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INVO_LEMCA
ID   INVO_LEMCA              Reviewed;         450 AA.
AC   P14590;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Involucrin;
GN   Name=IVL;
OS   Lemur catta (Ring-tailed lemur).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Lemuridae; Lemur.
OX   NCBI_TaxID=9447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3401924; DOI=10.1016/0092-8674(88)90070-0;
RA   Tseng H., Green H.;
RT   "Remodeling of the involucrin gene during primate evolution.";
RL   Cell 54:491-496(1988).
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; M21864; AAA36826.1; -; Genomic_DNA.
DR   PIR; A43733; A43733.
DR   AlphaFoldDB; P14590; -.
DR   SMR; P14590; -.
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; 9.
DR   Pfam; PF10583; Involucrin_N; 1.
DR   PROSITE; PS00795; INVOLUCRIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Keratinization; Repeat.
FT   CHAIN           1..450
FT                   /note="Involucrin"
FT                   /id="PRO_0000159738"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..278
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..370
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   450 AA;  50445 MW;  9F81B7328DD0410D CRC64;
     MSQQHTLPVT LPPTLSQELL KNVSPPADIQ QEQRKQPTPL PAPCQKVLSE LPVAVPSKHE
     EKHATPVKGL LEQECGQLQQ QEPQEQEVHL AKHQELQELQ EQELHLGKQP EPQEQELHLG
     KQQQQQESQE QELYLGKQPE PQDQELHLGK QQAPQEQELH LGKQPEPQEQ ELHLGKQPEP
     QDQELYLGKR LEPQEQELHL GKQQQQQESQ EQELDLGKQP EPQDQELHLG KQQAPQEQEL
     HLGKQPEPQE QELHLVKQQE PQDQELHLGK RLEPQEQELH LGKQQQPQEQ KLHPGEAAAA
     GVTGAGPAAS KAARRATGAG TAPGKAAAAA GATGAGTAAT APATAEERQK AESLEQQLEQ
     EKAQREEQLK EQLEEKKRIL DQQLDQEVAK RYEQLGVKKE QLLQPLGQQE GQLEKPVFVP
     APGQVQDIQP PQPPKGEVLL PAEQQQEPEV
 
 
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