O95372 (LYPA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyl-protein thioesterase 2
Short name=APT-2
EC=3.1.2.-

Alternative name(s):
Lysophospholipase II
Short name=LPL-II
Short name=LysoPLA II

Gene names

Name:	LYPLA2
Synonyms:	APT2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	231 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has lysophospholipase activity By similarity. Deacylates GAP43. Ref.5
Catalytic activity	Palmitoyl-protein + H2O = palmitate + protein.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the AB hydrolase superfamily. AB hydrolase 2 family.
Sequence caution	The sequence AAP97210.1 differs from that shown. Reason: Frameshift at positions 5, 164 and 179.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Cytoplasm
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 231	231	Acyl-protein thioesterase 2		PRO_0000102271
Sites
	Active site	122	1	Charge relay system By similarity
	Active site	176	1	Charge relay system By similarity
	Active site	210	1	Charge relay system By similarity

Sequences

	Sequence		Length	Mass (Da)
	O95372 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 813C9C71757C5135	FASTA	231	24,737
	10 20 30 40 50 60 MCGNTMSVPL LTDAATVSGA ERETAAVIFL HGLGDTGHSW ADALSTIRLP HVKYICPHAP 70 80 90 100 110 120 RIPVTLNMKM VMPSWFDLMG LSPDAPEDEA GIKKAAENIK ALIEHEMKNG IPANRIVLGG 130 140 150 160 170 180 FSQGGALSLY TALTCPHPLA GIVALSCWLP LHRAFPQAAN GSAKDLAILQ CHGELDPMVP 190 200 210 220 230 VRFGALTAEK LRSVVTPARV QFKTYPGVMH SSCPQEMAAV KEFLEKLLPP V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Kuznetsov S.R., Jones T.L.Z. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[2]	"Cloning and expression of a novel human cDNA homology to murine lysophospholipase I mRNA." Yue P., Yu L., Tu Q., Ding J.B., Fu S.N., Zhao S.Y. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]. Tissue: Colon and Placenta.
[5]	"Acyl-protein thioesterase 2 catalyzes the deacylation of peripheral membrane-associated GAP-43." Tomatis V.M., Trenchi A., Gomez G.A., Daniotti J.L. PLoS ONE 5:E15045-E15045(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DEACYLATION OF GAP43.
[6]	"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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF098668 mRNA. Translation: AAC72844.1. AF090423 mRNA. Translation: AAP97210.1. Frameshift. AL031295 Genomic DNA. Translation: CAB40158.1. BC017034 mRNA. Translation: AAH17034.1. BC017193 mRNA. Translation: AAH17193.1.
IPI	IPI00027032.
RefSeq	NP_009191.1. NM_007260.2.
UniGene	Hs.533479.
3D structure databases
ProteinModelPortal	O95372.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95372. 4 interactions.
STRING	9606.ENSP00000363638.
PTM databases
PhosphoSite	O95372.
2D gel databases
OGP	O95372.
Proteomic databases
PaxDb	O95372.
PRIDE	O95372.
Protocols and materials databases
DNASU	11313.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374514; ENSP00000363638; ENSG00000011009.
GeneID	11313.
KEGG	hsa:11313.
UCSC	uc001bht.3. human.
Organism-specific databases
CTD	11313.
GeneCards	GC01P024117.
HGNC	HGNC:6738. LYPLA2.
neXtProt	NX_O95372.
PharmGKB	PA30500.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0400.
HOGENOM	HOG000260139.
HOVERGEN	HBG052378.
InParanoid	O95372.
KO	K06130.
OMA	YTALTCQ.
OrthoDB	EOG4320ZX.
PhylomeDB	O95372.
Gene expression databases
ArrayExpress	O95372.
Bgee	O95372.
CleanEx	HS_LYPLA2.
Genevestigator	O95372.
GermOnline	ENSG00000011009. Homo sapiens.
Family and domain databases
InterPro	IPR003140. PLipase/COase/thioEstase. [Graphical view]
Pfam	PF02230. Abhydrolase_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1932891.
GenomeRNAi	11313.
NextBio	42975.

Entry information

Entry name

LYPA2_HUMAN

Accession

Primary (citable) accession number: O95372
Secondary accession number(s): Q7Z4Z2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 102 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.