INVO_CEBAL
ID INVO_CEBAL Reviewed; 428 AA.
AC P24709;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Involucrin;
GN Name=IVL;
OS Cebus albifrons (White-fronted capuchin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Cebinae; Cebus.
OX NCBI_TaxID=9514;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Esophageal 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}.
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DR EMBL; M67478; AAA35405.1; -; Genomic_DNA.
DR PIR; I36930; I36930.
DR AlphaFoldDB; P24709; -.
DR SMR; P24709; -.
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; 22.
DR Pfam; PF10583; Involucrin_N; 1.
DR PROSITE; PS00795; INVOLUCRIN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Keratinization; Repeat.
FT CHAIN 1..428
FT /note="Involucrin"
FT /id="PRO_0000159734"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 50126 MW; 03AB71A5FC34E802 CRC64;
MSQQHTLPVT LPPALSQELL NTVPPPINTQ QEQREQPVPL PPPCQKVPVE LPVEGPSKHE
EKHVTIVKGV PEHECEQQQQ AQGQERQQQH WGQNKEHQKA GNPEQQLKQE EAQREKQQLQ
GQLEEEKKLL DQQLDQELAK RDDQLGTKKK QLLEFPEQQE GQLKHLEQQE KPLELPEQQS
GQPKYLEQQE GQLKHLEEQK GQLKHLEQQE GQLELPEQVD QPKHLEQLEK QLEHPEQQEG
KLKKLEEEEE QLKHLEQQEE QLKHLEQQEG QLEHLEQQEG ELKHLEQCEG QLEHLEQQEG
QLELPEQQVG QSKHLEQEEK QLEHPEQQEG QLKHLGKQEA QLELPEQVGQ PKHLEQQEKQ
LEHPEQQEEQ QEGQLKDLEQ QERQLEQPVF APAPGQAQDI QQALPSKGEV LLPVDQQQQK
QEVQWQQK