INVO_PIG
ID INVO_PIG Reviewed; 347 AA.
AC P18175;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Involucrin;
GN Name=IVL;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2385171; DOI=10.1093/oxfordjournals.molbev.a040609;
RA Tseng H., Green H.;
RT "The involucrin genes of pig and dog: comparison of their segments of
RT repeats with those of prosimians and higher primates.";
RL Mol. Biol. Evol. 7:293-302(1990).
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; M34441; AAA31058.1; -; Genomic_DNA.
DR PIR; I46592; I46592.
DR RefSeq; NP_999613.1; NM_214448.1.
DR AlphaFoldDB; P18175; -.
DR STRING; 9823.ENSSSCP00000007032; -.
DR PaxDb; P18175; -.
DR GeneID; 407242; -.
DR KEGG; ssc:407242; -.
DR CTD; 3713; -.
DR eggNOG; ENOG502S84Y; Eukaryota.
DR InParanoid; P18175; -.
DR OrthoDB; 1609954at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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; 6.
DR Pfam; PF10583; Involucrin_N; 1.
DR PROSITE; PS00795; INVOLUCRIN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Keratinization; Reference proteome; Repeat.
FT CHAIN 1..347
FT /note="Involucrin"
FT /id="PRO_0000159741"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 347 AA; 41408 MW; 3DE579871CF1C829 CRC64;
MSQQYTLPVT LPPALSQEPL KPVSPPADTQ QEQVKQATPL PAPCQKMLSE LPVEVPLEDA
EKHTTLVKGV PEQECEPQPQ EPQQQELHVE QQQQQQESQV QELHVDQQQQ QQESQEQELH
VDQQQQQQES QEQELHVDQQ QQQESQVQEL HVGHHQQQQE SQEQELHVDH HQQQQESQEQ
ELHVDQQQQQ QESQEQELHV DQQQQQQESQ EQELHVDHHQ QQQESQVQEL HVDHQQQQQE
SQEQELHVDQ HQQQQESQEQ ELHVDQQQQE LQVQEVQQQQ QQQQEQQEDH QKAEHLEQEE
AQREQQLKGQ LEQEKKGVYQ HLDQELTKRD EHLEKKGEHC WSSRRSL