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Entry version 141 (12 Aug 2020)
Sequence version 1 (01 Nov 1998)
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Protein

60 kDa lysophospholipase

Gene

Aspg

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities (PubMed:9575212, PubMed:8119970, PubMed:10320809). Can catalyze three types of transacylation reactions: (1) acyl transfer from 1-acyl-sn-glycero-3-phosphocholine (1-acyl-GPC) to the sn-13 positions of glycerol and 2-acylglycerol (sn-1 to -13 transfer), (2) acyl transfer from 1-acyl-GPC to the sn-2 positions of 1-acyl-GPC, 1-acyl-sn-glycero-3-phosphoethanolamine (1-acyl-GPE), and other lysophospholipids (sn-1 to -2 transfer) and (3) acyl transfer from 2-acyl-GPC to the sn-1 position of 2-acyl-GPC and 2-acyl-GPE (sn-2 to -1 transfer) (PubMed:10320809). Mediates the synthesis of 1-arachidonoyl species of phospholipids by transferring the arachidonoyl residue from 2-arachidonoyl lysophospholipid to the sn-1 position of 2-acyl lysophospholipid (PubMed:10320809).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by phosphatidic acid.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=91 µM for 1-palmitoyl-glycerophosphocholine1 Publication
  1. Vmax=12.9 nmol/min/mg enzyme for 1-palmitoyl-glycerophosphocholine1 Publication

pH dependencei

Optimum pH is 6.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei19Acyl-ester intermediatePROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAcyltransferase, Hydrolase, Transferase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-8963693, Aspartate and asparagine metabolism

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000623

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
60 kDa lysophospholipase (EC:3.1.1.53 Publications)
Alternative name(s):
Lysophospholipase-transacylase3 Publications
Including the following 2 domains:
L-asparaginase (EC:3.5.1.11 Publication)
Alternative name(s):
L-asparagine amidohydrolase
1-alkyl-2-acetylglycerophosphocholine esterase (EC:3.1.1.471 Publication)
Alternative name(s):
Platelet-activating factor acetylhydrolase1 Publication
Short name:
PAF acetylhydrolase1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Aspg
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
708388, Aspg

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001710921 – 56460 kDa lysophospholipaseAdd BLAST564

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei478PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O88202

PRoteomics IDEntifications database

More...
PRIDEi
O88202

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O88202

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O88202

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000017454

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
O88202

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini9 – 355Asparaginase/glutaminasePROSITE-ProRule annotationAdd BLAST347
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati141 – 170ANK 1Add BLAST30
Repeati396 – 426ANK 2Add BLAST31
Repeati430 – 459ANK 3Add BLAST30
Repeati463 – 492ANK 4Add BLAST30
Repeati530 – 559ANK 5Add BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni41 – 350AsparaginaseAdd BLAST310
Regioni84 – 86Substrate bindingBy similarity3
Regioni116 – 117Substrate bindingBy similarity2

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the N-terminal section; belongs to the asparaginase 1 family.Curated

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0503, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O88202

KEGG Orthology (KO)

More...
KOi
K13278

Database of Orthologous Groups

More...
OrthoDBi
886725at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O88202

TreeFam database of animal gene trees

More...
TreeFami
TF315247

Family and domain databases

Conserved Domains Database

More...
CDDi
cd08963, L-asparaginase_I, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.20, 1 hit
3.40.50.1170, 1 hit
3.40.50.40, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR006033, AsnA_fam
IPR036152, Asp/glu_Ase-like_sf
IPR006034, Asparaginase/glutaminase-like
IPR027475, Asparaginase/glutaminase_AS2
IPR040919, Asparaginase_C
IPR027473, L-asparaginase_C
IPR041725, L-asparaginase_I
IPR027474, L-asparaginase_N
IPR037152, L-asparaginase_N_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00710, Asparaginase, 1 hit
PF17763, Asparaginase_C, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001220, L-ASNase_gatD, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01415, ANKYRIN
PR00139, ASNGLNASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00248, ANK, 4 hits
SM00870, Asparaginase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48403, SSF48403, 1 hit
SSF53774, SSF53774, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00519, asnASE_I, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 2 hits
PS00917, ASN_GLN_ASE_2, 1 hit
PS51732, ASN_GLN_ASE_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9DBB2F8FA8B1C477
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2JSM2A0A0G2JSM2_RAT
Asparaginase
Aspg LOC246266, rCG_27650
564Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti280I → L in AAH98655 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB009372 mRNA Translation: BAA31197.1
BC098655 mRNA Translation: AAH98655.1

NCBI Reference Sequences

More...
RefSeqi
NP_653351.1, NM_144750.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
246266

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:246266

UCSC genome browser

More...
UCSCi
RGD:708388, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009372 mRNA Translation: BAA31197.1
BC098655 mRNA Translation: AAH98655.1
RefSeqiNP_653351.1, NM_144750.2

3D structure databases

SMRiO88202
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017454

Chemistry databases

SwissLipidsiSLP:000000623

PTM databases

iPTMnetiO88202
PhosphoSitePlusiO88202

Proteomic databases

PaxDbiO88202
PRIDEiO88202

Genome annotation databases

GeneIDi246266
KEGGirno:246266
UCSCiRGD:708388, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
374569
RGDi708388, Aspg

Phylogenomic databases

eggNOGiKOG0503, Eukaryota
InParanoidiO88202
KOiK13278
OrthoDBi886725at2759
PhylomeDBiO88202
TreeFamiTF315247

Enzyme and pathway databases

ReactomeiR-RNO-8963693, Aspartate and asparagine metabolism

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O88202

Family and domain databases

CDDicd08963, L-asparaginase_I, 1 hit
Gene3Di1.25.40.20, 1 hit
3.40.50.1170, 1 hit
3.40.50.40, 1 hit
InterProiView protein in InterPro
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR006033, AsnA_fam
IPR036152, Asp/glu_Ase-like_sf
IPR006034, Asparaginase/glutaminase-like
IPR027475, Asparaginase/glutaminase_AS2
IPR040919, Asparaginase_C
IPR027473, L-asparaginase_C
IPR041725, L-asparaginase_I
IPR027474, L-asparaginase_N
IPR037152, L-asparaginase_N_sf
PfamiView protein in Pfam
PF00710, Asparaginase, 1 hit
PF17763, Asparaginase_C, 1 hit
PIRSFiPIRSF001220, L-ASNase_gatD, 1 hit
PRINTSiPR01415, ANKYRIN
PR00139, ASNGLNASE
SMARTiView protein in SMART
SM00248, ANK, 4 hits
SM00870, Asparaginase, 1 hit
SUPFAMiSSF48403, SSF48403, 1 hit
SSF53774, SSF53774, 1 hit
TIGRFAMsiTIGR00519, asnASE_I, 1 hit
PROSITEiView protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 2 hits
PS00917, ASN_GLN_ASE_2, 1 hit
PS51732, ASN_GLN_ASE_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLPP60_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O88202
Secondary accession number(s): Q4G088
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 1998
Last modified: August 12, 2020
This is version 141 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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