ID   INVO_CANLF              Reviewed;         285 AA.
AC   P18174;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Involucrin;
GN   Name=IVL;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2385171; DOI=10.1093/oxfordjournals.molbev.a040609;
RA   Tseng H., Green H.;
RT   "The involucrin genes of pig and dog: comparison of their segments of
RT   repeats with those of prosimians and higher primates.";
RL   Mol. Biol. Evol. 7:293-302(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; M34442; AAA30853.1; -; Genomic_DNA.
DR   PIR; I46207; I46207.
DR   AlphaFoldDB; P18174; -.
DR   SMR; P18174; -.
DR   STRING; 9612.ENSCAFP00000032077; -.
DR   PaxDb; P18174; -.
DR   eggNOG; ENOG502S84Y; Eukaryota.
DR   InParanoid; P18174; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR   InterPro; IPR019743; Involucrin_CS.
DR   InterPro; IPR019571; Involucrin_N.
DR   Pfam; PF10583; Involucrin_N; 1.
DR   PROSITE; PS00795; INVOLUCRIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Keratinization; Reference proteome; Repeat.
FT   CHAIN           1..285
FT                   /note="Involucrin"
FT                   /id="PRO_0000159733"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   285 AA;  33384 MW;  DCE1BD88B9248BEA CRC64;
     MSQQHTLPVT LPPALSQGPL KPESPPIDTQ QEQVKQPTSL PVLCQKMPSS LPGKVPLGHG
     EKHTSLVKGE PEQQCEPQEQ EQQQKQQESQ EQKLHLEQCL EQHQEQQESQ DQKLYPEQCL
     EQQQEQQESQ DQKLYPEQCL EQQQEQQESQ EKELHLEQEQ QKEELQQQEQ QQGKEQCEKH
     QEAKNLEQQL EQIGAQRKQQ QKEQLEQEKK LVDQHLDQEP AQRTEQPEKK EEQVLEQQGQ
     QEGQLEQPAF VPAQVQVREP LKGEVLPLIE QQHQKQEVHD PPEHQ