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ANL2_ARATH
ID   ANL2_ARATH              Reviewed;         802 AA.
AC   Q0WV12; O65281; P93041; Q9SWZ6;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Homeobox-leucine zipper protein ANTHOCYANINLESS 2 {ECO:0000303|PubMed:10402424};
DE   AltName: Full=HD-ZIP protein ANL2 {ECO:0000303|PubMed:10402424};
DE   AltName: Full=Homeodomain protein AHDP {ECO:0000303|PubMed:10402424};
DE   AltName: Full=Homeodomain transcription factor ANL2 {ECO:0000303|PubMed:10402424};
GN   Name=ANL2 {ECO:0000303|PubMed:10402424};
GN   OrderedLocusNames=At4g00730 {ECO:0000312|Araport:AT4G00730};
GN   ORFNames=F6N23.10 {ECO:0000312|EMBL:AAC13617.1};
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 [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=8989876; DOI=10.2307/3870458;
RA   Lu P., Porat R., Nadeau J.A., O'Neill S.D.;
RT   "Identification of a meristem L1 layer-specific gene in Arabidopsis that is
RT   expressed during embryonic pattern formation and defines a new class of
RT   homeobox genes.";
RL   Plant Cell 8:2155-2168(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=10402424; DOI=10.2307/3870744;
RA   Kubo H., Peeters A.J.M., Aarts M.G.M., Pereira A., Koornneef M.;
RT   "ANTHOCYANINLESS2, a homeobox gene affecting anthocyanin distribution and
RT   root development in Arabidopsis.";
RL   Plant Cell 11:1217-1226(1999).
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   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   GENE FAMILY.
RX   PubMed=10809443; DOI=10.1023/a:1006368316413;
RA   Tavares R., Aubourg S., Lecharny A., Kreis M.;
RT   "Organization and structural evolution of four multigene families in
RT   Arabidopsis thaliana: AtLCAD, AtLGT, AtMYST and AtHD-GL2.";
RL   Plant Mol. Biol. 42:703-717(2000).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16778018; DOI=10.1104/pp.106.077388;
RA   Nakamura M., Katsumata H., Abe M., Yabe N., Komeda Y., Yamamoto K.T.,
RA   Takahashi T.;
RT   "Characterization of the class IV homeodomain-leucine zipper gene family in
RT   Arabidopsis.";
RL   Plant Physiol. 141:1363-1375(2006).
RN   [8]
RP   INTERACTION WITH AIL7/PLT7; ANT; BBM AND AIL1.
RC   STRAIN=cv. Columbia;
RX   PubMed=25564655; DOI=10.1242/dev.117168;
RA   Horstman A., Fukuoka H., Muino J.M., Nitsch L., Guo C., Passarinho P.,
RA   Sanchez-Perez G., Immink R., Angenent G., Boutilier K.;
RT   "AIL and HDG proteins act antagonistically to control cell proliferation.";
RL   Development 142:454-464(2015).
CC   -!- FUNCTION: Probable transcription factor involved in the regulation of
CC       the tissue-specific accumulation of anthocyanins and in cellular
CC       organization of the primary root. {ECO:0000269|PubMed:10402424}.
CC   -!- SUBUNIT: Interacts with AIL7/PLT7, ANT, BBM and AIL1.
CC       {ECO:0000269|PubMed:25564655}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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=Q0WV12-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and floral buds.
CC       {ECO:0000269|PubMed:10402424}.
CC   -!- DISRUPTION PHENOTYPE: Plants display a strong reduction of anthocyanin
CC       content on the adaxial side of rosette leaves, a slight reduction onf
CC       the abaxial side, and extra cells between cortical and epidermal layers
CC       in roots. {ECO:0000269|PubMed:10402424}.
CC   -!- SIMILARITY: Belongs to the HD-ZIP homeobox family. Class IV subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB41901.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAB41901.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAC13617.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80882.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; U85254; AAB41901.1; ALT_SEQ; mRNA.
DR   EMBL; AF077335; AAD47139.1; -; Genomic_DNA.
DR   EMBL; AF058919; AAC13617.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161472; CAB80882.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE81926.1; -; Genomic_DNA.
DR   EMBL; AK226968; BAE99036.1; -; mRNA.
DR   PIR; T01237; T01237.
DR   RefSeq; NP_567183.2; NM_116298.4. [Q0WV12-1]
DR   AlphaFoldDB; Q0WV12; -.
DR   SMR; Q0WV12; -.
DR   STRING; 3702.AT4G00730.1; -.
DR   iPTMnet; Q0WV12; -.
DR   PaxDb; Q0WV12; -.
DR   PRIDE; Q0WV12; -.
DR   ProteomicsDB; 244989; -. [Q0WV12-1]
DR   EnsemblPlants; AT4G00730.1; AT4G00730.1; AT4G00730. [Q0WV12-1]
DR   GeneID; 828022; -.
DR   Gramene; AT4G00730.1; AT4G00730.1; AT4G00730. [Q0WV12-1]
DR   KEGG; ath:AT4G00730; -.
DR   Araport; AT4G00730; -.
DR   TAIR; locus:2127008; AT4G00730.
DR   eggNOG; ENOG502QUAY; Eukaryota.
DR   HOGENOM; CLU_015002_2_1_1; -.
DR   InParanoid; Q0WV12; -.
DR   OMA; PCIGMRP; -.
DR   OrthoDB; 226429at2759; -.
DR   PhylomeDB; Q0WV12; -.
DR   PRO; PR:Q0WV12; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q0WV12; baseline and differential.
DR   Genevisible; Q0WV12; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0043481; P:anthocyanin accumulation in tissues in response to UV light; IMP:TAIR.
DR   GO; GO:0006723; P:cuticle hydrocarbon biosynthetic process; IMP:TAIR.
DR   GO; GO:0009827; P:plant-type cell wall modification; IMP:TAIR.
DR   GO; GO:0048364; P:root development; IMP:TAIR.
DR   GO; GO:0048765; P:root hair cell differentiation; IMP:TAIR.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR042160; GLABRA2/ANL2/PDF2/ATML1-like.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR002913; START_lipid-bd_dom.
DR   PANTHER; PTHR45654; PTHR45654; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   Pfam; PF01852; START; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00234; START; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS50848; START; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; DNA-binding; Homeobox; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..802
FT                   /note="Homeobox-leucine zipper protein ANTHOCYANINLESS 2"
FT                   /id="PRO_0000331657"
FT   DOMAIN          315..546
FT                   /note="START"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT   DNA_BIND        134..193
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          71..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          182..221
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        78..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        286
FT                   /note="Missing (in Ref. 2; AAD47139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        463
FT                   /note="A -> P (in Ref. 2; AAD47139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        548
FT                   /note="I -> M (in Ref. 2; AAD47139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        735..736
FT                   /note="LP -> SS (in Ref. 2; AAD47139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        801
FT                   /note="E -> G (in Ref. 2; AAD47139)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   802 AA;  87194 MW;  C7BADF1697E708A8 CRC64;
     MNFGSLFDNT PGGGSTGARL LSGLSYGNHT AATNVLPGGA MAQAAAAASL FSPPLTKSVY
     ASSGLSLALE QPERGTNRGE ASMRNNNNVG GGGDTFDGSV NRRSREEEHE SRSGSDNVEG
     ISGEDQDAAD KPPRKKRYHR HTPQQIQELE SMFKECPHPD EKQRLELSKR LCLETRQVKF
     WFQNRRTQMK TQLERHENAL LRQENDKLRA ENMSIREAMR NPICTNCGGP AMLGDVSLEE
     HHLRIENARL KDELDRVCNL TGKFLGHHHN HHYNSSLELA VGTNNNGGHF AFPPDFGGGG
     GCLPPQQQQS TVINGIDQKS VLLELALTAM DELVKLAQSE EPLWVKSLDG ERDELNQDEY
     MRTFSSTKPT GLATEASRTS GMVIINSLAL VETLMDSNRW TEMFPCNVAR ATTTDVISGG
     MAGTINGALQ LMNAELQVLS PLVPVRNVNF LRFCKQHAEG VWAVVDVSID PVRENSGGAP
     VIRRLPSGCV VQDVSNGYSK VTWVEHAEYD ENQIHQLYRP LLRSGLGFGS QRWLATLQRQ
     CECLAILISS SVTSHDNTSI TPGGRKSMLK LAQRMTFNFC SGISAPSVHN WSKLTVGNVD
     PDVRVMTRKS VDDPGEPPGI VLSAATSVWL PAAPQRLYDF LRNERMRCEW DILSNGGPMQ
     EMAHITKGQD QGVSLLRSNA MNANQSSMLI LQETCIDASG ALVVYAPVDI PAMHVVMNGG
     DSSYVALLPS GFAVLPDGGI DGGGSGDGDQ RPVGGGSLLT VAFQILVNNL PTAKLTVESV
     ETVNNLISCT VQKIRAALQC ES
 
 
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