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INVO_CEPBA
ID   INVO_CEPBA              Reviewed;         387 AA.
AC   P24711;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Involucrin;
GN   Name=IVL;
OS   Cephalopachus bancanus (Western tarsier) (Tarsius bancanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Tarsiiformes; Tarsiidae;
OC   Cephalopachus.
OX   NCBI_TaxID=9477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=1905021; DOI=10.1073/pnas.88.12.5321;
RA   Djian P., Green H.;
RT   "Involucrin gene of tarsioids and other primates: alternatives in evolution
RT   of the segment of repeats.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:5321-5325(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}.
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DR   EMBL; M65124; AAA36960.1; -; Genomic_DNA.
DR   PIR; A43704; A43704.
DR   AlphaFoldDB; P24711; -.
DR   PRIDE; P24711; -.
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; 7.
DR   Pfam; PF10583; Involucrin_N; 1.
DR   PROSITE; PS00795; INVOLUCRIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Keratinization; Repeat.
FT   CHAIN           1..387
FT                   /note="Involucrin"
FT                   /id="PRO_0000159745"
FT   REGION          1..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..119
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   387 AA;  45077 MW;  146BAC2E490AA805 CRC64;
     MSQQQTLPVT LPPALSQELL KTVPPPANTQ QDQMKQPTPS PAPCQKGPSE LPVEKHPAPV
     KQVPEQECEP QQQDHQEPEL QLGRKQQEPQ EQEVHPGKQQ QKPQEQEAHL GKKQEPQGQE
     VHLGKQQQKT QEQEVHLGKQ QQELQEQEVH LEKQLQEPQE VHLEKQLQEQ EVHLEKQLQE
     PEPELNLGKQ QQEPQEQEAY LGKQQQELPE PQDPELHLGK QQQEPQEQEV QLEKQQEAQE
     QELHLGKQQQ ESQEQELHLR KLQQVPQEPQ DQELHLGKQQ QELQEQEVHL GKQLQEPQEQ
     ELHLGRQQQE LQEEEVHLGM KEEQLLKHVE QQEGQLEQQE GQLKQPVCIP TPGQVQDIQP
     AQPPKGEVLL PTEKQQKQEV QWPLKQE
 
 
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