BH112_ARATH
ID BH112_ARATH Reviewed; 393 AA.
AC Q94JL3; Q3ECK8; Q8LE61; Q9SYA1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Transcription factor bHLH112;
DE AltName: Full=Basic helix-loop-helix protein 112;
DE Short=AtbHLH112;
DE Short=bHLH 112;
DE AltName: Full=Transcription factor EN 64;
DE AltName: Full=bHLH transcription factor bHLH112;
GN Name=BHLH112; Synonyms=EN64; OrderedLocusNames=At1g61660;
GN ORFNames=T13M11.1;
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] (ISOFORM 1).
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] (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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 275-347 (ISOFORM 2), GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12679534; DOI=10.1093/molbev/msg088;
RA Heim M.A., Jakoby M., Werber M., Martin C., Weisshaar B., Bailey P.C.;
RT "The basic helix-loop-helix transcription factor family in plants: a
RT genome-wide study of protein structure and functional diversity.";
RL Mol. Biol. Evol. 20:735-747(2003).
RN [6]
RP GENE FAMILY.
RX PubMed=12897250; DOI=10.1105/tpc.013839;
RA Toledo-Ortiz G., Huq E., Quail P.H.;
RT "The Arabidopsis basic/helix-loop-helix transcription factor family.";
RL Plant Cell 15:1749-1770(2003).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14600211; DOI=10.1105/tpc.151140;
RA Bailey P.C., Martin C., Toledo-Ortiz G., Quail P.H., Huq E., Heim M.A.,
RA Jakoby M., Werber M., Weisshaar B.;
RT "Update on the basic helix-loop-helix transcription factor gene family in
RT Arabidopsis thaliana.";
RL Plant Cell 15:2497-2502(2003).
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- INTERACTION:
CC Q94JL3; O04292: ATHB-9; NbExp=3; IntAct=EBI-3133192, EBI-1536772;
CC Q94JL3; Q9M128: BHLH57; NbExp=3; IntAct=EBI-3133192, EBI-15195499;
CC Q94JL3; Q93Y00: BHLH7; NbExp=3; IntAct=EBI-3133192, EBI-4442198;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94JL3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94JL3-2; Sequence=VSP_036101, VSP_036102;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD21412.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005882; AAD21412.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33867.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33868.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60596.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60597.1; -; Genomic_DNA.
DR EMBL; AF380649; AAK55730.1; -; mRNA.
DR EMBL; AY113072; AAM47380.1; -; mRNA.
DR EMBL; AY085602; AAM62823.1; -; mRNA.
DR EMBL; AF488630; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A96642; A96642.
DR RefSeq; NP_001322872.1; NM_001333997.1. [Q94JL3-1]
DR RefSeq; NP_001322873.1; NM_001333996.1. [Q94JL3-2]
DR RefSeq; NP_564782.1; NM_104847.4. [Q94JL3-1]
DR RefSeq; NP_849836.1; NM_179505.1. [Q94JL3-2]
DR AlphaFoldDB; Q94JL3; -.
DR BioGRID; 27685; 46.
DR IntAct; Q94JL3; 44.
DR STRING; 3702.AT1G61660.1; -.
DR PaxDb; Q94JL3; -.
DR EnsemblPlants; AT1G61660.1; AT1G61660.1; AT1G61660. [Q94JL3-1]
DR EnsemblPlants; AT1G61660.2; AT1G61660.2; AT1G61660. [Q94JL3-2]
DR EnsemblPlants; AT1G61660.6; AT1G61660.6; AT1G61660. [Q94JL3-2]
DR EnsemblPlants; AT1G61660.7; AT1G61660.7; AT1G61660. [Q94JL3-1]
DR GeneID; 842462; -.
DR Gramene; AT1G61660.1; AT1G61660.1; AT1G61660. [Q94JL3-1]
DR Gramene; AT1G61660.2; AT1G61660.2; AT1G61660. [Q94JL3-2]
DR Gramene; AT1G61660.6; AT1G61660.6; AT1G61660. [Q94JL3-2]
DR Gramene; AT1G61660.7; AT1G61660.7; AT1G61660. [Q94JL3-1]
DR KEGG; ath:AT1G61660; -.
DR Araport; AT1G61660; -.
DR TAIR; locus:2195763; AT1G61660.
DR eggNOG; ENOG502QRNH; Eukaryota.
DR InParanoid; Q94JL3; -.
DR PhylomeDB; Q94JL3; -.
DR PRO; PR:Q94JL3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94JL3; baseline and differential.
DR Genevisible; Q94JL3; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0071215; P:cellular response to abscisic acid stimulus; IEP:TAIR.
DR GO; GO:0071472; P:cellular response to salt stress; IEP:TAIR.
DR GO; GO:0042631; P:cellular response to water deprivation; IEP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:2000214; P:regulation of proline metabolic process; IMP:TAIR.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd11393; bHLH_AtbHLH_like; 1.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR045239; bHLH95_bHLH.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..393
FT /note="Transcription factor bHLH112"
FT /id="PRO_0000358798"
FT DOMAIN 270..319
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 248..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 343..347
FT /note="ISGKS -> VQYTI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12679534"
FT /id="VSP_036101"
FT VAR_SEQ 348..393
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12679534"
FT /id="VSP_036102"
FT CONFLICT 17
FT /note="G -> S (in Ref. 4; AAM62823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 43041 MW; 73EC0BCBCE3959C1 CRC64;
MAEEFKATAS ICGGGGGAWW NSPRSVMSPS DHFLSPCFGA AITSNDFSSQ ENHLKSRMTC
TDNNNIVFGQ READSDSGGS TVTMDSTLQM MGLGFSSNCS SDWNQTILQE DLNSSFIRSS
QDQDHGQGFL STTTSPYILN PACSSSPSTS SSSSLIRTFY DPEPSPYNFV STTSGSINDP
QLSWANKTNP HHQVAYGLIN SFSNNANSRP FWNSSSTTNL NNTTPSNFVT TPQIISTRLE
DKTKNLKTRA QSESLKRAKD NESAAKKPRV TTPSPLPTFK VRKENLRDQI TSLQQLVSPF
GKTDTASVLQ EAIEYIKFLH DQVTVLSTPY MKQGASNQQQ QQISGKSKSQ DENENHELRG
HGLCLVPISS TFPVANETTA DFWTPTFGGN NFR
