INVO_AOTTR
ID INVO_AOTTR Reviewed; 544 AA.
AC P24708;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Involucrin;
GN Name=IVL;
OS Aotus trivirgatus (Three-striped night monkey) (Douroucouli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=9505;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2507864; DOI=10.1093/oxfordjournals.molbev.a040563;
RA Tseng H., Green H.;
RT "The involucrin gene of the owl monkey: origin of the early region.";
RL Mol. Biol. Evol. 6:460-468(1989).
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; M25313; AAA35375.1; -; Genomic_DNA.
DR PIR; I36911; I36911.
DR AlphaFoldDB; P24708; -.
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; 36.
DR Pfam; PF10583; Involucrin_N; 1.
DR PROSITE; PS00795; INVOLUCRIN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Keratinization; Repeat.
FT CHAIN 1..544
FT /note="Involucrin"
FT /id="PRO_0000159732"
FT REGION 1..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 63926 MW; 2A02ABA5E1499F9D CRC64;
MSQQHTLPVT LPPALSQELL DTVPPPVNTQ QEQRKQPAAL PPPCQEVPVE LPVEGPSKHE
EKHMTIVKGA PEQECEQQQQ PQEQKLQQQH WEQDEEHQKA ENPEQQLKQE KAQREKQQLQ
GQLEEEKKLL DQQPDHELAK SDEQLGTKKE QLLEFPEQQE GQLKCLEQQE GHLELPEQQE
GQLKCLEQQE GHQELPEQQE GQLKHLEQQE GQLKHLEQQE GQVKHLEQQE KQSELPEQQR
GQPKYLEQQE GQLKHLEEQK GQLKHLEHQE GQLELPEQVG QPKHLEQLEK QLEHPEQQEG
QLKQLEEQEG QVKHLEQQEE QLKHLEQQEG QPKHPEQLEK QLEHPEQQEG QLKQLEEQEG
QVKHLEQQEE QLKHLEQQEG QPKHLEQLEK QLEHLEQQEG QLKHLEQREE QLELPEQQVG
QSKHLEQEEK QLEHPEQQEG QLKHLGKQEA QLELPEQVGQ PKHLEQQEKQ LEHPEQQEGQ
LKPQEQQEGQ LKGLEQQERQ LEQPVFAPAP GQVQGIQQAL PPKGEVLLPV EQQQQKQEVQ
WQHK