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O88202

- LPP60_RAT

UniProt

O88202 - LPP60_RAT

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Protein

60 kDa lysophospholipase

Gene

Aspg

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities.2 Publications

Catalytic activityi

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.1 Publication
L-asparagine + H2O = L-aspartate + NH3.1 Publication
1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate.1 Publication

Enzyme regulationi

Inhibited by phosphatidic acid.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei19 – 191Acyl-ester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. 1-alkyl-2-acetylglycerophosphocholine esterase activity Source: RGD
  2. asparaginase activity Source: UniProtKB
  3. lysophospholipase activity Source: UniProtKB

GO - Biological processi

  1. asparagine metabolic process Source: UniProtKB
  2. lipid catabolic process Source: UniProtKB-KW
  3. phospholipid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
60 kDa lysophospholipase (EC:3.1.1.5)
Including the following 2 domains:
L-asparaginase (EC:3.5.1.1)
Alternative name(s):
L-asparagine amidohydrolase
Platelet-activating factor acetylhydrolase (EC:3.1.1.47)
Short name:
PAF acetylhydrolase
Gene namesi
Name:Aspg
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 6

Organism-specific databases

RGDi708388. Aspg.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 56456460 kDa lysophospholipasePRO_0000171092Add
BLAST

Proteomic databases

PaxDbiO88202.
PRIDEiO88202.

PTM databases

PhosphoSiteiO88202.

Expressioni

Tissue specificityi

Expressed at high levels in liver and kidney and at a low level in stomach. Barely detectable in lung, heart, spleen and brain.1 Publication

Gene expression databases

GenevestigatoriO88202.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017454.

Structurei

3D structure databases

ProteinModelPortaliO88202.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati141 – 17030ANK 1Add
BLAST
Repeati396 – 42631ANK 2Add
BLAST
Repeati430 – 45930ANK 3Add
BLAST
Repeati463 – 49230ANK 4Add
BLAST
Repeati530 – 55930ANK 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 350310AsparaginaseAdd
BLAST
Regioni84 – 863Substrate bindingBy similarity
Regioni116 – 1172Substrate bindingBy similarity

Sequence similaritiesi

In the N-terminal section; belongs to the asparaginase 1 family.Curated
Contains 5 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00390000001610.
HOGENOMiHOG000227974.
HOVERGENiHBG079531.
InParanoidiO88202.
KOiK13278.
OrthoDBiEOG7WDN22.
PhylomeDBiO88202.
TreeFamiTF315247.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR006033. AsnASEI.
IPR006034. Asparaginase/glutaminase.
IPR027475. Asparaginase/glutaminase_AS2.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view]
PfamiPF00023. Ank. 2 hits.
PF00710. Asparaginase. 1 hit.
[Graphical view]
PIRSFiPIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSiPR01415. ANKYRIN.
PR00139. ASNGLNASE.
SMARTiSM00248. ANK. 4 hits.
SM00870. Asparaginase. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF53774. SSF53774. 1 hit.
TIGRFAMsiTIGR00519. asnASE_I. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS00917. ASN_GLN_ASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88202-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARATGPEQR LLAIYTGGTI GMRSEGGVLV PGRGLAAVLR TLHMLHDEEY
60 70 80 90 100
ARAHSLPEDT LVLPPASSDQ RIIYKVLECQ PLFDSSDMTI TEWVQIAQTI
110 120 130 140 150
ERHYTQYQGF VVIHGTDTMA FAASVLSFML ENLQKPVILT GAQVPIHELW
160 170 180 190 200
SDGRENLLGA LLMAGQYVIP EVCLFFQNQL FRGNRTTKVD ARRFAAFCSP
210 220 230 240 250
NLPPLATVGA DVTINRELVR KASWKSHLVV HSNMEPDVGL LRLYPGIPAS
260 270 280 290 300
LVRTFLQPPL KGVVMETFGS GNGPTKPDLI QELRAAAERG LIIVNCTHCL
310 320 330 340 350
QGAVTSDYAP GMAMAGAGII SGFDMTSEAA LAKLSYVLGQ PGLSLSDRKK
360 370 380 390 400
LLAKDLRGEM TLPTTDDLLG DDMLGCRATW LLSMNGSQDA DAMKDVLLPG
410 420 430 440 450
LALAAAHAGD LDTLQAFVEL GRDLNLKDYS GQTPLHVAAR RGHASVVAML
460 470 480 490 500
LQKGVDVDAC NEDGQSPLLL AVRGRHQSVI RLLRAAGAHL SPQELEDVGT
510 520 530 540 550
ELCRLASRAD SEGLRAWWQA GADLGQPDYD GHCALQVAEA AGNADVVALL
560
QSLEDRVSAQ PQPH
Length:564
Mass (Da):60,795
Last modified:November 1, 1998 - v1
Checksum:i9DBB2F8FA8B1C477
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti280 – 2801I → L in AAH98655. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB009372 mRNA. Translation: BAA31197.1.
BC098655 mRNA. Translation: AAH98655.1.
RefSeqiNP_653351.1. NM_144750.2.
UniGeneiRn.29979.

Genome annotation databases

EnsembliENSRNOT00000017454; ENSRNOP00000017454; ENSRNOG00000012843.
GeneIDi246266.
KEGGirno:246266.
UCSCiRGD:708388. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB009372 mRNA. Translation: BAA31197.1 .
BC098655 mRNA. Translation: AAH98655.1 .
RefSeqi NP_653351.1. NM_144750.2.
UniGenei Rn.29979.

3D structure databases

ProteinModelPortali O88202.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000017454.

PTM databases

PhosphoSitei O88202.

Proteomic databases

PaxDbi O88202.
PRIDEi O88202.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000017454 ; ENSRNOP00000017454 ; ENSRNOG00000012843 .
GeneIDi 246266.
KEGGi rno:246266.
UCSCi RGD:708388. rat.

Organism-specific databases

CTDi 374569.
RGDi 708388. Aspg.

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00390000001610.
HOGENOMi HOG000227974.
HOVERGENi HBG079531.
InParanoidi O88202.
KOi K13278.
OrthoDBi EOG7WDN22.
PhylomeDBi O88202.
TreeFami TF315247.

Miscellaneous databases

NextBioi 623626.
PROi O88202.

Gene expression databases

Genevestigatori O88202.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR006033. AsnASEI.
IPR006034. Asparaginase/glutaminase.
IPR027475. Asparaginase/glutaminase_AS2.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view ]
Pfami PF00023. Ank. 2 hits.
PF00710. Asparaginase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSi PR01415. ANKYRIN.
PR00139. ASNGLNASE.
SMARTi SM00248. ANK. 4 hits.
SM00870. Asparaginase. 1 hit.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
SSF53774. SSF53774. 1 hit.
TIGRFAMsi TIGR00519. asnASE_I. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS00917. ASN_GLN_ASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of cDNA encoding rat liver 60-kDa lysophospholipase containing an asparaginase-like region and ankyrin repeat."
    Sugimoto H., Odani S., Yamashita S.
    J. Biol. Chem. 273:12536-12542(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 226-233 AND 428-440, TISSUE SPECIFICITY, ENZYME ACTIVITY.
    Tissue: Liver.
  2. "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: Liver.
  3. "Purification, characterization, and inhibition by phosphatidic acid of lysophospholipase transacylase from rat liver."
    Sugimoto H., Yamashita S.
    J. Biol. Chem. 269:6252-6258(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiLPP60_RAT
AccessioniPrimary (citable) accession number: O88202
Secondary accession number(s): Q4G088
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 1998
Last modified: October 1, 2014
This is version 107 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3