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Protein

Acyl-protein thioesterase 1

Gene

Lypla1

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

Functioni

Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has depalmitoylating activity toward KCNMA1. Has low lysophospholipase activity (By similarity).By similarity1 Publication

Catalytic activityi

Palmitoyl-protein + H2O = palmitate + protein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei119 – 1191Charge relay system
Active sitei174 – 1741Charge relay system
Active sitei208 – 2081Charge relay system

GO - Molecular functioni

GO - Biological processi

  • fatty acid metabolic process Source: UniProtKB-KW
  • negative regulation of Golgi to plasma membrane protein transport Source: MGI
  • protein depalmitoylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-MMU-203615. eNOS activation.

Protein family/group databases

ESTHERimouse-lypla1. LYsophospholipase_carboxylesterase.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-protein thioesterase 1 (EC:3.1.2.-)
Short name:
APT-1
Alternative name(s):
Lysophospholipase 1
Lysophospholipase I
Short name:
LPL-I
Short name:
LysoPLA I
Gene namesi
Name:Lypla1
Synonyms:Apt1, Pla1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1344588. Lypla1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi119 – 1191S → A: Abolishes lysophospholipase activity. 1 Publication
Mutagenesisi174 – 1741D → A: Abolishes lysophospholipase activity. 1 Publication
Mutagenesisi208 – 2081H → A: Abolishes lysophospholipase activity. 1 Publication

Chemistry

ChEMBLiCHEMBL3259479.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 230230Acyl-protein thioesterase 1PRO_0000102268Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei224 – 2241N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP97823.
MaxQBiP97823.
PaxDbiP97823.
PRIDEiP97823.

PTM databases

iPTMnetiP97823.
PhosphoSiteiP97823.
SwissPalmiP97823.

Expressioni

Gene expression databases

BgeeiP97823.
CleanExiMM_LYPLA1.
MM_PLA1A.
ExpressionAtlasiP97823. baseline and differential.
GenevisibleiP97823. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi202216. 1 interaction.
IntActiP97823. 4 interactions.
MINTiMINT-1868970.
STRINGi10090.ENSMUSP00000027036.

Structurei

3D structure databases

ProteinModelPortaliP97823.
SMRiP97823. Positions 6-229.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2112. Eukaryota.
COG0400. LUCA.
GeneTreeiENSGT00390000009648.
HOGENOMiHOG000260139.
HOVERGENiHBG052378.
InParanoidiP97823.
KOiK06128.
OMAiFSQGPIN.
PhylomeDBiP97823.
TreeFamiTF314619.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR003140. PLipase/COase/thioEstase.
[Graphical view]
PfamiPF02230. Abhydrolase_2. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: P97823-1) [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
MCGNNMSAPM PAVVPAARKA TAAVIFLHGL GDTGHGWAEA FAGIKSPHIK
60 70 80 90 100
YICPHAPVMP VTLNMNMAMP SWFDIVGLSP DSQEDESGIK QAAETVKALI
110 120 130 140 150
DQEVKNGIPS NRIILGGFSQ GGALSLYTAL TTQQKLAGVT ALSCWLPLRA
160 170 180 190 200
SFSQGPINSA NRDISVLQCH GDCDPLVPLM FGSLTVERLK ALINPANVTF
210 220 230
KIYEGMMHSS CQQEMMDVKH FIDKLLPPID
Length:230
Mass (Da):24,688
Last modified:May 1, 1997 - v1
Checksum:i89AF2017AEFC9FAC
GO
Isoform 2 (identifier: P97823-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     214-230: EMMDVKHFIDKLLPPID → VGVSGSSE

Note: May be due to an intron retention. No experimental confirmation available.
Show »
Length:221
Mass (Da):23,367
Checksum:i456BF0DCF6EE0F30
GO

Sequence cautioni

The sequence BAC34318.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti156 – 1561P → L in AAH52848 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei214 – 23017EMMDV…LPPID → VGVSGSSE in isoform 2. 1 PublicationVSP_009197Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89352 mRNA. Translation: AAB48627.1.
AK002674 mRNA. Translation: BAB22276.1.
AK050549 mRNA. Translation: BAC34318.1. Different initiation.
AK146874 mRNA. Translation: BAE27497.1.
AK167231 mRNA. Translation: BAE39355.1.
BC013536 mRNA. Translation: AAH13536.1.
BC052848 mRNA. Translation: AAH52848.1.
CCDSiCCDS14806.1. [P97823-1]
RefSeqiNP_032892.1. NM_008866.2. [P97823-1]
UniGeneiMm.299955.

Genome annotation databases

EnsembliENSMUST00000027036; ENSMUSP00000027036; ENSMUSG00000025903. [P97823-1]
ENSMUST00000150971; ENSMUSP00000137248; ENSMUSG00000025903. [P97823-2]
GeneIDi18777.
KEGGimmu:18777.
UCSCiuc007afh.1. mouse. [P97823-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89352 mRNA. Translation: AAB48627.1.
AK002674 mRNA. Translation: BAB22276.1.
AK050549 mRNA. Translation: BAC34318.1. Different initiation.
AK146874 mRNA. Translation: BAE27497.1.
AK167231 mRNA. Translation: BAE39355.1.
BC013536 mRNA. Translation: AAH13536.1.
BC052848 mRNA. Translation: AAH52848.1.
CCDSiCCDS14806.1. [P97823-1]
RefSeqiNP_032892.1. NM_008866.2. [P97823-1]
UniGeneiMm.299955.

3D structure databases

ProteinModelPortaliP97823.
SMRiP97823. Positions 6-229.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202216. 1 interaction.
IntActiP97823. 4 interactions.
MINTiMINT-1868970.
STRINGi10090.ENSMUSP00000027036.

Chemistry

ChEMBLiCHEMBL3259479.

Protein family/group databases

ESTHERimouse-lypla1. LYsophospholipase_carboxylesterase.

PTM databases

iPTMnetiP97823.
PhosphoSiteiP97823.
SwissPalmiP97823.

Proteomic databases

EPDiP97823.
MaxQBiP97823.
PaxDbiP97823.
PRIDEiP97823.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027036; ENSMUSP00000027036; ENSMUSG00000025903. [P97823-1]
ENSMUST00000150971; ENSMUSP00000137248; ENSMUSG00000025903. [P97823-2]
GeneIDi18777.
KEGGimmu:18777.
UCSCiuc007afh.1. mouse. [P97823-1]

Organism-specific databases

CTDi10434.
MGIiMGI:1344588. Lypla1.

Phylogenomic databases

eggNOGiKOG2112. Eukaryota.
COG0400. LUCA.
GeneTreeiENSGT00390000009648.
HOGENOMiHOG000260139.
HOVERGENiHBG052378.
InParanoidiP97823.
KOiK06128.
OMAiFSQGPIN.
PhylomeDBiP97823.
TreeFamiTF314619.

Enzyme and pathway databases

ReactomeiR-MMU-203615. eNOS activation.

Miscellaneous databases

ChiTaRSiLypla1. mouse.
PROiP97823.
SOURCEiSearch...

Gene expression databases

BgeeiP97823.
CleanExiMM_LYPLA1.
MM_PLA1A.
ExpressionAtlasiP97823. baseline and differential.
GenevisibleiP97823. MM.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR003140. PLipase/COase/thioEstase.
[Graphical view]
PfamiPF02230. Abhydrolase_2. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, and catalytic mechanism of murine lysophospholipase I."
    Wang A., Deems R.A., Dennis E.A.
    J. Biol. Chem. 272:12723-12729(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 98-105; 150-162 AND 191-201, MUTAGENESIS OF SER-119, FUNCTION.
    Tissue: Macrophage.
  2. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Kidney and Pancreas.
  3. "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] (ISOFORM 1).
    Tissue: Kidney and Osteoblast.
  4. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 136-149.
    Tissue: Brain.
  5. "Regiospecificity and catalytic triad of lysophospholipase I."
    Wang A., Loo R., Chen Z., Dennis E.A.
    J. Biol. Chem. 272:22030-22036(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-174 AND HIS-208.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "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-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiLYPA1_MOUSE
AccessioniPrimary (citable) accession number: P97823
Secondary accession number(s): Q3TJZ0, Q7TPX1, Q8BWM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: May 1, 1997
Last modified: June 8, 2016
This is version 133 of the entry and version 1 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. 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.