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