PlantTFDB - Plant Transcription Factor Database @ CBI, PKU

PlantRegMap/PlantTFDB v5.0

Plant Transcription Factor Database

Transcription Factor Information

Basic Information | Signature Domain | Sequence |

Basic Information? help Back to Top

TF ID

XP_010091789.1

Organism

Morus notabilis

Taxonomic ID

981085

Taxonomic Lineage

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Moraceae; Morus

Family

G2-like

Protein Properties

Length: 1529aa MW: 171984 Da PI: 6.3857

Description

G2-like family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
XP_010091789.1	genome	BGI	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	G2-like	105.5	3e-33	267	321	1	55
G2-like 1 kprlrWtpeLHerFveaveqLGGsekAtPktilelmkvkgLtlehvkSHLQkYRl 55 kpr+rWtpeLHe+Fveav+qLGGse+AtPk +l+lmkv++Lt++hvkSHLQkYR+ XP_010091789.1 267 KPRMRWTPELHEAFVEAVNQLGGSERATPKGVLKLMKVESLTIYHVKSHLQKYRT 321 79****************************************************8 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
Gene3D	G3DSA:1.10.10.60	2.4E-31	264	323	IPR009057	Homeodomain-like
PROSITE profile	PS51294	11.229	264	324	IPR017930	Myb domain
SuperFamily	SSF46689	2.51E-17	265	321	IPR009057	Homeodomain-like
TIGRFAMs	TIGR01557	5.3E-24	267	321	IPR006447	Myb domain, plants
Pfam	PF00249	8.1E-9	269	320	IPR001005	SANT/Myb domain
Pfam	PF14379	3.9E-23	352	397	IPR025756	MYB-CC type transcription factor, LHEQLE-containing domain
Gene3D	G3DSA:3.30.40.10	6.6E-29	531	618	IPR013083	Zinc finger, RING/FYVE/PHD-type
SuperFamily	SSF57850	5.42E-33	533	615	No hit	No description
Pfam	PF14569	1.4E-37	537	610	IPR027934	Cellulose synthase, RING-type zinc finger
Pfam	PF03552	3.4E-283	816	1342	IPR005150	Cellulose synthase
SuperFamily	SSF53448	3.19E-10	829	886	IPR029044	Nucleotide-diphospho-sugar transferases
SuperFamily	SSF53448	3.19E-10	984	1043	IPR029044	Nucleotide-diphospho-sugar transferases
SuperFamily	SSF53448	3.19E-10	1081	1140	IPR029044	Nucleotide-diphospho-sugar transferases
SuperFamily	SSF53448	3.19E-10	1237	1371	IPR029044	Nucleotide-diphospho-sugar transferases

Gene Ontology ? help Back to Top
GO Term	GO Category	GO Description
GO:0006355	Biological Process	regulation of transcription, DNA-templated
GO:0009834	Biological Process	plant-type secondary cell wall biogenesis
GO:0030244	Biological Process	cellulose biosynthetic process
GO:0042742	Biological Process	defense response to bacterium
GO:0050832	Biological Process	defense response to fungus
GO:0071555	Biological Process	cell wall organization
GO:0005634	Cellular Component	nucleus
GO:0005886	Cellular Component	plasma membrane
GO:0016021	Cellular Component	integral component of membrane
GO:0003677	Molecular Function	DNA binding
GO:0016760	Molecular Function	cellulose synthase (UDP-forming) activity
GO:0046872	Molecular Function	metal ion binding

Sequence ? help Back to Top
Protein Sequence Length: 1529 aa Download sequence Send to blast
MEARPALSIP RSGTTQLTNM GVSGAFTSSL PVLPTPYEES YPKLPDSQQV SIERELMTSP 60 LTHASHLTSN SGVMGHIFSS SSGFSSDLHY SSVSLSQQKI QSRNTPFIPQ SSTNGVSFSV 120 PQSSYSTLLH STTSSHYTKE NSASWCTDSV EDLLDFSVNT PVENSQVESS SCSGIVASDE 180 FGRRNDWQDW ADQLITDNNA LNSSWDEFLA DTNVAEMEPK MAYQVEKPPS FQAQHPQLHQ 240 QHSAPSGEIQ TVATPSCSTN SATASAKPRM RWTPELHEAF VEAVNQLGGS ERATPKGVLK 300 LMKVESLTIY HVKSHLQKYR TARYRPESSE GSSEKRLTPI DEISSLDLKT GIEITEALRL 360 QMEVQKRLHE QLEIQRNLQL RIEEQGRYLQ IMFEKQKSGM DKLKASSSTL GNPSAVSSDA 420 IQGSPEKGEQ EASKIDDGKT ENDSSDAKTT TRGGSDELGE QKEAPQGKVP DNHEPDVCET 480 DPTPSHITTS SFASLHQPCF LHITFFAFAM AGFVTGSHTR NDLQVSDAEQ NSRPLTRQAA 540 SRICRVCGDE IGYKENGDLF VACHVCGFPV CRPCYDYERS DGNQSCPQCN TRYRRHKGCP 600 RVAGDDDDSD DGDDFDDEFR MKNHHSDNSD DHRINPLTNN SDNGEHNQQQ WQPNGHAFSV 660 AGSAAKEFEG EKEVYGNDEW KDRVEKWKVR QERRGNLLNK DDGNNDQGDD EDYLLAEARQ 720 PLWRKIPIPS SLISPYRIVI VLRLLILCFF FRFRILTPAY DAFPLWLISV ICEIWFAFSW 780 ILDQFPKWCP VTRQTYLDRL SIRFERDGEP NRLSPVDVYV STVDPLKEPP IITANTVLSI 840 LSVDYPVDKV CCYVSDDGAS MLLFDSLAET AEFARRWVPF CKKHNIEPRT PEFYFSEKID 900 YLKDKVHPSF VKERRAMKRE YEEFKVRINA LVAKAQKKPE DGWVMQDGTP WPGNNTRDHP 960 GMIQVYLGSG GALDVEGKEL PRLVYISREK RPGYQHHKKA GAMNALVRVS AVLSNAPFML 1020 NLDCDHYINN SKALREAMCF LMDPQLGKKL CYVQFPQRFD GIDLHDRYAN RNTVFFDINM 1080 KGLDGIQGPV YVGTGTVFNR QALYGYDPPV SEKRPKMTCD CWPSWCCCCC GSSRKSKSKK 1140 KGLASLLGGL YTKKKKMMGK NYVRKGSGAM FDLEEIEEGL EGYEELEKSS LMSQKNFEKR 1200 FGQSPVFIAS TLMEDGGLPE GTNSTTLIKE AIHVISCGYE EKTEWGKEIG WIYGSVTEDI 1260 LTGFKMHCRG WKSVYCIPKR PAFKGSAPIN LSDRLHQVLR WALGSVEIFL SRHCPLWYGY 1320 GGKLKLLERL AYINTILNNL ASVWFLALFL SIIATGVLEL RWSGVSLEDW WRNEQFWVIG 1380 GVSAHLFAVF QGLLKVLAGV DTNFTVTAKA ADDAEFGELY LFKWTTLLIP PTTLIILNMV 1440 GVVAGISDAI NNGYGSWGPL FGKLFFSFWV ILHLYPFLKG LMGRQNRTPT IVVLWSILLA 1500 SIFSLVWVRI DPFLPKQTGP ILKQCGVEC

Sequence ? help Back to Top

Protein Sequence Length: 1529 aa Download sequence Send to blast

MEARPALSIP RSGTTQLTNM GVSGAFTSSL PVLPTPYEES YPKLPDSQQV SIERELMTSP  60
LTHASHLTSN SGVMGHIFSS SSGFSSDLHY SSVSLSQQKI QSRNTPFIPQ SSTNGVSFSV  120
PQSSYSTLLH STTSSHYTKE NSASWCTDSV EDLLDFSVNT PVENSQVESS SCSGIVASDE  180
FGRRNDWQDW ADQLITDNNA LNSSWDEFLA DTNVAEMEPK MAYQVEKPPS FQAQHPQLHQ  240
QHSAPSGEIQ TVATPSCSTN SATASAKPRM RWTPELHEAF VEAVNQLGGS ERATPKGVLK  300
LMKVESLTIY HVKSHLQKYR TARYRPESSE GSSEKRLTPI DEISSLDLKT GIEITEALRL  360
QMEVQKRLHE QLEIQRNLQL RIEEQGRYLQ IMFEKQKSGM DKLKASSSTL GNPSAVSSDA  420
IQGSPEKGEQ EASKIDDGKT ENDSSDAKTT TRGGSDELGE QKEAPQGKVP DNHEPDVCET  480
DPTPSHITTS SFASLHQPCF LHITFFAFAM AGFVTGSHTR NDLQVSDAEQ NSRPLTRQAA  540
SRICRVCGDE IGYKENGDLF VACHVCGFPV CRPCYDYERS DGNQSCPQCN TRYRRHKGCP  600
RVAGDDDDSD DGDDFDDEFR MKNHHSDNSD DHRINPLTNN SDNGEHNQQQ WQPNGHAFSV  660
AGSAAKEFEG EKEVYGNDEW KDRVEKWKVR QERRGNLLNK DDGNNDQGDD EDYLLAEARQ  720
PLWRKIPIPS SLISPYRIVI VLRLLILCFF FRFRILTPAY DAFPLWLISV ICEIWFAFSW  780
ILDQFPKWCP VTRQTYLDRL SIRFERDGEP NRLSPVDVYV STVDPLKEPP IITANTVLSI  840
LSVDYPVDKV CCYVSDDGAS MLLFDSLAET AEFARRWVPF CKKHNIEPRT PEFYFSEKID  900
YLKDKVHPSF VKERRAMKRE YEEFKVRINA LVAKAQKKPE DGWVMQDGTP WPGNNTRDHP  960
GMIQVYLGSG GALDVEGKEL PRLVYISREK RPGYQHHKKA GAMNALVRVS AVLSNAPFML  1020
NLDCDHYINN SKALREAMCF LMDPQLGKKL CYVQFPQRFD GIDLHDRYAN RNTVFFDINM  1080
KGLDGIQGPV YVGTGTVFNR QALYGYDPPV SEKRPKMTCD CWPSWCCCCC GSSRKSKSKK  1140
KGLASLLGGL YTKKKKMMGK NYVRKGSGAM FDLEEIEEGL EGYEELEKSS LMSQKNFEKR  1200
FGQSPVFIAS TLMEDGGLPE GTNSTTLIKE AIHVISCGYE EKTEWGKEIG WIYGSVTEDI  1260
LTGFKMHCRG WKSVYCIPKR PAFKGSAPIN LSDRLHQVLR WALGSVEIFL SRHCPLWYGY  1320
GGKLKLLERL AYINTILNNL ASVWFLALFL SIIATGVLEL RWSGVSLEDW WRNEQFWVIG  1380
GVSAHLFAVF QGLLKVLAGV DTNFTVTAKA ADDAEFGELY LFKWTTLLIP PTTLIILNMV  1440
GVVAGISDAI NNGYGSWGPL FGKLFFSFWV ILHLYPFLKG LMGRQNRTPT IVVLWSILLA  1500
SIFSLVWVRI DPFLPKQTGP ILKQCGVEC

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
5jnp_A	8e-70	859	984	3	128	Probable cellulose synthase A catalytic subunit 8 [UDP-forming]
5jnp_B	8e-70	859	984	3	128	Probable cellulose synthase A catalytic subunit 8 [UDP-forming]
Search in ModeBase

Nucleic Localization Signal ? help Back to Top

No.	Start	End	Sequence
1	1138	1155	KKKGLASLLGGLYTKKKK

Functional Description ? help Back to Top
Source	Description
UniProt	Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the secondary cell wall formation. Required for the xylem cell wall thickening. {ECO:0000269\|PubMed:12538856, ECO:0000269\|PubMed:17351116}.

Cis-element ? help Back to Top
Source	Link
PlantRegMap	XP_010091789.1

Regulation -- PlantRegMap ? help Back to Top
Source	Upstream Regulator	Target Gene
PlantRegMap	Retrieve	-

Annotation -- Protein ? help Back to Top
Source	Hit ID	E-value	Description
Refseq	XP_024018384.1	0.0	LOW QUALITY PROTEIN: cellulose synthase A catalytic subunit 4 [UDP-forming]
Swissprot	Q84JA6	0.0	CESA4_ARATH; Cellulose synthase A catalytic subunit 4 [UDP-forming]
TrEMBL	W9RB71	0.0	W9RB71_9ROSA; Cellulose synthase
STRING	XP_010091789.1	0.0	(Morus notabilis)

Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID	E-value	Description
AT4G28610.1	1e-93	phosphate starvation response 1

Link Out ? help Back to Top
Entrez Gene	21398936

Publications ? help Back to Top
Holland N, et al. A comparative analysis of the plant cellulose synthase (CesA) gene family. Plant Physiol., 2000. 123(4): p. 1313-24 [PMID:10938350] Richmond T Higher plant cellulose synthases. Genome Biol., 2000. 1(4): p. REVIEWS3001 [PMID:11178255] Beeckman T, et al. Genetic complexity of cellulose synthase a gene function in Arabidopsis embryogenesis. Plant Physiol., 2002. 130(4): p. 1883-93 [PMID:12481071] Taylor NG,Howells RM,Huttly AK,Vickers K,Turner SR Interactions among three distinct CesA proteins essential for cellulose synthesis. Proc. Natl. Acad. Sci. U.S.A., 2003. 100(3): p. 1450-5 [PMID:12538856] Gardiner JC,Taylor NG,Turner SR Control of cellulose synthase complex localization in developing xylem. Plant Cell, 2003. 15(8): p. 1740-8 [PMID:12897249] Nühse TS,Stensballe A,Jensen ON,Peck SC Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database. Plant Cell, 2004. 16(9): p. 2394-405 [PMID:15308754] Sibout R, et al. CINNAMYL ALCOHOL DEHYDROGENASE-C and -D are the primary genes involved in lignin biosynthesis in the floral stem of Arabidopsis. Plant Cell, 2005. 17(7): p. 2059-76 [PMID:15937231] Brembu T,Winge P,Bones AM The small GTPase AtRAC2/ROP7 is specifically expressed during late stages of xylem differentiation in Arabidopsis. J. Exp. Bot., 2005. 56(419): p. 2465-76 [PMID:16061508] Somerville C Cellulose synthesis in higher plants. Annu. Rev. Cell Dev. Biol., 2006. 22: p. 53-78 [PMID:16824006] Roberts AW,Bushoven JT The cellulose synthase (CESA) gene superfamily of the moss Physcomitrella patens. Plant Mol. Biol., 2007. 63(2): p. 207-19 [PMID:17006591] Bosca S, et al. Interactions between MUR10/CesA7-dependent secondary cellulose biosynthesis and primary cell wall structure. Plant Physiol., 2006. 142(4): p. 1353-63 [PMID:17041031] Taylor NG Identification of cellulose synthase AtCesA7 (IRX3) in vivo phosphorylation sites--a potential role in regulating protein degradation. Plant Mol. Biol., 2007. 64(1-2): p. 161-71 [PMID:17427041] Srinivasasainagendra V,Page GP,Mehta T,Coulibaly I,Loraine AE CressExpress: a tool for large-scale mining of expression data from Arabidopsis. Plant Physiol., 2008. 147(3): p. 1004-16 [PMID:18467456] Mutwil M,Obro J,Willats WG,Persson S GeneCAT--novel webtools that combine BLAST and co-expression analyses. Nucleic Acids Res., 2008. 36(Web Server issue): p. W320-6 [PMID:18480120] Atanassov II,Pittman JK,Turner SR Elucidating the mechanisms of assembly and subunit interaction of the cellulose synthase complex of Arabidopsis secondary cell walls. J. Biol. Chem., 2009. 284(6): p. 3833-41 [PMID:19056734] Minic Z, et al. Transcriptomic analysis of Arabidopsis developing stems: a close-up on cell wall genes. BMC Plant Biol., 2009. 9: p. 6 [PMID:19149885] Timmers J, et al. Interactions between membrane-bound cellulose synthases involved in the synthesis of the secondary cell wall. FEBS Lett., 2009. 583(6): p. 978-82 [PMID:19258017] Betancur L, et al. Phylogenetically distinct cellulose synthase genes support secondary wall thickening in arabidopsis shoot trichomes and cotton fiber. J Integr Plant Biol, 2010. 52(2): p. 205-20 [PMID:20377682] Heyndrickx KS,Vandepoele K Systematic identification of functional plant modules through the integration of complementary data sources. Plant Physiol., 2012. 159(3): p. 884-901 [PMID:22589469] Carroll A, et al. Complexes with mixed primary and secondary cellulose synthases are functional in Arabidopsis plants. Plant Physiol., 2012. 160(2): p. 726-37 [PMID:22926318] Li S,Lei L,Gu Y Functional analysis of complexes with mixed primary and secondary cellulose synthases. Plant Signal Behav, 2013. 8(3): p. e23179 [PMID:23299322] Handakumbura PP, et al. Perturbation of Brachypodium distachyon CELLULOSE SYNTHASE A4 or 7 results in abnormal cell walls. BMC Plant Biol., 2013. 13: p. 131 [PMID:24024469] Hill JL,Hammudi MB,Tien M The Arabidopsis cellulose synthase complex: a proposed hexamer of CESA trimers in an equimolar stoichiometry. Plant Cell, 2014. 26(12): p. 4834-42 [PMID:25490917] Taylor-Teeples M, et al. An Arabidopsis gene regulatory network for secondary cell wall synthesis. Nature, 2015. 517(7536): p. 571-5 [PMID:25533953] Sun X, et al. A R2R3-MYB transcription factor that is specifically expressed in cotton (Gossypium hirsutum) fibers affects secondary cell wall biosynthesis and deposition in transgenic Arabidopsis. Physiol Plant, 2015. 154(3): p. 420-32 [PMID:25534543] Zhang Y, et al. Golgi-localized STELLO proteins regulate the assembly and trafficking of cellulose synthase complexes in Arabidopsis. Nat Commun, 2016. 7: p. 11656 [PMID:27277162] Kumar M, et al. S-Acylation of the cellulose synthase complex is essential for its plasma membrane localization. Science, 2016. 353(6295): p. 166-9 [PMID:27387950] Kumar M, et al. Exploiting CELLULOSE SYNTHASE (CESA) Class Specificity to Probe Cellulose Microfibril Biosynthesis. Plant Physiol., 2018. 177(1): p. 151-167 [PMID:29523715] Pear JR,Kawagoe Y,Schreckengost WE,Delmer DP,Stalker DM Higher plants contain homologs of the bacterial celA genes encoding the catalytic subunit of cellulose synthase. Proc. Natl. Acad. Sci. U.S.A., 1996. 93(22): p. 12637-42 [PMID:8901635]