Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 156 (02 Dec 2020)
Sequence version 2 (31 Oct 2012)
Previous versions | rss
Add a publicationFeedback
Protein

85/88 kDa calcium-independent phospholipase A2

Gene

Pla2g6

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

Calcium-independent phospholipase involved in phospholipid remodeling with implications in cellular membrane homeostasis, mitochondrial integrity and signal transduction. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 and A2 activity respectively), producing lysophospholipids that are used in deacylation-reacylation cycles (PubMed:18937505, PubMed:9111008). Hydrolyzes both saturated and unsaturated long fatty acyl chains in various glycerophospholipid classes such as phosphatidylcholines, phosphatidylethanolamines and phosphatidates, with a preference for hydrolysis at sn-2 position. Can further hydrolyze lysophospholipids carrying saturated fatty acyl chains (lysophospholipase activity) (PubMed:18937505). Upon oxidative stress, contributes to remodeling of mitochondrial phospholipids in pancreatic beta cells, in a repair mechanism to reduce oxidized lipid content (PubMed:24648512). Preferentially hydrolyzes oxidized polyunsaturated fatty acyl chains from cardiolipins, yielding monolysocardiolipins that can be reacylated with unoxidized fatty acyls to regenerate native cardiolipin species. Hydrolyzes oxidized glycerophosphoethanolamines present in pancreatic islets, releasing oxidized polyunsaturated fatty acids such as hydroxyeicosatetraenoates (HETEs) (PubMed:24648512). Has thioesterase activity toward fatty-acyl CoA releasing CoA-SH known to facilitate fatty acid transport and beta-oxidation in mitochondria particularly in skeletal muscle (PubMed:18937505). Plays a role in regulation of membrane dynamics and homeostasis. Selectively hydrolyzes sn-2 arachidonoyl group in plasmalogen phospholipids, structural components of lipid rafts and myelin (By similarity). Regulates F-actin polymerization at the pseudopods, which is required for both speed and directionality of MCP1/CCL2-induced monocyte chemotaxis (By similarity). Targets membrane phospholipids to produce potent lipid signaling messengers. Generates lysophosphatidate (LPA, 1-acyl-glycerol-3-phosphate), which acts via G-protein receptors in various cell types. Has phospholipase A2 activity toward platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), likely playing a role in inactivation of this potent proinflammatory signaling lipid (By similarity). In response to glucose, amplifies calcium influx in pancreatic beta cells to promote INS secretion (By similarity).By similarity3 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

Activated by ATP (PubMed:18937505, PubMed:9111008). Inhibited by calcium-activated calmodulin (PubMed:11118454, PubMed:18937505). Inhibited by bromoenol lactone (BEL) (PubMed:18937505).3 Publications

<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>pH dependencei

Optimum pH is 7.1 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 sitei520NucleophilePROSITE-ProRule annotation1
Active sitei653Proton acceptorPROSITE-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 functionCalmodulin-binding, Hydrolase
Biological processChemotaxis, Lipid metabolism, Phospholipid metabolism

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1482788, Acyl chain remodelling of PC
R-RNO-1482839, Acyl chain remodelling of PE
R-RNO-2029485, Role of phospholipids in phagocytosis
R-RNO-6811436, COPI-independent Golgi-to-ER retrograde traffic

<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:
85/88 kDa calcium-independent phospholipase A2 (EC:3.1.1.42 Publications)
Short name:
CaI-PLA2
Alternative name(s):
2-lysophosphatidylcholine acylhydrolase (EC:3.1.1.5By similarity)
Group VI phospholipase A2
Short name:
GVI PLA2
Intracellular membrane-associated calcium-independent phospholipase A2 beta
Short name:
iPLA2-beta
Palmitoyl-CoA hydrolase (EC:3.1.2.21 Publication)
Patatin-like phospholipase domain-containing protein 9
Short name:
PNPLA9
<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:Pla2g6
Synonyms:Pnpla9
<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)
<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: Chromosome 7
  • UP000234681 Componentsi: Chromosome 7, Unassembled WGS sequence

Organism-specific databases

Rat genome database

More...
RGDi
628867, Pla2g6

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei481 – 501HelicalSequence analysisAdd BLAST21
Transmembranei512 – 532HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Membrane, Mitochondrion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1075318

<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_00000670391 – 80785/88 kDa calcium-independent phospholipase A2Add BLAST807

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 residuei13PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P97570

PRoteomics IDEntifications database

More...
PRIDEi
P97570

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P97570

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

More...
PhosphoSitePlusi
P97570

<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 in pancreatic beta-cells (PubMed:9111008). Expressed in skeletal muscle (at protein level) (PubMed:18937505).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000012295, Expressed in testis and 22 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P97570, RN

<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

Homodimer formed by catalytic domains tightly interacting through a large hydrophobic interface. The contact area involves 3 alpha helices, several loops and a part of the beta sheet from each monomer. Both active sites of the dimer are in close proximity adopting an open conformation that provide sufficient space for phospholipid access and favoring cooperativity in deacylation-reacylation reactions. Each monomer has 9 ankyrin repeats stacked side-by-side in an elongated structure oriented outwards from the catalytic core.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P97570, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000017104

<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
P97570

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 '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>Repeati120 – 147ANK 1By similarityAdd BLAST28
Repeati151 – 181ANK 1Sequence analysisAdd BLAST31
Repeati185 – 215ANK 2Sequence analysisAdd BLAST31
Repeati219 – 248ANK 3Sequence analysisAdd BLAST30
Repeati251 – 281ANK 4Sequence analysisAdd BLAST31
Repeati286 – 312ANK 5Sequence analysisAdd BLAST27
Repeati316 – 345ANK 6Sequence analysisAdd BLAST30
Repeati349 – 378ANK 7Sequence analysisAdd BLAST30
Repeati382 – 403ANK 9By similarityAdd BLAST22
<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>Domaini482 – 666PNPLAPROSITE-ProRule annotationAdd BLAST185

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>Regioni678 – 687Calmodulin-binding (1-9-14 motif)1 Publication10
Regioni749 – 760Calmodulin-binding (IQ motif)1 PublicationAdd BLAST12

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi486 – 491GXGXXGPROSITE-ProRule annotation6
Motifi518 – 522GXSXGPROSITE-ProRule annotation5
Motifi653 – 655DGA/GPROSITE-ProRule annotation3

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Has two putative calmodulin binding domains, the 1-9-14 and IQ motifs (PubMed:11118454). One calmodulin molecule interacts with PLA2G6 dimer, likely through 1-9-14 motif on each monomer (By similarity). Binds calmodulin in a calcium-dependent way (PubMed:11118454).By similarity1 Publication

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0513, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000158756

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_010817_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P97570

Identification of Orthologs from Complete Genome Data

More...
OMAi
DSWTRPY

Database of Orthologous Groups

More...
OrthoDBi
841851at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P97570

TreeFam database of animal gene trees

More...
TreeFami
TF319230

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.20, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016035, Acyl_Trfase/lysoPLipase
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR002641, PNPLA_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12796, Ank_2, 1 hit
PF01734, Patatin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01415, ANKYRIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00248, ANK, 6 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48403, SSF48403, 1 hit
SSF52151, SSF52151, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 4 hits
PS51635, PNPLA, 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>Sequences (2)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 describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform Long (identifier: P97570-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MQFFGRLVNT LSSVTNLFSN PFRVKEVSLA DYASSERVRE EGQLILLQNA
60 70 80 90 100
SNRTWDCVLV SPRNPQSGFR LFQLESEADA LVNFQQYSSQ LPPFYESSVQ
110 120 130 140 150
VLHVEVLQHL TDLIRNHPSW TVTHLAVELG IRECFHHSRI ISCANSTENE
160 170 180 190 200
EGCTPLHLAC RKGDSEILVE LVQYCHAQMD VTDNKGETAF HYAVQGDNPQ
210 220 230 240 250
VLQLLGKNAS AGLNQVNNQG LTPLHLACQM GKQEMVRVLL LCNARCNIMG
260 270 280 290 300
PGGFPIHTAM KFSQKGCAEM IISMDSNQIH SKDPRYGASP LHWAKNAEMA
310 320 330 340 350
RMLLKRGCDV DSTSASGNTA LHVAVTRNRF DCVMVLLTYG ANAGARGEHG
360 370 380 390 400
NTPLHLAMSK DNMEMVKALI VFGAEVDTPN DFGETPAFIA SKISKLITRK
410 420 430 440 450
ALLTLLKTVG ADYHFPFIQG VSTEQSSAAG PHPFFSLDRT QPPTISLNNL
460 470 480 490 500
ELQDLMPVSR ARKPAFILSS MRDEKRSHDH LLCLDGGGVK GLVIIQLLIA
510 520 530 540 550
IEKASGVATK DLFDWVAGTS TGGILALAIL HSKSMAYMRG VYFRMKDEVF
560 570 580 590 600
RGSRPYESGP LEEFLKREFG EHTKMTDVKK PKVMLTGTLS DRQPAELHLF
610 620 630 640 650
RNYDAPEAVR EPRCTPNINL KPPTQPADQL VWRAARSSGA APTYFRPNGR
660 670 680 690 700
FLDGGLLANN PTLDAMTEIH EYNQDMIRKG QGNKVKKLSI VVSLGTGKSP
710 720 730 740 750
QVPVTCVDVF RPSNPWELAK TVFGAKELGK MVVDCCTDPD GRAVDRARAW
760 770 780 790 800
CEMVGIQYFR LNPQLGSDIM LDEVSDAVLV NALWETEVYI YEHREEFQKL

VQLLLSP
Length:807
Mass (Da):89,556
Last modified:October 31, 2012 - v2
<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:i1B9018AE1B2D252F
GO
Isoform Short (identifier: P97570-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     396-451: LITRKALLTLLKTVGADYHFPFIQGVSTEQSSAAGPHPFFSLDRTQPPTISLNNLE → Q

Show »
Length:752
Mass (Da):83,562
Checksum:iE622616FB108FDA0
GO

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 conflicti24V → A in AAC53136 (PubMed:9111008).Curated1
Sequence conflicti58V → D in AAC53136 (PubMed:9111008).Curated1
Sequence conflicti68G → D in AAC53136 (PubMed:9111008).Curated1
Sequence conflicti80A → V in AAC53136 (PubMed:9111008).Curated1
Sequence conflicti99V → E in AAC53136 (PubMed:9111008).Curated1
Sequence conflicti109Missing in AAC53136 (PubMed:9111008).Curated1
Sequence conflicti142S → T in AAC53136 (PubMed:9111008).Curated1
Sequence conflicti477S → T in AAC53136 (PubMed:9111008).Curated1
Sequence conflicti793H → Y in AAC53136 (PubMed:9111008).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_044365396 – 451LITRK…LNNLE → Q in isoform Short. 1 PublicationAdd BLAST56

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
U51898 mRNA Translation: AAC53136.1
AABR06052011 Genomic DNA No translation available.
CH473950 Genomic DNA Translation: EDM15808.1
CH473950 Genomic DNA Translation: EDM15809.1
BC081916 mRNA Translation: AAH81916.1

NCBI Reference Sequences

More...
RefSeqi
NP_001005560.1, NM_001005560.1 [P97570-1]
NP_001257725.1, NM_001270796.1 [P97570-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000016827; ENSRNOP00000016827; ENSRNOG00000012295 [P97570-2]
ENSRNOT00000017108; ENSRNOP00000017104; ENSRNOG00000012295 [P97570-1]
ENSRNOT00000087344; ENSRNOP00000072104; ENSRNOG00000012295 [P97570-1]
ENSRNOT00000090565; ENSRNOP00000075311; ENSRNOG00000012295 [P97570-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
360426

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:360426

UCSC genome browser

More...
UCSCi
RGD:628867, rat [P97570-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
U51898 mRNA Translation: AAC53136.1
AABR06052011 Genomic DNA No translation available.
CH473950 Genomic DNA Translation: EDM15808.1
CH473950 Genomic DNA Translation: EDM15809.1
BC081916 mRNA Translation: AAH81916.1
RefSeqiNP_001005560.1, NM_001005560.1 [P97570-1]
NP_001257725.1, NM_001270796.1 [P97570-2]

3D structure databases

SMRiP97570
ModBaseiSearch...

Protein-protein interaction databases

IntActiP97570, 1 interactor
STRINGi10116.ENSRNOP00000017104

Chemistry databases

ChEMBLiCHEMBL1075318

PTM databases

iPTMnetiP97570
PhosphoSitePlusiP97570

Proteomic databases

PaxDbiP97570
PRIDEiP97570

Genome annotation databases

EnsembliENSRNOT00000016827; ENSRNOP00000016827; ENSRNOG00000012295 [P97570-2]
ENSRNOT00000017108; ENSRNOP00000017104; ENSRNOG00000012295 [P97570-1]
ENSRNOT00000087344; ENSRNOP00000072104; ENSRNOG00000012295 [P97570-1]
ENSRNOT00000090565; ENSRNOP00000075311; ENSRNOG00000012295 [P97570-2]
GeneIDi360426
KEGGirno:360426
UCSCiRGD:628867, rat [P97570-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8398
RGDi628867, Pla2g6

Phylogenomic databases

eggNOGiKOG0513, Eukaryota
GeneTreeiENSGT00940000158756
HOGENOMiCLU_010817_0_0_1
InParanoidiP97570
OMAiDSWTRPY
OrthoDBi841851at2759
PhylomeDBiP97570
TreeFamiTF319230

Enzyme and pathway databases

ReactomeiR-RNO-1482788, Acyl chain remodelling of PC
R-RNO-1482839, Acyl chain remodelling of PE
R-RNO-2029485, Role of phospholipids in phagocytosis
R-RNO-6811436, COPI-independent Golgi-to-ER retrograde traffic

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P97570

Gene expression databases

BgeeiENSRNOG00000012295, Expressed in testis and 22 other tissues
GenevisibleiP97570, RN

Family and domain databases

Gene3Di1.25.40.20, 2 hits
InterProiView protein in InterPro
IPR016035, Acyl_Trfase/lysoPLipase
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR002641, PNPLA_dom
PfamiView protein in Pfam
PF12796, Ank_2, 1 hit
PF01734, Patatin, 1 hit
PRINTSiPR01415, ANKYRIN
SMARTiView protein in SMART
SM00248, ANK, 6 hits
SUPFAMiSSF48403, SSF48403, 1 hit
SSF52151, SSF52151, 1 hit
PROSITEiView protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 4 hits
PS51635, PNPLA, 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 nameiPLPL9_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: P97570
Secondary accession number(s): G3V7M8, Q66HD1
<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: May 30, 2000
Last sequence update: October 31, 2012
Last modified: December 2, 2020
This is version 156 of the entry and version 2 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

Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again