Q9CPY7 (AMPL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytosol aminopeptidase
EC=3.4.11.1

Alternative name(s):
Leucine aminopeptidase 3
Short name=LAP-3
Leucyl aminopeptidase
Proline aminopeptidase
EC=3.4.11.5
Prolyl aminopeptidase

Gene names

Name:	Lap3
Synonyms:	Lapep

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	519 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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. One zinc ion is tightly bound and essential for enzyme activity, while the second metal coordination site can be occupied by zinc, magnesium or manganese to give enzymes of different activities By similarity.
Subunit structure	Homohexamer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the peptidase M17 family.
Sequence caution	The sequence BAB23958.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB25769.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB27726.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE39141.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE40823.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative initiation
Ligand	Magnesium Manganese Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Protease
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
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...

Alternative products

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

Isoform 1 (identifier: Q9CPY7-1)

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: Q9CPY7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.

Note: The initiator methionine is removed. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 519	519	Cytosol aminopeptidase		PRO_0000165826
Sites
	Active site	294	1	By similarity
	Active site	368	1	By similarity
	Metal binding	282	1	Zinc 2 By similarity
	Metal binding	287	1	Zinc 1 By similarity
	Metal binding	287	1	Zinc 2 By similarity
	Metal binding	305	1	Zinc 2 By similarity
	Metal binding	364	1	Zinc 1 By similarity
	Metal binding	366	1	Zinc 1 By similarity
	Metal binding	366	1	Zinc 2 By similarity
Amino acid modifications
	Modified residue	33	1	N-acetylthreonine By similarity
	Modified residue	221	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	1 – 31	31	Missing in isoform 2.		VSP_022632
Experimental info
	Sequence conflict	46	1	D → G in CAJ18509. Ref.2
	Sequence conflict	93	1	F → L in CAJ18445. Ref.2
	Sequence conflict	123	1	A → D in BAB26987. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 46729A9CE4C060A5	FASTA	519	56,141
	10 20 30 40 50 60 MYLLPLPAAA RVALRRLGVR GLWDRGLSTA DMTKGLVLGI YAKDKDDDLP QFTSAGESFN 70 80 90 100 110 120 KLVSGKLREM LNISGPPLKA GKTRTFYGLH QDFPSVVVVG LGKRSAGVDD QENWHEGKEN 130 140 150 160 170 180 IRAAVAAGCR QVQDLELPSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKKK VAVSAKLHGS 190 200 210 220 230 240 GDLEAWEKGV LFASGQNLAR HLMESPANEM TPTRFAEIIE KNLKSASSKT KVHIRPKSWI 250 260 270 280 290 300 EEQEMGSFLS VAKGSEEPPV FLEIHYMGSP NATEAPLVFV GKGITFDSGG ISIKASANMD 310 320 330 340 350 360 LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV RARNGKTIQV 370 380 390 400 410 420 DNTDAEGRLI LADALCYAHT FNPKVIINAA TLTGAMDVAL GSGATGVFTN SSWLWNKLFE 430 440 450 460 470 480 ASVETGDRVW RMPLFEHYTR QVIDCQLADV NNLGKYRSAG ACTAAAFLRE FVTHTKWAHL 490 500 510 DIAGVMTNKD EIPYLRKGMS GRPTRTLIEF LLRFSKDSS
	Isoform 2 [UniParc]. Checksum: E6800977EC37A2AC	FASTA	488	52,750
	10 20 30 40 50 60 MTKGLVLGIY AKDKDDDLPQ FTSAGESFNK LVSGKLREML NISGPPLKAG KTRTFYGLHQ 70 80 90 100 110 120 DFPSVVVVGL GKRSAGVDDQ ENWHEGKENI RAAVAAGCRQ VQDLELPSVE VDPCGDAQAA 130 140 150 160 170 180 AEGAVLGLYE YDDLKQKKKV AVSAKLHGSG DLEAWEKGVL FASGQNLARH LMESPANEMT 190 200 210 220 230 240 PTRFAEIIEK NLKSASSKTK VHIRPKSWIE EQEMGSFLSV AKGSEEPPVF LEIHYMGSPN 250 260 270 280 290 300 ATEAPLVFVG KGITFDSGGI SIKASANMDL MRADMGGAAT ICSAIVSAAK LNLPINIIGL 310 320 330 340 350 360 APLCENMPSG KANKPGDVVR ARNGKTIQVD NTDAEGRLIL ADALCYAHTF NPKVIINAAT 370 380 390 400 410 420 LTGAMDVALG SGATGVFTNS SWLWNKLFEA SVETGDRVWR MPLFEHYTRQ VIDCQLADVN 430 440 450 460 470 480 NLGKYRSAGA CTAAAFLREF VTHTKWAHLD IAGVMTNKDE IPYLRKGMSG RPTRTLIEFL LRFSKDSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mammalian Lap-D proteins related to ovarian development and differentiation." Zhuang D.Z., Gunnarsson D., Toffia O., Lind M., Lundgren P., Selstam G. Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6.
[2]	"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)." Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Amnion, Bone marrow, Cerebellum, Embryo, Kidney, Lung, Placenta and Small intestine.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[5]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 474-481, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF334160 mRNA. Translation: AAK13495.1. CT010237 mRNA. Translation: CAJ18445.1. CT010301 mRNA. Translation: CAJ18509.1. AK002819 mRNA. No translation available. AK005334 mRNA. Translation: BAB23958.1. Different initiation. AK008600 mRNA. Translation: BAB25769.1. Different initiation. AK010502 mRNA. Translation: BAB26987.1. AK011604 mRNA. Translation: BAB27726.1. Different initiation. AK166958 mRNA. Translation: BAE39141.1. Different initiation. AK169032 mRNA. Translation: BAE40823.1. Different initiation. BC016536 mRNA. Translation: AAH16536.1.
IPI	IPI00331436. IPI00828469.
RefSeq	NP_077754.3. NM_024434.6.
UniGene	Mm.286830.
3D structure databases
ProteinModelPortal	Q9CPY7.
SMR	Q9CPY7. Positions 33-516.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9CPY7. 1 interaction.
STRING	Q9CPY7.
Protein family/group databases
MEROPS	M17.001.
PTM databases
PhosphoSite	Q9CPY7.
2D gel databases
REPRODUCTION-2DPAGE	IPI00828469.
Proteomic databases
PRIDE	Q9CPY7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000046122; ENSMUSP00000040222; ENSMUSG00000039682.
GeneID	66988.
KEGG	mmu:66988.
UCSC	uc008xiy.2. mouse.
Organism-specific databases
CTD	51056.
MGI	MGI:1914238. Lap3.
Phylogenomic databases
eggNOG	roNOG09682.
GeneTree	ENSGT00530000063255.
HOGENOM	HBG742580.
HOVERGEN	HBG003320.
InParanoid	Q9CPY7.
OMA	KLFEASV.
OrthoDB	EOG4P2Q21.
PhylomeDB	Q9CPY7.
Gene expression databases
ArrayExpress	Q9CPY7.
Bgee	Q9CPY7.
CleanEx	MM_LAP3.
Genevestigator	Q9CPY7.
GermOnline	ENSMUSG00000039682. Mus musculus.
Family and domain databases
InterPro	IPR011356. Peptidase_M17. IPR000819. Peptidase_M17_C. IPR023042. Peptidase_M17_cytosol_amino. IPR008283. Peptidase_M17_N. [Graphical view]
KO	K11142.
Pfam	PF00883. Peptidase_M17. 1 hit. PF02789. Peptidase_M17_N. 1 hit. [Graphical view]
PRINTS	PR00481. LAMNOPPTDASE.
PROSITE	PS00631. CYTOSOL_AP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	323224.
SOURCE	Search...

Entry information

Entry name

AMPL_MOUSE

Accession

Primary (citable) accession number: Q9CPY7
Secondary accession number(s): Q3TFS5 , Q4FJV1, Q4FK15, Q99P44, Q9CWN8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program