HTH_ARATH
ID HTH_ARATH Reviewed; 594 AA.
AC Q9S746; Q9SXZ3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein HOTHEAD;
DE AltName: Full=Protein ADHESION OF CALYX EDGES;
DE Flags: Precursor;
GN Name=HTH; Synonyms=ACE; OrderedLocusNames=At1g72970; ORFNames=F3N23.17;
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], AND VARIANT LYS-478.
RC STRAIN=cv. Columbia, and cv. No-0;
RA Nakatani-Goto M., Araki T., Iwabuchi M.;
RT "ADHESION OF CALYX EDGES, a gene involved in the regulation of postgenital
RT fusion in Arabidopsis.";
RL Plant Cell Physiol. 39:S64-S64(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-218; ARG-227;
RP GLY-294; GLY-356; GLY-435; PRO-564; GLY-565 AND THR-566, FUNCTION, TISSUE
RP SPECIFICITY, AND VARIANT LYS-478.
RC STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=12904212; DOI=10.1046/j.1365-313x.2003.01824.x;
RA Krolikowski K.A., Victor J.L., Wagler T.N., Lolle S.J., Pruitt R.E.;
RT "Isolation and characterization of the Arabidopsis organ fusion gene
RT HOTHEAD.";
RL Plant J. 35:501-511(2003).
RN [3]
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 [4]
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 [5]
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 [6]
RP MUTANTS HTH-2; HTH-3; HTH-4; HTH-5; HTH-6; HTH-7; HTH-8; HTH-10 AND HTH-11.
RX PubMed=9611177; DOI=10.1093/genetics/149.2.607;
RA Lolle S.J., Hsu W., Pruitt R.E.;
RT "Genetic analysis of organ fusion in Arabidopsis thaliana.";
RL Genetics 149:607-619(1998).
RN [7]
RP FUNCTION.
RX PubMed=15785770; DOI=10.1038/nature03380;
RA Lolle S.J., Victor J.L., Young J.M., Pruitt R.E.;
RT "Genome-wide non-Mendelian inheritance of extra-genomic information in
RT Arabidopsis.";
RL Nature 434:505-509(2005).
CC -!- FUNCTION: Probable FAD-dependent enzyme. Involved in regulating post-
CC genital organ fusion. Required to limit cellular interactions between
CC contacting epidermal cells during floral development.
CC {ECO:0000269|PubMed:12904212, ECO:0000269|PubMed:15785770}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9S746-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, inflorescences
CC and siliques. Found not only in epidermis but also in all sub-epidermal
CC cell layers. {ECO:0000269|PubMed:12904212}.
CC -!- MISCELLANEOUS: Mutations in the gene for this protein reveals an
CC unusual pattern of genetic transmission in which progeny plants
CC inherit, at relatively high frequency, DNA sequences different from
CC those carried by their parents. The instability observed is not random
CC but seems to be confined to the restoration of sequence information in
CC progeny plants that, although absent from the parent genome, was
CC present in the genome of an earlier ancestor.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AB027458; BAA77837.1; -; mRNA.
DR EMBL; AB027507; BAA77842.1; -; Genomic_DNA.
DR EMBL; AC008017; AAD55644.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35397.1; -; Genomic_DNA.
DR EMBL; AY054193; AAL06854.1; -; mRNA.
DR EMBL; BT002648; AAO11564.1; -; mRNA.
DR PIR; T50764; T50764.
DR PIR; T50765; T50765.
DR RefSeq; NP_565050.1; NM_105955.4. [Q9S746-1]
DR AlphaFoldDB; Q9S746; -.
DR SMR; Q9S746; -.
DR STRING; 3702.AT1G72970.1; -.
DR PaxDb; Q9S746; -.
DR PRIDE; Q9S746; -.
DR ProteomicsDB; 232092; -. [Q9S746-1]
DR EnsemblPlants; AT1G72970.1; AT1G72970.1; AT1G72970. [Q9S746-1]
DR GeneID; 843628; -.
DR Gramene; AT1G72970.1; AT1G72970.1; AT1G72970. [Q9S746-1]
DR KEGG; ath:AT1G72970; -.
DR Araport; AT1G72970; -.
DR TAIR; locus:2032627; AT1G72970.
DR eggNOG; KOG1238; Eukaryota.
DR InParanoid; Q9S746; -.
DR OMA; NFHDHLH; -.
DR PhylomeDB; Q9S746; -.
DR BioCyc; ARA:AT1G72970-MON; -.
DR BioCyc; MetaCyc:AT1G72970-MON; -.
DR PRO; PR:Q9S746; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S746; baseline and differential.
DR Genevisible; Q9S746; AT.
DR GO; GO:0005576; C:extracellular region; ISS:TAIR.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:TAIR.
DR GO; GO:0046593; F:mandelonitrile lyase activity; ISS:TAIR.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0007267; P:cell-cell signaling; IMP:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0010430; P:fatty acid omega-oxidation; IMP:TAIR.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; FAD; Flavoprotein; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..594
FT /note="Protein HOTHEAD"
FT /id="PRO_0000012345"
FT ACT_SITE 529
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 64..91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT VARIANT 478
FT /note="N -> K (in strain: cv. No-0 and cv. Wassilewskija)"
FT /evidence="ECO:0000269|PubMed:12904212, ECO:0000269|Ref.1"
FT MUTAGEN 218
FT /note="G->S: In hth-6; fused organs and increased genetic
FT instability."
FT /evidence="ECO:0000269|PubMed:12904212"
FT MUTAGEN 227
FT /note="R->C: In hth-4; fused organs and increased genetic
FT instability."
FT /evidence="ECO:0000269|PubMed:12904212"
FT MUTAGEN 294
FT /note="G->E: In hth-2; fused organs and increased genetic
FT instability."
FT /evidence="ECO:0000269|PubMed:12904212"
FT MUTAGEN 356
FT /note="G->E: In hth-10; fused organs and increased genetic
FT instability."
FT /evidence="ECO:0000269|PubMed:12904212"
FT MUTAGEN 435
FT /note="G->R: In hth-3; fused organs and increased genetic
FT instability."
FT /evidence="ECO:0000269|PubMed:12904212"
FT MUTAGEN 564
FT /note="P->S: In hth-5 and hth-11; fused organs and
FT increased genetic instability."
FT /evidence="ECO:0000269|PubMed:12904212"
FT MUTAGEN 565
FT /note="G->R: In hth-8; fused organs and increased genetic
FT instability."
FT /evidence="ECO:0000269|PubMed:12904212"
FT MUTAGEN 566
FT /note="T->I: In hth-7; fused organs and increased genetic
FT instability."
FT /evidence="ECO:0000269|PubMed:12904212"
SQ SEQUENCE 594 AA; 65344 MW; D6A8682FBBF73881 CRC64;
MALKLFLFAL LLCLPTSLSS TASKGKEKKS KFNPYRYTFI DKASTFSSSS SSSFSSNGQD
SSYDYIVIGG GTAGCPLAAT LSQNFSVLVL ERGGVPFTNA NVSFLRNFHI GLADISASSA
SQAFVSTDGV YNARARVLGG GSCINAGFYS RADAAFVKRA GWDPKLVKES YPWVEREIVH
QPKLTLWQKA LRDSLLEVGV RPFNGFTYDH VSGTKIGGTI FDRFGRRHTA AELLAYANPQ
KLRVLIYATV QKIVFDTSGT RPRVTGVIFK DEKGNQHQAL LSNRKGSEVI LSSGAIGSPQ
MLMLSGIGPK KELQRLKIPV VLENEHVGKG MADNPMNTIL VPSKAPIEQS LIQTVGITKM
GVYVEASTGF GQSPESIHTH YGIMSNKNEL FSTIPAKQRR PEATQAYITR NKYQLHEAFN
GSFILEKLAY PISRGHLSLV NTNVDDNPSV TFNYFKHPVD LQRCVEAIRL VSKVVTSNRF
LNYTQCDKQN VHKMLSLSVK ANINLRPKQL NDTKSMAQFC KDTVVTIWHY HGGCLVGKVV
SPNRKVLGVD RLRVIDGSTF DESPGTNPQA TMMMMGRYMG VKILRERLGN KAGV
