O75608 (LYPA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	230 AA.
Sequence status	Complete.
Protein existence	Evidence 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 2 family.
Sequence caution	The sequence AAB88180.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW nitric oxide metabolic process Traceable author statement. Source: Reactome regulation of nitric-oxide synthase activity Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	lysophospholipase activity Traceable author statement. Source: ProtInc palmitoyl-(protein) hydrolase activity Inferred from mutant phenotype Ref.6. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 230

230

Acyl-protein thioesterase 1

PRO_0000102267

Sites

Active site

119

1

Charge relay system

Active site

174

1

Charge relay system

Active site

208

1

Charge relay system

Natural variations

Alternative sequence

57 – 72

16

Missing in isoform 2.

VSP_009196

Natural variant

153

1

P → S.
Corresponds to variant rs11549448 [ dbSNP | Ensembl ].

VAR_060991

Experimental info

Sequence conflict

127 – 131

5

YTALT → SLIRG in AAB88180. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

230

Helix Strand Turn

Details...

Beta strand

12 – 14

3

Beta strand

21 – 27

7

Beta strand

30 – 32

3

Helix

34 – 42

9

Beta strand

49 – 53

5

Beta strand

58 – 60

3

Helix

62 – 64

3

Beta strand

68 – 70

3

Helix

86 – 105

20

Helix

110 – 112

3

Beta strand

113 – 118

6

Helix

120 – 129

10

Beta strand

137 – 143

7

Helix

149 – 151

3

Turn

160 – 163

4

Beta strand

166 – 171

6

Beta strand

175 – 177

3

Helix

179 – 192

14

Helix

195 – 197

3

Beta strand

198 – 203

6

Helix

212 – 225

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 90C0522F765F1AC6	FASTA	230	24,670
	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
	Isoform 2 [UniParc]. Checksum: 63BCCC806F509CE8	FASTA	214	22,875
	10 20 30 40 50 60 MCGNNMSTPL PAIVPAARKA TAAVIFLHGL GDTGHGWAEA FAGIRSSHIK YICPHAFDII 70 80 90 100 110 120 GLSPDSQEDE SGIKQAAENI KALIDQEVKN GIPSNRIILG GFSQGGALSL YTALTTQQKL 130 140 150 160 170 180 AGVTALSCWL PLRASFPQGP IGGANRDISI LQCHGDCDPL VPLMFGSLTV EKLKTLVNPA 190 200 210 NVTFKTYEGM MHSSCQQEMM DVKQFIDKLL PPID

References

	« Hide 'large scale' referencesShow '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: 11080636] [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. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [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: 15489334] [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: 20418879] [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: 21269460] [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.

IPI

IPI00007321.
IPI00398727.

RefSeq

NP_006321.1. NM_006330.2.

UniGene

Hs.435850.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FJ2	X-ray	1.50	A/B	6-230	[»]

ProteinModelPortal

O75608.

SMR

O75608. Positions 6-229.

ModBase

Search...

Protein-protein interaction databases

IntAct

O75608. 1 interaction.

STRING

O75608.

Protein family/group databases

MEROPS

S09.026.

2D gel databases

OGP

O75608.

PMMA-2DPAGE

O75608.

Proteomic databases

PeptideAtlas

O75608.

PRIDE

O75608.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000316963; ENSP00000320043; ENSG00000120992.
ENST00000419058; ENSP00000397807; ENSG00000120992.

GeneID

10434.

KEGG

hsa:10434.

UCSC

uc003xry.1. human.
uc003xrz.1. human.

Organism-specific databases

CTD

10434.

GeneCards

GC08M055008.

H-InvDB

HIX0007507.

HGNC

HGNC:6737. LYPLA1.

MIM

605599. gene.

neXtProt

NX_O75608.

PharmGKB

PA30499.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08317.

HOVERGEN

HBG052378.

InParanoid

O75608.

OrthoDB

EOG4320ZX.

PhylomeDB

O75608.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

O75608.

Bgee

O75608.

CleanEx

HS_LYPLA1.

Genevestigator

O75608.

GermOnline

ENSG00000120992. Homo sapiens.

Family and domain databases

InterPro

IPR003140. PLipase/COase/thioEstase.
[Graphical view]

KO

K06128.

Pfam

PF02230. Abhydrolase_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

39546.

SOURCE

Search...

Entry information

Entry name

LYPA1_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.