ID   INVO_SAGOE              Reviewed;         493 AA.
AC   P24712;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Involucrin;
GN   Name=IVL;
OS   Saguinus oedipus (Cotton-top tamarin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Saguinus.
OX   NCBI_TaxID=9490;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Vaginal fibroblast;
RX   PubMed=1766360; DOI=10.1093/oxfordjournals.molbev.a040674;
RA   Phillips M., Rice R.H., Djian P., Green H.;
RT   "The involucrin genes of the white-fronted capuchin and cottontop tamarin:
RT   the platyrrhine middle region.";
RL   Mol. Biol. Evol. 8:579-591(1991).
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; M67477; AAA36950.1; -; Genomic_DNA.
DR   PIR; A57783; A57783.
DR   AlphaFoldDB; P24712; -.
DR   PRIDE; P24712; -.
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; 30.
DR   Pfam; PF10583; Involucrin_N; 1.
DR   PROSITE; PS00795; INVOLUCRIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Keratinization; Repeat.
FT   CHAIN           1..493
FT                   /note="Involucrin"
FT                   /id="PRO_0000159744"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          60..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..360
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  57920 MW;  A626FC4E7799AEC9 CRC64;
     MSQQHTLPVT LPAALSQKLL DTVPPPVNTQ QEQRKQPAPL PPPCQKVPVE LPVEVLSKHE
     EKHMTIVKGV PEQECEQQQP QEQELQQQHW EQDKEHQKAE NPEQQLKQEK VQREKQQLQG
     QLEEEKKLLD QQLDQELAKR DEQLGTKKEQ LLEFPEQQEG QLKHLEQEEG HLELPEQQEG
     QLKNLEHQEK PLELPEQQEG QLKHLEQQEK PLELPEQQEG QLKHLEQQEG QSELPEQQRG
     QPKYLEQEEG QLKHLEEQKG QLKHLEHEEG QLELPEQVGQ PKHLEQLEKQ LEHPEQQEGQ
     LKHLEEEEGQ VKHLGEQEEQ LKHLEQQEEQ LKHLEQQEGQ LEHLEQQEGQ LKHLEQHEGQ
     LELPEQQVGQ SKHLEQEEKQ LEHPEQQEGQ LKHLGKQKAQ LELTEQVGQP KHLEQQEKQL
     EHPQQQEEQL KPQEQQEGQL KDLEQQERQL EQPVFASAPG QVQDIQQALP PKGEVLLPVE
     QQQQKQEVQG QHE