KNAT5_ARATH
ID KNAT5_ARATH Reviewed; 383 AA.
AC P48002; O49387; Q548P2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Homeobox protein knotted-1-like 5;
DE AltName: Full=Homeodomain-containing protein 1;
DE AltName: Full=Protein KNAT5;
GN Name=KNAT5; Synonyms=ATH1; OrderedLocusNames=At4g32040; ORFNames=F10N7.150;
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 INTERACTION WITH BEL1.
RC STRAIN=cv. Columbia;
RX PubMed=11701881; DOI=10.2307/3871587;
RA Bellaoui M., Pidkowich M.S., Samach A., Kushalappa K., Kohalmi S.E.,
RA Modrusan Z., Crosby W.L., Haughn G.W.;
RT "The Arabidopsis BELL1 and KNOX TALE homeodomain proteins interact through
RT a domain conserved between plants and animals.";
RL Plant Cell 13:2455-2470(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RA Koganeya T., Fujisawa T., Tasaka M.;
RT "A novel homeobox-containing gene with enriched expression in leaves of
RT Arabidopsis thaliana.";
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clone.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 280-383.
RX PubMed=8980519; DOI=10.1007/bf00020208;
RA Serikawa K.A., Martinez-Laborda A., Zambryski P.C.;
RT "Three knotted1-like homeobox genes in Arabidopsis.";
RL Plant Mol. Biol. 32:673-683(1996).
RN [7]
RP INTERACTION WITH OFP1; OFP2; OFP3 AND OFP4.
RX PubMed=15781858; DOI=10.1073/pnas.0501181102;
RA Hackbusch J., Richter K., Muller J., Salamini F., Uhrig J.F.;
RT "A central role of Arabidopsis thaliana ovate family proteins in networking
RT and subcellular localization of 3-aa loop extension homeodomain proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4908-4912(2005).
RN [8]
RP INTERACTION WITH BEL1; BLH1 AND BLH2.
RX PubMed=17873098; DOI=10.1105/tpc.106.048769;
RA Kumar R., Kushalappa K., Godt D., Pidkowich M.S., Pastorelli S.,
RA Hepworth S.R., Haughn G.W.;
RT "The Arabidopsis BEL1-LIKE HOMEODOMAIN proteins SAW1 and SAW2 act
RT redundantly to regulate KNOX expression spatially in leaf margins.";
RL Plant Cell 19:2719-2735(2007).
CC -!- SUBUNIT: May form heterodimeric complex with the TALE/BELL protein
CC BEL1, BLH1 and BLH2. Interacts with OFP1, OFP2, OFP3 and OFP4.
CC {ECO:0000269|PubMed:11701881, ECO:0000269|PubMed:15781858,
CC ECO:0000269|PubMed:17873098}.
CC -!- INTERACTION:
CC P48002; Q38897: BEL1; NbExp=3; IntAct=EBI-1153922, EBI-1153783;
CC P48002; Q9FXG8: BLH10; NbExp=3; IntAct=EBI-1153922, EBI-1153895;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TALE/KNOX homeobox family.
CC {ECO:0000255|PROSITE-ProRule:PRU00559}.
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DR EMBL; AF306661; AAL37042.1; -; mRNA.
DR EMBL; D43962; BAA22602.1; -; mRNA.
DR EMBL; AL021636; CAA16585.1; -; Genomic_DNA.
DR EMBL; AL161580; CAB79922.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85997.1; -; Genomic_DNA.
DR EMBL; BT026033; ABG48389.1; -; mRNA.
DR EMBL; X92394; CAA63132.1; -; mRNA.
DR PIR; T04641; T04641.
DR RefSeq; NP_194932.1; NM_119356.4.
DR AlphaFoldDB; P48002; -.
DR SMR; P48002; -.
DR BioGRID; 14621; 25.
DR IntAct; P48002; 21.
DR STRING; 3702.AT4G32040.1; -.
DR PaxDb; P48002; -.
DR PRIDE; P48002; -.
DR ProteomicsDB; 237045; -.
DR EnsemblPlants; AT4G32040.1; AT4G32040.1; AT4G32040.
DR GeneID; 829335; -.
DR Gramene; AT4G32040.1; AT4G32040.1; AT4G32040.
DR KEGG; ath:AT4G32040; -.
DR Araport; AT4G32040; -.
DR TAIR; locus:2116632; AT4G32040.
DR eggNOG; KOG0773; Eukaryota.
DR HOGENOM; CLU_040111_1_0_1; -.
DR InParanoid; P48002; -.
DR OMA; DWKSASC; -.
DR OrthoDB; 1070344at2759; -.
DR PhylomeDB; P48002; -.
DR PRO; PR:P48002; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P48002; baseline and differential.
DR Genevisible; P48002; 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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0071369; P:cellular response to ethylene stimulus; IDA:TAIR.
DR GO; GO:0009727; P:detection of ethylene stimulus; IEP:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR005539; ELK_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR008422; Homeobox_KN_domain.
DR InterPro; IPR005540; KNOX1.
DR InterPro; IPR005541; KNOX2.
DR Pfam; PF03789; ELK; 1.
DR Pfam; PF05920; Homeobox_KN; 1.
DR Pfam; PF03790; KNOX1; 1.
DR Pfam; PF03791; KNOX2; 1.
DR SMART; SM01188; ELK; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM01255; KNOX1; 1.
DR SMART; SM01256; KNOX2; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51213; ELK; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Homeobox; Nucleus; Reference proteome.
FT CHAIN 1..383
FT /note="Homeobox protein knotted-1-like 5"
FT /id="PRO_0000048961"
FT DOMAIN 281..301
FT /note="ELK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00559"
FT DNA_BIND 302..365
FT /note="Homeobox; TALE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 43284 MW; D9B91F16F088E10F CRC64;
MSFNSSHLLP PQEDLPLRHF TDQSQQPPPQ RHFSETPSLV TASFLNLPTT LTTADSDLAP
PHRNGDNSVA DTNPRWLSFH SEMQNTGEVR SEVIDGVNAD GETILGVVGG EDWRSASYKA
AILRHPMYEQ LLAAHVACLR VATPVDQIPR IDAQLSQLHT VAAKYSTLGV VVDNKELDHF
MSHYVVLLCS FKEQLQHHVC VHAMEAITAC WEIEQSLQSL TGVSPSESNG KTMSDDEDDN
QVESEVNMFD GSLDGSDCLM GFGPLVPTER ERSLMERVKK ELKHELKQGF KEKIVDIREE
IMRKRRAGKL PGDTTSVLKE WWRTHSKWPY PTEEDKAKLV QETGLQLKQI NNWFINQRKR
NWNSNSSTSS TLTKNKRKRT GKS
