PRKX

Functionⁱ

Serine/threonine protein kinase regulated by and mediating cAMP signaling in cells. Acts through phosphorylation of downstream targets that may include CREB, SMAD6 and PKD1 and has multiple functions in cellular differentiation and epithelial morphogenesis. Regulates myeloid cell differentiation through SMAD6 phosphorylation. Involved in nephrogenesis by stimulating renal epithelial cell migration and tubulogenesis. Also involved in angiogenesis through stimulation of endothelial cell proliferation, migration and vascular-like structure formation.7 Publications

Catalytic activityⁱ

ATP + a protein = ADP + a phosphoprotein.2 Publications

Enzyme regulationⁱ

Binding of cAMP to the PRKAR1A or PRKAR1B regulatory subunits induces dissociation of the holoenzyme heterotetramer. The released monomeric PRKX is then active and able to phosphorylate its substrates.3 Publications

Kineticsⁱ

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	78	ATPPROSITE-ProRule annotation		1
Active siteⁱ	172	Proton acceptorPROSITE-ProRule annotation		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	55 – 63	ATPPROSITE-ProRule annotation		9

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW
cAMP-dependent protein kinase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 10026146
- 17980165

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

angiogenesis
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21684272
cell adhesion
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21684272
cell-substrate adhesion
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 16491121
endothelial cell migration
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21684272
endothelial cell proliferation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21684272
epithelial tube morphogenesis
Source: UniProtKB
Inferred from direct assayⁱ
- 17980165
kidney morphogenesis
Source: UniProtKB
Inferred from direct assayⁱ
- 17980165
myeloid cell differentiation
Source: UniProtKB
Inferred from direct assayⁱ
- 9860982
peptidyl-serine phosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 16491121
protein autophosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 10026146
- 16491121
regulation of cell adhesion
Source: UniProtKB
Inferred from direct assayⁱ
- 17980165
regulation of cell migration
Source: UniProtKB
Inferred from direct assayⁱ
- 17980165
regulation of epithelial cell differentiation involved in kidney development
Source: UniProtKB
Inferred from direct assayⁱ
- 17980165

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase
Biological process	Angiogenesis, Differentiation
Ligand	ATP-binding, cAMP, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	2.7.11.1 2681
SABIO-RKⁱ	P51817
SignaLinkⁱ	P51817
SIGNORⁱ	P51817

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: cAMP-dependent protein kinase catalytic subunit PRKX (EC:2.7.11.1) Short name: PrKX Short name: Protein kinase X Short name: Protein kinase X-linked Short name: Serine/threonine-protein kinase PRKX Alternative name(s): Protein kinase PKX1
Gene namesⁱ	Name:PRKX Synonyms:PKX1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome X

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000183943.5
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9441 PRKX
MIMⁱ	300083 gene
neXtProtⁱ	NX_P51817

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

A chromosomal aberration involving PRKX is a cause of sex reversal disorder. Translocation t(X;Y)(p22;p11) with PRKY. Chromosomal translocations proximal to PRKY account for about 30% of the cases of sex reversal disorder in XX males and XY females.

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	78	K → R: Loss of function. 1 Publication	1
Mutagenesisⁱ	93	H → Q: Constitutive kinase activity; when associated with R-202. 1 Publication	1
Mutagenesisⁱ	202	W → R: Constitutive kinase activity; when associated with Q-93. 1 Publication	1
Mutagenesisⁱ	283	R → L: Increases the affinity for PRKAR2A and PRKAR2B. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5613
Open Targets More...OpenTargetsⁱ	ENSG00000183943
PharmGKBⁱ	PA33786

Chemistry databases

ChEMBLⁱ	CHEMBL5818
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2175

Polymorphism and mutation databases

BioMutaⁱ	PRKX
DMDMⁱ	1709648

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000086582	1 – 358	cAMP-dependent protein kinase catalytic subunit PRKXAdd BLAST		358

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	1	N-acetylmethionineCombined sources		1
Modified residueⁱ	203	PhosphothreonineBy similarity		1

Post-translational modificationⁱ

Phosphorylated; autophosphorylates in vitro.

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	P51817
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P51817
PaxDbⁱ	P51817
PeptideAtlas More...PeptideAtlasⁱ	P51817
PRIDEⁱ	P51817
ProteomicsDBⁱ	56426

PTM databases

iPTMnetⁱ	P51817
PhosphoSitePlusⁱ	P51817

Expressionⁱ

Tissue specificityⁱ

Widely expressed (at protein level). Specifically expressed in blood by macrophages and granulocytes according to PubMed:9860982.4 Publications

Developmental stageⁱ

Expression is developmentally regulated being high and specific in a wide range of developing tissues including liver, kidney, brain and pancreas (at protein level).3 Publications

Inductionⁱ

Up-regulated by phorbol 12-myristate 13-acetate (PMA).2 Publications

Gene expression databases

Bgeeⁱ	ENSG00000183943
CleanExⁱ	HS_PRKX
ExpressionAtlasⁱ	P51817 baseline and differential
Genevisibleⁱ	P51817 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA015324

HPAⁱ

HPA015324

Interactionⁱ

Subunit structureⁱ

Like other cAMP-dependent protein kinases, the inactive holoenzyme is probably composed of 2 PRKX catalytic subunits and a dimer of regulatory subunits. Interacts (cAMP-dependent) specifically with the regulatory subunits PRKAR1A and PRKAR1B. Compared to other cAMP-dependent serine/threonine protein kinases, does not interact with the 2 other PKA regulatory subunits PRKAR2A and PRKAR2B. Interacts with cAMP-dependent protein kinase inhibitor/PKI proteins; inhibits PRKX. Interacts with GPKOW. Interacts with SMAD6. Interacts with PKD1; involved in differentiation and controlled morphogenesis of the kidney. Interacts with PIN1 (via WW domain).5 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
GPKOW	Q92917	2	EBI-4302903,EBI-746309
HSP90AB1	P08238	2	EBI-4302903,EBI-352572
PRKAR1A	P10644	2	EBI-4302903,EBI-476431
SMAD6	O43541	5	EBI-4302903,EBI-976374

Show more details

Protein-protein interaction databases

BioGridⁱ	111599, 8 interactors
IntActⁱ	P51817, 6 interactors
STRINGⁱ	9606.ENSP00000262848

Chemistry databases

BindingDBⁱ

P51817

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P51817
SMRⁱ	P51817
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	49 – 303	Protein kinasePROSITE-ProRule annotationAdd BLAST		255
Domainⁱ	304 – 358	AGC-kinase C-terminalAdd BLAST		55

Sequence similaritiesⁱ

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cAMP subfamily.Curated

Phylogenomic databases

eggNOGⁱ	KOG0616 Eukaryota ENOG410XPQQ LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00810000125385
HOGENOMⁱ	HOG000233033
HOVERGENⁱ	HBG108317
InParanoidⁱ	P51817
KEGG Orthology (KO) More...KOⁱ	K19584
OMAⁱ	WWACGIL
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G10O8
PhylomeDBⁱ	P51817
TreeFamⁱ	TF313399

Family and domain databases

InterProⁱ	View protein in InterPro IPR000961 AGC-kinase_C IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR008271 Ser/Thr_kinase_AS
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00069 Pkinase, 1 hit
SMARTⁱ	View protein in SMART SM00133 S_TK_X, 1 hit SM00220 S_TKc, 1 hit
SUPFAMⁱ	SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS51285 AGC_KINASE_CTER, 1 hit PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P51817-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MEAPGLAQAA AAESDSRKVA EETPDGAPAL CPSPEALSPE PPVYSLQDFD 
        60         70         80         90        100
TLATVGTGTF GRVHLVKEKT AKHFFALKVM SIPDVIRLKQ EQHVHNEKSV 
       110        120        130        140        150
LKEVSHPFLI RLFWTWHDER FLYMLMEYVP GGELFSYLRN RGRFSSTTGL 
       160        170        180        190        200
FYSAEIICAI EYLHSKEIVY RDLKPENILL DRDGHIKLTD FGFAKKLVDR 
       210        220        230        240        250
TWTLCGTPEY LAPEVIQSKG HGRAVDWWAL GILIFEMLSG FPPFFDDNPF 
       260        270        280        290        300
GIYQKILAGK IDFPRHLDFH VKDLIKKLLV VDRTRRLGNM KNGANDVKHH 
       310        320        330        340        350
RWFRSVDWEA VPQRKLKPPI VPKIAGDGDT SNFETYPEND WDTAAPVPQK 

DLEIFKNF

Length:358

Mass (Da):40,896

Last modified:October 1, 1996 - v1

Checksum:ⁱB603834E3541CB56

GO

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_061744	43	V → A. Corresponds to variant dbSNP:rs3752362Ensembl.		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X85545 mRNA Translation: CAA59733.1 BC041073 mRNA Translation: AAH41073.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS14125.1
PIRⁱ	I38121
NCBI Reference Sequences More...RefSeqⁱ	NP_005035.1, NM_005044.4
UniGeneⁱ	Hs.390788

Genome annotation databases

Ensemblⁱ	ENST00000262848; ENSP00000262848; ENSG00000183943
GeneIDⁱ	5613
KEGGⁱ	hsa:5613
UCSC genome browser More...UCSCⁱ	uc010nde.4 human

Keywords - Coding sequence diversityⁱ

Chromosomal rearrangement, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length
P51817	Protein kinase, X-linked, isoform CRA_b		HUMAN		358
cAMP-dependent protein kinase catalytic subunit PRKX		CALJA		359
PRKX isoform 1		PANTR		358
Protein kinase, X-linked		GORGO		358
Serine/threonine-protein kinase PRKX		MACMU		358
+26

Protein	Similar proteins		Species	Score	Length
P51817	Protein kinase, X-linked, isoform CRA_b		HUMAN		358
cAMP-dependent protein kinase catalytic subunit PRKX		CALJA		359
Protein kinase, X-linked		PANTR		358
Protein kinase, X-linked		PAPAN		358
Serine/threonine-protein kinase PRKX		MACMU		358
+326

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X85545 mRNA Translation: CAA59733.1 BC041073 mRNA Translation: AAH41073.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS14125.1
PIRⁱ	I38121
NCBI Reference Sequences More...RefSeqⁱ	NP_005035.1, NM_005044.4
UniGeneⁱ	Hs.390788

3D structure databases

ProteinModelPortalⁱ	P51817
SMRⁱ	P51817
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	111599, 8 interactors
IntActⁱ	P51817, 6 interactors
STRINGⁱ	9606.ENSP00000262848

Chemistry databases

BindingDBⁱ	P51817
ChEMBLⁱ	CHEMBL5818
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2175

PTM databases

iPTMnetⁱ	P51817
PhosphoSitePlusⁱ	P51817

Polymorphism and mutation databases

BioMutaⁱ	PRKX
DMDMⁱ	1709648

Proteomic databases

EPDⁱ	P51817
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P51817
PaxDbⁱ	P51817
PeptideAtlas More...PeptideAtlasⁱ	P51817
PRIDEⁱ	P51817
ProteomicsDBⁱ	56426

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	5613
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000262848; ENSP00000262848; ENSG00000183943
GeneIDⁱ	5613
KEGGⁱ	hsa:5613
UCSC genome browser More...UCSCⁱ	uc010nde.4 human

Organism-specific databases

CTDⁱ	5613
DisGeNET More...DisGeNETⁱ	5613
EuPathDBⁱ	HostDB:ENSG00000183943.5
GeneCardsⁱ	PRKX
H-InvDBⁱ	HIX0202211
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9441 PRKX
Human Protein Atlas More...HPAⁱ	HPA015324
MIMⁱ	300083 gene
neXtProtⁱ	NX_P51817
Open Targets More...OpenTargetsⁱ	ENSG00000183943
PharmGKBⁱ	PA33786
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0616 Eukaryota ENOG410XPQQ LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00810000125385
HOGENOMⁱ	HOG000233033
HOVERGENⁱ	HBG108317
InParanoidⁱ	P51817
KEGG Orthology (KO) More...KOⁱ	K19584
OMAⁱ	WWACGIL
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G10O8
PhylomeDBⁱ	P51817
TreeFamⁱ	TF313399

Enzyme and pathway databases

BRENDAⁱ	2.7.11.1 2681
SABIO-RKⁱ	P51817
SignaLinkⁱ	P51817
SIGNORⁱ	P51817

Miscellaneous databases

GenomeRNAiⁱ	5613
Protein Ontology More...PROⁱ	PR:P51817
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000183943
CleanExⁱ	HS_PRKX
ExpressionAtlasⁱ	P51817 baseline and differential
Genevisibleⁱ	P51817 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR000961 AGC-kinase_C IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR008271 Ser/Thr_kinase_AS
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00069 Pkinase, 1 hit
SMARTⁱ	View protein in SMART SM00133 S_TK_X, 1 hit SM00220 S_TKc, 1 hit
SUPFAMⁱ	SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS51285 AGC_KINASE_CTER, 1 hit PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PRKX_HUMAN
Accessionⁱ	P51817Primary (citable) accession number: P51817
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
	Last sequence update:	October 1, 1996
	Last modified:	July 18, 2018
	This is version 162 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

Human chromosome X
Human chromosome X: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Human and mouse protein kinases
Human and mouse protein kinases: classification and index
SIMILARITY comments
Index of protein domains and families

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UniProtKB - P51817 (PRKX_HUMAN)

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cAMP-dependent protein kinase catalytic subunit PRKX

Select a section on the left to see content.

<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

<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

<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

Sites

Regions

<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

<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 - Biological processi

Enzyme and pathway databases

<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

Organism-specific databases

<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

Nucleus

Other locations

Nucleus

Other locations

<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

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<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

Amino acid modifications

Proteomic databases

PTM databases

<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

Gene expression databases

Organism-specific databases

<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

Chemistry databases

<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

<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

<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

Phylogenomic databases

Family and domain databases

Natural variant

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<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 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

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Functionⁱ

Enzyme regulationⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ