ID   INVO_MOUSE              Reviewed;         467 AA.
AC   P48997;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Involucrin;
GN   Name=Ivl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NIH Swiss;
RX   PubMed=8277848; DOI=10.1093/oxfordjournals.molbev.a040069;
RA   Djian P., Phillips M., Easley K., Huang E., Simon M., Rice R.H., Green H.;
RT   "The involucrin genes of the mouse and the rat: study of their shared
RT   repeats.";
RL   Mol. Biol. Evol. 10:1136-1149(1993).
RN   [2]
RP   INTERACTION WITH INVOLUCRIN.
RX   PubMed=15147942; DOI=10.1016/j.bbrc.2004.04.109;
RA   Michibata H., Chiba H., Wakimoto K., Seishima M., Kawasaki S., Okubo K.,
RA   Mitsui H., Torii H., Imai Y.;
RT   "Identification and characterization of a novel component of the cornified
RT   envelope, cornifelin.";
RL   Biochem. Biophys. Res. Commun. 318:803-813(2004).
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   -!- 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; L28819; AAA39330.1; -; Genomic_DNA.
DR   PIR; A49377; A49377.
DR   AlphaFoldDB; P48997; -.
DR   STRING; 10090.ENSMUSP00000059780; -.
DR   iPTMnet; P48997; -.
DR   PhosphoSitePlus; P48997; -.
DR   MaxQB; P48997; -.
DR   PaxDb; P48997; -.
DR   PRIDE; P48997; -.
DR   ProteomicsDB; 266997; -.
DR   MGI; MGI:96626; Ivl.
DR   eggNOG; ENOG502REJ9; Eukaryota.
DR   InParanoid; P48997; -.
DR   PhylomeDB; P48997; -.
DR   PRO; PR:P48997; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P48997; protein.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR   GO; GO:0030216; P:keratinocyte differentiation; ISO:MGI.
DR   GO; GO:0018149; P:peptide cross-linking; ISO:MGI.
DR   GO; GO:0002786; P:regulation of antibacterial peptide production; IGI:MGI.
DR   GO; GO:0010224; P:response to UV-B; ISO:MGI.
DR   InterPro; IPR009733; Involucrin2.
DR   InterPro; IPR019743; Involucrin_CS.
DR   InterPro; IPR019571; Involucrin_N.
DR   Pfam; PF06994; Involucrin2; 6.
DR   Pfam; PF10583; Involucrin_N; 1.
DR   PROSITE; PS00795; INVOLUCRIN; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Keratinization; Reference proteome; Repeat.
FT   CHAIN           1..467
FT                   /note="Involucrin"
FT                   /id="PRO_0000159739"
FT   REGION          48..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   467 AA;  54919 MW;  603E1E51B435737D CRC64;
     MSHQHTLPVT VPAVVQGPLK TVCSPDHIQQ EQAKQPTPHP TQCQVFTEIQ EKGFPKHEEK
     RPNPVKDLPD QKCEHQQQPG PQKQQLQVKK SQQELQEQEL HLEKQQLPQE PQGLLCLEQQ
     QQQEPQMQEQ HLRQQQQQQQ QQQQQQQQQQ QQETQEQGLC LGQKQQQQQQ DMLVPQELHL
     RQHQEKLQDP ELHLGQQQKT PEEQKLIPGE KQQELHLGQR HQEPQEQELH LGQKQKQKLH
     EPELQLGKQQ HQKPSEPELP LGKQQQESPE PELPLGKQQQ QESPEPELQL GKQQQSHEPD
     MAGDQKEKQK LHKPELYLRK QQYQESPDPE LSLGKQQHQE CQEPELQLEE KQHQKPPEPE
     LHLGKQQESH EPDMAEDLEE KQKLGEPELH LGKQQQQQIE REGYQGPKSL GQSLKQEKAS
     REQQLDYSHL EQEKELSDQP LDQALVKKGK QLERKKHELE NRTQQEK