ID   K1C12_RABIT             Reviewed;         411 AA.
AC   Q28706;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Keratin, type I cytoskeletal 12;
DE   AltName: Full=Cytokeratin-12;
DE            Short=CK-12;
DE   AltName: Full=Keratin-12;
DE            Short=K12;
DE   Flags: Fragment;
GN   Name=KRT12;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Cornea;
RX   PubMed=7511548; DOI=10.1046/j.1432-0436.1994.5520137.x;
RA   Wu R.-L., Zhu G., Galvin S., Xu C., Haseba T., Chaloin-Dufau C.,
RA   Dhouailly D., Wei Z.-G., Lavker R.M., Kao W.-Y., Sun T.-T.;
RT   "Lineage-specific and differentiation-dependent expression of K12 keratin
RT   in rabbit corneal/limbal epithelial cells: cDNA cloning and northern blot
RT   analysis.";
RL   Differentiation 55:137-144(1994).
CC   -!- FUNCTION: Involved in corneal epithelium organization, integrity and
CC       corneal keratin expression. {ECO:0000250|UniProtKB:Q64291}.
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       Keratin-3 associates with keratin-12.
CC   -!- TISSUE SPECIFICITY: Cornea specific. Associated mainly with all layers
CC       of the central corneal epithelium and also found in the suprabasal
CC       limbal epithelium. {ECO:0000269|PubMed:7511548}.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC       keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; X77665; CAA54741.1; -; mRNA.
DR   PIR; S45318; S45318.
DR   AlphaFoldDB; Q28706; -.
DR   SMR; Q28706; -.
DR   STRING; 9986.ENSOCUP00000015186; -.
DR   PRIDE; Q28706; -.
DR   eggNOG; ENOG502QV0B; Eukaryota.
DR   InParanoid; Q28706; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0061303; P:cornea development in camera-type eye; ISS:UniProtKB.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; ISS:UniProtKB.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR23239; PTHR23239; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   PROSITE; PS00226; IF_ROD_1; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Intermediate filament; Keratin; Reference proteome.
FT   CHAIN           <1..411
FT                   /note="Keratin, type I cytoskeletal 12"
FT                   /id="PRO_0000063646"
FT   DOMAIN          43..359
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          <1..42
FT                   /note="Head"
FT   REGION          43..78
FT                   /note="Coil 1A"
FT   REGION          83..101
FT                   /note="Linker 1"
FT   REGION          102..193
FT                   /note="Coil 1B"
FT   REGION          194..216
FT                   /note="Linker 12"
FT   REGION          217..354
FT                   /note="Coil 2"
FT   REGION          355..411
FT                   /note="Tail"
FT   REGION          356..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   411 AA;  45727 MW;  0B22E9A4D9DCC250 CRC64;
     DHDYEFPGIQ AFAGLGMGFG GSPGGGSLYL PSGNDGGLLS GSEKETMQNL NDRLASYLDK
     VRALEDANAE LENKIREWYE ARGHGHGDCG PQHDYSKYHP LIEDLRNKII SASIGNAQLI
     LQIDNARLAA DDFRMKFENE AALRQTVEAD INGLRRVLDE LTLARADLEA QIESLTEELA
     YMKKNHEEEL QSCRAGGPGE VSVEMDAAPG VDLTRLLNDM RAQYEAIAEQ NRKDAEAWFI
     EKSGELRKEI STNTEQLQSS KSEVTDLRRA LQNLEIELQS QLAMKKSLED SLAETEGDYC
     GQLSQVQQLV GDLEAQLQQV RSDTERQNMD YQRLLNVKAR LELEIETYRR LLDGEAQGDG
     LDESSAMTGS RSQAQSIDSS KDPSKTRKIK TIVQEVVNGE VVSSQVQEIQ N