SPRR1_RABIT
ID SPRR1_RABIT Reviewed; 126 AA.
AC P35324;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Cornifin alpha;
DE AltName: Full=Small proline-rich protein I;
DE Short=SPR-I;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Trachea;
RX PubMed=1438308; DOI=10.1073/pnas.89.22.11026;
RA Marvin K.W., George M.D., Fujimoto W., Saunders N.A., Bernacki S.H.,
RA Jetten A.M.;
RT "Cornifin, a cross-linked envelope precursor in keratinocytes that is down-
RT regulated by retinoids.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11026-11030(1992).
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: Suprabasal layers of squamous-differentiated
CC tissues such as epidermis, esophagus, tongue and trachea.
CC -!- DEVELOPMENTAL STAGE: Expressed during differentiation of squamous
CC cells.
CC -!- INDUCTION: During squamous differentiation of epidermal keratinocytes.
CC This induction is repressed by retinoids.
CC -!- SIMILARITY: Belongs to the cornifin (SPRR) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A46375; A46375.
DR AlphaFoldDB; P35324; -.
DR STRING; 9986.ENSOCUP00000025830; -.
DR PRIDE; P35324; -.
DR Ensembl; ENSOCUT00000027006; ENSOCUP00000025830; ENSOCUG00000026830.
DR eggNOG; ENOG502SCIR; Eukaryota.
DR GeneTree; ENSGT00940000163019; -.
DR Proteomes; UP000001811; Chromosome 13.
DR Bgee; ENSOCUG00000026830; Expressed in skin of back and 13 other tissues.
DR ExpressionAtlas; P35324; baseline.
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; 1.
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..126
FT /note="Cornifin alpha"
FT /id="PRO_0000150002"
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..86
FT /note="7"
FT REPEAT 87..94
FT /note="8"
FT REPEAT 95..102
FT /note="9"
FT REPEAT 103..110
FT /note="10"
FT REPEAT 111..118
FT /note="11"
FT REGION 3..29
FT /note="2 X 12 AA approximate repeats"
FT REGION 20..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..122
FT /note="11 X 8 AA approximate tandem repeats"
FT REGION 104..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..43
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 126 AA; 14044 MW; 01834CF39B854929 CRC64;
MSSQQQKQPC TLPPQLQQHQ VKQPCQPPPQ EPCVPKTKEP CQPKVPEPCQ PKVPEPCQPK
VPEPCQPKVP QPCQPKVPEP CQPKVPEPCQ PKVPEPCQPK VPEPCQSKVP QPCQPKVPEP
CQTKQK
