SPR1A_RAT
ID SPR1A_RAT Reviewed; 152 AA.
AC Q63532;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Cornifin-A;
DE AltName: Full=Small proline-rich protein 1A;
DE Short=SPR1A;
DE Short=SPRR1;
GN Name=Sprr1a; Synonyms=Spr, Sprr1;
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=Fischer 344/N; TISSUE=Nasal vestibule;
RX PubMed=8624253; DOI=10.1165/ajrcmb.14.5.8624253;
RA Tesfaigzi J., Th'ng J., Hotchkiss J.A., Harkema J.R., Wright P.S.;
RT "A small proline-rich protein, SPRR1, is upregulated early during tobacco
RT smoke-induced squamous metaplasia in rat nasal epithelia.";
RL Am. J. Respir. Cell Mol. Biol. 14:478-486(1996).
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: In squamous epithelia lining the nasal vestibule
CC and in the hard palate.
CC -!- INDUCTION: During squamous metaplasia induced by cigarette smoke
CC exposure.
CC -!- SIMILARITY: Belongs to the cornifin (SPRR) family. {ECO:0000305}.
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DR EMBL; L46593; AAC42092.1; -; Genomic_DNA.
DR AlphaFoldDB; Q63532; -.
DR STRING; 10116.ENSRNOP00000012174; -.
DR PaxDb; Q63532; -.
DR PRIDE; Q63532; -.
DR RGD; 1593163; Sprr1a.
DR eggNOG; ENOG502SCIR; Eukaryota.
DR InParanoid; Q63532; -.
DR PhylomeDB; Q63532; -.
DR PRO; PR:Q63532; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030280; F:structural constituent of skin epidermis; 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 InterPro; IPR003302; SPRR1/SPRR3.
DR PANTHER; PTHR23263:SF28; PTHR23263:SF28; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Keratinization; Reference proteome; Repeat.
FT CHAIN 1..152
FT /note="Cornifin-A"
FT /id="PRO_0000149999"
FT REPEAT 27..34
FT /note="1"
FT REPEAT 35..42
FT /note="2"
FT REPEAT 43..49
FT /note="3"
FT REPEAT 50..57
FT /note="4"
FT REPEAT 58..65
FT /note="5"
FT REPEAT 66..73
FT /note="6"
FT REPEAT 74..81
FT /note="7"
FT REPEAT 82..89
FT /note="8"
FT REPEAT 90..97
FT /note="9"
FT REPEAT 98..105
FT /note="10"
FT REPEAT 106..113
FT /note="11"
FT REPEAT 114..121
FT /note="12"
FT REPEAT 122..129
FT /note="13"
FT REPEAT 130..137
FT /note="14"
FT REGION 20..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 27..137
FT /note="14 X 8 AA approximate tandem repeats"
FT COMPBIAS 25..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 152 AA; 16734 MW; C8BD2865F69707F9 CRC64;
MSSQQQKQPC TVPPQLHQHE VKQPCQPPPQ EPCAPKTKEP CHPIPEPCNP KVPEPCQPKV
PEPCQPKVPE PCQPKVPEPC QPKVPEPCQP KVPEPCQPKV PEPCHPKAPE PCHPVVPEPC
QPVAPEPCQP VVPEPCPPTV TPSPYQQKTK QK
