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HAT22_ARATH
ID   HAT22_ARATH             Reviewed;         278 AA.
AC   P46604; Q546G6;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 155.
DE   RecName: Full=Homeobox-leucine zipper protein HAT22;
DE   AltName: Full=Homeodomain-leucine zipper protein HAT22;
DE            Short=HD-ZIP protein 22;
GN   Name=HAT22; OrderedLocusNames=At4g37790; ORFNames=T28I19.70;
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 / MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=7915839; DOI=10.1073/pnas.91.18.8393;
RA   Schena M., Davis R.W.;
RT   "Structure of homeobox-leucine zipper genes suggests a model for the
RT   evolution of gene families.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:8393-8397(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sessa G., Carabelli M., Ciarbelli A.R., Ruzza V., Steindler C., Ruberti I.;
RT   "Nucleotide sequence of the Arabidopsis HAT22 mRNA, encoding an HD-Zip II
RT   protein related to ATHB-2.";
RL   Submitted (APR-2002) 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;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 166-221.
RC   STRAIN=cv. Columbia;
RX   PubMed=1349174; DOI=10.1073/pnas.89.9.3894;
RA   Schena M., Davis R.W.;
RT   "HD-Zip proteins: members of an Arabidopsis homeodomain protein
RT   superfamily.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:3894-3898(1992).
RN   [8]
RP   GENE FAMILY.
RX   PubMed=16055682; DOI=10.1104/pp.105.063461;
RA   Henriksson E., Olsson A.S.B., Johannesson H., Johansson H., Hanson J.,
RA   Engstroem P., Soederman E.;
RT   "Homeodomain leucine zipper class I genes in Arabidopsis. Expression
RT   patterns and phylogenetic relationships.";
RL   Plant Physiol. 139:509-518(2005).
RN   [9]
RP   SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
CC   -!- FUNCTION: Probable transcription factor. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P46604; Q8GXM7: ATHB-X; NbExp=3; IntAct=EBI-4448318, EBI-3133795;
CC       P46604; P46602: HAT3; NbExp=3; IntAct=EBI-4448318, EBI-4450405;
CC       P46604; Q05466: HAT4; NbExp=3; IntAct=EBI-4448318, EBI-4428728;
CC       P46604; Q9XI84: LSMT-L; NbExp=3; IntAct=EBI-4448318, EBI-15192835;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC       ECO:0000269|PubMed:19245862}.
CC   -!- SIMILARITY: Belongs to the HD-ZIP homeobox family. Class II subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U09336; AAA56902.1; -; mRNA.
DR   EMBL; U09337; AAA56903.1; -; Genomic_DNA.
DR   EMBL; AJ441254; CAD29653.1; -; mRNA.
DR   EMBL; AL035709; CAB38927.1; -; Genomic_DNA.
DR   EMBL; AL161592; CAB80444.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86838.1; -; Genomic_DNA.
DR   EMBL; BT002318; AAN86151.1; -; mRNA.
DR   EMBL; AY087563; AAM65105.1; -; mRNA.
DR   EMBL; M90417; AAA32817.1; -; mRNA.
DR   PIR; T06026; T06026.
DR   RefSeq; NP_195493.1; NM_119941.4.
DR   AlphaFoldDB; P46604; -.
DR   SMR; P46604; -.
DR   BioGRID; 15216; 19.
DR   IntAct; P46604; 17.
DR   STRING; 3702.AT4G37790.1; -.
DR   iPTMnet; P46604; -.
DR   PaxDb; P46604; -.
DR   PRIDE; P46604; -.
DR   ProteomicsDB; 230381; -.
DR   EnsemblPlants; AT4G37790.1; AT4G37790.1; AT4G37790.
DR   GeneID; 829935; -.
DR   Gramene; AT4G37790.1; AT4G37790.1; AT4G37790.
DR   KEGG; ath:AT4G37790; -.
DR   Araport; AT4G37790; -.
DR   TAIR; locus:2137599; AT4G37790.
DR   eggNOG; KOG0483; Eukaryota.
DR   HOGENOM; CLU_049516_0_0_1; -.
DR   InParanoid; P46604; -.
DR   OMA; RERDICG; -.
DR   OrthoDB; 1333079at2759; -.
DR   PhylomeDB; P46604; -.
DR   PRO; PR:P46604; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; P46604; baseline and differential.
DR   Genevisible; P46604; 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:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR   GO; GO:0009735; P:response to cytokinin; IEP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR003106; Leu_zip_homeo.
DR   Pfam; PF02183; HALZ; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   SMART; SM00340; HALZ; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Homeobox; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..278
FT                   /note="Homeobox-leucine zipper protein HAT22"
FT                   /id="PRO_0000049141"
FT   DNA_BIND        123..182
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          68..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..211
FT                   /note="Leucine-zipper"
FT   COMPBIAS        68..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         92
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19245862"
FT   CONFLICT        221
FT                   /note="Y -> S (in Ref. 7; AAA32817)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   278 AA;  30730 MW;  C36E8344DED8A1CE CRC64;
     MGLDDSCNTG LVLGLGLSPT PNNYNHAIKK SSSTVDHRFI RLDPSLTLSL SGESYKIKTG
     AGAGDQICRQ TSSHSGISSF SSGRVKRERE ISGGDGEEEA EETTERVVCS RVSDDHDDEE
     GVSARKKLRL TKQQSALLED NFKLHSTLNP KQKQALARQL NLRPRQVEVW FQNRRARTKL
     KQTEVDCEFL KKCCETLTDE NRRLQKELQD LKALKLSQPF YMHMPAATLT MCPSCERLGG
     GGVGGDTTAV DEETAKGAFS IVTKPRFYNP FTNPSAAC
 
 
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