ID   SPRR3_RABIT             Reviewed;         231 AA.
AC   Q28658;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Small proline-rich protein 3;
DE   AltName: Full=Cornifin beta;
GN   Name=SPRR3;
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 [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Trachea;
RX   PubMed=8631988; DOI=10.1074/jbc.271.7.3737;
RA   Austin S.J., Fujimoto W., Marvin K.W., Vollberg T.M., Lorand L.,
RA   Jetten A.M.;
RT   "Cloning and regulation of cornifin beta, a new member of the cornifin/spr
RT   family. Suppression by retinoic acid receptor-selective retinoids.";
RL   J. Biol. Chem. 271:3737-3742(1996).
CC   -!- FUNCTION: Can serve as a substrate in transglutaminase-catalyzed cross
CC       linking reactions and can function as a cross-linked envelope
CC       precursor.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Suprabasal layers of the squamous epithelia of
CC       esophagus, tongue and oral mucosa.
CC   -!- INDUCTION: Suppressed by retinoic acid. RAR-selective retinoid is more
CC       effective than RXR-selective retinoid.
CC   -!- SIMILARITY: Belongs to the cornifin (SPRR) family. {ECO:0000305}.
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DR   EMBL; U40631; AAC48514.1; -; mRNA.
DR   RefSeq; NP_001075835.1; NM_001082366.1.
DR   AlphaFoldDB; Q28658; -.
DR   GeneID; 100009219; -.
DR   KEGG; ocu:100009219; -.
DR   CTD; 6707; -.
DR   InParanoid; Q28658; -.
DR   OrthoDB; 1603381at2759; -.
DR   Proteomes; UP000001811; 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; 5.
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..231
FT                   /note="Small proline-rich protein 3"
FT                   /id="PRO_0000150005"
FT   REPEAT          55..62
FT                   /note="1"
FT   REPEAT          63..70
FT                   /note="2"
FT   REPEAT          71..78
FT                   /note="3"
FT   REPEAT          79..86
FT                   /note="4"
FT   REPEAT          87..94
FT                   /note="5"
FT   REPEAT          95..102
FT                   /note="6"
FT   REPEAT          103..110
FT                   /note="7"
FT   REPEAT          111..118
FT                   /note="8"
FT   REPEAT          119..126
FT                   /note="9"
FT   REPEAT          127..134
FT                   /note="10"
FT   REPEAT          135..142
FT                   /note="11"
FT   REPEAT          143..150
FT                   /note="12"
FT   REPEAT          151..158
FT                   /note="13"
FT   REPEAT          159..166
FT                   /note="14"
FT   REPEAT          167..174
FT                   /note="15"
FT   REPEAT          175..182
FT                   /note="16"
FT   REPEAT          183..190
FT                   /note="17"
FT   REPEAT          191..198
FT                   /note="18"
FT   REPEAT          199..206
FT                   /note="19"
FT   REPEAT          207..214
FT                   /note="20"
FT   REPEAT          215..222
FT                   /note="21"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..222
FT                   /note="21 X 8 AA approximate tandem repeats"
FT   REGION          188..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..34
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..231
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   231 AA;  24139 MW;  D72D444DF01A7EDD CRC64;
     MSSYQQKQPF TPPPQPQQHQ VKQPCQPPPQ DTFVPITKDP CHPNVPSPGN TNIAEQGYVK
     IPEQGSIKVP DTGYTKIPDS GNTKVPESGC TSVPGSGYSV VPQPGYTKVP DQGYTKVPES
     GCTSVPGSGY SVVPQPGYTK VPESGCTSVP GPGYPTVPQP GYTKVPESGC TSVPGSGYSV
     IPQPSYTKVP ESGCTSVPGP GYPTVPQPGY TKVQEPNPSI VTPGLSQKKT K