ID   INVO_HYLLA              Reviewed;         522 AA.
AC   P17941;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Involucrin;
GN   Name=IVL;
OS   Hylobates lar (Common gibbon) (White-handed gibbon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Hylobates.
OX   NCBI_TaxID=9580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2359362; DOI=10.1093/oxfordjournals.molbev.a040601;
RA   Djian P., Green H.;
RT   "The involucrin gene of the gibbon: the middle region shared by the
RT   hominoids.";
RL   Mol. Biol. Evol. 7:220-227(1990).
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       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Constituent of the scaffolding of
CC       the cornified envelope.
CC   -!- TISSUE SPECIFICITY: Keratinocytes of epidermis and other stratified
CC       squamous epithelia.
CC   -!- PTM: Substrate of transglutaminase. Specific glutamines or lysines are
CC       cross-linked to keratins, desmoplakin and to inter involucrin
CC       molecules.
CC   -!- SIMILARITY: Belongs to the involucrin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M35447; AAA35456.1; -; Genomic_DNA.
DR   PIR; I37037; I37037.
DR   AlphaFoldDB; P17941; -.
DR   SMR; P17941; -.
DR   GO; GO:0001533; C:cornified envelope; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR   GO; GO:0030216; P:keratinocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0018149; P:peptide cross-linking; ISS:UniProtKB.
DR   GO; GO:0010224; P:response to UV-B; ISS:UniProtKB.
DR   InterPro; IPR019743; Involucrin_CS.
DR   InterPro; IPR019571; Involucrin_N.
DR   InterPro; IPR000354; Involucrin_rpt.
DR   Pfam; PF00904; Involucrin; 33.
DR   Pfam; PF10583; Involucrin_N; 1.
DR   PROSITE; PS00795; INVOLUCRIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Keratinization; Repeat.
FT   CHAIN           1..522
FT                   /note="Involucrin"
FT                   /id="PRO_0000159737"
FT   REGION          1..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..194
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..419
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..461
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  61045 MW;  87B0EC98E049B568 CRC64;
     MSQQHTLPVT LSPALSQELL KTVPPPVNTQ QEQMKQPTPL PPPCQKVLGE LPVEVPSKQE
     EKHMTTVKGL PEQECEQQQQ EPQEQELQQQ HWEQHEEHQK AENPEQQLKQ EKAQRDQQLN
     EHLEEEKKLL DQQLNQELIK RDEQLGIKKE QLLELTEQQE GQLEHLEQQE GQLELPEQQE
     GQLEHLEQQE GQLKHLDQQG KQPELPEQQV AQLKHLEQQE GQLKHLEHQK GELQVPEEQV
     GQLKYLEQQE GQLKHLDQQE KQPELPEQQV GQLKHLEQQE GQLEHMEHQE GQLGLPEQQV
     GQLKQLEEQE GQPKHLEEEE GQLKHLVQQE GQLEHLVQQE RQLEQQEGKV QHLEQQVEQL
     KHLEEQEGQL KHLEQQQGQL EVSEQQVGQP KHLEQEGKQL ELPEQQEGQL KHLEKQEAQL
     ELPEQQVGQP KHPEQQEKQL EHPEQQEGQL KHLEQQEGQL KDLEQQKGQL EQQQGQLEQP
     VFAPAPGQVQ DIQPVLPTKG EALLPVEQQQ QKQEVQWPPK HK