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SCRM2_ARATH
ID   SCRM2_ARATH             Reviewed;         450 AA.
AC   Q9LPW3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Transcription factor SCREAM2;
DE   AltName: Full=Basic helix-loop-helix protein 33;
DE            Short=AtbHLH33;
DE            Short=bHLH 33;
DE   AltName: Full=Transcription factor EN 44;
DE   AltName: Full=bHLH transcription factor bHLH033;
GN   Name=SCRM2; Synonyms=BHLH33, EN44; OrderedLocusNames=At1g12860;
GN   ORFNames=F13K23.12;
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], FUNCTION, MUTAGENESIS OF ARG-203, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH SPCH; MUTE AND FAMA,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=18641265; DOI=10.1105/tpc.108.060848;
RA   Kanaoka M.M., Pillitteri L.J., Fujii H., Yoshida Y., Bogenschutz N.L.,
RA   Takabayashi J., Zhu J.-K., Torii K.U.;
RT   "SCREAM/ICE1 and SCREAM2 specify three cell-state transitional steps
RT   leading to arabidopsis stomatal differentiation.";
RL   Plant Cell 20:1775-1785(2008).
RN   [2]
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   [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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
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 [MRNA] OF 278-450, TISSUE SPECIFICITY, GENE FAMILY, AND
RP   NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=12679534; DOI=10.1093/molbev/msg088;
RA   Heim M.A., Jakoby M., Werber M., Martin C., Weisshaar B., Bailey P.C.;
RT   "The basic helix-loop-helix transcription factor family in plants: a
RT   genome-wide study of protein structure and functional diversity.";
RL   Mol. Biol. Evol. 20:735-747(2003).
RN   [7]
RP   GENE FAMILY.
RX   PubMed=12897250; DOI=10.1105/tpc.013839;
RA   Toledo-Ortiz G., Huq E., Quail P.H.;
RT   "The Arabidopsis basic/helix-loop-helix transcription factor family.";
RL   Plant Cell 15:1749-1770(2003).
RN   [8]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=14600211; DOI=10.1105/tpc.151140;
RA   Bailey P.C., Martin C., Toledo-Ortiz G., Quail P.H., Huq E., Heim M.A.,
RA   Jakoby M., Werber M., Weisshaar B.;
RT   "Update on the basic helix-loop-helix transcription factor gene family in
RT   Arabidopsis thaliana.";
RL   Plant Cell 15:2497-2502(2003).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH SPCH.
RC   STRAIN=cv. Columbia;
RX   PubMed=28507175; DOI=10.1104/pp.17.00615;
RA   de Marcos A., Houbaert A., Trivino M., Delgado D., Martin-Trillo M.,
RA   Russinova E., Fenoll C., Mena M.;
RT   "A mutation in the bHLH domain of the SPCH transcription factor uncovers a
RT   BR-dependent mechanism for stomatal development.";
RL   Plant Physiol. 174:823-842(2017).
CC   -!- FUNCTION: Mediates stomatal differentiation in the epidermis probably
CC       by controlling successive roles of SPCH, MUTE, and FAMA
CC       (PubMed:18641265). Functions as a dimer with SPCH during stomatal
CC       initiation (PubMed:18641265, PubMed:28507175).
CC       {ECO:0000269|PubMed:18641265, ECO:0000269|PubMed:28507175}.
CC   -!- SUBUNIT: Homodimer (Probable). Heterodimers with SPCH, MUTE, and FAMA.
CC       {ECO:0000269|PubMed:18641265, ECO:0000269|PubMed:28507175,
CC       ECO:0000305}.
CC   -!- INTERACTION:
CC       Q9LPW3; Q39026: MPK6; NbExp=4; IntAct=EBI-4451593, EBI-349548;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC       ECO:0000269|PubMed:18641265}.
CC   -!- TISSUE SPECIFICITY: Expressed constitutively in roots, leaves, stems,
CC       and flowers. Broad expression within stomatal cell lineages of leaf
CC       epidermis, except in mature guard-cells. {ECO:0000269|PubMed:12679534,
CC       ECO:0000269|PubMed:18641265}.
CC   -!- DISRUPTION PHENOTYPE: The ice1-2 scrm2-1 double mutant lacks stomata so
CC       that the epidermis only contains pavement cells.
CC       {ECO:0000269|PubMed:18641265}.
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DR   EMBL; EU369670; ACA63683.1; -; mRNA.
DR   EMBL; AC012187; AAF78492.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28940.1; -; Genomic_DNA.
DR   EMBL; AK118011; BAC42644.1; -; mRNA.
DR   EMBL; BT005377; AAO63441.1; -; mRNA.
DR   EMBL; AF488572; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; C86262; C86262.
DR   RefSeq; NP_172746.2; NM_101157.3.
DR   AlphaFoldDB; Q9LPW3; -.
DR   SMR; Q9LPW3; -.
DR   BioGRID; 23083; 11.
DR   IntAct; Q9LPW3; 3.
DR   STRING; 3702.AT1G12860.1; -.
DR   PaxDb; Q9LPW3; -.
DR   PRIDE; Q9LPW3; -.
DR   ProteomicsDB; 232887; -.
DR   EnsemblPlants; AT1G12860.1; AT1G12860.1; AT1G12860.
DR   GeneID; 837843; -.
DR   Gramene; AT1G12860.1; AT1G12860.1; AT1G12860.
DR   KEGG; ath:AT1G12860; -.
DR   Araport; AT1G12860; -.
DR   TAIR; locus:2010311; AT1G12860.
DR   eggNOG; ENOG502QQ2A; Eukaryota.
DR   HOGENOM; CLU_035660_5_0_1; -.
DR   InParanoid; Q9LPW3; -.
DR   OMA; EQCQEDH; -.
DR   OrthoDB; 1119564at2759; -.
DR   PhylomeDB; Q9LPW3; -.
DR   PRO; PR:Q9LPW3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LPW3; baseline and differential.
DR   Genevisible; Q9LPW3; AT.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0010444; P:guard mother cell differentiation; IMP:TAIR.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0050826; P:response to freezing; IMP:TAIR.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..450
FT                   /note="Transcription factor SCREAM2"
FT                   /id="PRO_0000358855"
FT   DOMAIN          263..312
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   DOMAIN          378..450
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         203
FT                   /note="R->H: Excessive stomatal differentiation."
FT                   /evidence="ECO:0000269|PubMed:18641265"
FT   CONFLICT        284
FT                   /note="Y -> N (in Ref. 5; AF488572)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   450 AA;  49796 MW;  69FB1B9C525C8646 CRC64;
     MNSDGVWLDG SGESPEVNNG EAASWVRNPD EDWFNNPPPP QHTNQNDFRF NGGFPLNPSE
     NLLLLLQQSI DSSSSSSPLL HPFTLDAASQ QQQQQQQQQE QSFLATKACI VSLLNVPTIN
     NNTFDDFGFD SGFLGQQFHG NHQSPNSMNF TGLNHSVPDF LPAPENSSGS CGLSPLFSNR
     AKVLKPLQVM ASSGSQPTLF QKRAAMRQSS SSKMCNSESS SEMRKSSYER EIDDTSTGII
     DISGLNYESD DHNTNNNKGK KKGMPAKNLM AERRRRKKLN DRLYMLRSVV PKISKMDRAS
     ILGDAIDYLK ELLQRINDLH TELESTPPSS SSLHPLTPTP QTLSYRVKEE LCPSSSLPSP
     KGQQPRVEVR LREGKAVNIH MFCGRRPGLL LSTMRALDNL GLDVQQAVIS CFNGFALDVF
     RAEQCQEDHD VLPEQIKAVL LDTAGYAGLV
 
 
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