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UniProtKB - Q0TV31 (PHLC_CLOP1)

Entry version 95 (02 Jun 2021)
Sequence version 1 (05 Sep 2006)
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Protein

Phospholipase C

Gene

plc

Organism
Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)
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

Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Constitutes an essential virulence factor in gas gangrene. Binds to eukaryotic membranes where it hydrolyzes both phosphatidylcholine and sphingomyelin. The diacylglycerol produced can activate both the arachidonic acid pathway, leading to modulation of the inflammatory response cascade and thrombosis, and protein kinase C, leading to activation of eukaryotic phospholipases and further membrane damage. Acts on human and mouse erythrocytes, but not on rabbit or horse erythrocytes.

Miscellaneous

Two main forms of alpha-toxin can be purified from C.perfringens; a major form with a pI of 5.48, and a minor form with a pI of 5.6. Both are equally active. Variations seen in PLC activity between different strains may be due to transcriptional regulation.
Mutating residues 303 or 359 of the C.perfringens toxin to match those found in C.bifermentans (301 and 358 respectively) reduces toxicity considerably.

<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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi29Zinc 11
Metal bindingi39Zinc 11
Metal bindingi84Zinc 31
Metal bindingi96Zinc 31
Metal bindingi154Zinc 31
Metal bindingi158Zinc 11
Metal bindingi158Zinc 31
Metal bindingi164Zinc 2Curated1
Metal bindingi176Zinc 2Curated1
Metal bindingi180Zinc 2Curated1
Metal bindingi297Calcium 11
Metal bindingi299Calcium 1; via carbonyl oxygen1
Metal bindingi300Calcium 31
Metal bindingi301Calcium 31
Metal bindingi321Calcium 21
Metal bindingi322Calcium 21
Metal bindingi324Calcium 2; via carbonyl oxygen1
Metal bindingi325Calcium 31
Metal bindingi326Calcium 21
Metal bindingi326Calcium 31
Metal bindingi364Calcium 11
Metal bindingi365Calcium 1; via carbonyl oxygen1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionHydrolase, Toxin
Biological processCytolysis, Hemolysis, Virulence
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		CPER195103:G1G5R-44-MONOMER

<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:
Phospholipase C (EC:3.1.4.3)
Short name:
PLC
Alternative name(s):
Alpha-toxin
Hemolysin
Lecithinase
Phosphatidylcholine cholinephosphohydrolase
<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:plc
Synonyms:cpa
Ordered Locus Names:CPF_0042
<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>OrganismiClostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)
<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 identifieri195103 [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 lineageiBacteria › Firmicutes › Clostridia › Eubacteriales › Clostridiaceae › Clostridium ›
<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
  • UP000001823 <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

<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

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 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Vaccination of mice with a fragment (residues 275-398) protects them against a subsequent challenge with purified alpha-toxin.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi278 – 398Missing : Loss of sphingomyelinase, hemolytic activity and lethality. 1 PublicationAdd BLAST121
Mutagenesisi297D → Y: Binds less Ca(2+), small decrease in PLC, sphingomyelinase and myotoxicity, increased hemolytic and cytotoxic activities. 2 Publications1
Mutagenesisi303Y → F or N: Increased dependence of PLC on Ca(2+). Dramatically decreases hemolytic, cytotoxic and myotoxic activities. 1 Publication1
Mutagenesisi321D → S: Reduces affinity for Ca(2+), decreases toxin activity. 1 Publication1
Mutagenesisi333D → G: Decreases toxin activity in vivo and against aggregated substrates in vitro. May destabilize interactions between the N and C-terminal domains. 1 Publication1
Mutagenesisi335Y → F: Dramatically decreases hemolytic and cytotoxic activities. 1 Publication1
Mutagenesisi358K → E: Decreases toxin activity in vivo and against aggregated substrates in vitro. 1 Publication1
Mutagenesisi359Y → F or L: Dramatically decreases hemolytic and cytotoxic activities. 2 Publications1
Mutagenesisi362F → I: Dramatically decreases sphingomyelinase, cytotoxicity and hemolytic and myotoxic activities. 1 Publication1
Mutagenesisi364D → N: Increased dependence of PLC on Ca(2+). Dramatically decreases hemolytic, cytotoxic and myotoxic activities. 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 – 282 PublicationsAdd BLAST28
<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_000025945629 – 398Phospholipase CAdd BLAST370

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		Q0TV31

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		195103.CPF_0042

<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

1398
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		Q0TV31

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q0TV31

<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>Domaini29 – 278Zn-dependent PLCPROSITE-ProRule annotationAdd BLAST250
Domaini284 – 398PLATPROSITE-ProRule annotationAdd BLAST115

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>Regioni275 – 283Linker9

<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

The protein is composed of 2 domains; the N-terminal domain contains the phospholipase C active site (PLC), in a cleft which is also occupied by the 3 zinc ions. The C-terminal domain is a putative phospholipid-recognition domain, which shows structural homology with phospholipid-binding C2-like domains from a range of eukaryotic proteins. The ability to bind membrane phospholipids in a Ca2+ dependent manner and toxicity is conferred by this C-terminal domain, which also contributes to the sphingomyelinase activity.

<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

Belongs to the bacterial zinc-metallophospholipase C family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG5033QPJ, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_690198_0_0_9

Identification of Orthologs from Complete Genome Data

More...OMAi		DHFWDPD

Database of Orthologous Groups

More...OrthoDBi		753730at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.575.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001024, PLAT/LH2_dom
IPR036392, PLAT/LH2_dom_sf
IPR008947, PLipase_C/P1_nuclease_dom_sf
IPR029002, PLPC/GPLD1
IPR001531, Zn_PLipaseC

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01477, PLAT, 1 hit
PF00882, Zn_dep_PLPC, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00479, PRPHPHLPASEC

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00770, Zn_dep_PLPC, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48537, SSF48537, 1 hit
SSF49723, SSF49723, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50095, PLAT, 1 hit
PS00384, PROKAR_ZN_DEPEND_PLPC_1, 1 hit
PS51346, PROKAR_ZN_DEPEND_PLPC_2, 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>Sequencei

<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.

<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 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.

Q0TV31-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKRKICKALI CAALATSLWA GASTKVYAWD GKIDGTGTHA MIVTQGVSIL 
        60         70         80         90        100
ENDLSKNEPE SVRKNLEILK ENMHELQLGS TYPDYDKNAY DLYQDHFWDP 
       110        120        130        140        150
DTDNNFSKDN SWYLAYSIPD TGESQIRKFS ALARYEWQRG NYKQATFYLG 
       160        170        180        190        200
EAMHYFGDID TPYHPANVTA VDSAGHVKFE TFAEERKEQY KINTAGCKTN 
       210        220        230        240        250
EAFYTDILKN KDFNAWSKEY ARGFAKTGKS IYYSHASMSH SWDDWDYAAK 
       260        270        280        290        300
VTLANSQKGT AGYIYRFLHD VSEGNDPSVG KNVKELVAYI STSGEKDAGT 
       310        320        330        340        350
DDYMYFGIKT KDGKTQEWEM DNPGNDFMTG SKDTYTFKLK DENLKIDDIQ 
       360        370        380        390 
NMWIRKRKYT AFSDAYKPEN IKIIANGKVV VDKDINEWIS GNSTYNIK
Length:398
Mass (Da):45,476
Last modified:September 5, 2006 - 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:i4A36E7E2A7139724
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 conflicti17S → T (PubMed:2536356).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
M24904 Genomic DNA Translation: AAA23272.1
X13608 Genomic DNA Translation: CAA31943.1
CP000246 Genomic DNA Translation: ABG84486.1

Protein sequence database of the Protein Information Resource

More...PIRi		A30565

NCBI Reference Sequences

More...RefSeqi		WP_011590041.1, NC_008261.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		ABG84486; ABG84486; CPF_0042

Database of genes from NCBI RefSeq genomes

More...GeneIDi		29569865

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		cpf:CPF_0042

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24904 Genomic DNA Translation: AAA23272.1
X13608 Genomic DNA Translation: CAA31943.1
CP000246 Genomic DNA Translation: ABG84486.1
PIRiA30565
RefSeqiWP_011590041.1, NC_008261.1

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
1QM6X-ray2.50A/B29-398[»]
1QMDX-ray2.20A/B29-398[»]
2WXTX-ray2.00A29-398[»]
2WXUX-ray1.80A29-398[»]
2WY6X-ray3.20A/B/C29-398[»]
SMRiQ0TV31
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi195103.CPF_0042

Proteomic databases

PRIDEiQ0TV31

Genome annotation databases

EnsemblBacteriaiABG84486; ABG84486; CPF_0042
GeneIDi29569865
KEGGicpf:CPF_0042

Phylogenomic databases

eggNOGiENOG5033QPJ, Bacteria
HOGENOMiCLU_690198_0_0_9
OMAiDHFWDPD
OrthoDBi753730at2

Enzyme and pathway databases

BioCyciCPER195103:G1G5R-44-MONOMER

Miscellaneous databases

EvolutionaryTraceiQ0TV31

Family and domain databases

Gene3Di1.10.575.10, 1 hit
InterProiView protein in InterPro
IPR001024, PLAT/LH2_dom
IPR036392, PLAT/LH2_dom_sf
IPR008947, PLipase_C/P1_nuclease_dom_sf
IPR029002, PLPC/GPLD1
IPR001531, Zn_PLipaseC
PfamiView protein in Pfam
PF01477, PLAT, 1 hit
PF00882, Zn_dep_PLPC, 1 hit
PRINTSiPR00479, PRPHPHLPASEC
SMARTiView protein in SMART
SM00770, Zn_dep_PLPC, 1 hit
SUPFAMiSSF48537, SSF48537, 1 hit
SSF49723, SSF49723, 1 hit
PROSITEiView protein in PROSITE
PS50095, PLAT, 1 hit
PS00384, PROKAR_ZN_DEPEND_PLPC_1, 1 hit
PS51346, PROKAR_ZN_DEPEND_PLPC_2, 1 hit

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 nameiPHLC_CLOP1
<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: Q0TV31
Secondary accession number(s): P15310
, P94658, Q46246, Q46279, Q46280, Q46281, Q46282, Q57317, Q59303, Q59304, Q59305, Q59313, Q60121
<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: October 31, 2006
Last sequence update: September 5, 2006
Last modified: June 2, 2021
This is version 95 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 programProkaryotic 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

Documents

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