ID   INVO_TUPGL              Reviewed;         400 AA.
AC   Q95337;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Involucrin;
GN   Name=IVL;
OS   Tupaia glis (Common tree shrew) (Sorex glis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX   NCBI_TaxID=9395;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9073063; DOI=10.1016/s0378-1119(96)00654-3;
RA   Phillips M., Rice R.H., Djian P., Green H.;
RT   "The involucrin gene of the tree shrew: recent repeat additions and the
RT   relocation of cysteine codons.";
RL   Gene 187:29-34(1997).
CC   -!- FUNCTION: Part of the insoluble cornified cell envelope (CE) of
CC       stratified squamous epithelia. {ECO:0000250}.
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. {ECO:0000250}.
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 molecules
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the involucrin family. {ECO:0000305}.
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DR   EMBL; U65922; AAC48703.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q95337; -.
DR   SMR; Q95337; -.
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; 6.
DR   Pfam; PF10583; Involucrin_N; 1.
DR   PROSITE; PS00795; INVOLUCRIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Keratinization; Repeat.
FT   CHAIN           1..400
FT                   /note="Involucrin"
FT                   /id="PRO_0000260314"
FT   REGION          1..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          273..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   400 AA;  47399 MW;  D10804D455595C06 CRC64;
     MSQQHTLPVT LPAALSQEPL KTVSPPPNTQ QEHTKQPTPL PAPCQEVPSE LPVEDPSKHK
     EKHTTPVKGV PEQEHELQQQ QDSQEQELHL GQQQQQQEYQ EQELHLGQQQ QQQEYQEQEL
     HLGQQQQQEY QEQELHLGQH QQQTSQEQKL HLGQQQQHQE SQEQKLHLEQ QQQEPQKQEL
     HLGQQEAQEE ELHLKQQQQE CQKEEVHLEQ QQQECQKEEV HLEQQQQECQ KEEVHLEQQQ
     QECQKEEVHL EQQQQECQKE EVHLEQQQQE CQKEEVHLEQ QQQETQELQQ HQGAGILEQK
     LHQEKAQSEQ QLKGQLDWEE KLLDQQLEQE LAKRDEQLGK KEEQLLEPSE QQEGLLEQPT
     LVPAPSQLHE NQAAQVPKGE VLLPIEQQRQ QEVQWPVKHK