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

Achn352661

Organism

Actinidia chinensis

Taxonomic ID

3625

Taxonomic Lineage

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; Ericales; Actinidiaceae; Actinidia

Family

G2-like

Protein Properties

Length: 1220aa MW: 136831 Da PI: 6.4312

Description

G2-like family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
Achn352661	genome	IKGC	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	G2-like	44.3	4e-14	217	253	1	37
G2-like 1 kprlrWtpeLHerFveaveqLGGsekAtPktilelmk 37 kpr+rWtpeLHe+Fveav++LGGse+ t k++ + + Achn352661 217 KPRMRWTPELHEAFVEAVNRLGGSERSTEKKLTPMEE 253 79***************************99876655 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
Gene3D	G3DSA:1.10.10.60	7.1E-11	216	249	IPR009057	Homeodomain-like
TIGRFAMs	TIGR01557	1.2E-7	217	248	IPR006447	Myb domain, plants
Pfam	PF14379	4.4E-23	263	309	IPR025756	MYB-CC type transcription factor, LHEQLE-containing domain
SuperFamily	SSF57850	8.83E-33	440	516	No hit	No description
Gene3D	G3DSA:3.30.40.10	9.4E-29	440	524	IPR013083	Zinc finger, RING/FYVE/PHD-type
Pfam	PF14569	2.5E-36	447	515	IPR027934	Cellulose synthase, RING-type zinc finger
PROSITE profile	PS50089	8.801	450	496	IPR001841	Zinc finger, RING-type
Pfam	PF03552	8.5E-56	725	827	IPR005150	Cellulose synthase
Pfam	PF03552	9.0E-22	912	1019	IPR005150	Cellulose synthase
Pfam	PF03552	1.5E-95	1022	1212	IPR005150	Cellulose synthase

Gene Ontology ? help Back to Top
GO Term	GO Category	GO Description
GO:0030244	Biological Process	cellulose biosynthetic process
GO:0016020	Cellular Component	membrane
GO:0003677	Molecular Function	DNA binding
GO:0005515	Molecular Function	protein binding
GO:0008270	Molecular Function	zinc ion binding
GO:0016760	Molecular Function	cellulose synthase (UDP-forming) activity

Sequence ? help Back to Top
Protein Sequence Length: 1220 aa Download sequence Send to blast
MELLEHYHHL YPFFLLGWKR SIISIPTPNS NEVVGPMFSS TSGFSSNLHY SSISPTGKHT 60 RKSPFIYQSS NNGESLPLTL CDSRMLQSTS NNESWCRDSL PNFFDYPANT PVRNTQLGSS 120 SNGDSSMATE DLGKRSDWQN WADQLITDDD SLTSNWNDFF ADSNVEDPEP KVAFQVAKPS 180 INVLTTQPQV LGQIPLPSGE SSSAPNTTSL PGGAPTKPRM RWTPELHEAF VEAVNRLGGS 240 ERSTEKKLTP MEELASLDLK TGIEITEALR LQIEVQKRLH EQLEIQKSLQ LRIEEQGRCL 300 QMMFEKQCTA GGMLKTSPSS LEIPSADAKD TVPNSPDKNE SGTSQLDHEE KENVIAASVP 360 PSRKLGKKQK LQESEVSEDV EENVVEGSSS QPLKRAKAET CLSLPLPLPC FWLAMAGLFA 420 GSHGRNELHV LHSKDEPRSP THGQKLAKIC RVCSDEIGLK VNGEMFVACH ECGFPVCRPC 480 YEYERSEGNQ SCPQCNTRYK RHKGCARVDG DEEDNFDAED FDDEFQIKHQ QHSPDHHHQA 540 ANHSENGDNN QQKWHHNASP SSFASVAGSV DGGKEFEGEK ETNTNNAEWK ERVEKWKTRQ 600 EKRGMSNKDD EGNEQGDDDD EYLTAEARQP LWRKVPISSS LINPYRIVIV LRLIILAFFF 660 RFRILTPAHD AYPLWLISVI CEIWFGFSWI LDQFPKWLPI TRETYLDRLS LRFEREGEPN 720 RLAPVDVYVS TVDPLKEPPI ITANTVLSIL AVDYPVENVS CYVSDDGASM LLFDALAETA 780 EFARRWVPFC KKYAVEPRTP EFYFSEKIDY LKDKVQPTFV KDRRAMKVYL GSEGALDVEG 840 KELPKLVYVS REKRPGYQHH KKAGAMNAMV YLGSEGALDV EGKELPKLVY VSREKRPGYQ 900 HHKKAGAMNA MINMKGLDGI QGPVYVGTGC VFNRPALYGY DPPVSEKRQK MTCDCLSSWC 960 CCCCGGSRKK SKSKKKGLKA LLGLGGLYSK KKKIMGKNYS RKSSSGPVFD LEEIEEGLEG 1020 LYFYAQLNNL ASIWFMALFL SIIVTGVLEL RWSGVSIQDW WRNEQFWVIG GVSAHLFAVF 1080 QGLLKVLAGV DTNFTVTAKA AEDAEFGELY LFKWTTLLIP PTTLIILNMV GVVAGVSDAI 1140 NNGYGSWGPL FGKLLFAFWV IVHLYPFLKG LMGRQNRTPT IVVLWSILLA SIFSLIWVRI 1200 DPFLPKQTGP ILKQCGVEC*

Sequence ? help Back to Top

Protein Sequence Length: 1220 aa Download sequence Send to blast

MELLEHYHHL YPFFLLGWKR SIISIPTPNS NEVVGPMFSS TSGFSSNLHY SSISPTGKHT  60
RKSPFIYQSS NNGESLPLTL CDSRMLQSTS NNESWCRDSL PNFFDYPANT PVRNTQLGSS  120
SNGDSSMATE DLGKRSDWQN WADQLITDDD SLTSNWNDFF ADSNVEDPEP KVAFQVAKPS  180
INVLTTQPQV LGQIPLPSGE SSSAPNTTSL PGGAPTKPRM RWTPELHEAF VEAVNRLGGS  240
ERSTEKKLTP MEELASLDLK TGIEITEALR LQIEVQKRLH EQLEIQKSLQ LRIEEQGRCL  300
QMMFEKQCTA GGMLKTSPSS LEIPSADAKD TVPNSPDKNE SGTSQLDHEE KENVIAASVP  360
PSRKLGKKQK LQESEVSEDV EENVVEGSSS QPLKRAKAET CLSLPLPLPC FWLAMAGLFA  420
GSHGRNELHV LHSKDEPRSP THGQKLAKIC RVCSDEIGLK VNGEMFVACH ECGFPVCRPC  480
YEYERSEGNQ SCPQCNTRYK RHKGCARVDG DEEDNFDAED FDDEFQIKHQ QHSPDHHHQA  540
ANHSENGDNN QQKWHHNASP SSFASVAGSV DGGKEFEGEK ETNTNNAEWK ERVEKWKTRQ  600
EKRGMSNKDD EGNEQGDDDD EYLTAEARQP LWRKVPISSS LINPYRIVIV LRLIILAFFF  660
RFRILTPAHD AYPLWLISVI CEIWFGFSWI LDQFPKWLPI TRETYLDRLS LRFEREGEPN  720
RLAPVDVYVS TVDPLKEPPI ITANTVLSIL AVDYPVENVS CYVSDDGASM LLFDALAETA  780
EFARRWVPFC KKYAVEPRTP EFYFSEKIDY LKDKVQPTFV KDRRAMKVYL GSEGALDVEG  840
KELPKLVYVS REKRPGYQHH KKAGAMNAMV YLGSEGALDV EGKELPKLVY VSREKRPGYQ  900
HHKKAGAMNA MINMKGLDGI QGPVYVGTGC VFNRPALYGY DPPVSEKRQK MTCDCLSSWC  960
CCCCGGSRKK SKSKKKGLKA LLGLGGLYSK KKKIMGKNYS RKSSSGPVFD LEEIEEGLEG  1020
LYFYAQLNNL ASIWFMALFL SIIVTGVLEL RWSGVSIQDW WRNEQFWVIG GVSAHLFAVF  1080
QGLLKVLAGV DTNFTVTAKA AEDAEFGELY LFKWTTLLIP PTTLIILNMV GVVAGVSDAI  1140
NNGYGSWGPL FGKLLFAFWV IVHLYPFLKG LMGRQNRTPT IVVLWSILLA SIFSLIWVRI  1200
DPFLPKQTGP ILKQCGVEC*

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
5jnp_A	9e-33	768	889	3	128	Probable cellulose synthase A catalytic subunit 8 [UDP-forming]
5jnp_B	9e-33	768	889	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	973	992	KKKGLKALLGLGGLYSKKKK

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}.

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_028065958.1	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	3e-60	phosphate starvation response 1

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]