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P07476

- INVO_HUMAN

UniProt

P07476 - INVO_HUMAN

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Protein
Involucrin
Gene
IVL
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia.

GO - Molecular functioni

  1. protein binding, bridging Source: UniProtKB
  2. structural molecule activity Source: UniProtKB

GO - Biological processi

  1. isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine Source: UniProtKB
  2. keratinization Source: UniProtKB-KW
  3. keratinocyte differentiation Source: UniProtKB
  4. peptide cross-linking Source: UniProtKB
  5. response to UV-B Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Keratinization

Names & Taxonomyi

Protein namesi
Recommended name:
Involucrin
Gene namesi
Name:IVL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6187. IVL.

Subcellular locationi

Cytoplasm
Note: Constituent of the scaffolding of the cornified envelope.

GO - Cellular componenti

  1. cornified envelope Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29985.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 585585Involucrin
PRO_0000159736Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi79 – 791Omega-hydroxyceramide glutamate ester Inferred
Lipidationi90 – 901Omega-hydroxyceramide glutamate ester Inferred
Lipidationi118 – 1181Omega-hydroxyceramide glutamate ester Inferred
Lipidationi133 – 1331Omega-hydroxyceramide glutamate ester Inferred
Cross-linki496 – 496Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-? in other proteins)

Post-translational modificationi

Substrate of transglutaminase. Some glutamines and lysines are cross-linked to other involucrin molecules, to other proteins such as keratin, desmoplakin, periplakin and envoplakin, and to lipids like omega-hydroxyceramide.

Keywords - PTMi

Isopeptide bond, Lipoprotein

Proteomic databases

MaxQBiP07476.
PaxDbiP07476.
PRIDEiP07476.

PTM databases

PhosphoSiteiP07476.

Expressioni

Tissue specificityi

Keratinocytes of epidermis and other stratified squamous epithelia.

Gene expression databases

ArrayExpressiP07476.
BgeeiP07476.
CleanExiHS_IVL.
GenevestigatoriP07476.

Organism-specific databases

HPAiCAB002243.
HPA055211.

Interactioni

Subunit structurei

Directly or indirectly cross-linked to cornifelin (CNFN).

Protein-protein interaction databases

BioGridi109917. 9 interactions.
STRINGi9606.ENSP00000357753.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi313 – 3186
Helixi323 – 3286
Helixi333 – 3386
Helixi343 – 3486
Helixi353 – 3586

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EU0model-A312-361[»]
DisProtiDP00221.
ProteinModelPortaliP07476.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati153 – 162101
Repeati163 – 172102
Repeati173 – 182103
Repeati183 – 192104
Repeati193 – 202105
Repeati203 – 212106
Repeati213 – 222107
Repeati223 – 232108
Repeati233 – 242109
Repeati243 – 2521010
Repeati253 – 2621011
Repeati263 – 2721012
Repeati273 – 2821013
Repeati283 – 2921014
Repeati293 – 3021015
Repeati303 – 3121016
Repeati313 – 3221017
Repeati323 – 3321018
Repeati333 – 3421019
Repeati343 – 3521020
Repeati353 – 3621021
Repeati363 – 3721022
Repeati373 – 3821023
Repeati383 – 3921024; approximate
Repeati393 – 4021025
Repeati403 – 4121026
Repeati413 – 4221027
Repeati423 – 4321028
Repeati433 – 4421029
Repeati443 – 4521030
Repeati453 – 4621031
Repeati463 – 4721032
Repeati473 – 4821033
Repeati483 – 4921034
Repeati493 – 5021035
Repeati503 – 5121036; approximate
Repeati513 – 5221037
Repeati523 – 5321038
Repeati533 – 5421039; approximate

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni153 – 54239039 X 10 AA approximate tandem repeats of [LP]-[EKG]-[LHVYQEK]-[PLSQE]-[EQDV]-[QHEKRGA]-Q-[EMVQLP]-[GKLE]-[QHVNLD]
Add
BLAST

Sequence similaritiesi

Belongs to the involucrin family.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG80441.
HOVERGENiHBG006166.
InParanoidiP07476.
OMAiPEQQVGQ.
OrthoDBiEOG747PMZ.
PhylomeDBiP07476.
TreeFamiTF340025.

Family and domain databases

InterProiIPR002360. Involucrin.
IPR019743. Involucrin_CS.
IPR019571. Involucrin_N.
IPR000354. Involucrin_rpt.
[Graphical view]
PANTHERiPTHR13905. PTHR13905. 1 hit.
PfamiPF00904. Involucrin. 40 hits.
PF10583. Involucrin_N. 1 hit.
[Graphical view]
PROSITEiPS00795. INVOLUCRIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07476-1 [UniParc]FASTAAdd to Basket

« Hide

MSQQHTLPVT LSPALSQELL KTVPPPVNTH QEQMKQPTPL PPPCQKVPVE    50
LPVEVPSKQE EKHMTAVKGL PEQECEQQQK EPQEQELQQQ HWEQHEEYQK 100
AENPEQQLKQ EKTQRDQQLN KQLEEEKKLL DQQLDQELVK RDEQLGMKKE 150
QLLELPEQQE GHLKHLEQQE GQLKHPEQQE GQLELPEQQE GQLELPEQQE 200
GQLELPEQQE GQLELPEQQE GQLELPEQQE GQLELPQQQE GQLELSEQQE 250
GQLELSEQQE GQLKHLEHQE GQLEVPEEQM GQLKYLEQQE GQLKHLDQQE 300
KQPELPEQQM GQLKHLEQQE GQPKHLEQQE GQLEQLEEQE GQLKHLEQQE 350
GQLEHLEHQE GQLGLPEQQV LQLKQLEKQQ GQPKHLEEEE GQLKHLVQQE 400
GQLKHLVQQE GQLEQQERQV EHLEQQVGQL KHLEEQEGQL KHLEQQQGQL 450
EVPEQQVGQP KNLEQEEKQL ELPEQQEGQV KHLEKQEAQL ELPEQQVGQP 500
KHLEQQEKHL EHPEQQDGQL KHLEQQEGQL KDLEQQKGQL EQPVFAPAPG 550
QVQDIQPALP TKGEVLLPVE HQQQKQEVQW PPKHK 585
Length:585
Mass (Da):68,479
Last modified:July 28, 2009 - v2
Checksum:i775D2AFB90F647E8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti113 – 1131T → A.
Corresponds to variant rs2229496 [ dbSNP | Ensembl ].
VAR_029019
Natural varianti166 – 1661L → P.
Corresponds to variant rs11205133 [ dbSNP | Ensembl ].
VAR_029020
Natural varianti174 – 1741K → E.
Corresponds to variant rs12035307 [ dbSNP | Ensembl ].
VAR_029021
Natural varianti227 – 2271E → Q.2 Publications
Corresponds to variant rs11807064 [ dbSNP | Ensembl ].
VAR_058411
Natural varianti236 – 2361P → S.2 Publications
Corresponds to variant rs17855670 [ dbSNP | Ensembl ].
VAR_058412
Natural varianti237 – 2371Q → E.2 Publications
Corresponds to variant rs7520711 [ dbSNP | Ensembl ].
VAR_029022
Natural varianti312 – 3121Q → K.
Corresponds to variant rs11205137 [ dbSNP | Ensembl ].
VAR_029023
Natural varianti480 – 4801V → L.
Corresponds to variant rs7545520 [ dbSNP | Ensembl ].
VAR_029024

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M13903 Genomic DNA. Translation: AAA59186.1.
AL162596 Genomic DNA. Translation: CAI19553.1.
BC046391 mRNA. Translation: AAH46391.1.
CCDSiCCDS1030.1.
PIRiA24168.
RefSeqiNP_005538.2. NM_005547.2.
XP_006711363.1. XM_006711300.1.
UniGeneiHs.516439.

Genome annotation databases

EnsembliENST00000368764; ENSP00000357753; ENSG00000163207.
GeneIDi3713.
KEGGihsa:3713.
UCSCiuc001fau.3. human.

Polymorphism databases

DMDMi254763301.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M13903 Genomic DNA. Translation: AAA59186.1 .
AL162596 Genomic DNA. Translation: CAI19553.1 .
BC046391 mRNA. Translation: AAH46391.1 .
CCDSi CCDS1030.1.
PIRi A24168.
RefSeqi NP_005538.2. NM_005547.2.
XP_006711363.1. XM_006711300.1.
UniGenei Hs.516439.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EU0 model - A 312-361 [» ]
DisProti DP00221.
ProteinModelPortali P07476.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109917. 9 interactions.
STRINGi 9606.ENSP00000357753.

PTM databases

PhosphoSitei P07476.

Polymorphism databases

DMDMi 254763301.

Proteomic databases

MaxQBi P07476.
PaxDbi P07476.
PRIDEi P07476.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368764 ; ENSP00000357753 ; ENSG00000163207 .
GeneIDi 3713.
KEGGi hsa:3713.
UCSCi uc001fau.3. human.

Organism-specific databases

CTDi 3713.
GeneCardsi GC01P152881.
H-InvDB HIX0023860.
HGNCi HGNC:6187. IVL.
HPAi CAB002243.
HPA055211.
MIMi 147360. gene.
neXtProti NX_P07476.
PharmGKBi PA29985.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG80441.
HOVERGENi HBG006166.
InParanoidi P07476.
OMAi PEQQVGQ.
OrthoDBi EOG747PMZ.
PhylomeDBi P07476.
TreeFami TF340025.

Miscellaneous databases

ChiTaRSi IVL. human.
GeneWikii Involucrin.
GenomeRNAii 3713.
NextBioi 14551.
PROi P07476.
SOURCEi Search...

Gene expression databases

ArrayExpressi P07476.
Bgeei P07476.
CleanExi HS_IVL.
Genevestigatori P07476.

Family and domain databases

InterProi IPR002360. Involucrin.
IPR019743. Involucrin_CS.
IPR019571. Involucrin_N.
IPR000354. Involucrin_rpt.
[Graphical view ]
PANTHERi PTHR13905. PTHR13905. 1 hit.
Pfami PF00904. Involucrin. 40 hits.
PF10583. Involucrin_N. 1 hit.
[Graphical view ]
PROSITEi PS00795. INVOLUCRIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and evolution of the human involucrin gene."
    Eckert R.L., Green H.
    Cell 46:583-589(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-227; SER-236 AND GLU-237.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLN-227; SER-236 AND GLU-237.
    Tissue: Skin.
  4. "S100A11, S100A10, annexin I, desmosomal proteins, small proline-rich proteins, plasminogen activator inhibitor-2, and involucrin are components of the cornified envelope of cultured human epidermal keratinocytes."
    Robinson N.A., Lapic S., Welter J.F., Eckert R.L.
    J. Biol. Chem. 272:12035-12046(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 281-290.
    Tissue: Keratinocyte.
  5. "Biophysical characterization of involucrin reveals a molecule ideally suited to function as an intermolecular cross-bridge of the keratinocyte cornified envelope."
    Yaffe M.B., Beegen H., Eckert R.L.
    J. Biol. Chem. 267:12233-12238(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURAL STUDIES.
  6. "The glutamine residues reactive in transglutaminase-catalyzed cross-linking of involucrin."
    Simon M., Green H.
    J. Biol. Chem. 263:18093-18098(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLN-LYS CROSS-LINK.
  7. "Ceramides are bound to structural proteins of the human foreskin epidermal cornified cell envelope."
    Marekov L.N., Steinert P.M.
    J. Biol. Chem. 273:17763-17770(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIPIDATION.
  8. "Identification and characterization of a novel component of the cornified envelope, cornifelin."
    Michibata H., Chiba H., Wakimoto K., Seishima M., Kawasaki S., Okubo K., Mitsui H., Torii H., Imai Y.
    Biochem. Biophys. Res. Commun. 318:803-813(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INVOLUCRIN.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiINVO_HUMAN
AccessioniPrimary (citable) accession number: P07476
Secondary accession number(s): Q5T7P4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: July 28, 2009
Last modified: July 9, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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