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 108 (13 Nov 2019)
Sequence version 1 (01 Nov 1988)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Phospholipase A2 homolog crotoxin acid subunit CA

Gene
N/A
Organism
Crotalus durissus terrificus (South American rattlesnake)
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

Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission. It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non-enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4). The complex acts by binding to a specific 48-kDa protein (R48/CAPT) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit (PubMed:12657321). At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor. In addition to neurotoxicity, crotoxin has been found to exert myotoxicity, nephrotoxicity, and cardiovascular toxicity (PubMed:20109480). Moreover, anti-inflammatory, immunomodulatory, anti-tumor and analgesic effects of crotoxin have also been reported (PubMed:20109480).2 Publications
CAalpha-CAbeta-CAgamma: The acidic subunit of crotoxin (CA) is a heterotrimer of three disulfide-linked chains generated by post-translational maturation of a PLA2-like precursor. CA has no PLA2 activity and is not neurotoxic by itself, but plays several important functions in the crotoxin complex by increasing the lethal potency of the uncomplexed CB subunit. It acts by physically occluding the hydrophobic interfacial binding surface (IBS) of CB (PubMed:21787789 and PubMed:21787789). This effect decreases the adsorption of CB to phospholipid membranes, targeting the crotoxin complex to reach the specific presynaptic receptor (R48) at the neuromuscular junction. It also prevents the formation of the reactive CB dimer. Moreover, the CA subunit inhibits the catalytic activity by partially masking the catalytic site of CB (PubMed:21787789) and inhibits its anticoagulant activity.1 Publication
CAgamma: Crotalphine corresponds to the gamma chain of the acid subunit of crotoxin. It has been found in the venom as a monomer and is stabilized by one disulfide bond (Cys-131 and Cys-138) (PubMed:18495297). This peptide induces potent antinociceptive effects in neuropathic pain by acting at peripheral opioid receptors (OPRD1, OPRK1, OPRL1 or OPRM1) (PubMed:18703042).2 Publications

Miscellaneous

The crotoxin heterodimer is inhibited by the crotoxin inhibitor from Crotalus serum (CICS). CICS neutralizes the lethal potency of crotoxin and inhibits its PLA2 activity. CICS only binds tightly to the CB subunit and induces the dissociation of the heterodimer (By similarity). Tested on the CA2-CBd heterodimer (PubMed:10903514).By similarity1 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=0.05 µM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (class 2 heterodimer CA2-CBa2)1 Publication
  2. KM=0.05 µM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (class 2 heterodimer CA3-CBa2)1 Publication
  3. KM=0.3 µM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (class 2 heterodimer CA2-CBb)1 Publication
  4. KM=0.2 µM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (class 2 heterodimer CA3-CBb)1 Publication
  5. KM=0.22 µM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (class 2 heterodimer CA2-CBc)1 Publication
  6. KM=0.2 µM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (class 2 heterodimer CA3-CBc)1 Publication
  7. KM=0.35 µM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (class 2 heterodimer CA2-CBd)1 Publication
  8. KM=0.3 µM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (class 2 heterodimer CA3-CBd)1 Publication
  1. Vmax=25 µmol/min/mg enzyme (class 2 heterodimer CA2-CBa2)1 Publication
  2. Vmax=24 µmol/min/mg enzyme (class 2 heterodimer CA3-CBa2)1 Publication
  3. Vmax=10 µmol/min/mg enzyme (class 2 heterodimer CA2-CBb)1 Publication
  4. Vmax=9 µmol/min/mg enzyme (class 2 heterodimer CA3-CBb)1 Publication
  5. Vmax=7 µmol/min/mg enzyme (class 2 heterodimer CA2-CBc)1 Publication
  6. Vmax=6.6 µmol/min/mg enzyme (class 2 heterodimer CA3-CBc)1 Publication
  7. Vmax=4.6 µmol/min/mg enzyme (class 2 heterodimer CA2-CBd)1 Publication
  8. Vmax=4 µmol/min/mg enzyme (class 2 heterodimer CA3-CBd)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei43Binds Val-18 of CBb1 Publication1
Sitei45Binds Asn-16 of CBb1 Publication1
Sitei45Binds Val-18 of CBb1 Publication1
Sitei49Binds Arg-14 of CBb1 Publication1
Sitei93Binds Gly-31 of CBb1 Publication1
Sitei95Binds Trp-61 of CA2, important for stability (Asp-89)1 Publication1
Sitei105Binds Trp-30 of CA2, important for stability (Asp-99)1 Publication1

<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 functionG-protein coupled receptor impairing toxin, Neurotoxin, Presynaptic neurotoxin, Toxin

<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_and_taxonomy_section">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:
Phospholipase A2 homolog crotoxin acid subunit CA
Short name:
CTX subunit CA
Alternative name(s):
Crotapotin
Cleaved into the following 5 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiCrotalus durissus terrificus (South American rattlesnake)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri8732 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCrotalus

<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

Keywords - Cellular componenti

Secreted

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the lethal dose (LD), paralytic dose (PD), effect dose (ED) or lethal concentration (LC) of a protein toxin.<p><a href='/help/toxic_dose' target='_top'>More...</a></p>Toxic dosei

In class 2 heterodimer CA2-CBa2, LD50 is 420 µg/kg by intravenous injection into mice.1 Publication
In class 2 heterodimer CA2-CBa2, LD50 is 650 µg/kg by subcutaneous injection into mice.1 Publication
In class 2 heterodimer CA3-CBa2, LD50 is 450 µg/kg by intravenous injection into mice.1 Publication
In class 1 heterodimer CA2-CBb, LD50 is 110 µg/kg by intravenous injection into mice.1 Publication
In class 1 heterodimer CA3-CBb, LD50 is 95 µg/kg by intravenous injection into mice.1 Publication
In class 1 heterodimer CA2-CBc, LD50 is 80 µg/kg by intravenous injection into mice.1 Publication
In class 1 heterodimer CA3-CBc, LD50 is 110 µg/kg by intravenous injection into mice.1 Publication
In class 1 heterodimer CA2-CBd, LD50 is 70 µg/kg by intravenous injection into mice.1 Publication
In class 1 heterodimer CA2-CBd, LD50 is 150 µg/kg by subcutaneous injection into mice.1 Publication
In class 1 heterodimer CA3-CBd, LD50 is 90 µg/kg by intravenous injection into mice.1 Publication

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>Pharmaceutical usei

Crotoxin (CA-CBc) is under phase II clinical trial as an anti-tumor drug.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi136Q → K: No change in analgesic activity (in crotalphine). 1 Publication1

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 371 PublicationAdd BLAST37
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000042045338 – 78Crotoxin chain alpha CA3Add BLAST41
ChainiPRO_000002285438 – 76Crotoxin chain alpha CA1, CA2 and CA4Add BLAST39
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002285579 – 821 Publication4
ChainiPRO_000042045483 – 118Crotoxin chain beta CA1Add BLAST36
ChainiPRO_000002285684 – 118Crotoxin chain beta CA2, CA3 and CA4Add BLAST35
PropeptideiPRO_0000022857119 – 1246
ChainiPRO_0000022858125 – 138Crotoxin chain gammaAdd BLAST14

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi42 ↔ 131Interchain (between alpha and gamma chains)1 Publication
Disulfide bondi44 ↔ 601 Publication
Disulfide bondi59 ↔ 111Interchain (between alpha and beta chains)1 Publication
Disulfide bondi65 ↔ 138Interchain (between alpha and gamma chains)1 Publication
Disulfide bondi66 ↔ 104Interchain (between alpha and beta chains)1 Publication
Disulfide bondi73 ↔ 97Interchain (between alpha and beta chains)1 Publication
<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 residuei84Pyrrolidone carboxylic acid; in beta chain1 Publication1
Disulfide bondi91 ↔ 1021 Publication
Modified residuei125Pyrrolidone carboxylic acid; in gamma chain1 Publication1

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

<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 by the venom gland.

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterodimer of one of the acidic (CA1, CA2, CA3 or CA4) and one of the basic (CBa1, CBa2, CBb, CBc or CBd) subunits; non-covalently linked. The acidic subunit is non-toxic, without enzymatic activity and comprises 3 peptides that are cross-linked by 5 disulfide bridges. The basic subunit is toxic, has phospholipase A2 activity and is composed of a single chain. Multiple variants of each subunit give different crotoxin complexes that can be subdivided into 2 classes: (1) those of high toxicity, low PLA2 activity (CBb, CBc and CBd linked with high affinity to any CA) and high stability (K(d)=4.5 nM) and (2) those of moderate toxicity, high PLA2 activity (CBa2 linked with low affinity to any CA) and low stability (K(d)=25 nM).

2 Publications

<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

Secondary structure

1138
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P08878

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

<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

Keywords - Domaini

Signal

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00125 PLA2c, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.90.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001211 PLipase_A2
IPR033112 PLipase_A2_Asp_AS
IPR016090 PLipase_A2_dom
IPR036444 PLipase_A2_dom_sf
IPR033113 PLipase_A2_His_AS

The PANTHER Classification System

More...
PANTHERi
PTHR11716 PTHR11716, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00068 Phospholip_A2_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00389 PHPHLIPASEA2

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00085 PA2c, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48619 SSF48619, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00119 PA2_ASP, 1 hit
PS00118 PA2_HIS, 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_length">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P08878-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRALWIVAVL LVGVEGSLVE FETLMMKIAG RSGISYYSSY GCYCGAGGQG
60 70 80 90 100
WPQDASDRCC FEHDCCYAKL TGCDPTTDVY TYRQEDGEIV CGEDDPCGTQ
110 120 130
ICECDKAAAI CFRNSMDTYD YKYLQFSPEN CQGESQPC
Length:138
Mass (Da):15,273
Last modified:November 1, 1988 - 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:iF32771BE091CD888
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 conflicti74D → N AA sequence (PubMed:4084559).Curated1

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 1534.6 Da from positions 125 - 138. Determined by MALDI. Monoisotopic mass.1 Publication

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
X12606 mRNA Translation: CAA31126.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S01392 PSRSAT

<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
X12606 mRNA Translation: CAA31126.1
PIRiS01392 PSRSAT

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3R0LX-ray1.35A38-76[»]
B84-118[»]
C125-138[»]
SMRiP08878
ModBaseiSearch...
PDBe-KBiSearch...

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P08878

Family and domain databases

CDDicd00125 PLA2c, 1 hit
Gene3Di1.20.90.10, 1 hit
InterProiView protein in InterPro
IPR001211 PLipase_A2
IPR033112 PLipase_A2_Asp_AS
IPR016090 PLipase_A2_dom
IPR036444 PLipase_A2_dom_sf
IPR033113 PLipase_A2_His_AS
PANTHERiPTHR11716 PTHR11716, 1 hit
PfamiView protein in Pfam
PF00068 Phospholip_A2_1, 1 hit
PRINTSiPR00389 PHPHLIPASEA2
SMARTiView protein in SMART
SM00085 PA2c, 1 hit
SUPFAMiSSF48619 SSF48619, 1 hit
PROSITEiView protein in PROSITE
PS00119 PA2_ASP, 1 hit
PS00118 PA2_HIS, 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 nameiPA1A_CRODU
<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: P08878
<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_and_isoforms">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, 1988
Last sequence update: November 1, 1988
Last modified: November 13, 2019
This is version 108 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 programAnimal Toxin Annotation Program
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

3D-structure, Direct protein sequencing, Pharmaceutical

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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