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O75608 (LYPA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl-protein thioesterase 1

Short name=APT-1
Short name=hAPT1
EC=3.1.2.-
Alternative name(s):
Lysophospholipase 1
Lysophospholipase I
Short name=LPL-I
Short name=LysoPLA I
Gene names
Name:LYPLA1
Synonyms:APT1, LPL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has depalmitoylating activity and also low lysophospholipase activity. Ref.6

Catalytic activity

Palmitoyl-protein + H2O = palmitate + protein.

Enzyme regulation

Inhibited by palmostatin-B, leading to impair depalmitoylating of Ras. Ref.6

Subunit structure

Homodimer. Ref.2

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the AB hydrolase superfamily. AB hydrolase 2 family.

Sequence caution

The sequence AAB88180.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75608-1)

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: O75608-2)

The sequence of this isoform differs from the canonical sequence as follows:
     57-72: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 230230Acyl-protein thioesterase 1
PRO_0000102267

Sites

Active site1191Charge relay system
Active site1741Charge relay system
Active site2081Charge relay system

Natural variations

Alternative sequence57 – 7216Missing in isoform 2.
VSP_009196
Natural variant1531P → S.
Corresponds to variant rs11549448 [ dbSNP | Ensembl ].
VAR_060991

Experimental info

Sequence conflict127 – 1315YTALT → SLIRG in AAB88180. Ref.5

Secondary structure

......................................... 230
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 90C0522F765F1AC6

FASTA23024,670
        10         20         30         40         50         60 
MCGNNMSTPL PAIVPAARKA TAAVIFLHGL GDTGHGWAEA FAGIRSSHIK YICPHAPVRP 

        70         80         90        100        110        120 
VTLNMNVAMP SWFDIIGLSP DSQEDESGIK QAAENIKALI DQEVKNGIPS NRIILGGFSQ 

       130        140        150        160        170        180 
GGALSLYTAL TTQQKLAGVT ALSCWLPLRA SFPQGPIGGA NRDISILQCH GDCDPLVPLM 

       190        200        210        220        230 
FGSLTVEKLK TLVNPANVTF KTYEGMMHSS CQQEMMDVKQ FIDKLLPPID 

« Hide

Isoform 2 [UniParc].

Checksum: 63BCCC806F509CE8
Show »

FASTA21422,875

References

« Hide 'large scale' references
[1]Hu G.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A."
Devedjiev Y., Dauter Z., Kuznetsov S.R., Jones T.L.Z., Derewenda Z.S.
Structure 8:1137-1146(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 6-230, SUBUNIT.
Tissue: Testis.
[3]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Umbilical cord blood.
[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] (ISOFORM 1).
Tissue: Bone marrow and Eye.
[5]Yu W., Sarginson J., Gibbs R.A.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-230 (ISOFORM 1).
Tissue: Brain.
[6]"Small-molecule inhibition of APT1 affects Ras localization and signaling."
Dekker F.J., Rocks O., Vartak N., Menninger S., Hedberg C., Balamurugan R., Wetzel S., Renner S., Gerauer M., Scholermann B., Rusch M., Kramer J.W., Rauh D., Coates G.W., Brunsveld L., Bastiaens P.I., Waldmann H.
Nat. Chem. Biol. 6:449-456(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, FUNCTION.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF081281 mRNA. Translation: AAC31610.1.
AF291053 mRNA. Translation: AAG10063.1.
AF077198 mRNA. Translation: AAD26993.1.
AF077199 mRNA. Translation: AAD26994.1.
BC008652 mRNA. Translation: AAH08652.1.
BC010397 mRNA. Translation: AAH10397.1.
AF035293 mRNA. Translation: AAB88180.1. Different initiation.
IPIIPI00007321.
IPI00398727.
RefSeqNP_006321.1. NM_006330.2.
UniGeneHs.435850.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJ2X-ray1.50A/B6-230[»]
ProteinModelPortalO75608.
ModBaseSearch...

Protein-protein interaction databases

IntActO75608. 2 interactions.
STRING9606.ENSP00000320043.

Protein family/group databases

MEROPSS09.026.

PTM databases

PhosphoSiteO75608.

2D gel databases

OGPO75608.

Proteomic databases

PaxDbO75608.
PeptideAtlasO75608.
PRIDEO75608.

Protocols and materials databases

DNASU10434.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316963; ENSP00000320043; ENSG00000120992.
ENST00000343231; ENSP00000344477; ENSG00000120992.
GeneID10434.
KEGGhsa:10434.
UCSCuc003xry.3. human.
uc003xrz.3. human.

Organism-specific databases

CTD10434.
GeneCardsGC08M055008.
HGNCHGNC:6737. LYPLA1.
HPAHPA050941.
MIM605599. gene.
neXtProtNX_O75608.
PharmGKBPA30499.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0400.
HOGENOMHOG000260139.
HOVERGENHBG052378.
InParanoidO75608.
KOK06128.
OMAGYIMRAW.
OrthoDBEOG4320ZX.
PhylomeDBO75608.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO75608.
BgeeO75608.
CleanExHS_LYPLA1.
GenevestigatorO75608.
GermOnlineENSG00000120992. Homo sapiens.

Family and domain databases

InterProIPR003140. PLipase/COase/thioEstase.
[Graphical view]
PfamPF02230. Abhydrolase_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBO75608.
ChEMBLCHEMBL1681631.
ChiTaRSLYPLA1. human.
EvolutionaryTraceO75608.
GenomeRNAi10434.
NextBio39546.
SOURCESearch...

Entry information

Entry nameLYPA1_HUMAN
AccessionPrimary (citable) accession number: O75608
Secondary accession number(s): O43202, Q9UQF9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1998
Last modified: May 1, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families