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

Sme2.5_04506.1_g00005.1

Organism

Solanum melongena

Taxonomic ID

4111

Taxonomic Lineage

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum

Family

G2-like

Protein Properties

Length: 143aa MW: 16302.6 Da PI: 7.9241

Description

G2-like family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
Sme2.5_04506.1_g00005.1	genome	EGD	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	G2-like	90.3	1.7e-28	46	100	1	55
G2-like 1 kprlrWtpeLHerFveaveqLGGsekAtPktilelmkvkgLtlehvkSHLQkYRl 55 kpr rWt eLHe Fv+av++LGG+ +AtPk+i++lm+ +++t +h+kSHLQkYR Sme2.5_04506.1_g00005.1 46 KPRFRWTVELHELFVKAVNELGGPYEATPKNIVKLMDDEDITPDHIKSHLQKYRQ 100 79****************************************************6 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
PROSITE profile	PS51294	10.228	43	103	IPR017930	Myb domain
Gene3D	G3DSA:1.10.10.60	5.4E-26	44	101	IPR009057	Homeodomain-like
SuperFamily	SSF46689	2.51E-16	45	101	IPR009057	Homeodomain-like
TIGRFAMs	TIGR01557	1.7E-22	46	101	IPR006447	Myb domain, plants
Pfam	PF00249	2.3E-8	50	99	IPR001005	SANT/Myb domain

Gene Ontology ? help Back to Top
GO Term	GO Category	GO Description
GO:0003677	Molecular Function	DNA binding

Sequence ? help Back to Top
Protein Sequence Length: 143 aa Download sequence Send to blast
MFFRHILSCR IPGITTEDCE NMPEHSKKQK GETSEKVGAS HDLNKKPRFR WTVELHELFV 60 KAVNELGGPY EATPKNIVKL MDDEDITPDH IKSHLQKYRQ SKDIINNNRS ISKAHKSLIQ 120 CGETCRISKE VSSEINVCGE VLA

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
6j4k_A	2e-18	46	102	2	58	Protein PHOSPHATE STARVATION RESPONSE 1
6j4k_B	2e-18	46	102	2	58	Protein PHOSPHATE STARVATION RESPONSE 1
6j4r_A	2e-18	46	102	1	57	Protein PHOSPHATE STARVATION RESPONSE 1
6j4r_B	2e-18	46	102	1	57	Protein PHOSPHATE STARVATION RESPONSE 1
6j4r_C	2e-18	46	102	1	57	Protein PHOSPHATE STARVATION RESPONSE 1
6j4r_D	2e-18	46	102	1	57	Protein PHOSPHATE STARVATION RESPONSE 1
6j5b_A	2e-18	46	102	2	58	Protein PHOSPHATE STARVATION RESPONSE 1
6j5b_C	2e-18	46	102	2	58	Protein PHOSPHATE STARVATION RESPONSE 1
6j5b_D	2e-18	46	102	2	58	Protein PHOSPHATE STARVATION RESPONSE 1
6j5b_F	2e-18	46	102	2	58	Protein PHOSPHATE STARVATION RESPONSE 1
6j5b_H	2e-18	46	102	2	58	Protein PHOSPHATE STARVATION RESPONSE 1
6j5b_J	2e-18	46	102	2	58	Protein PHOSPHATE STARVATION RESPONSE 1
Search in ModeBase

Functional Description ? help Back to Top
Source	Description
UniProt	Transcription factor involved in phosphate starvation signaling. Binds to P1BS, an imperfect palindromic sequence 5'-GNATATNC-3', to promote the expression of inorganic phosphate (Pi) starvation-responsive genes. Functionally redundant with PHR1 and PHR3 in regulating Pi starvation response and Pi homeostasis. PHR2 binding to DNA is repressed redundantly by SPX1, SPX2 and SPX4 in a PI-dependent manner. {ECO:0000250\|UniProtKB:Q6Z156}.
UniProt	Transcription factor involved in phosphate starvation signaling (PubMed:18263782, PubMed:26082401). Binds to P1BS, an imperfect palindromic sequence 5'-GNATATNC-3', to promote the expression of inorganic phosphate (Pi) starvation-responsive genes (PubMed:25657119, PubMed:26082401). Functionally redundant with PHR1 and PHR3 in regulating Pi starvation response and Pi homeostasis (PubMed:26082401). Involved in both systematic and local Pi-signaling pathways (PubMed:19704822). Regulates several Pi transporters (PubMed:18263782). Regulates the expression of PT2 (PubMed:20149131). Directly up-regulates SPX1 and SPX2 expression, but PHR2 binding to DNA is repressed redundantly by SPX1 and SPX2 in a PI-dependent manner (PubMed:25271318). The DNA-binding activity is also repressed by SPX4 (PubMed:24692424). Involved in root growth under Pi deprivation (PubMed:18263782). {ECO:0000269\|PubMed:18263782, ECO:0000269\|PubMed:19704822, ECO:0000269\|PubMed:20149131, ECO:0000269\|PubMed:24692424, ECO:0000269\|PubMed:25271318, ECO:0000269\|PubMed:25657119, ECO:0000269\|PubMed:26082401}.

Regulation -- Description ? help Back to Top
Source	Description
UniProt	INDUCTION: Not regulated by Pi starvation. {ECO:0000269\|PubMed:18263782, ECO:0000269\|PubMed:26082401}.

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_016579061.1	1e-55	PREDICTED: probable transcription factor KAN3
Swissprot	B8B5N8	1e-17	PHR2_ORYSI; Protein PHOSPHATE STARVATION RESPONSE 2
Swissprot	Q6Z156	1e-17	PHR2_ORYSJ; Protein PHOSPHATE STARVATION RESPONSE 2
TrEMBL	A0A1U8H6E1	3e-54	A0A1U8H6E1_CAPAN; probable transcription factor KAN3
STRING	PGSC0003DMT400016464	2e-41	(Solanum tuberosum)

Orthologous Group ? help Back to Top
Lineage	Orthologous Group ID	Taxa Number	Gene Number
Asterids	OGEA12062	16	23

Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID	E-value	Description
AT4G13640.1	1e-19	G2-like family protein

Publications ? help Back to Top
Kikuchi S, et al. Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice. Science, 2003. 301(5631): p. 376-9 [PMID:12869764] Wang C, et al. Involvement of OsSPX1 in phosphate homeostasis in rice. Plant J., 2009. 57(5): p. 895-904 [PMID:19000161] Zhang Q,Wang C,Tian J,Li K,Shou H Identification of rice purple acid phosphatases related to phosphate starvation signalling. Plant Biol (Stuttg), 2011. 13(1): p. 7-15 [PMID:21143719] Wu Z,Ren H,McGrath SP,Wu P,Zhao FJ Investigating the contribution of the phosphate transport pathway to arsenic accumulation in rice. Plant Physiol., 2011. 157(1): p. 498-508 [PMID:21715673] Chen J, et al. OsPHF1 regulates the plasma membrane localization of low- and high-affinity inorganic phosphate transporters and determines inorganic phosphate uptake and translocation in rice. Plant Physiol., 2011. 157(1): p. 269-78 [PMID:21753117] Wang C, et al. Functional characterization of the rice SPX-MFS family reveals a key role of OsSPX-MFS1 in controlling phosphate homeostasis in leaves. New Phytol., 2012. 196(1): p. 139-48 [PMID:22803610] Tian J, et al. Overexpression of OsPAP10a, a root-associated acid phosphatase, increased extracellular organic phosphorus utilization in rice. J Integr Plant Biol, 2012. 54(9): p. 631-9 [PMID:22805094] Shen C, et al. OsARF16, a transcription factor, is required for auxin and phosphate starvation response in rice (Oryza sativa L.). Plant Cell Environ., 2013. 36(3): p. 607-20 [PMID:22913536] Wu P,Shou H,Xu G,Lian X Improvement of phosphorus efficiency in rice on the basis of understanding phosphate signaling and homeostasis. Curr. Opin. Plant Biol., 2013. 16(2): p. 205-12 [PMID:23566853] Wang S, et al. Auxin response factor (OsARF12), a novel regulator for phosphate homeostasis in rice (Oryza sativa). New Phytol., 2014. 201(1): p. 91-103 [PMID:24111723] Shi J, et al. The paralogous SPX3 and SPX5 genes redundantly modulate Pi homeostasis in rice. J. Exp. Bot., 2014. 65(3): p. 859-70 [PMID:24368504] Li S,Wang C,Zhou L,Shou H Oxygen deficit alleviates phosphate overaccumulation toxicity in OsPHR2 overexpression plants. J. Plant Res., 2014. 127(3): p. 433-40 [PMID:24687599] Zhou Z, et al. SPX proteins regulate Pi homeostasis and signaling in different subcellular level. Plant Signal Behav, 2015. 10(9): p. e1061163 [PMID:26224365] Zhang K, et al. Down-regulation of OsSPX1 caused semi-male sterility, resulting in reduction of grain yield in rice. Plant Biotechnol. J., 2016. 14(8): p. 1661-72 [PMID:26806409] Cao Y, et al. Identification and expression analysis of OsLPR family revealed the potential roles of OsLPR3 and 5 in maintaining phosphate homeostasis in rice. BMC Plant Biol., 2016. 16(1): p. 210 [PMID:27716044]