PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
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(e.g., LFY)
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID MDP0000286589
Organism
Malus domestica
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Rosaceae; Maloideae; Maleae; Malus
Family bHLH
Protein Properties Length: 2499aa    MW: 277621 Da    PI: 5.7332
Description bHLH family protein
Gene Model
Gene Model ID Type Source Coding Sequence
MDP0000286589genomeGDRView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1HLH33.38.9e-11510555555
                    HHHHHHHHHHHHHHHHHHHHCTSCCC...TTS-STCHHHHHHHHHHHHHHH CS
            HLH   5 hnerErrRRdriNsafeeLrellPkaskapskKlsKaeiLekAveYIksLq 55 
                    h+++Er RR++i +++ +L+el+Pk+      + +Ka++L + +eY++ Lq
  MDP0000286589 510 HSIAERLRREKISDRMKNLQELVPKS-----NRTDKASMLDEIIEYVRFLQ 555
                    99***********************7.....59*****************9 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
Gene3DG3DSA:3.30.40.102.8E-4116184IPR013083Zinc finger, RING/FYVE/PHD-type
SuperFamilySSF578505.0E-14120202No hitNo description
SMARTSM001840.11125172IPR001841Zinc finger, RING-type
PROSITE profilePS500899.996125171IPR001841Zinc finger, RING-type
PROSITE patternPS005180143152IPR017907Zinc finger, RING-type, conserved site
SMARTSM006471.0E-11193255IPR002867IBR domain
SuperFamilySSF578507.42E-5200260No hitNo description
PfamPF014852.3E-8207255IPR002867IBR domain
SMARTSM006471.1265328IPR002867IBR domain
SuperFamilySSF578505.16E-12266328No hitNo description
SMARTSM001844.9285328IPR001841Zinc finger, RING-type
CDDcd000832.48E-11503559No hitNo description
SuperFamilySSF474593.66E-14503560IPR011598Myc-type, basic helix-loop-helix (bHLH) domain
PROSITE profilePS5088816.66505554IPR011598Myc-type, basic helix-loop-helix (bHLH) domain
Gene3DG3DSA:4.10.280.102.9E-14507559IPR011598Myc-type, basic helix-loop-helix (bHLH) domain
PfamPF000104.8E-8510555IPR011598Myc-type, basic helix-loop-helix (bHLH) domain
SMARTSM003531.1E-12511560IPR011598Myc-type, basic helix-loop-helix (bHLH) domain
SMARTSM000641.3E-18706781IPR000306FYVE zinc finger
SuperFamilySSF579034.56E-19709781IPR011011Zinc finger, FYVE/PHD-type
Gene3DG3DSA:3.30.40.103.3E-20710781IPR013083Zinc finger, RING/FYVE/PHD-type
PfamPF013631.4E-16711780IPR000306FYVE zinc finger
PROSITE profilePS5017812.718714780IPR017455Zinc finger, FYVE-related
SMARTSM001848717775IPR001841Zinc finger, RING-type
CDDcd033345.77E-13210651337No hitNo description
PfamPF001181.0E-3010851333IPR002423Chaperonin Cpn60/TCP-1 family
Gene3DG3DSA:3.50.7.103.8E-4711301303IPR027409GroEL-like apical domain
SuperFamilySSF520296.02E-4011311303IPR027409GroEL-like apical domain
PROSITE profilePS5145559.3221452469IPR002498Phosphatidylinositol-4-phosphate 5-kinase, core
SMARTSM003305.6E-13021792470IPR002498Phosphatidylinositol-4-phosphate 5-kinase, core
SuperFamilySSF561041.37E-7921802469No hitNo description
Gene3DG3DSA:3.30.800.103.6E-2722042326IPR027484Phosphatidylinositol-4-phosphate 5-kinase, N-terminal domain
PfamPF015047.3E-4622452467IPR002498Phosphatidylinositol-4-phosphate 5-kinase, core
Gene3DG3DSA:3.30.810.105.4E-3523302469IPR027483Phosphatidylinositol-4-phosphate 5-kinase, C-terminal
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0046488Biological Processphosphatidylinositol metabolic process
GO:0005524Molecular FunctionATP binding
GO:0008270Molecular Functionzinc ion binding
GO:0016307Molecular Functionphosphatidylinositol phosphate kinase activity
GO:0046983Molecular Functionprotein dimerization activity
Sequence ? help Back to Top
Protein Sequence    Length: 2499 aa     Download sequence    Send to blast
MENPLSSHSX SRINFIDIED DTFXFTPTSR NPSTNPINXD DEDRGLRSIT ASLLKSVPTP  60
AEADNFIDLS EETLDFYXGD EELRILRFKP SKTPFGKRGK XLFSDFSVTE SGQSSNSKND  120
PDFVCEICVE PKSGIESFRI ENCSHGYCTE CMVKYVASKL QENITSIRCP VPDCIGLLEP  180
EYCRPILPPE VFDQWGTALC EAVILGSEKF YCPYKECSAM LIDDGKEVVR QSACPNCWRM  240
FCAQCKAPWH EGIECEEFLK LNKDERERED IMLKNLAQKQ QWRRCPKCRF YVEKSMGCMF  300
MMCRCRTAFC YRCGDVLENI RDHYCPSCGG XKKEEDXFLL TMDKYINQIF SSSSWSDVDA  360
KEIPSWACCE SEQPNAALLG SVVAVDEHEN NSAPTYLTNS NSLESLVAQD GVSPAPASGM  420
GQRKMCSFGI NGDYGDYVMP SDPNNLAVFV STEKGMQDVQ NYPLPSFASA PRMSGLQSLP  480
QNTSTNPVGE CNGNRKLRMR ARRGQATDPH SIAERLRREK ISDRMKNLQE LVPKSNRTDK  540
ASMLDEIIEY VRFLQLQVKV GNGLPQFRTA GDVSFDEIAL EQLVRLMESD ADKAMQHLQS  600
KGFCLMPVAL ADAISAAKES SSSWPSAPVP DDWKKKETCF TDIGVVQNNS RSSSNSSSSP  660
DQIKRERRVA IEEERKLLMG TPDNKLSELV DIFRSWIPRR SEPPNVSRDF WMPDQSCRVC  720
YDCDSQFTIF NRRHHCRLCG RVFCAKCTAN SIPAASDEPR AGREDWERIR VCYYCFKQWE  780
QGVAAPDNGA APAASPGLSP SPSATSLAST KSSCTCHSSS STIGSTPYST GPYQHVPYSS  840
GRSPSQSSSQ IDSVPVQQDN VTSQTSISSD VAMAEPSPNQ YGFCLNRSDD EDDDYGVYRL  900
DSEPSHLSHG NDYYGAVTIE EFASVYGPQN VHLDGDNTSS LLPGNFDTED AVGIQKIEEE  960
PYAHDNGDEC GTSPYDLQST NTEPVDFENN GLLWLPPEPE DEEDEREAVL FDDDDYDGGG  1020
SGGGVGEWGY LGSSHSFGNG ECRTREKSIE EHRKAMKNVV EGHFRALVSQ LLQVENLPLG  1080
DEGNNESWLD IITSLSWEAA TLLKPDTSKG GGMDPGGYVK VKCIACGRRT DSTVVKGVVC  1140
KKNVAHRRMT SKIEKPRFLI LGGALEYQRV SNLLSSFDTL LQQEMDHLKM AVAKIDSHHP  1200
SVLLVEKSVS RYAQDYLLAK DISLVLNIKR PLLERIARCT GAQIVPSIDH LTSPKLGFCD  1260
MFHVEKFLEV HGSAGQGGKK LTKTLMFCEG CPKPLGVTIL LHGANGDELK KVKHVVQYGV  1320
FAAYHLALET SFLADEGASL PELPLKSXIT VALPDKPSSI DRSISTIPGF SVPPAGKPQG  1380
PDASRELQKS NQRLISYSNS STTSGPILNM QGADSICSSK ACSQAFLIEH ALSSRESRSP  1440
FTSLSPQEED ITESYRKELP SICASENKID VGSKDSCLDN TAQVGEALVN GSLISNFLAT  1500
SESLGHGGGA LAANHGETPE LTSIKHHSDY QNEEVGSSKE EFPPSPSDHQ SILVSLSTRC  1560
VWKGTVCERS HLFRIKYYGS FDKPLGRFLR DHLFDQNYLC RSCGMPSEAH VHCYTHRQGS  1620
LTISVKKVPE ILLPGEREGK IWMWHRCLKC PRANGFPPAT RRVVMSDAAW GLSFGKFLEL  1680
SFSNHAAANR VATCGHSLHR DCLRFYGFGR MVACFRYASI HVHSVYLPPQ KLEFNYDNQE  1740
WIQKEAEEVG HRAELLFTEL CNALNQILEK RPISGTPDGG KKAPESSHQI VELEEMLQKE  1800
REDFEESLRK AMHREVKCGR PAIDILEINR LRRQLLFHSY IWDQRLIQAA SLSKNSFQEG  1860
LRSSLPKLKE KPISSMEKLV ETNINSKPGK GFSRCDSSLR ETKPDVSIYQ GGDVGGFSQP  1920
EGEQKKNEIV QNLNHSNEAK ISTRSSENAI DKSDPLESGI SARRALSEGN ESLVVANLSD  1980
TLDAAWTGES HPTSTIPKEN GYSKPDSTLV NSPTMMRKVA SNSDLQNCAV DQAGVQTTAA  2040
THSLSSTSSL KVFDKSYSLN AQKIIIGEYN PVNVPMFRES ERQSGARLLL PIGVNDTVIP  2100
VFDDEPTSVI AYALVSPDYH VQISESERPR DAMDGSVSAP LFDSANLLSL SSFDESLSET  2160
YRNLGSSDES MSSVSRSWSS QALDSLLSKD IHARVSFTDD GPLGKVKYTV TCYYATRFEA  2220
LRRTCCPSER DFVRSLSRCK KWGAQGGKSN VFFAKTLDDR FIIKQVTKIE LESFIKFAPS  2280
YFKYLSESIS TRSPTCLAKI LGIYQVSSKH GKAGKESKMD VLVMENLLFR RNVTRLYDLK  2340
GSSRSRYNPD TSGSNKVLLD QNLIEAMPTS PIFVGSKAKR LLERAVWNDT AFLASIDVMD  2400
YSLLVGVDEE KDELVLGIID FMRQYTWDKH LETWVKTSGI LGGPKNTSPT VISPQQYKKR  2460
FRKAMTSYFL MVPDQWSPLT IVPSXSQSDL GEETAQDPS
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
5gw4_G3e-2011131361198435T-complex protein 1 subunit gamma
5gw5_G3e-2011131361198435T-complex protein 1 subunit gamma
Search in ModeBase
Expression -- UniGene ? help Back to Top
UniGene ID E-value Expressed in
Mdo.116670.0leaf| root| stem
Expression -- Description ? help Back to Top
Source Description
UniprotTISSUE SPECIFICITY: Ubiquitous with highest expression levels in the root hair zone, pollen, and stamens. {ECO:0000269|PubMed:19846542}.
Functional Description ? help Back to Top
Source Description
UniProtThe PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate (By similarity). Plays an important role in maintenance of endomembrane homeostasis including endocytosis, vacuole formation, and vacuolar acidification processes. Required for development of viable pollen. Might mediate recycling of auxin transporters. {ECO:0000250, ECO:0000269|PubMed:19846542, ECO:0000269|PubMed:21173023, ECO:0000269|PubMed:21412048}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_008391859.20.01-phosphatidylinositol-3-phosphate 5-kinase FAB1A
RefseqXP_008391864.20.01-phosphatidylinositol-3-phosphate 5-kinase FAB1A
RefseqXP_008391869.20.01-phosphatidylinositol-3-phosphate 5-kinase FAB1A
SwissprotQ9LUM00.0FAB1B_ARATH; 1-phosphatidylinositol-3-phosphate 5-kinase FAB1B
TrEMBLA0A498KFS50.0A0A498KFS5_MALDO; Uncharacterized protein
STRINGXP_008391859.10.0(Malus domestica)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF253122
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT4G30980.12e-38LJRHL1-like 2
Publications ? help Back to Top
  1. Mueller-Roeber B,Pical C
    Inositol phospholipid metabolism in Arabidopsis. Characterized and putative isoforms of inositol phospholipid kinase and phosphoinositide-specific phospholipase C.
    Plant Physiol., 2002. 130(1): p. 22-46
    [PMID:12226484]
  2. van Leeuwen W,Okrész L,Bögre L,Munnik T
    Learning the lipid language of plant signalling.
    Trends Plant Sci., 2004. 9(8): p. 378-84
    [PMID:15358268]
  3. Lee Y, et al.
    The Arabidopsis phosphatidylinositol 3-kinase is important for pollen development.
    Plant Physiol., 2008. 147(4): p. 1886-97
    [PMID:18515640]
  4. Whitley P,Hinz S,Doughty J
    Arabidopsis FAB1/PIKfyve proteins are essential for development of viable pollen.
    Plant Physiol., 2009. 151(4): p. 1812-22
    [PMID:19846542]
  5. Wywial E,Singh SM
    Identification and structural characterization of FYVE domain-containing proteins of Arabidopsis thaliana.
    BMC Plant Biol., 2010. 10: p. 157
    [PMID:20678208]
  6. Hirano T,Matsuzawa T,Takegawa K,Sato MH
    Loss-of-function and gain-of-function mutations in FAB1A/B impair endomembrane homeostasis, conferring pleiotropic developmental abnormalities in Arabidopsis.
    Plant Physiol., 2011. 155(2): p. 797-807
    [PMID:21173023]
  7. Hirano T,Sato MH
    Arabidopsis FAB1A/B is possibly involved in the recycling of auxin transporters.
    Plant Signal Behav, 2011. 6(4): p. 583-5
    [PMID:21412048]
  8. Bak G, et al.
    Rapid structural changes and acidification of guard cell vacuoles during stomatal closure require phosphatidylinositol 3,5-bisphosphate.
    Plant Cell, 2013. 25(6): p. 2202-16
    [PMID:23757398]
  9. Serrazina S,Dias FV,Malhó R
    Characterization of FAB1 phosphatidylinositol kinases in Arabidopsis pollen tube growth and fertilization.
    New Phytol., 2014. 203(3): p. 784-93
    [PMID:24807078]