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