P54970 (ILL2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
IAA-amino acid hydrolase ILR1-like 2
EC=3.5.1.-

Gene names

Name:	ILL2
Ordered Locus Names:	At5g56660
ORF Names:	MIK19.11

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	439 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes certain amino acid conjugates of the plant growth regulator indole-3-acetic acid (IAA), including IAA-Ala.
Cofactor	Manganese. The ion enhances activity.
Subcellular location	Endoplasmic reticulum lumen Potential.
Sequence similarities	Belongs to the peptidase M20 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Ligand	Manganese
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	auxin metabolic process Inferred from direct assay Ref.6. Source: TAIR
Cellular component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	IAA-Ala conjugate hydrolase activity Inferred from direct assay Ref.6. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 439

418

IAA-amino acid hydrolase ILR1-like 2

PRO_0000001190

Regions

Motif

436 – 439

4

Prevents secretion from ER Potential

Experimental info

Sequence conflict

131

1

A → P in AAC49016. Ref.1

Sequence conflict

236

1

Q → H in AAC49016. Ref.1

Sequence conflict

240

1

D → G in AAL59907. Ref.5

Secondary structure

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439

Helix Strand Turn

Details...

Helix

39 – 43

5

Helix

45 – 60

16

Helix

69 – 82

14

Beta strand

85 – 90

6

Turn

91 – 93

3

Beta strand

94 – 104

11

Beta strand

106 – 112

7

Helix

139 – 155

17

Helix

156 – 159

4

Beta strand

161 – 169

9

Turn

172 – 175

4

Helix

177 – 183

7

Turn

184 – 189

6

Beta strand

190 – 203

14

Beta strand

207 – 209

3

Beta strand

211 – 215

5

Beta strand

218 – 227

10

Helix

240 – 255

16

Beta strand

266 – 274

9

Beta strand

285 – 296

12

Helix

298 – 314

17

Turn

315 – 317

3

Beta strand

318 – 325

8

Helix

326 – 328

3

Beta strand

335 – 337

3

Helix

339 – 352

14

Turn

355 – 357

3

Helix

371 – 374

4

Turn

375 – 378

4

Beta strand

379 – 387

9

Beta strand

396 – 398

3

Helix

405 – 407

3

Helix

408 – 426

19

Sequences

	Sequence		Length	Mass (Da)
	P54970 [UniParc]. Last modified May 27, 2002. Version 2. Checksum: BFA5F35AF4C4F508	FASTA	439	47,856
	10 20 30 40 50 60 MALNKLLSLT FQLLLFLLSV SSESPWIAED TSQIQTKLLE FAKSPEVFDW MVKIRRKIHE 70 80 90 100 110 120 NPELGYEELE TSKLIRSELE LIGIKYRYPV AITGVIGYIG TGEPPFVALR ADMDALPIQE 130 140 150 160 170 180 GVEWEHKSKI AGKMHACGHD GHVTMLLGAA KILHEHRHHL QGTVVLIFQP AEEGLSGAKK 190 200 210 220 230 240 MREEGALKNV EAIFGIHLSA RIPFGKAASR AGSFLAGAGV FEAVITGKGG HAAIPQHTID 250 260 270 280 290 300 PVVAASSIVL SLQQLVSRET DPLDSKVVTV SKVNGGNAFN VIPDSITIGG TLRAFTGFTQ 310 320 330 340 350 360 LQQRVKEVIT KQAAVHRCNA SVNLTPNGRE PMPPTVNNKD LYKQFKKVVR DLLGQEAFVE 370 380 390 400 410 420 AAPVMGSEDF SYFAETIPGH FSLLGMQDET NGYASSHSPL YRINEDVLPY GAAIHASMAV 430 QYLKEKASKG SVSGFHEEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ILR1, an amidohydrolase that releases active indole-3-acetic acid from conjugates." Bartel B., Fink G.R. Science 268:1745-1748(1995) [PubMed: 7792599] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Landsberg erecta.
[2]	"IAR3 encodes an auxin conjugate hydrolase from Arabidopsis." Davies R.T., Goetz D.H., Lasswell J.E., Anderson M.N., Bartel B. Plant Cell 11:365-376(1999) [PubMed: 10072397] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones." Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S. DNA Res. 5:203-216(1998) [PubMed: 9734815] [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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Characterization of a family of IAA-amino acid conjugate hydrolases from Arabidopsis." LeClere S., Tellez R., Rampey R.A., Matsuda S.P.T., Bartel B. J. Biol. Chem. 277:20446-20452(2002) [PubMed: 11923288] [Abstract] Cited for: GENE FAMILY.
[7]	"X-ray structure of IAA-aminoacid hydrolase from Arabidopsis thaliana gene At5g56660." Wesenberg G.E., Smith D.W., Phillips G.N. Jr., Bitto E., Bingman C.A., Allard S.T.M. Submitted (OCT-2004) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-439.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U23796 mRNA. Translation: AAC49016.1.
AF047031 Genomic DNA. Translation: AAC04866.1.
AB013392 Genomic DNA. Translation: BAB09884.1.
CP002688 Genomic DNA. Translation: AED96793.1.
AY072084 mRNA. Translation: AAL59907.1.

IPI

IPI00536072.

RefSeq

NP_200477.1. NM_125049.3.

UniGene

At.46738.
At.66661.
At.66838.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XMB	X-ray	2.00	A	22-439	[»]
2Q43	X-ray	2.00	A	22-439	[»]

ProteinModelPortal

P54970.

SMR

P54970. Positions 37-428.

ModBase

Search...

Protein-protein interaction databases

STRING

P54970.

Protein family/group databases

MEROPS

M20.014.

Proteomic databases

PRIDE

P54970.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT5G56660.1; AT5G56660.1; AT5G56660.

GeneID

835767.

GenomeReviews

Gene locus AT5G56660 in contig BA000015_GR.

KEGG

ath:AT5G56660.

Organism-specific databases

GeneFarm

1960. 187.

TAIR

At5g56660.

Phylogenomic databases

eggNOG

euNOG11243.

HOGENOM

HBG708500.

InParanoid

P54970.

OMA

RYPVAIT.

PhylomeDB

P54970.

ProtClustDB

PLN02693.

Gene expression databases

Genevestigator

P54970.

GermOnline

AT5G56660. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR017439. Amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]

KO

K14664.

Pfam

PF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]

PIRSF

PIRSF005962. Pept_M20D_amidohydro. 1 hit.

SUPFAM

SSF55031. Peptidase_M20_dimer. 1 hit.

TIGRFAMs

TIGR01891. Amidohydrolases. 1 hit.

PROSITE

PS00014. ER_TARGET. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ILL2_ARATH

Accession

Primary (citable) accession number: P54970
Secondary accession number(s): O49221

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 27, 2002
Last modified:	December 14, 2011
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