ID   INVO_OTOCR              Reviewed;         384 AA.
AC   P24710;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Involucrin;
GN   Name=IVL;
OS   Otolemur crassicaudatus (Brown greater galago) (Galago crassicaudatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=9463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Skin fibroblast;
RX   PubMed=2335506; DOI=10.1016/s0021-9258(19)39000-3;
RA   Phillips M., Djian P., Green H.;
RT   "The involucrin gene of the galago. Existence of a correction process
RT   acting on its segment of repeats.";
RL   J. Biol. Chem. 265:7804-7807(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}.
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DR   EMBL; J05437; AAA35450.1; -; Genomic_DNA.
DR   PIR; A43710; A43710.
DR   AlphaFoldDB; P24710; -.
DR   PRIDE; P24710; -.
DR   GO; GO:0001533; C:cornified envelope; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR   InterPro; IPR009733; Involucrin2.
DR   InterPro; IPR019743; Involucrin_CS.
DR   InterPro; IPR019571; Involucrin_N.
DR   Pfam; PF06994; Involucrin2; 4.
DR   Pfam; PF10583; Involucrin_N; 1.
DR   PROSITE; PS00795; INVOLUCRIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Keratinization; Repeat.
FT   CHAIN           1..384
FT                   /note="Involucrin"
FT                   /id="PRO_0000159735"
FT   REGION          1..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   384 AA;  44059 MW;  DE7F0AED4D492D6E CRC64;
     MSQQHTLPVT LPPALRQELL GTLSPPAAAQ QEQRKQPTPL PTACQKVGSE LPGEVPSKHE
     EKGTDPVKGV LEQECGQQEP ELHLGKQQDV HLMKRQDPQE PELHLGKQPE PEGPEPHLGK
     EQQHQESQDP ELHLGKQQQQ ESQEQELYPG KQQEPQDPEL HLGKQQQQES QEQGLCLIKQ
     REPQESQEQR LHLGKEQESQ EQRLHLGEEQ ASQEQRLHLG EEQASQEQRL HLGEEQASPE
     QRLQLLPQGP QEQELHLGKQ QQQQESQQHQ EQHEEHQKAE DLGQQHRQEK AQREQQLEEQ
     LDEGKKLLDQ QLDQEAVKRH EQLQRDEQFG MKKEQLLEPP GQQKGQLEKP VFVPVPGQVQ
     DIQPAQTAKG EALLLPEQPQ EPEV