Q8RX72 (AMPL2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Leucine aminopeptidase 2, chloroplastic
EC=3.4.11.1

Alternative name(s):
Leucyl aminopeptidase 2
Short name=LAP 2
Proline aminopeptidase 2
EC=3.4.11.5
Prolyl aminopeptidase 2

Gene names

Ordered Locus Names:	At4g30910
ORF Names:	F6I18.180

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

General annotation (Comments)

Function	Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides By similarity.
Catalytic activity	Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of N-terminal proline from a peptide.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homohexamer Probable.
Subcellular location	Plastid › chloroplast Potential.
Sequence similarities	Belongs to the peptidase M17 family.
Sequence caution	The sequence CAA18202.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB79809.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast stroma Inferred from direct assay. Source: TAIR
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: InterPro metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 50	50	Chloroplast Potential
	Chain	51 – 581	531	Leucine aminopeptidase 2, chloroplastic		PRO_0000045811
Regions
	Compositional bias	178 – 185	8	Poly-Ala
Sites
	Active site	362	1	Potential
	Active site	439	1	Potential
	Metal binding	350	1	Zinc 2 By similarity
	Metal binding	355	1	Zinc 1 By similarity
	Metal binding	355	1	Zinc 2 By similarity
	Metal binding	375	1	Zinc 2 By similarity
	Metal binding	435	1	Zinc 1 By similarity
	Metal binding	437	1	Zinc 1 By similarity
	Metal binding	437	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8RX72 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: C4B674CFF40F1DC0	FASTA	581	61,290
	10 20 30 40 50 60 MAVTLVTSCA SSSRFHFRSF SSSPSSLSSC FVRFQLLSRL RVSFAITPLY CSSKATAHTI 70 80 90 100 110 120 AHATLGLTQA NSVDHPKISF SGKEIDVTEW KGDILAVGVT EKDMAKDANS KFENPILKKL 130 140 150 160 170 180 DAHLGGLLAD VSAEEDFSGK PGQSTVLRLP GLGSKRVGLI GLGKSASTPS AFQSLGEAVA 190 200 210 220 230 240 AAAKASQASS VAVVLASSES FSDESKLSSA SDIASGTVLG LFEDSRYKSE SKKPSLKSVV 250 260 270 280 290 300 FIGFGTGPEL ENKLKYAEHV SYGVIFTKEL VNSPANVLSP AVLAEEASNL ASMYSNVMTA 310 320 330 340 350 360 NILKEEQCKE LKMGSYLAVA AASANPPHFI HLIYKPSSGP VKTKLALVGK GLTFDSGGYN 370 380 390 400 410 420 IKIGPELIIE LMKIDVGGSA AVLGAAKAIG EIKPPGVEVH FIVAACENMI SGTGMRPGDV 430 440 450 460 470 480 ITASNGKTIE VNDTDSEGRL TLADALVYAC NQGVDKIVDI ATLTGEIIVA LGPSMAGMYT 490 500 510 520 530 540 ASDELAKEVI AASQRSGEKL WRMPMEESYW EMMKSGVADM VNFGGRAGGS ITAALFLKRF 550 560 570 580 VSENVEWLHI DMAGRVWNEK KKAATGFGVA TLVEWVQNNS S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL022198 Genomic DNA. Translation: CAA18202.1. Sequence problems. AL161577 Genomic DNA. Translation: CAB79809.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE85829.1. AY090346 mRNA. Translation: AAL91252.1. AY125537 mRNA. Translation: AAM78047.1.
IPI	IPI00539733.
PIR	H85361.
RefSeq	NP_194820.1. NM_119238.4.
UniGene	At.31791.
3D structure databases
ProteinModelPortal	Q8RX72.
SMR	Q8RX72. Positions 76-579.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8RX72.
Protein family/group databases
MEROPS	M17.A02.
Proteomic databases
PRIDE	Q8RX72.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G30910.1; AT4G30910.1; AT4G30910.
GeneID	829215.
GenomeReviews	Gene locus AT4G30910 in contig CT486007_GR.
KEGG	ath:AT4G30910.
NMPDR	fig|3702.1.peg.21081.
Organism-specific databases
GeneFarm	2141. 195.
TAIR	At4g30910.
Phylogenomic databases
eggNOG	KOG2597.
GeneTree	EPGT00070000029661.
HOGENOM	HBG742580.
InParanoid	Q8RX72.
OMA	PASSCIA.
PhylomeDB	Q8RX72.
ProtClustDB	CLSN2683023.
Gene expression databases
Genevestigator	Q8RX72.
GermOnline	AT4G30910. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR011356. Peptidase_M17. IPR000819. Peptidase_M17_C. IPR023042. Peptidase_M17_cytosol_amino. IPR008283. Peptidase_M17_N. [Graphical view]
KO	K01255.
Pfam	PF00883. Peptidase_M17. 1 hit. PF02789. Peptidase_M17_N. 1 hit. [Graphical view]
PRINTS	PR00481. LAMNOPPTDASE.
PROSITE	PS00631. CYTOSOL_AP. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPL2_ARATH

Accession

Primary (citable) accession number: Q8RX72
Secondary accession number(s): O65558

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	June 1, 2002
Last modified:	January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program