SPRR1_PIG
ID SPRR1_PIG Reviewed; 97 AA.
AC P35323;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Cornifin;
DE AltName: Full=SPRP;
DE AltName: Full=Small proline-rich protein I;
DE Short=SPR-I;
DE AltName: Full=Small proline-rich squamous cell marker;
GN Name=SPRP;
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 [MRNA].
RC TISSUE=Trachea;
RX PubMed=8398182; DOI=10.1165/ajrcmb/9.4.434;
RA Tesfaigzi J., Wright P.S., Oreffo V., An G., Wu R., Carlson D.M.;
RT "A small proline-rich protein regulated by vitamin A in tracheal epithelial
RT cells is induced in lung tumors.";
RL Am. J. Respir. Cell Mol. Biol. 9:434-440(1993).
CC -!- FUNCTION: Cross-linked envelope protein of keratinocytes. It is a
CC keratinocyte protein that first appears in the cell cytosol, but
CC ultimately becomes cross-linked to membrane proteins by
CC transglutaminase. All that results in the formation of an insoluble
CC envelope beneath the plasma membrane.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Not detected in normal lung tissue but seen in
CC tumor tissues. Cells around the keratin pearls contain high levels.
CC -!- INDUCTION: During squamous differentiation of epidermal keratinocytes.
CC -!- SIMILARITY: Belongs to the cornifin (SPRR) family. {ECO:0000305}.
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DR EMBL; M88166; AAA03608.1; -; mRNA.
DR PIR; I51926; I51926.
DR AlphaFoldDB; P35323; -.
DR STRING; 9823.ENSSSCP00000027207; -.
DR PaxDb; P35323; -.
DR PeptideAtlas; P35323; -.
DR eggNOG; ENOG502SCIR; Eukaryota.
DR InParanoid; P35323; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0018149; P:peptide cross-linking; IEA:InterPro.
DR InterPro; IPR003302; SPRR1/SPRR3.
DR PANTHER; PTHR23263:SF28; PTHR23263:SF28; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Keratinization; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC9"
FT CHAIN 2..97
FT /note="Cornifin"
FT /id="PRO_0000150001"
FT REPEAT 3..14
FT /note="1"
FT REPEAT 18..29
FT /note="2"
FT REPEAT 31..38
FT /note="1"
FT REPEAT 39..46
FT /note="2"
FT REPEAT 47..54
FT /note="3"
FT REPEAT 55..62
FT /note="4"
FT REPEAT 63..70
FT /note="5"
FT REPEAT 71..78
FT /note="6"
FT REPEAT 79..85
FT /note="7"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3..29
FT /note="2 X 12 AA approximate repeats"
FT REGION 31..85
FT /note="7 X 8 AA approximate tandem repeats"
FT COMPBIAS 9..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC9"
SQ SEQUENCE 97 AA; 10724 MW; 3C5B1077F2F37282 CRC64;
MSSQQQKQPC TPPPQPQQQQ VKQPCQPPPQ EPCVPKTKEP CHPKVPEPCQ PKVPEPCQPK
VPEPCHPKVP EPCQPKVPEP CPSPVIPAPA QQKTKQK
