {ECO:0000303|PubMed:15029955};
DE Short=ANAC014 {ECO:0000303|PubMed:15029955};
DE AltName: Full=Protein NTM1-like 2 {ECO:0000303|PubMed:17158162};
GN Name=NAC014 {ECO:0000312|EMBL:AEE31559.1};
GN Synonyms=NTL2 {ECO:0000303|PubMed:17158162};
GN OrderedLocusNames=At1g33060 {ECO:0000312|Araport:AT1G33060};
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].
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15029955; DOI=10.1093/dnares/10.6.239;
RA Ooka H., Satoh K., Doi K., Nagata T., Otomo Y., Murakami K., Matsubara K.,
RA Osato N., Kawai J., Carninci P., Hayashizaki Y., Suzuki K., Kojima K.,
RA Takahara Y., Yamamoto K., Kikuchi S.;
RT "Comprehensive analysis of NAC family genes in Oryza sativa and Arabidopsis
RT thaliana.";
RL DNA Res. 10:239-247(2003).
RN [5]
RP GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17158162; DOI=10.1093/nar/gkl1068;
RA Kim S.Y., Kim S.G., Kim Y.S., Seo P.J., Bae M., Yoon H.K., Park C.M.;
RT "Exploring membrane-associated NAC transcription factors in Arabidopsis:
RT implications for membrane biology in genome regulation.";
RL Nucleic Acids Res. 35:203-213(2007).
CC -!- FUNCTION: Transcriptional activator activated by proteolytic cleavage
CC through regulated intramembrane proteolysis (RIP).
CC {ECO:0000250|UniProtKB:Q949N0}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q949N0}; Single-
CC pass membrane protein {ECO:0000255}. Nucleus
CC {ECO:0000250|UniProtKB:Q949N0, ECO:0000255|PROSITE-ProRule:PRU00353}.
CC Note=Localized primarily in plasma membrane or endoplasmic reticulum
CC membrane as dormant form and, upon specific stress or signal, is
CC processed into a transcriptionally active and nuclear form after a
CC proteolytic cleavage through regulated intramembrane proteolysis (RIP).
CC {ECO:0000250|UniProtKB:Q949N0}.
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=B5X570-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, cauline leaves,
CC shoot apex, stems and flowers. {ECO:0000269|PubMed:17158162}.
CC -!- INDUCTION: By cold, heat and drought stresses.
CC {ECO:0000269|PubMed:17158162}.
CC -!- DOMAIN: The NAC domain includes a DNA binding domain and a dimerization
CC domain. {ECO:0000255|PROSITE-ProRule:PRU00353}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF31292.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006424; AAF31292.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31559.1; -; Genomic_DNA.
DR EMBL; BT046189; ACI49788.1; -; mRNA.
DR RefSeq; NP_973954.1; NM_202225.2. [B5X570-1]
DR AlphaFoldDB; B5X570; -.
DR SMR; B5X570; -.
DR STRING; 3702.AT1G33060.2; -.
DR iPTMnet; B5X570; -.
DR PaxDb; B5X570; -.
DR PRIDE; B5X570; -.
DR ProteomicsDB; 251281; -. [B5X570-1]
DR EnsemblPlants; AT1G33060.2; AT1G33060.2; AT1G33060. [B5X570-1]
DR GeneID; 840202; -.
DR Gramene; AT1G33060.2; AT1G33060.2; AT1G33060. [B5X570-1]
DR KEGG; ath:AT1G33060; -.
DR Araport; AT1G33060; -.
DR TAIR; locus:2037920; AT1G33060.
DR eggNOG; ENOG502QQI4; Eukaryota.
DR InParanoid; B5X570; -.
DR PhylomeDB; B5X570; -.
DR PRO; PR:B5X570; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; B5X570; baseline and differential.
DR Genevisible; B5X570; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR Gene3D; 2.170.150.80; -; 1.
DR InterPro; IPR003441; NAC-dom.
DR InterPro; IPR036093; NAC_dom_sf.
DR Pfam; PF02365; NAM; 1.
DR SUPFAM; SSF101941; SSF101941; 1.
DR PROSITE; PS51005; NAC; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; DNA-binding; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Stress response; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..652
FT /note="NAC domain-containing protein 14"
FT /id="PRO_0000432441"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 24..174
FT /note="NAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT DNA_BIND 123..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT REGION 198..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9SCK6"
SQ SEQUENCE 652 AA; 74048 MW; 67ED31749FB1CB32 CRC64;
MNQIKNKTLP EMTTEQALLS MEALPLGFRF RPTDEELINH YLRLKINGRD LEVRVIPEID
VCKWEPWDLP GLSVIKTDDQ EWFFFCPRDR KYPSGHRSNR ATDIGYWKAT GKDRTIKSKK
MIIGMKKTLV FYRGRAPRGE RTNWIMHEYR ATDKELDGTG PGQNPYVLCR LFHKPSDSCD
PAHCEEIEKV NFTPTTTTRC SPDDTSSEMV QETATSGVHA LDRSDDTERC LSDKGNNDVK
PDVSVINNTS VNHAETSRAK DRNLGKTLVE ENPLLRDVPT LHGPILSEKS YYPGQSSIGF
ATSHMDSMYS SDFGNCDYGL HFQDGASEQD ASLTDVLDEV FHNHNESSND RKDFVLPNMM
HWPGNTRLLS TEYPFLKDSV AFVDGSAEVS GSQQFVPDIL ASRWVSEQNV DSKEAVEILS
STGSSRTLTP LHNNVFGQYA SSSYAAIDPF NYNVNQPEQS SFEQSHVDRN ISPSNIFEFK
ARSRENQRDL DSVVDQGTAP RRIRLQIEQP LTPVTNKKER DADNYEEEDE VQSAMSKVVE
EEPANLSAQG TAQRRIRLQT RLRKPLITLN NTKRNSNGRE GEASHRKCEM QEKEDISSSS
SWQKQKKSLV QFSSVVIIVA VIVVLVEIWK ESRDAKCSFL FHQLDSFKGM FT
