ID   SPRR1_MACMU             Reviewed;          89 AA.
AC   P35322;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Cornifin;
DE   AltName: Full=Small proline-rich protein I;
DE            Short=SPR-I;
DE   AltName: Full=Small proline-rich squamous cell marker;
GN   Name=SPRR1; Synonyms=SPR1;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Tracheobronchial epithelium;
RX   PubMed=1627333; DOI=10.1165/ajrcmb/7.1.104;
RA   An G., Huang T.H., Tesfaigzi J., Garcia-Heras J., Ledbetter D.H.,
RA   Carlson D.M., Wu R.;
RT   "An unusual expression of a squamous cell marker, small proline-rich
RT   protein gene, in tracheobronchial epithelium: differential regulation and
RT   gene mapping.";
RL   Am. J. Respir. Cell Mol. Biol. 7:104-111(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   -!- INDUCTION: During squamous differentiation of epidermal keratinocytes.
CC   -!- SIMILARITY: Belongs to the cornifin (SPRR) family. {ECO:0000305}.
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DR   EMBL; M83999; AAA36907.1; -; mRNA.
DR   EMBL; S40060; AAB22513.1; -; mRNA.
DR   RefSeq; NP_001028135.1; NM_001032963.1.
DR   AlphaFoldDB; P35322; -.
DR   STRING; 9544.ENSMMUP00000018166; -.
DR   GeneID; 613022; -.
DR   KEGG; mcc:613022; -.
DR   CTD; 6699; -.
DR   eggNOG; ENOG502SCIR; Eukaryota.
DR   HOGENOM; CLU_186226_0_0_1; -.
DR   InParanoid; P35322; -.
DR   OMA; PNPCVPR; -.
DR   OrthoDB; 1613497at2759; -.
DR   TreeFam; TF338205; -.
DR   Proteomes; UP000006718; 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..89
FT                   /note="Cornifin"
FT                   /id="PRO_0000149997"
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   REGION          1..29
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..78
FT                   /note="6 X 8 AA approximate tandem repeats"
FT   REGION          68..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBC9"
SQ   SEQUENCE   89 AA;  9852 MW;  E07D6EF2102EBFD6 CRC64;
     MSSQQQKQPC TPPPQLQQQQ VKQPCQPPPQ EPCIPKTKEP CLPKVPEPCH PKVPEPCQPK
     VPEPCHPKVP EPCPSTVTPA PAQQKTKQK