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HDG1_ARATH
ID   HDG1_ARATH              Reviewed;         808 AA.
AC   Q9M2E8; Q9LFW5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Homeobox-leucine zipper protein HDG1 {ECO:0000303|PubMed:16778018};
DE   AltName: Full=HD-ZIP protein HDG1 {ECO:0000303|PubMed:16778018};
DE   AltName: Full=Homeodomain GLABRA 2-like protein 1 {ECO:0000303|PubMed:10809443};
DE            Short=AtHD-GL2-1 {ECO:0000303|PubMed:10809443};
DE   AltName: Full=Homeodomain transcription factor HDG1 {ECO:0000303|PubMed:16778018};
DE   AltName: Full=Protein HOMEODOMAIN GLABROUS 1 {ECO:0000303|PubMed:16778018};
GN   Name=HDG1 {ECO:0000303|PubMed:16778018};
GN   Synonyms=ASK-beta {ECO:0000303|PubMed:9804971},
GN   HD-GL2-1 {ECO:0000303|PubMed:10809443},
GN   HDGL2-1 {ECO:0000303|PubMed:10809443};
GN   OrderedLocusNames=At3g61150 {ECO:0000312|Araport:AT3G61150};
GN   ORFNames=T20K12.50 {ECO:0000312|EMBL:CAB71045.1};
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 [GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9804971; DOI=10.1016/s0167-4781(98)00187-0;
RA   Tichtinsky G., Tavares R., Takvorian A., Schwebel-Dugue N., Twell D.,
RA   Kreis M.;
RT   "An evolutionary conserved group of plant GSK-3/shaggy-like protein kinase
RT   genes preferentially expressed in developing pollen.";
RL   Biochim. Biophys. Acta 1442:261-273(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
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   [4]
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   [5]
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   [6]
RP   TISSUE SPECIFICITY, 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   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH CFL1.
RC   STRAIN=cv. Columbia;
RX   PubMed=21954461; DOI=10.1105/tpc.111.088625;
RA   Wu R., Li S., He S., Wassmann F., Yu C., Qin G., Schreiber L., Qu L.-J.,
RA   Gu H.;
RT   "CFL1, a WW domain protein, regulates cuticle development by modulating the
RT   function of HDG1, a class IV homeodomain transcription factor, in rice and
RT   Arabidopsis.";
RL   Plant Cell 23:3392-3411(2011).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Columbia;
RX   PubMed=23590515; DOI=10.1111/tpj.12211;
RA   Kamata N., Okada H., Komeda Y., Takahashi T.;
RT   "Mutations in epidermis-specific HD-ZIP IV genes affect floral organ
RT   identity in Arabidopsis thaliana.";
RL   Plant J. 75:430-440(2013).
RN   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH BBM, AND DEVELOPMENTAL
RP   STAGE.
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 (By similarity). Promotes
CC       cuticle development probably by modulating the expression of the
CC       downstream genes BDG and FDH, possibly repressed in a CFL1-dependent
CC       manner (PubMed:21954461). Involved, together with PDF2, in the
CC       regulation of flower organs development by promoting the expression of
CC       APETALA 3 (AP3) in the epidermis and internal cell layers of developing
CC       flowers (PubMed:23590515). In opposition to BBM, seems to promote cell
CC       differentiation and giant cell identity via transcriptionnal repression
CC       of meristem and cell proliferation genes (PubMed:25564655).
CC       {ECO:0000250|UniProtKB:Q0WV12, ECO:0000269|PubMed:21954461,
CC       ECO:0000269|PubMed:23590515, ECO:0000269|PubMed:25564655}.
CC   -!- SUBUNIT: Interacts with CFL1 (PubMed:21954461). Binds with BBM
CC       (PubMed:25564655). {ECO:0000269|PubMed:21954461,
CC       ECO:0000269|PubMed:25564655}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in trichomes forming at the base of young
CC       leaves, in endodermal cell lines around emergent lateral roots and in
CC       the epidermal layer of the stamen filament.
CC       {ECO:0000269|PubMed:16778018}.
CC   -!- DEVELOPMENTAL STAGE: During embryogenesis, first observed at low levels
CC       in the embryo protoderm starting at the late globular stage
CC       (PubMed:25564655). In primary and lateral roots, observed in the
CC       epidermis, the outer layer of columella cells and lateral root cap
CC       (PubMed:25564655). Restricted to the epidermal cell layer during floral
CC       organ formation (PubMed:23590515). Also present in flower meristems,
CC       shoot apical mersitems (SAM) and leaf primordia (PubMed:25564655).
CC       {ECO:0000269|PubMed:23590515, ECO:0000269|PubMed:25564655}.
CC   -!- DISRUPTION PHENOTYPE: Defective cuticle phenotypes leading to curly
CC       flag leaves and organ fusion (PubMed:21954461). The double mutant pdf2-
CC       1 hdg1-1 exhibits abnormal flowers with sepaloid petals and carpelloid
CC       stamens in association with a reduced expression of APETALA 3 (AP3) in
CC       the epidermis and internal cell layers of developing flowers
CC       (PubMed:23590515). Increased cell division leading to cell
CC       overproliferation (PubMed:25564655). {ECO:0000269|PubMed:21954461,
CC       ECO:0000269|PubMed:23590515, ECO:0000269|PubMed:25564655}.
CC   -!- SIMILARITY: Belongs to the HD-ZIP homeobox family. Class IV subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ224338; CAB45018.1; -; Genomic_DNA.
DR   EMBL; AL137898; CAB71045.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE80161.1; -; Genomic_DNA.
DR   EMBL; AY050866; AAK92803.1; -; mRNA.
DR   EMBL; AY096757; AAM20391.1; -; mRNA.
DR   PIR; T47907; T47907.
DR   RefSeq; NP_191674.1; NM_115979.5.
DR   AlphaFoldDB; Q9M2E8; -.
DR   SMR; Q9M2E8; -.
DR   BioGRID; 10601; 7.
DR   IntAct; Q9M2E8; 10.
DR   STRING; 3702.AT3G61150.1; -.
DR   iPTMnet; Q9M2E8; -.
DR   PaxDb; Q9M2E8; -.
DR   PRIDE; Q9M2E8; -.
DR   ProteomicsDB; 230313; -.
DR   EnsemblPlants; AT3G61150.1; AT3G61150.1; AT3G61150.
DR   GeneID; 825287; -.
DR   Gramene; AT3G61150.1; AT3G61150.1; AT3G61150.
DR   KEGG; ath:AT3G61150; -.
DR   Araport; AT3G61150; -.
DR   TAIR; locus:2098866; AT3G61150.
DR   eggNOG; ENOG502QUAY; Eukaryota.
DR   HOGENOM; CLU_015002_2_1_1; -.
DR   InParanoid; Q9M2E8; -.
DR   OMA; TEYDENR; -.
DR   OrthoDB; 226429at2759; -.
DR   PhylomeDB; Q9M2E8; -.
DR   PRO; PR:Q9M2E8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M2E8; baseline and differential.
DR   Genevisible; Q9M2E8; 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:0048497; P:maintenance of floral organ identity; IGI: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   Coiled coil; DNA-binding; Homeobox; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..808
FT                   /note="Homeobox-leucine zipper protein HDG1"
FT                   /id="PRO_0000331663"
FT   DOMAIN          310..541
FT                   /note="START"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT   DNA_BIND        110..169
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          57..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          158..233
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        57..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        597
FT                   /note="E -> K (in Ref. 1; CAB45018)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   808 AA;  88167 MW;  E0D768753EEDC7B5 CRC64;
     MNFNGFLDDG AGASKLLSDA PYNNHFSFSA VDTMLGSAAI APSQSLPFSS SGLSLGLQTN
     GEMSRNGEIM ESNVSRKSSR GEDVESRSES DNAEAVSGDD LDTSDRPLKK KKRYHRHTPK
     QIQDLESVFK ECAHPDEKQR LDLSRRLNLD PRQVKFWFQN RRTQMKTQIE RHENALLRQE
     NDKLRAENMS VREAMRNPMC GNCGGPAVIG EISMEEQHLR IENSRLKDEL DRVCALTGKF
     LGRSNGSHHI PDSALVLGVG VGSGGCNVGG GFTLSSPLLP QASPRFEISN GTGSGLVATV
     NRQQPVSVSD FDQRSRYLDL ALAAMDELVK MAQTREPLWV RSSDSGFEVL NQEEYDTSFS
     RCVGPKQDGF VSEASKEAGT VIINSLALVE TLMDSERWAE MFPSMVSRTS TTEIISSGMG
     GRNGALHLMH AELQLLSPLV PVRQVSFLRF CKQHAEGVWA VVDVSIDSIR EGSSSSCRRL
     PSGCLVQDMA NGYSKVTWIE HTEYDENHIH RLYRPLLRCG LAFGAHRWMA ALQRQCECLT
     ILMSSTVSTS TNPSPINCNG RKSMLKLAKR MTDNFCGGVC ASSLQKWSKL NVGNVDEDVR
     IMTRKSVNNP GEPPGIILNA ATSVWMPVSP RRLFDFLGNE RLRSEWDILS NGGPMKEMAH
     IAKGHDRSNS VSLLRASAIN ANQSSMLILQ ETSIDAAGAV VVYAPVDIPA MQAVMNGGDS
     AYVALLPSGF AILPNGQAGT QRCAAEERNS IGNGGCMEEG GSLLTVAFQI LVNSLPTAKL
     TVESVETVNN LISCTVQKIK AALHCDST
 
 
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