P48486 (PP16_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase PP1 isozyme 6
EC=3.1.3.16

Gene names

Name:	TOPP6
Synonyms:	PP1BG
Ordered Locus Names:	At4g11240
ORF Names:	F8L21.30

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Tissue specificity	Strongly up-regulated within developing flowers, especially in the tapetum, the developing and mature pollen and in the ovaries.
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.
Sequence caution	The sequence CAB51408.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB81225.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from direct assay PubMed 21222654. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 322	322	Serine/threonine-protein phosphatase PP1 isozyme 6		PRO_0000058802
Sites
	Active site	122	1	Proton donor By similarity
	Metal binding	61	1	Iron By similarity
	Metal binding	63	1	Iron By similarity
	Metal binding	89	1	Iron By similarity
	Metal binding	89	1	Manganese By similarity
	Metal binding	121	1	Manganese By similarity
	Metal binding	170	1	Manganese By similarity
	Metal binding	245	1	Manganese By similarity
Experimental info
	Sequence conflict	248	1	V → D Ref.1
	Sequence conflict	248	1	V → D Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P48486 [UniParc]. Last modified May 29, 2007. Version 2. Checksum: B2320EB8E472AEDF	FASTA	322	36,567
	10 20 30 40 50 60 MDETLLDDII RRLLATNNGR TVKQAQITET EIRQLCLASK EVFLSQPNLL ELEAPIKICG 70 80 90 100 110 120 DVHGQFPDLL RLFEYGGYPP AANYLFLGDY VDRGKQSIET ICLLLAYKVK YKFNFFLLRG 130 140 150 160 170 180 NHECASINRV YGFYDECKRR YNVRLWKTFT ECFNCLPVSA LIDDKILCMH GGLSPDIKSL 190 200 210 220 230 240 DDIRRIPRPI DVPDQGILCD LLWADPDREI QGWGENDRGV SYTFGADKVA EFLQTHDLDL 250 260 270 280 290 300 ICRAHQVVED GYEFFAKRQL VTIFSAPNYC GEFDNAGALM SVDDSLTCSF QILKASEKKG 310 320 RFGFNNNVPR PGTPPHKGGK GR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel Arabidopsis type 1 protein phosphatase is highly expressed in male and female tissues and functionally complements a conditional cell cycle mutant of Aspergillus." Arundhati A., Feiler H., Traas J., Zhang H., Lunness P.A., Doonan J.H. Plant J. 7:823-834(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning and chromosomal mapping of type one serine/threonine protein phosphatases in Arabidopsis thaliana." Lin Q., Li J., Smith R.D., Walker J.C. Plant Mol. Biol. 37:471-481(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Arabidopsis PPP family of serine/threonine phosphatases." Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C. Trends Plant Sci. 12:169-176(2007) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z46253 mRNA. Translation: CAA86339.1. U80921 Genomic DNA. Translation: AAC39460.1. AL096882 Genomic DNA. Translation: CAB51408.1. Sequence problems. AL161531 Genomic DNA. Translation: CAB81225.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE82988.1. AY090365 mRNA. Translation: AAL91268.1. AY122904 mRNA. Translation: AAM67437.1. AY086060 mRNA. Translation: AAM63269.1.
IPI	IPI00524068.
PIR	T13015.
RefSeq	NP_567375.1. NM_117195.4.
UniGene	At.3651.
3D structure databases
ProteinModelPortal	P48486.
SMR	P48486. Positions 6-294.
ModBase	Search...
Protein-protein interaction databases
IntAct	P48486. 2 interactions.
Proteomic databases
PaxDb	P48486.
PRIDE	P48486.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G11240.1; AT4G11240.1; AT4G11240.
GeneID	826726.
KEGG	ath:AT4G11240.
Organism-specific databases
TAIR	At4g11240.
Phylogenomic databases
eggNOG	COG0639.
HOGENOM	HOG000172697.
InParanoid	P48486.
KO	K06269.
OMA	LATNNGR.
PhylomeDB	P48486.
ProtClustDB	CLSN2917530.
Gene expression databases
Genevestigator	P48486.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PP16_ARATH

Accession

Primary (citable) accession number: P48486
Secondary accession number(s): Q8RX64, Q9SUT7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	May 29, 2007
Last modified:	May 1, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program