Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
0  structures 8  species 0  interactions 301  sequences 8  architectures

Family: Involucrin (PF00904)

Summary: Involucrin repeat

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Involucrin". More...

Involucrin Edit Wikipedia article

IVL
Available structures
PDB Human UniProt search: PDBe RCSB
Identifiers
Aliases IVL
External IDs HomoloGene: 136793 GeneCards: IVL
RNA expression pattern
PBB GE IVL 214599 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005547

n/a

RefSeq (protein)

NP_005538

n/a

Location (UCSC) Chr 1: 152.91 – 152.91 Mb n/a
PubMed search [1] n/a
Wikidata
View/Edit Human
Involucrin of squamous epithelia N-terminus
Identifiers
Symbol Involucrin_N
Pfam PF10583
InterPro IPR019571
Involucrin repeat
Identifiers
Symbol Involucrin
Pfam PF00904
InterPro IPR000354
SCOP 1eu0
SUPERFAMILY 1eu0
Involucrin repeat
Identifiers
Symbol Involucrin2
Pfam PF06994
InterPro IPR009733

Involucrin is a protein component of human skin and in humans is encoded by the IVL gene.[2][3] In binding the protein loricrin, involucrin contributes to the formation of a cell envelope that protects corneocytes in the skin.

Gene

This gene is mapped to 1q21, among calpactin I light chain, trichohyalin, profillaggrin, loricrin, and calcyclin.[3]

Function

Involucrin is a highly reactive, soluble, transglutaminase substrate protein present in keratinocytes of epidermis and other stratified squamous epithelia.[4][5] It first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase thus helping in the formation of an insoluble envelope beneath the plasma membrane functioning as a glutamyl donor during assembly of the cornified envelope.[6]

Involucrin is synthesised in the stratum spinosum and cross linked in the stratum granulosum by the transglutaminase enzyme that makes it highly stable. Thus it provides structural support to the cell, thereby allowing the cell to resist invasion by micro-organisms.[citation needed]

Apigenin, a plant-derived flavanoid that has significant promise as a skin cancer chemopreventive agent, has been found to regulate normal human keratinocyte differentiation by suppressing involucrin, and this is associated with reduced cell proliferation without apoptosis.[7]

Clinical significance

As one of the precursor proteins of the cornified cell envelope, involucrin is markedly increased in inflammatory skin diseases such as psoriasis[8]

Lamellar ichthyosis involves a decrease in expression of involucrin. This decrease could contribute to the altered desquamation process seen in the disease, since the clinical improvement associated with retinoid treatment is accompanied by increased expression of involucrin.[9]

Structure

Involucrin consists of a conserved N-terminal region of about 75 amino acid residues followed by two extremely variable length segments that contain glutamine-rich tandem repeats. The glutamine residues in the tandem repeats are the substrate for the transglutaminase in the cross-linking reaction. The total size of the protein varies from 285 residues (in dog) to 835 residues (in orangutan).[citation needed]

References

  1. ^ "Human PubMed Reference:". 
  2. ^ Eckert RL, Green H (August 1986). "Structure and evolution of the human involucrin gene". Cell. 46 (4): 583–9. doi:10.1016/0092-8674(86)90884-6. PMID 2873896. 
  3. ^ a b "Entrez Gene: IVL involucrin". 
  4. ^ Green H, Djian P (November 1992). "Consecutive actions of different gene-altering mechanisms in the evolution of involucrin". Molecular Biology and Evolution. 9 (6): 977–1017. PMID 1359382. 
  5. ^ Djian P, Phillips M, Easley K, Huang E, Simon M, Rice RH, Green H (November 1993). "The involucrin genes of the mouse and the rat: study of their shared repeats". Molecular Biology and Evolution. 10 (6): 1136–49. PMID 8277848. 
  6. ^ Eckert RL, Yaffe MB, Crish JF, Murthy S, Rorke EA, Welter JF (May 1993). "Involucrin--structure and role in envelope assembly". The Journal of Investigative Dermatology. 100 (5): 613–7. doi:10.1111/1523-1747.ep12472288. PMID 8098344. 
  7. ^ Balasubramanian S, Zhu L, Eckert RL (November 2006). "Apigenin inhibition of involucrin gene expression is associated with a specific reduction in phosphorylation of protein kinase Cdelta Tyr311". The Journal of Biological Chemistry. 281 (47): 36162–72. doi:10.1074/jbc.M605368200. PMID 16982614. 
  8. ^ Takahashi H, Hashimoto Y, Ishida-Yamamoto A, Iizuka H (September 2005). "Roxithromycin suppresses involucrin expression by modulation of activator protein-1 and nuclear factor-kappaB activities of keratinocytes". Journal of Dermatological Science. 39 (3): 175–82. doi:10.1016/j.jdermsci.2005.03.006. PMID 16140218. 
  9. ^ Peña-Penabad C, de Unamuno P, García Silva J, Ludeña MD, González Sarmiento R, Pérez-Arellano JL (1999). "Altered expression of immunoreactive involucrin in lamellar ichthyosis". European Journal of Dermatology. 9 (3): 197–201. PMID 10210784. 

Further reading

This article incorporates text from the public domain Pfam and InterPro IPR019571

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Involucrin repeat Provide feedback

No Pfam abstract.

Literature references

  1. Eckert RL, Yaffe MB, Crish JF, Murthy S, Rorke EA, Welter JF; , J Invest Dermatol 1993;100:613-617.: Involucrin--structure and role in envelope assembly. PUBMED:8098344 EPMC:8098344


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000354

Involucrin [PUBMED:1359382, PUBMED:8277848] is a protein present in keratinocytes of epidermis and other stratified squamous epithelia. Involucrin first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase thus helping in the formation of an insoluble envelope beneath the plasma membrane.

Structurally involucrin consists of a conserved region of about 75 amino acid residues followed by two extremely variable length segments that contain glutamine-rich tandem repeats. The glutamine residues in the tandem repeats are the substrate for the tranglutaminase in the cross-linking reaction. The total size of the protein varies from 285 residues (in dog) to 835 residues (in orangutan).

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

Loading domain graphics...

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(36)
Full
(301)
Representative proteomes UniProt
(754)
NCBI
(1369)
Meta
(0)
RP15
(40)
RP35
(40)
RP55
(40)
RP75
(240)
Jalview View  View  View  View  View  View  View  View   
HTML View  View               
PP/heatmap 1 View               

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(36)
Full
(301)
Representative proteomes UniProt
(754)
NCBI
(1369)
Meta
(0)
RP15
(40)
RP35
(40)
RP55
(40)
RP75
(240)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(36)
Full
(301)
Representative proteomes UniProt
(754)
NCBI
(1369)
Meta
(0)
RP15
(40)
RP35
(40)
RP55
(40)
RP75
(240)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download    
Gzipped Download   Download   Download   Download   Download   Download   Download   Download    

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_1158 (release 3.0)
Previous IDs: none
Type: Repeat
Author: Bateman A
Number in seed: 36
Number in full: 301
Average length of the domain: 9.80 aa
Average identity of full alignment: 65 %
Average coverage of the sequence by the domain: 64.99 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 15.0 0.1
Trusted cut-off 15.6 0.8
Noise cut-off 13.4 -0.2
Model length: 10
Family (HMM) version: 16
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Hide

Weight segments by...


Change the size of the sunburst

Small
Large

Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

Align selected sequences to HMM

Generate a FASTA-format file

Clear selection

This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

Loading sunburst data...

Tree controls

Hide

The tree shows the occurrence of this domain across different species. More...

Loading...

Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.