Full text data of IVL
IVL
[Confidence: low (only semi-automatic identification from reviews)]
Involucrin
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Involucrin
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P07476
ID INVO_HUMAN Reviewed; 585 AA.
AC P07476; Q5T7P4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 28-JUL-2009, sequence version 2.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=Involucrin;
GN Name=IVL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-227; SER-236 AND
RP GLU-237.
RX PubMed=2873896; DOI=10.1016/0092-8674(86)90884-6;
RA Eckert R.L., Green H.;
RT "Structure and evolution of the human involucrin gene.";
RL Cell 46:583-589(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLN-227; SER-236
RP AND GLU-237.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 281-290.
RC TISSUE=Keratinocyte;
RX PubMed=9115270; DOI=10.1074/jbc.272.18.12035;
RA Robinson N.A., Lapic S., Welter J.F., Eckert R.L.;
RT "S100A11, S100A10, annexin I, desmosomal proteins, small proline-rich
RT proteins, plasminogen activator inhibitor-2, and involucrin are
RT components of the cornified envelope of cultured human epidermal
RT keratinocytes.";
RL J. Biol. Chem. 272:12035-12046(1997).
RN [5]
RP STRUCTURAL STUDIES.
RX PubMed=1601889;
RA Yaffe M.B., Beegen H., Eckert R.L.;
RT "Biophysical characterization of involucrin reveals a molecule ideally
RT suited to function as an intermolecular cross-bridge of the
RT keratinocyte cornified envelope.";
RL J. Biol. Chem. 267:12233-12238(1992).
RN [6]
RP GLN-LYS CROSS-LINK.
RX PubMed=2461365;
RA Simon M., Green H.;
RT "The glutamine residues reactive in transglutaminase-catalyzed cross-
RT linking of involucrin.";
RL J. Biol. Chem. 263:18093-18098(1988).
RN [7]
RP LIPIDATION.
RX PubMed=9651377; DOI=10.1074/jbc.273.28.17763;
RA Marekov L.N., Steinert P.M.;
RT "Ceramides are bound to structural proteins of the human foreskin
RT epidermal cornified cell envelope.";
RL J. Biol. Chem. 273:17763-17770(1998).
RN [8]
RP INTERACTION WITH INVOLUCRIN.
RX PubMed=15147942; DOI=10.1016/j.bbrc.2004.04.109;
RA Michibata H., Chiba H., Wakimoto K., Seishima M., Kawasaki S.,
RA Okubo K., Mitsui H., Torii H., Imai Y.;
RT "Identification and characterization of a novel component of the
RT cornified envelope, cornifelin.";
RL Biochem. Biophys. Res. Commun. 318:803-813(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Part of the insoluble cornified cell envelope (CE) of
CC stratified squamous epithelia.
CC -!- SUBUNIT: Directly or indirectly cross-linked to cornifelin (CNFN).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Constituent of the
CC scaffolding of the cornified envelope.
CC -!- TISSUE SPECIFICITY: Keratinocytes of epidermis and other
CC stratified squamous epithelia.
CC -!- PTM: Substrate of transglutaminase. Some glutamines and lysines
CC are cross-linked to other involucrin molecules, to other proteins
CC such as keratin, desmoplakin, periplakin and envoplakin, and to
CC lipids like omega-hydroxyceramide.
CC -!- SIMILARITY: Belongs to the involucrin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M13903; AAA59186.1; -; Genomic_DNA.
DR EMBL; AL162596; CAI19553.1; -; Genomic_DNA.
DR EMBL; BC046391; AAH46391.1; -; mRNA.
DR PIR; A24168; A24168.
DR RefSeq; NP_005538.2; NM_005547.2.
DR UniGene; Hs.516439; -.
DR PDB; 1EU0; Model; -; A=312-361.
DR PDBsum; 1EU0; -.
DR DisProt; DP00221; -.
DR ProteinModelPortal; P07476; -.
DR STRING; 9606.ENSP00000357753; -.
DR PhosphoSite; P07476; -.
DR DMDM; 254763301; -.
DR PaxDb; P07476; -.
DR PRIDE; P07476; -.
DR Ensembl; ENST00000368764; ENSP00000357753; ENSG00000163207.
DR GeneID; 3713; -.
DR KEGG; hsa:3713; -.
DR UCSC; uc001fau.3; human.
DR CTD; 3713; -.
DR GeneCards; GC01P152881; -.
DR H-InvDB; HIX0023860; -.
DR HGNC; HGNC:6187; IVL.
DR HPA; CAB002243; -.
DR MIM; 147360; gene.
DR neXtProt; NX_P07476; -.
DR PharmGKB; PA29985; -.
DR eggNOG; NOG80441; -.
DR HOVERGEN; HBG006166; -.
DR InParanoid; P07476; -.
DR OMA; PEQQVGQ; -.
DR OrthoDB; EOG747PMZ; -.
DR ChiTaRS; IVL; human.
DR GeneWiki; Involucrin; -.
DR GenomeRNAi; 3713; -.
DR NextBio; 14551; -.
DR PRO; PR:P07476; -.
DR ArrayExpress; P07476; -.
DR Bgee; P07476; -.
DR CleanEx; HS_IVL; -.
DR Genevestigator; P07476; -.
DR GO; GO:0001533; C:cornified envelope; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030674; F:protein binding, bridging; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR GO; GO:0018153; P:isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine; TAS:UniProtKB.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB.
DR GO; GO:0010224; P:response to UV-B; IDA:UniProtKB.
DR InterPro; IPR002360; Involucrin.
DR InterPro; IPR019743; Involucrin_CS.
DR InterPro; IPR019571; Involucrin_N.
DR InterPro; IPR000354; Involucrin_rpt.
DR PANTHER; PTHR13905; PTHR13905; 1.
DR Pfam; PF00904; Involucrin; 40.
DR Pfam; PF10583; Involucrin_N; 1.
DR PROSITE; PS00795; INVOLUCRIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Keratinization; Lipoprotein; Polymorphism;
KW Reference proteome; Repeat.
FT CHAIN 1 585 Involucrin.
FT /FTId=PRO_0000159736.
FT REPEAT 153 162 1.
FT REPEAT 163 172 2.
FT REPEAT 173 182 3.
FT REPEAT 183 192 4.
FT REPEAT 193 202 5.
FT REPEAT 203 212 6.
FT REPEAT 213 222 7.
FT REPEAT 223 232 8.
FT REPEAT 233 242 9.
FT REPEAT 243 252 10.
FT REPEAT 253 262 11.
FT REPEAT 263 272 12.
FT REPEAT 273 282 13.
FT REPEAT 283 292 14.
FT REPEAT 293 302 15.
FT REPEAT 303 312 16.
FT REPEAT 313 322 17.
FT REPEAT 323 332 18.
FT REPEAT 333 342 19.
FT REPEAT 343 352 20.
FT REPEAT 353 362 21.
FT REPEAT 363 372 22.
FT REPEAT 373 382 23.
FT REPEAT 383 392 24; approximate.
FT REPEAT 393 402 25.
FT REPEAT 403 412 26.
FT REPEAT 413 422 27.
FT REPEAT 423 432 28.
FT REPEAT 433 442 29.
FT REPEAT 443 452 30.
FT REPEAT 453 462 31.
FT REPEAT 463 472 32.
FT REPEAT 473 482 33.
FT REPEAT 483 492 34.
FT REPEAT 493 502 35.
FT REPEAT 503 512 36; approximate.
FT REPEAT 513 522 37.
FT REPEAT 523 532 38.
FT REPEAT 533 542 39; approximate.
FT REGION 153 542 39 X 10 AA approximate tandem repeats of
FT [LP]-[EKG]-[LHVYQEK]-[PLSQE]-[EQDV]-
FT [QHEKRGA]-Q-[EMVQLP]-[GKLE]-[QHVNLD].
FT LIPID 79 79 Omega-hydroxyceramide glutamate ester
FT (Probable).
FT LIPID 90 90 Omega-hydroxyceramide glutamate ester
FT (Probable).
FT LIPID 118 118 Omega-hydroxyceramide glutamate ester
FT (Probable).
FT LIPID 133 133 Omega-hydroxyceramide glutamate ester
FT (Probable).
FT CROSSLNK 496 496 Isoglutamyl lysine isopeptide (Gln-Lys)
FT (interchain with K-? in other proteins).
FT VARIANT 113 113 T -> A (in dbSNP:rs2229496).
FT /FTId=VAR_029019.
FT VARIANT 166 166 L -> P (in dbSNP:rs11205133).
FT /FTId=VAR_029020.
FT VARIANT 174 174 K -> E (in dbSNP:rs12035307).
FT /FTId=VAR_029021.
FT VARIANT 227 227 E -> Q (in dbSNP:rs11807064).
FT /FTId=VAR_058411.
FT VARIANT 236 236 P -> S (in dbSNP:rs17855670).
FT /FTId=VAR_058412.
FT VARIANT 237 237 Q -> E (in dbSNP:rs7520711).
FT /FTId=VAR_029022.
FT VARIANT 312 312 Q -> K (in dbSNP:rs11205137).
FT /FTId=VAR_029023.
FT VARIANT 480 480 V -> L (in dbSNP:rs7545520).
FT /FTId=VAR_029024.
FT HELIX 313 318
FT HELIX 323 328
FT HELIX 333 338
FT HELIX 343 348
FT HELIX 353 358
SQ SEQUENCE 585 AA; 68479 MW; 775D2AFB90F647E8 CRC64;
MSQQHTLPVT LSPALSQELL KTVPPPVNTH QEQMKQPTPL PPPCQKVPVE LPVEVPSKQE
EKHMTAVKGL PEQECEQQQK EPQEQELQQQ HWEQHEEYQK AENPEQQLKQ EKTQRDQQLN
KQLEEEKKLL DQQLDQELVK RDEQLGMKKE QLLELPEQQE GHLKHLEQQE GQLKHPEQQE
GQLELPEQQE GQLELPEQQE GQLELPEQQE GQLELPEQQE GQLELPEQQE GQLELPQQQE
GQLELSEQQE GQLELSEQQE GQLKHLEHQE GQLEVPEEQM GQLKYLEQQE GQLKHLDQQE
KQPELPEQQM GQLKHLEQQE GQPKHLEQQE GQLEQLEEQE GQLKHLEQQE GQLEHLEHQE
GQLGLPEQQV LQLKQLEKQQ GQPKHLEEEE GQLKHLVQQE GQLKHLVQQE GQLEQQERQV
EHLEQQVGQL KHLEEQEGQL KHLEQQQGQL EVPEQQVGQP KNLEQEEKQL ELPEQQEGQV
KHLEKQEAQL ELPEQQVGQP KHLEQQEKHL EHPEQQDGQL KHLEQQEGQL KDLEQQKGQL
EQPVFAPAPG QVQDIQPALP TKGEVLLPVE HQQQKQEVQW PPKHK
//
ID INVO_HUMAN Reviewed; 585 AA.
AC P07476; Q5T7P4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 28-JUL-2009, sequence version 2.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=Involucrin;
GN Name=IVL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-227; SER-236 AND
RP GLU-237.
RX PubMed=2873896; DOI=10.1016/0092-8674(86)90884-6;
RA Eckert R.L., Green H.;
RT "Structure and evolution of the human involucrin gene.";
RL Cell 46:583-589(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLN-227; SER-236
RP AND GLU-237.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 281-290.
RC TISSUE=Keratinocyte;
RX PubMed=9115270; DOI=10.1074/jbc.272.18.12035;
RA Robinson N.A., Lapic S., Welter J.F., Eckert R.L.;
RT "S100A11, S100A10, annexin I, desmosomal proteins, small proline-rich
RT proteins, plasminogen activator inhibitor-2, and involucrin are
RT components of the cornified envelope of cultured human epidermal
RT keratinocytes.";
RL J. Biol. Chem. 272:12035-12046(1997).
RN [5]
RP STRUCTURAL STUDIES.
RX PubMed=1601889;
RA Yaffe M.B., Beegen H., Eckert R.L.;
RT "Biophysical characterization of involucrin reveals a molecule ideally
RT suited to function as an intermolecular cross-bridge of the
RT keratinocyte cornified envelope.";
RL J. Biol. Chem. 267:12233-12238(1992).
RN [6]
RP GLN-LYS CROSS-LINK.
RX PubMed=2461365;
RA Simon M., Green H.;
RT "The glutamine residues reactive in transglutaminase-catalyzed cross-
RT linking of involucrin.";
RL J. Biol. Chem. 263:18093-18098(1988).
RN [7]
RP LIPIDATION.
RX PubMed=9651377; DOI=10.1074/jbc.273.28.17763;
RA Marekov L.N., Steinert P.M.;
RT "Ceramides are bound to structural proteins of the human foreskin
RT epidermal cornified cell envelope.";
RL J. Biol. Chem. 273:17763-17770(1998).
RN [8]
RP INTERACTION WITH INVOLUCRIN.
RX PubMed=15147942; DOI=10.1016/j.bbrc.2004.04.109;
RA Michibata H., Chiba H., Wakimoto K., Seishima M., Kawasaki S.,
RA Okubo K., Mitsui H., Torii H., Imai Y.;
RT "Identification and characterization of a novel component of the
RT cornified envelope, cornifelin.";
RL Biochem. Biophys. Res. Commun. 318:803-813(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Part of the insoluble cornified cell envelope (CE) of
CC stratified squamous epithelia.
CC -!- SUBUNIT: Directly or indirectly cross-linked to cornifelin (CNFN).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Constituent of the
CC scaffolding of the cornified envelope.
CC -!- TISSUE SPECIFICITY: Keratinocytes of epidermis and other
CC stratified squamous epithelia.
CC -!- PTM: Substrate of transglutaminase. Some glutamines and lysines
CC are cross-linked to other involucrin molecules, to other proteins
CC such as keratin, desmoplakin, periplakin and envoplakin, and to
CC lipids like omega-hydroxyceramide.
CC -!- SIMILARITY: Belongs to the involucrin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M13903; AAA59186.1; -; Genomic_DNA.
DR EMBL; AL162596; CAI19553.1; -; Genomic_DNA.
DR EMBL; BC046391; AAH46391.1; -; mRNA.
DR PIR; A24168; A24168.
DR RefSeq; NP_005538.2; NM_005547.2.
DR UniGene; Hs.516439; -.
DR PDB; 1EU0; Model; -; A=312-361.
DR PDBsum; 1EU0; -.
DR DisProt; DP00221; -.
DR ProteinModelPortal; P07476; -.
DR STRING; 9606.ENSP00000357753; -.
DR PhosphoSite; P07476; -.
DR DMDM; 254763301; -.
DR PaxDb; P07476; -.
DR PRIDE; P07476; -.
DR Ensembl; ENST00000368764; ENSP00000357753; ENSG00000163207.
DR GeneID; 3713; -.
DR KEGG; hsa:3713; -.
DR UCSC; uc001fau.3; human.
DR CTD; 3713; -.
DR GeneCards; GC01P152881; -.
DR H-InvDB; HIX0023860; -.
DR HGNC; HGNC:6187; IVL.
DR HPA; CAB002243; -.
DR MIM; 147360; gene.
DR neXtProt; NX_P07476; -.
DR PharmGKB; PA29985; -.
DR eggNOG; NOG80441; -.
DR HOVERGEN; HBG006166; -.
DR InParanoid; P07476; -.
DR OMA; PEQQVGQ; -.
DR OrthoDB; EOG747PMZ; -.
DR ChiTaRS; IVL; human.
DR GeneWiki; Involucrin; -.
DR GenomeRNAi; 3713; -.
DR NextBio; 14551; -.
DR PRO; PR:P07476; -.
DR ArrayExpress; P07476; -.
DR Bgee; P07476; -.
DR CleanEx; HS_IVL; -.
DR Genevestigator; P07476; -.
DR GO; GO:0001533; C:cornified envelope; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030674; F:protein binding, bridging; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR GO; GO:0018153; P:isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine; TAS:UniProtKB.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB.
DR GO; GO:0010224; P:response to UV-B; IDA:UniProtKB.
DR InterPro; IPR002360; Involucrin.
DR InterPro; IPR019743; Involucrin_CS.
DR InterPro; IPR019571; Involucrin_N.
DR InterPro; IPR000354; Involucrin_rpt.
DR PANTHER; PTHR13905; PTHR13905; 1.
DR Pfam; PF00904; Involucrin; 40.
DR Pfam; PF10583; Involucrin_N; 1.
DR PROSITE; PS00795; INVOLUCRIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Keratinization; Lipoprotein; Polymorphism;
KW Reference proteome; Repeat.
FT CHAIN 1 585 Involucrin.
FT /FTId=PRO_0000159736.
FT REPEAT 153 162 1.
FT REPEAT 163 172 2.
FT REPEAT 173 182 3.
FT REPEAT 183 192 4.
FT REPEAT 193 202 5.
FT REPEAT 203 212 6.
FT REPEAT 213 222 7.
FT REPEAT 223 232 8.
FT REPEAT 233 242 9.
FT REPEAT 243 252 10.
FT REPEAT 253 262 11.
FT REPEAT 263 272 12.
FT REPEAT 273 282 13.
FT REPEAT 283 292 14.
FT REPEAT 293 302 15.
FT REPEAT 303 312 16.
FT REPEAT 313 322 17.
FT REPEAT 323 332 18.
FT REPEAT 333 342 19.
FT REPEAT 343 352 20.
FT REPEAT 353 362 21.
FT REPEAT 363 372 22.
FT REPEAT 373 382 23.
FT REPEAT 383 392 24; approximate.
FT REPEAT 393 402 25.
FT REPEAT 403 412 26.
FT REPEAT 413 422 27.
FT REPEAT 423 432 28.
FT REPEAT 433 442 29.
FT REPEAT 443 452 30.
FT REPEAT 453 462 31.
FT REPEAT 463 472 32.
FT REPEAT 473 482 33.
FT REPEAT 483 492 34.
FT REPEAT 493 502 35.
FT REPEAT 503 512 36; approximate.
FT REPEAT 513 522 37.
FT REPEAT 523 532 38.
FT REPEAT 533 542 39; approximate.
FT REGION 153 542 39 X 10 AA approximate tandem repeats of
FT [LP]-[EKG]-[LHVYQEK]-[PLSQE]-[EQDV]-
FT [QHEKRGA]-Q-[EMVQLP]-[GKLE]-[QHVNLD].
FT LIPID 79 79 Omega-hydroxyceramide glutamate ester
FT (Probable).
FT LIPID 90 90 Omega-hydroxyceramide glutamate ester
FT (Probable).
FT LIPID 118 118 Omega-hydroxyceramide glutamate ester
FT (Probable).
FT LIPID 133 133 Omega-hydroxyceramide glutamate ester
FT (Probable).
FT CROSSLNK 496 496 Isoglutamyl lysine isopeptide (Gln-Lys)
FT (interchain with K-? in other proteins).
FT VARIANT 113 113 T -> A (in dbSNP:rs2229496).
FT /FTId=VAR_029019.
FT VARIANT 166 166 L -> P (in dbSNP:rs11205133).
FT /FTId=VAR_029020.
FT VARIANT 174 174 K -> E (in dbSNP:rs12035307).
FT /FTId=VAR_029021.
FT VARIANT 227 227 E -> Q (in dbSNP:rs11807064).
FT /FTId=VAR_058411.
FT VARIANT 236 236 P -> S (in dbSNP:rs17855670).
FT /FTId=VAR_058412.
FT VARIANT 237 237 Q -> E (in dbSNP:rs7520711).
FT /FTId=VAR_029022.
FT VARIANT 312 312 Q -> K (in dbSNP:rs11205137).
FT /FTId=VAR_029023.
FT VARIANT 480 480 V -> L (in dbSNP:rs7545520).
FT /FTId=VAR_029024.
FT HELIX 313 318
FT HELIX 323 328
FT HELIX 333 338
FT HELIX 343 348
FT HELIX 353 358
SQ SEQUENCE 585 AA; 68479 MW; 775D2AFB90F647E8 CRC64;
MSQQHTLPVT LSPALSQELL KTVPPPVNTH QEQMKQPTPL PPPCQKVPVE LPVEVPSKQE
EKHMTAVKGL PEQECEQQQK EPQEQELQQQ HWEQHEEYQK AENPEQQLKQ EKTQRDQQLN
KQLEEEKKLL DQQLDQELVK RDEQLGMKKE QLLELPEQQE GHLKHLEQQE GQLKHPEQQE
GQLELPEQQE GQLELPEQQE GQLELPEQQE GQLELPEQQE GQLELPEQQE GQLELPQQQE
GQLELSEQQE GQLELSEQQE GQLKHLEHQE GQLEVPEEQM GQLKYLEQQE GQLKHLDQQE
KQPELPEQQM GQLKHLEQQE GQPKHLEQQE GQLEQLEEQE GQLKHLEQQE GQLEHLEHQE
GQLGLPEQQV LQLKQLEKQQ GQPKHLEEEE GQLKHLVQQE GQLKHLVQQE GQLEQQERQV
EHLEQQVGQL KHLEEQEGQL KHLEQQQGQL EVPEQQVGQP KNLEQEEKQL ELPEQQEGQV
KHLEKQEAQL ELPEQQVGQP KHLEQQEKHL EHPEQQDGQL KHLEQQEGQL KDLEQQKGQL
EQPVFAPAPG QVQDIQPALP TKGEVLLPVE HQQQKQEVQW PPKHK
//
MIM
147360
*RECORD*
*FIELD* NO
147360
*FIELD* TI
*147360 INVOLUCRIN; IVL
*FIELD* TX
DESCRIPTION
The crosslinked envelope of the keratinocyte is formed in the last stage
read moreof its terminal differentiation. This envelope is made up of membrane
and cytosolic proteins crosslinked by glutamyl lysine isopeptide bonds.
The most abundant component is involucrin, a keratinocyte protein that
appears first in the cytoplasm but ultimately becomes crosslinked to
membrane proteins by transglutaminase (summary by Eckert and Green,
1986).
CLONING
Eckert and Green (1986) cloned the involucrin gene and studied its
structure and evolution. The gene consists of 585 amino acids, 390 of
which form a central decapeptide repeat, rich in glutamine and glutamic
acid.
EVOLUTION
Teumer and Green (1989) described the divergent evolution of the IVL
gene in gorilla and human.
Green and Djian (1992) reviewed the alterations in the involucrin gene
during evolution of primates from nonprimates. As reflected in the 17
species examined, the changes involved short tandem repeats. Evolution
of the IVL gene took place through mechanisms that shortened the length
of the repeats, increased their number, and changed their codon
sequence. As part of this trend, one entire segment of repeats was
replaced by another located elsewhere in the coding region.
Green (1993) pointed to the relevance of the expanded poly(CAG) in the
coding region of genes leading to 3 disorders: spinal and bulbar
muscular atrophy (313200), Huntington disease (143100), and
spinocerebellar ataxia type I (164400). Multiple glutamine residues,
usually encoded by CAG, are necessary for the crosslinking of involucrin
to other proteins by the keratinocyte transglutaminase during terminal
differentiation in the keratinocytes with formation of the insoluble
envelope of the corneocyte. Reiteration of the CAG codon appears to be
very frequent. Of all the animal and plant protein sequences in 2
databases, Green (1993) found that 33 contained a sequence of 16 or more
reiterated glutamines, but not one contained a run of more than 38
glutamines; hence, all showed a number of repeats lower than that in the
abnormal alleles of the 3 human diseases of CAG reiteration. Therefore,
reiteration must in some way be restricted in order to prevent genomic
havoc.
The IVL gene has evolved rapidly in higher primates (Green and Djian,
1992). Djian et al. (1995) observed that, although all mammalian IVL
genes examined to date possess a segment of short tandem repeats in the
coding region, the higher primates possess a segment of repeats that is
different from that of other mammals. This segment has enlarged
progressively mainly in the region not far from the 5-prime end of the
segment of repeats. The site of recent repeat additions is located in
the late region, which is polymorphic with respect to number of repeats
in most higher primates, including the human. The repeat pattern in the
late region of the human IVL gene does not resemble that of other
hominoids. Caucasians and Africans were found by Simon et al. (1991) and
by Urquhart and Gill (1993) to differ in repeat patterns within this
region and at certain nucleotide positions. Djian et al. (1995) observed
that there are over 8 polymorphic forms based on the number and kind of
10-codon tandem repeats in that part of the coding region most recently
added in the human lineage. The IVL alleles of Caucasians and Africans
differ both in nucleotide sequence and repeat patterns. Djian et al.
(1995) showed that the IVL alleles in East Asians (Chinese and Japanese)
can be divided into 2 populations according to whether they possess the
2 marker nucleotides typical of Africans or Caucasians. The Asian
population bearing Caucasian-type marker nucleotides had repeat patterns
similar to those of Caucasians, whereas Asians bearing African-type
marker nucleotides had repeat patterns resembling those of Africans more
than those of Caucasians. The existence of 2 populations of East Asian
IVL alleles gave support for the existence of a Eurasian stem lineage
from which Caucasians and a part of the Asian population originated.
GENE STRUCTURE
Lopez-Bayghen et al. (1996) characterized the 5-prime noncoding region
of IVL and concluded that the region contains a distal
CaCl(2)-responsive enhancer, a putative transcriptional silencer, and a
proximal enhancer.
MAPPING
Stroh et al. (1987) used a genomic clone to probe a panel of
human-rodent somatic cell hybrids and map the involucrin gene to
chromosome 1. By in situ hybridization using the same probe, maximal
hybridization was observed to bands 1q21-q22, with weak hybridization to
1p35-p36. They concluded that band 1q21 is the most likely location of
the IVL gene. Simon et al. (1989) presented the data for mapping of the
IVL gene. They also described a PstI RFLP, which they demonstrated in 1
individual to be the absence of 39 repeats that make up two-thirds of
the coding region of the IVL gene. Simon et al. (1991) gave further
information on the polymorphism in the coding region in the involucrin
gene in higher primates, which results from the variable number of
tandem repeats (VNTR) of a 10-codon sequence. Confirmation of the
localization of the IVL gene to 1q21 was provided by Volz et al. (1993),
who demonstrated physical linkage within 2.05 Mb of DNA to several other
genes involved in epidermal differentiation and known to be located in
that area.
*FIELD* RF
1. Djian, P.; Delhomme, B.; Green, H.: Origin of the polymorphism
of the involucrin gene in Asians. Am. J. Hum. Genet. 56: 1367-1372,
1995.
2. Eckert, R. L.; Green, H.: Structure and evolution of the human
involucrin gene. Cell 46: 583-589, 1986.
3. Green, H.: Human genetic diseases due to codon reiteration: relationship
to an evolutionary mechanism. Cell 74: 955-956, 1993.
4. Green, H.; Djian, P.: Consecutive actions of different gene-altering
mechanisms in the evolution of involucrin. Molec. Biol. Evol. 9:
977-1017, 1992.
5. Lopez-Bayghen, E.; Vega, A.; Cadena, A.; Granados, S. E.; Jave,
L. F.; Gariglio, P.; Alvarez-Salas, L. M.: Transcriptional analysis
of the 5-prime-noncoding region of the human involucrin gene. J.
Biol. Chem. 271: 512-520, 1996.
6. Simon, M.; Phillips, M.; Green, H.: Polymorphism due to variable
number of repeats in the human involucrin gene. Genomics 9: 576-580,
1991.
7. Simon, M.; Phillips, M.; Green, H.; Stroh, H.; Glatt, K.; Burns,
G.; Latt, S. A.: Absence of a single repeat from the coding region
of the human involucrin gene leading to RFLP. Am. J. Hum. Genet. 45:
910-916, 1989.
8. Stroh, H.; Tseng, H.; Harris, P.; Bruns, G.; Green, H.; Latt, S.
A.: Chromosomal mapping of the human involucrin gene (IVL). (Abstract) Cytogenet.
Cell Genet. 46: 700 only, 1987.
9. Teumer, J.; Green, H.: Divergent evolution of part of the involucrin
gene in the hominoids: unique intragenic duplications in the gorilla
and human. Proc. Nat. Acad. Sci. 86: 1283-1286, 1989.
10. Urquhart, A.; Gill, P.: Tandem-repeat internal mapping (TRIM)
of the involucrin gene: repeat number and repeat-pattern polymorphism
within a coding region in human populations. Am. J. Hum. Genet. 53:
279-286, 1993.
11. Volz, A.; Korge, B. P.; Compton, J. G.; Ziegler, A.; Steinert,
P. M.; Mischke, D.: Physical mapping of a functional cluster of epidermal
differentiation genes on chromosome 1q21. Genomics 18: 92-99, 1993.
*FIELD* CN
Alan F. Scott - updated: 9/24/1996
*FIELD* CD
Victor A. McKusick: 10/16/1986
*FIELD* ED
carol: 01/17/2014
mark: 9/24/1996
mark: 7/18/1995
carol: 5/16/1994
terry: 5/10/1994
carol: 10/19/1993
carol: 10/14/1993
carol: 1/4/1993
*RECORD*
*FIELD* NO
147360
*FIELD* TI
*147360 INVOLUCRIN; IVL
*FIELD* TX
DESCRIPTION
The crosslinked envelope of the keratinocyte is formed in the last stage
read moreof its terminal differentiation. This envelope is made up of membrane
and cytosolic proteins crosslinked by glutamyl lysine isopeptide bonds.
The most abundant component is involucrin, a keratinocyte protein that
appears first in the cytoplasm but ultimately becomes crosslinked to
membrane proteins by transglutaminase (summary by Eckert and Green,
1986).
CLONING
Eckert and Green (1986) cloned the involucrin gene and studied its
structure and evolution. The gene consists of 585 amino acids, 390 of
which form a central decapeptide repeat, rich in glutamine and glutamic
acid.
EVOLUTION
Teumer and Green (1989) described the divergent evolution of the IVL
gene in gorilla and human.
Green and Djian (1992) reviewed the alterations in the involucrin gene
during evolution of primates from nonprimates. As reflected in the 17
species examined, the changes involved short tandem repeats. Evolution
of the IVL gene took place through mechanisms that shortened the length
of the repeats, increased their number, and changed their codon
sequence. As part of this trend, one entire segment of repeats was
replaced by another located elsewhere in the coding region.
Green (1993) pointed to the relevance of the expanded poly(CAG) in the
coding region of genes leading to 3 disorders: spinal and bulbar
muscular atrophy (313200), Huntington disease (143100), and
spinocerebellar ataxia type I (164400). Multiple glutamine residues,
usually encoded by CAG, are necessary for the crosslinking of involucrin
to other proteins by the keratinocyte transglutaminase during terminal
differentiation in the keratinocytes with formation of the insoluble
envelope of the corneocyte. Reiteration of the CAG codon appears to be
very frequent. Of all the animal and plant protein sequences in 2
databases, Green (1993) found that 33 contained a sequence of 16 or more
reiterated glutamines, but not one contained a run of more than 38
glutamines; hence, all showed a number of repeats lower than that in the
abnormal alleles of the 3 human diseases of CAG reiteration. Therefore,
reiteration must in some way be restricted in order to prevent genomic
havoc.
The IVL gene has evolved rapidly in higher primates (Green and Djian,
1992). Djian et al. (1995) observed that, although all mammalian IVL
genes examined to date possess a segment of short tandem repeats in the
coding region, the higher primates possess a segment of repeats that is
different from that of other mammals. This segment has enlarged
progressively mainly in the region not far from the 5-prime end of the
segment of repeats. The site of recent repeat additions is located in
the late region, which is polymorphic with respect to number of repeats
in most higher primates, including the human. The repeat pattern in the
late region of the human IVL gene does not resemble that of other
hominoids. Caucasians and Africans were found by Simon et al. (1991) and
by Urquhart and Gill (1993) to differ in repeat patterns within this
region and at certain nucleotide positions. Djian et al. (1995) observed
that there are over 8 polymorphic forms based on the number and kind of
10-codon tandem repeats in that part of the coding region most recently
added in the human lineage. The IVL alleles of Caucasians and Africans
differ both in nucleotide sequence and repeat patterns. Djian et al.
(1995) showed that the IVL alleles in East Asians (Chinese and Japanese)
can be divided into 2 populations according to whether they possess the
2 marker nucleotides typical of Africans or Caucasians. The Asian
population bearing Caucasian-type marker nucleotides had repeat patterns
similar to those of Caucasians, whereas Asians bearing African-type
marker nucleotides had repeat patterns resembling those of Africans more
than those of Caucasians. The existence of 2 populations of East Asian
IVL alleles gave support for the existence of a Eurasian stem lineage
from which Caucasians and a part of the Asian population originated.
GENE STRUCTURE
Lopez-Bayghen et al. (1996) characterized the 5-prime noncoding region
of IVL and concluded that the region contains a distal
CaCl(2)-responsive enhancer, a putative transcriptional silencer, and a
proximal enhancer.
MAPPING
Stroh et al. (1987) used a genomic clone to probe a panel of
human-rodent somatic cell hybrids and map the involucrin gene to
chromosome 1. By in situ hybridization using the same probe, maximal
hybridization was observed to bands 1q21-q22, with weak hybridization to
1p35-p36. They concluded that band 1q21 is the most likely location of
the IVL gene. Simon et al. (1989) presented the data for mapping of the
IVL gene. They also described a PstI RFLP, which they demonstrated in 1
individual to be the absence of 39 repeats that make up two-thirds of
the coding region of the IVL gene. Simon et al. (1991) gave further
information on the polymorphism in the coding region in the involucrin
gene in higher primates, which results from the variable number of
tandem repeats (VNTR) of a 10-codon sequence. Confirmation of the
localization of the IVL gene to 1q21 was provided by Volz et al. (1993),
who demonstrated physical linkage within 2.05 Mb of DNA to several other
genes involved in epidermal differentiation and known to be located in
that area.
*FIELD* RF
1. Djian, P.; Delhomme, B.; Green, H.: Origin of the polymorphism
of the involucrin gene in Asians. Am. J. Hum. Genet. 56: 1367-1372,
1995.
2. Eckert, R. L.; Green, H.: Structure and evolution of the human
involucrin gene. Cell 46: 583-589, 1986.
3. Green, H.: Human genetic diseases due to codon reiteration: relationship
to an evolutionary mechanism. Cell 74: 955-956, 1993.
4. Green, H.; Djian, P.: Consecutive actions of different gene-altering
mechanisms in the evolution of involucrin. Molec. Biol. Evol. 9:
977-1017, 1992.
5. Lopez-Bayghen, E.; Vega, A.; Cadena, A.; Granados, S. E.; Jave,
L. F.; Gariglio, P.; Alvarez-Salas, L. M.: Transcriptional analysis
of the 5-prime-noncoding region of the human involucrin gene. J.
Biol. Chem. 271: 512-520, 1996.
6. Simon, M.; Phillips, M.; Green, H.: Polymorphism due to variable
number of repeats in the human involucrin gene. Genomics 9: 576-580,
1991.
7. Simon, M.; Phillips, M.; Green, H.; Stroh, H.; Glatt, K.; Burns,
G.; Latt, S. A.: Absence of a single repeat from the coding region
of the human involucrin gene leading to RFLP. Am. J. Hum. Genet. 45:
910-916, 1989.
8. Stroh, H.; Tseng, H.; Harris, P.; Bruns, G.; Green, H.; Latt, S.
A.: Chromosomal mapping of the human involucrin gene (IVL). (Abstract) Cytogenet.
Cell Genet. 46: 700 only, 1987.
9. Teumer, J.; Green, H.: Divergent evolution of part of the involucrin
gene in the hominoids: unique intragenic duplications in the gorilla
and human. Proc. Nat. Acad. Sci. 86: 1283-1286, 1989.
10. Urquhart, A.; Gill, P.: Tandem-repeat internal mapping (TRIM)
of the involucrin gene: repeat number and repeat-pattern polymorphism
within a coding region in human populations. Am. J. Hum. Genet. 53:
279-286, 1993.
11. Volz, A.; Korge, B. P.; Compton, J. G.; Ziegler, A.; Steinert,
P. M.; Mischke, D.: Physical mapping of a functional cluster of epidermal
differentiation genes on chromosome 1q21. Genomics 18: 92-99, 1993.
*FIELD* CN
Alan F. Scott - updated: 9/24/1996
*FIELD* CD
Victor A. McKusick: 10/16/1986
*FIELD* ED
carol: 01/17/2014
mark: 9/24/1996
mark: 7/18/1995
carol: 5/16/1994
terry: 5/10/1994
carol: 10/19/1993
carol: 10/14/1993
carol: 1/4/1993