ID   INVO_RAT                Reviewed;         568 AA.
AC   P48998;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Involucrin;
GN   Name=Ivl;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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; L28818; AAA41445.1; -; Genomic_DNA.
DR   PIR; I61106; I61106.
DR   RefSeq; NP_071531.1; NM_022195.1.
DR   AlphaFoldDB; P48998; -.
DR   STRING; 10116.ENSRNOP00000012343; -.
DR   iPTMnet; P48998; -.
DR   PhosphoSitePlus; P48998; -.
DR   PaxDb; P48998; -.
DR   GeneID; 60583; -.
DR   KEGG; rno:60583; -.
DR   UCSC; RGD:620141; rat.
DR   CTD; 3713; -.
DR   RGD; 620141; Ivl.
DR   eggNOG; ENOG502REJ9; Eukaryota.
DR   InParanoid; P48998; -.
DR   OrthoDB; 1543299at2759; -.
DR   PhylomeDB; P48998; -.
DR   PRO; PR:P48998; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR   GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR   GO; GO:0018149; P:peptide cross-linking; ISO:RGD.
DR   GO; GO:0010224; P:response to UV-B; ISO:RGD.
DR   InterPro; IPR009733; Involucrin2.
DR   InterPro; IPR019743; Involucrin_CS.
DR   InterPro; IPR019571; Involucrin_N.
DR   Pfam; PF06994; Involucrin2; 10.
DR   Pfam; PF10583; Involucrin_N; 1.
DR   PROSITE; PS00795; INVOLUCRIN; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Keratinization; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..568
FT                   /note="Involucrin"
FT                   /id="PRO_0000159743"
FT   REGION          23..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..331
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..450
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..499
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..555
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         472
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   568 AA;  67021 MW;  E2B07740FE779345 CRC64;
     MSHQHTVPVT VPAVVQESLK TVCSPAQTQQ EQTKQPTPYP AQCQVFTDTQ EKGFPKHEEK
     EANPVKDLPE QESEHHQQPG PQKQQLQVKK PEQELQEQEL HSEKQPQEPQ GLLCLGQQQQ
     REPQEQEQHL RQHQQPQQES QGQGLCLGQQ QDVLAPQELH MGQHQKEKLQ EPELPLGQQQ
     KTPEEQELIL GEKQQKLHLV ERHQEPQEQE LHHGQKQKQQ QPQEQELQLV QHQKQKQHEP
     ELCLRKQQQQ ESHERELHLG KQQQQESHEP ELHLGKQQHQ ESHEPELHLG KQQHQESCEP
     ELHLGEQQHQ EQQQHQESCE PELHLGKQQH QETQESELQL GKQQKPHEPD MVLDPKEKQK
     LHDPELHLGK QQHQESQESE LQVEKKQHEK SPEPELHLGK QQELHEPDMT EDQKEKQSLH
     EPELHLGKQQ ESHEPDMTED QKEKQSLYEP ELHLGKQQEQ QIEYEGYQRS KSLNQLLKQE
     KASRGQELDD SHLEQEKELL DQRLDQELVN KDEQLERKKH KLENLTQKEK QIKQLVPSTD
     RVQETQPIQP VKEDSLTTKK QQHSHEVQ