Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cytosol aminopeptidase

Gene

Lap3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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.

Cofactori

Note: 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi282 – 2821Zinc 2By similarity
Metal bindingi287 – 2871Zinc 1By similarity
Metal bindingi287 – 2871Zinc 2By similarity
Active sitei294 – 2941By similarity
Metal bindingi305 – 3051Zinc 2By similarity
Metal bindingi364 – 3641Zinc 1By similarity
Metal bindingi366 – 3661Zinc 1By similarity
Metal bindingi366 – 3661Zinc 2By similarity
Active sitei368 – 3681By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, Zinc

Protein family/group databases

MEROPSiM17.001.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Lap3
Synonyms:Lapep
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1914238. Lap3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 519519Cytosol aminopeptidasePRO_0000165826Add
BLAST
Isoform 2 (identifier: Q9CPY7-2)
Initiator methionineiRemoved

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451N6-succinyllysineCombined sources
Modified residuei54 – 541PhosphoserineBy similarity
Modified residuei61 – 611N6-succinyllysineCombined sources
Modified residuei103 – 1031N6-succinyllysineCombined sources
Modified residuei180 – 1801PhosphoserineCombined sources
Modified residuei194 – 1941PhosphoserineBy similarity
Modified residuei221 – 2211N6-acetyllysine; alternateCombined sources
Modified residuei221 – 2211N6-succinyllysine; alternateCombined sources
Modified residuei238 – 2381PhosphoserineCombined sources
Modified residuei455 – 4551N6-acetyllysine; alternateCombined sources
Modified residuei455 – 4551N6-succinyllysine; alternateCombined sources
Modified residuei476 – 4761N6-succinyllysineCombined sources
Modified residuei489 – 4891N6-acetyllysine; alternateCombined sources
Modified residuei489 – 4891N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CPY7.
MaxQBiQ9CPY7.
PaxDbiQ9CPY7.
PeptideAtlasiQ9CPY7.
PRIDEiQ9CPY7.

2D gel databases

REPRODUCTION-2DPAGEIPI00828469.

PTM databases

iPTMnetiQ9CPY7.
PhosphoSiteiQ9CPY7.
SwissPalmiQ9CPY7.

Expressioni

Gene expression databases

BgeeiQ9CPY7.
CleanExiMM_LAP3.
ExpressionAtlasiQ9CPY7. baseline and differential.
GenevisibleiQ9CPY7. MM.

Interactioni

Subunit structurei

Homohexamer.By similarity

Protein-protein interaction databases

IntActiQ9CPY7. 5 interactions.
MINTiMINT-1869867.
STRINGi10090.ENSMUSP00000040222.

Structurei

3D structure databases

ProteinModelPortaliQ9CPY7.
SMRiQ9CPY7. Positions 33-516.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M17 family.Curated

Phylogenomic databases

eggNOGiKOG2597. Eukaryota.
COG0260. LUCA.
GeneTreeiENSGT00530000063255.
HOGENOMiHOG000243129.
HOVERGENiHBG003320.
InParanoidiQ9CPY7.
KOiK11142.
OMAiGIVGMKS.
OrthoDBiEOG7F24SG.
PhylomeDBiQ9CPY7.
TreeFamiTF314954.

Family and domain databases

HAMAPiMF_00181. Cytosol_peptidase_M17.
InterProiIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view]
PANTHERiPTHR11963. PTHR11963. 1 hit.
PfamiPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSiPR00481. LAMNOPPTDASE.
PROSITEiPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: Q9CPY7-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MYLLPLPAAA RVALRRLGVR GLWDRGLSTA DMTKGLVLGI YAKDKDDDLP
60 70 80 90 100
QFTSAGESFN KLVSGKLREM LNISGPPLKA GKTRTFYGLH QDFPSVVVVG
110 120 130 140 150
LGKRSAGVDD QENWHEGKEN IRAAVAAGCR QVQDLELPSV EVDPCGDAQA
160 170 180 190 200
AAEGAVLGLY EYDDLKQKKK VAVSAKLHGS GDLEAWEKGV LFASGQNLAR
210 220 230 240 250
HLMESPANEM TPTRFAEIIE KNLKSASSKT KVHIRPKSWI EEQEMGSFLS
260 270 280 290 300
VAKGSEEPPV FLEIHYMGSP NATEAPLVFV GKGITFDSGG ISIKASANMD
310 320 330 340 350
LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV
360 370 380 390 400
RARNGKTIQV DNTDAEGRLI LADALCYAHT FNPKVIINAA TLTGAMDVAL
410 420 430 440 450
GSGATGVFTN SSWLWNKLFE ASVETGDRVW RMPLFEHYTR QVIDCQLADV
460 470 480 490 500
NNLGKYRSAG ACTAAAFLRE FVTHTKWAHL DIAGVMTNKD EIPYLRKGMS
510
GRPTRTLIEF LLRFSKDSS
Length:519
Mass (Da):56,141
Last modified:January 23, 2007 - v3
Checksum:i46729A9CE4C060A5
GO
Isoform 2 (identifier: Q9CPY7-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:488
Mass (Da):52,750
Checksum:iE6800977EC37A2AC
GO

Sequence cautioni

The sequence BAB23958.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB25769.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB27726.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE39141.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE40823.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461D → G in CAJ18509 (Ref. 2) Curated
Sequence conflicti93 – 931F → L in CAJ18445 (Ref. 2) Curated
Sequence conflicti123 – 1231A → D in BAB26987 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3131Missing in isoform 2. CuratedVSP_022632Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19274.1. [Q9CPY7-1]
RefSeqiNP_077754.3. NM_024434.6. [Q9CPY7-1]
UniGeneiMm.286830.

Genome annotation databases

EnsembliENSMUST00000046122; ENSMUSP00000040222; ENSMUSG00000039682. [Q9CPY7-1]
GeneIDi66988.
KEGGimmu:66988.
UCSCiuc008xiy.2. mouse. [Q9CPY7-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19274.1. [Q9CPY7-1]
RefSeqiNP_077754.3. NM_024434.6. [Q9CPY7-1]
UniGeneiMm.286830.

3D structure databases

ProteinModelPortaliQ9CPY7.
SMRiQ9CPY7. Positions 33-516.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CPY7. 5 interactions.
MINTiMINT-1869867.
STRINGi10090.ENSMUSP00000040222.

Protein family/group databases

MEROPSiM17.001.

PTM databases

iPTMnetiQ9CPY7.
PhosphoSiteiQ9CPY7.
SwissPalmiQ9CPY7.

2D gel databases

REPRODUCTION-2DPAGEIPI00828469.

Proteomic databases

EPDiQ9CPY7.
MaxQBiQ9CPY7.
PaxDbiQ9CPY7.
PeptideAtlasiQ9CPY7.
PRIDEiQ9CPY7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000046122; ENSMUSP00000040222; ENSMUSG00000039682. [Q9CPY7-1]
GeneIDi66988.
KEGGimmu:66988.
UCSCiuc008xiy.2. mouse. [Q9CPY7-1]

Organism-specific databases

CTDi51056.
MGIiMGI:1914238. Lap3.

Phylogenomic databases

eggNOGiKOG2597. Eukaryota.
COG0260. LUCA.
GeneTreeiENSGT00530000063255.
HOGENOMiHOG000243129.
HOVERGENiHBG003320.
InParanoidiQ9CPY7.
KOiK11142.
OMAiGIVGMKS.
OrthoDBiEOG7F24SG.
PhylomeDBiQ9CPY7.
TreeFamiTF314954.

Miscellaneous databases

ChiTaRSiLap3. mouse.
PROiQ9CPY7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CPY7.
CleanExiMM_LAP3.
ExpressionAtlasiQ9CPY7. baseline and differential.
GenevisibleiQ9CPY7. MM.

Family and domain databases

HAMAPiMF_00181. Cytosol_peptidase_M17.
InterProiIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view]
PANTHERiPTHR11963. PTHR11963. 1 hit.
PfamiPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSiPR00481. LAMNOPPTDASE.
PROSITEiPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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/6J.
  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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180 AND SER-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-45; LYS-61; LYS-103; LYS-221; LYS-455; LYS-476 AND LYS-489, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  9. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221; LYS-455 AND LYS-489, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAMPL_MOUSE
AccessioniPrimary (citable) accession number: Q9CPY7
Secondary accession number(s): Q3TFS5
, Q4FJV1, Q4FK15, Q99P44, Q9CWN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.