Q9SYK4 (IP5PD_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Type I inositol-1,4,5-trisphosphate 5-phosphatase 13
Short name=At5PTase13
EC=3.1.3.56

Gene names

Name:	5PTASE13
Synonyms:	IPP6
Ordered Locus Names:	At1g05630
ORF Names:	F3F20.8

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	1136 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) to inositol 1,4-bisphosphate. Modulates cotyledon vein development through regulating auxin homeostasis. Involved in blue light responses. Decreases the amount of KIN10 degraded by the proteasome under low nutrient conditions. Ref.1 Ref.4 Ref.5 Ref.6
Catalytic activity	D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate. 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.
Cofactor	Magnesium. Ref.1
Subunit structure	Interacts with KIN10, but not with PHOT1. Ref.5 Ref.6
Subcellular location	Nucleus Ref.6.
Tissue specificity	Expressed in young seedlings and flowers. Highly expressed in anther and pollen grains, but not in pistils. Not detected in maturated roots, stems and rosette leaves. Ref.1 Ref.4
Developmental stage	Detected in cotyledons prior to seed germination. Restricted to the cotyledon tip until 2 days after seed germination and then detected in the cotyledon or cotyledon veins on days 3 to 7. Ref.4
Induction	By abscisic acid, wounding and at a lower level, by cold and salt treatment. Down-regulated by blue light irradiation. Ref.1 Ref.5
Domain	The WD40 domain (1-533) is interacting with KIN10.
Disruption phenotype	Defect in development of the cotyledon veins. Altered auxin homeostasis and reduced abscisic acid sensitivity. Shortened hypocotyls and expanded cotyledons in response to blue light irradiation. Increased expression of 5PTase12 in order to compensate for the loss of 5PTase13 function. Ref.4 Ref.5 Ref.6
Sequence similarities	Belongs to the inositol-1,4,5-trisphosphate 5-phosphatase type I family. Contains 5 WD repeats.
Biophysicochemical properties	Kinetic parameters: KM=651 µM for Ins(1,4,5)P3 Ref.1
Sequence caution	The sequence CAC82096.1 differs from that shown. Reason: Frameshift at position 1051.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat WD repeat
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	auxin homeostasis Inferred from mutant phenotype Ref.4. Source: TAIR phloem or xylem histogenesis Inferred from mutant phenotype Ref.4. Source: TAIR response to abscisic acid stimulus Inferred from mutant phenotype Ref.6. Source: TAIR response to blue light Inferred from expression pattern Ref.5. Source: TAIR response to nutrient Inferred from mutant phenotype Ref.6. Source: TAIR response to wounding Inferred from expression pattern Ref.1. Source: TAIR root development Inferred from mutant phenotype Ref.6. Source: TAIR sugar mediated signaling pathway Inferred from mutant phenotype Ref.6. Source: TAIR
Cellular component	nucleus Inferred from direct assay Ref.6. Source: TAIR
Molecular function	inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity Inferred from electronic annotation. Source: EC inositol-1,3,4-trisphosphate 4-phosphatase activity Inferred from mutant phenotype Ref.6. Source: TAIR inositol-1,4,5-trisphosphate 5-phosphatase activity Inferred from electronic annotation. Source: EC inositol-polyphosphate 5-phosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9SYK4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9SYK4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     752-785: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1136	1136	Type I inositol-1,4,5-trisphosphate 5-phosphatase 13		PRO_0000359743
Regions
	Repeat	147 – 185	39	WD 1
	Repeat	205 – 244	40	WD 2
	Repeat	259 – 297	39	WD 3
	Repeat	436 – 475	40	WD 4
	Repeat	515 – 552	38	WD 5
Natural variations
	Alternative sequence	752 – 785	34	Missing in isoform 2.		VSP_036161
Experimental info
	Sequence conflict	739	1	V → I in CAC82096. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 4E90EE8E43900687	FASTA	1,136	125,698
	10 20 30 40 50 60 MDSLIIEEED EEALATLVPV PPRRKTHSYS LQFDHKPHHQ IRKHSLDEVP RSATLASEAV 70 80 90 100 110 120 YFDSSDDEFS TGGNITENAA DETNAGAEEY TIVNPPPNVG LGDDDTEPLP EFIGAGGGSG 130 140 150 160 170 180 IFKVPVRAAV HPGRPPCLEL RPHPLRETQT GRFLRNIACT ETQLWAGQEN GIRFWNLEDA 190 200 210 220 230 240 YEAGCGIGGQ VPRGDEDTAP FHESVTTSPT MCLVADQSNK LLWSGHKDGK IRAWKMDQSS 250 260 270 280 290 300 VSHDDDDSDP FKERVSWLAH RGPVNSIVIS SYGDMWSCSE GGVIKIWPWD TLEKSLLLKP 310 320 330 340 350 360 EEKHMAALLV ERSAIDLRSQ VTVNGTCSIS SSEVKFLLAD SVRAKVWAVQ SLSFSIWDAR 370 380 390 400 410 420 SKDLLKVLNV DGQVENRGDL PPIQDQQVDD EMKLKFFSAS KREKPQGFLQ RSRNAIMGAA 430 440 450 460 470 480 GAVRRVATRS AGAFSEDTRK TEAIVLAVDG TIWTGSISGL IVQWDGNGNR LRDVNHHHRP 490 500 510 520 530 540 VLCFCTFGDR IYVGYASGYI QVLDLDGKLI SSWVSHNEPV IKLAAGGGFI FSLATHGGVR 550 560 570 580 590 600 GWYVTSPGPL DNIIRTELSQ KETLYARQDN VRILIGTWNV GQGRASHDAL MSWLGSVTSD 610 620 630 640 650 660 VGIVAVGLQE VEMGAGFLAM SAAKETVGLE GSAVGQWWID AIGKALDEKN TFERMGSRQL 670 680 690 700 710 720 AGLLISLWAR KDIRTHVGDL DVAAVPCGFG RAIGNKGGVG LRIRVYDRIM CFVNCHLAAH 730 740 750 760 770 780 LEAVNRRNAD FNHIFRLMVF SRGQNLSNAA AAGVSTSAYT TKSNTIPSTG AEEIKSDLAA 790 800 810 820 830 840 ADMVAFFGDF NYRLFGITYD EARDFISQRS FDWLRERDQL RAEMKVGKVF QGMREALITF 850 860 870 880 890 900 PPTYKFERNR SGLGGYDSGE KKRIPAWCDR VIYRDTQSSP FSESNLQCPV VSSVIMYEAC 910 920 930 940 950 960 MDVTESDHKP VRCKFHATIA HVDKSVRRQE LGKIIRSNEK ILSIFEDLRF VPETSVSTNN 970 980 990 1000 1010 1020 IVLQSQDTVI LTITNNSPTS QAIFNILCGG QAVVKDDGED ADYNPRGSFG LPRWLEVSPA 1030 1040 1050 1060 1070 1080 AGIINPEGSV DVKVHHEDFY SMEEYVDGIP QNWWCEDTRD KEAILMVNIR GSCSTTLRSH 1090 1100 1110 1120 1130 SVKVRHCFSA RVCLLENRPT NLTKNLGGSR RYPTDITRNG STRPRTEDSV RRGKSR
	Isoform 2 [UniParc]. Checksum: FDAB8DBCEF393418	FASTA	1,102	122,357
	10 20 30 40 50 60 MDSLIIEEED EEALATLVPV PPRRKTHSYS LQFDHKPHHQ IRKHSLDEVP RSATLASEAV 70 80 90 100 110 120 YFDSSDDEFS TGGNITENAA DETNAGAEEY TIVNPPPNVG LGDDDTEPLP EFIGAGGGSG 130 140 150 160 170 180 IFKVPVRAAV HPGRPPCLEL RPHPLRETQT GRFLRNIACT ETQLWAGQEN GIRFWNLEDA 190 200 210 220 230 240 YEAGCGIGGQ VPRGDEDTAP FHESVTTSPT MCLVADQSNK LLWSGHKDGK IRAWKMDQSS 250 260 270 280 290 300 VSHDDDDSDP FKERVSWLAH RGPVNSIVIS SYGDMWSCSE GGVIKIWPWD TLEKSLLLKP 310 320 330 340 350 360 EEKHMAALLV ERSAIDLRSQ VTVNGTCSIS SSEVKFLLAD SVRAKVWAVQ SLSFSIWDAR 370 380 390 400 410 420 SKDLLKVLNV DGQVENRGDL PPIQDQQVDD EMKLKFFSAS KREKPQGFLQ RSRNAIMGAA 430 440 450 460 470 480 GAVRRVATRS AGAFSEDTRK TEAIVLAVDG TIWTGSISGL IVQWDGNGNR LRDVNHHHRP 490 500 510 520 530 540 VLCFCTFGDR IYVGYASGYI QVLDLDGKLI SSWVSHNEPV IKLAAGGGFI FSLATHGGVR 550 560 570 580 590 600 GWYVTSPGPL DNIIRTELSQ KETLYARQDN VRILIGTWNV GQGRASHDAL MSWLGSVTSD 610 620 630 640 650 660 VGIVAVGLQE VEMGAGFLAM SAAKETVGLE GSAVGQWWID AIGKALDEKN TFERMGSRQL 670 680 690 700 710 720 AGLLISLWAR KDIRTHVGDL DVAAVPCGFG RAIGNKGGVG LRIRVYDRIM CFVNCHLAAH 730 740 750 760 770 780 LEAVNRRNAD FNHIFRLMVF SRGQNLSNAA AFFGDFNYRL FGITYDEARD FISQRSFDWL 790 800 810 820 830 840 RERDQLRAEM KVGKVFQGMR EALITFPPTY KFERNRSGLG GYDSGEKKRI PAWCDRVIYR 850 860 870 880 890 900 DTQSSPFSES NLQCPVVSSV IMYEACMDVT ESDHKPVRCK FHATIAHVDK SVRRQELGKI 910 920 930 940 950 960 IRSNEKILSI FEDLRFVPET SVSTNNIVLQ SQDTVILTIT NNSPTSQAIF NILCGGQAVV 970 980 990 1000 1010 1020 KDDGEDADYN PRGSFGLPRW LEVSPAAGII NPEGSVDVKV HHEDFYSMEE YVDGIPQNWW 1030 1040 1050 1060 1070 1080 CEDTRDKEAI LMVNIRGSCS TTLRSHSVKV RHCFSARVCL LENRPTNLTK NLGGSRRYPT 1090 1100 DITRNGSTRP RTEDSVRRGK SR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular and biochemical characterization of three WD-repeat-domain-containing inositol polyphosphate 5-phosphatases in Arabidopsis thaliana." Zhong R., Ye Z.-H. Plant Cell Physiol. 45:1720-1728(2004) [PubMed: 15574849] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INDUCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"At5PTase13 modulates cotyledon vein development through regulating auxin homeostasis." Lin W.-H., Wang Y., Mueller-Roeber B., Brearley C.A., Xu Z.-H., Xue H.-W. Plant Physiol. 139:1677-1691(2005) [PubMed: 16299182] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1060 (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE. Strain: cv. Columbia. Tissue: Hypocotyl.
[5]	"An inositol polyphosphate 5-phosphatase functions in PHOTOTROPIN1 signaling in Arabidopis by altering cytosolic Ca2+." Chen X., Lin W.-H., Wang Y., Luan S., Xue H.-W. Plant Cell 20:353-366(2008) [PubMed: 18252844] [Abstract] Cited for: FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, LACK OF INTERACTION WITH PHOT1. Strain: cv. Columbia.
[6]	"Interaction of the WD40 domain of a myoinositol polyphosphate 5-phosphatase with SnRK1 links inositol, sugar, and stress signaling." Ananieva E.A., Gillaspy G.E., Ely A., Burnette R.N., Erickson F.L. Plant Physiol. 148:1868-1882(2008) [PubMed: 18931139] [Abstract] Cited for: INTERACTION WITH KIN10, FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY761188 mRNA. Translation: AAV87315.1. AY761192 Genomic DNA. Translation: AAV87319.1. AC007153 Genomic DNA. Translation: AAD30615.1. CP002684 Genomic DNA. Translation: AEE27869.1. AJ297426 mRNA. Translation: CAC82096.1. Frameshift.
IPI	IPI00656703. IPI00919329.
PIR	D86190.
RefSeq	NP_001030976.1. NM_001035899.1.
UniGene	At.42385.
3D structure databases
HSSP	HSSP built from PDB template 1I9Z based on UniProtKB O43001.
ProteinModelPortal	Q9SYK4.
SMR	Q9SYK4. Positions 204-229, 257-291, 437-940.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9SYK4.
Proteomic databases
PRIDE	Q9SYK4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G05630.2; AT1G05630.2; AT1G05630.
GeneID	837069.
GenomeReviews	Gene locus AT1G05630 in contig CT485782_GR.
KEGG	ath:AT1G05630.
Organism-specific databases
GeneFarm	3166. 267.
TAIR	At1g05630.
Phylogenomic databases
eggNOG	KOG0565.
GeneTree	EPGT00070000028707.
HOGENOM	HBG319261.
PhylomeDB	Q9SYK4.
ProtClustDB	CLSN2683268.
Enzyme and pathway databases
BRENDA	3.1.3.36. 399.
Gene expression databases
Genevestigator	Q9SYK4.
Family and domain databases
InterPro	IPR005135. Endo/exonuclease/phosphatase. IPR000300. IPPc. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 2 hits.
Pfam	PF03372. Exo_endo_phos. 1 hit. [Graphical view]
SMART	SM00128. IPPc. 1 hit. SM00320. WD40. 4 hits. [Graphical view]
SUPFAM	SSF56219. Exo_endo_phos. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. False negative. PS50082. WD_REPEATS_2. False negative. PS50294. WD_REPEATS_REGION. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IP5PD_ARATH

Accession

Primary (citable) accession number: Q9SYK4
Secondary accession number(s): Q712D7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	May 1, 2000
Last modified:	November 16, 2011
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program