ID   K1C15_PROAT             Reviewed;         441 AA.
AC   Q5K2P2;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Keratin, type I cytoskeletal 15;
DE   AltName: Full=Cytokeratin-15;
DE            Short=CK-15;
DE   AltName: Full=Keratin-15;
DE            Short=K15;
DE   Flags: Fragment;
GN   Name=KRT15;
OS   Protopterus aethiopicus (Marbled lungfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Dipnomorpha; Ceratodontiformes; Lepidosirenoidei; Protopteridae;
OC   Protopterus.
OX   NCBI_TaxID=7886;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAH05045.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Skin {ECO:0000269|PubMed:15819414};
RX   PubMed=15819414; DOI=10.1016/j.ejcb.2004.12.006;
RA   Schaffeld M., Bremer M., Hunzinger C., Markl J.;
RT   "Evolution of tissue-specific keratins as deduced from novel cDNA sequences
RT   of the lungfish Protopterus aethiopicus.";
RL   Eur. J. Cell Biol. 84:363-377(2005).
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in skin. {ECO:0000269|PubMed:15819414}.
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; AJ785789; CAH05045.1; -; mRNA.
DR   AlphaFoldDB; Q5K2P2; -.
DR   SMR; Q5K2P2; -.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
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   1: Evidence at protein level;
KW   Coiled coil; Intermediate filament; Keratin.
FT   CHAIN           <1..441
FT                   /note="Keratin, type I cytoskeletal 15"
FT                   /id="PRO_0000063661"
FT   DOMAIN          92..407
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          2..91
FT                   /note="Head"
FT                   /evidence="ECO:0000255"
FT   REGION          92..127
FT                   /note="Coil 1A"
FT                   /evidence="ECO:0000255"
FT   REGION          128..149
FT                   /note="Linker 1"
FT                   /evidence="ECO:0000255"
FT   REGION          150..241
FT                   /note="Coil 1B"
FT                   /evidence="ECO:0000255"
FT   REGION          242..261
FT                   /note="Linker 12"
FT                   /evidence="ECO:0000255"
FT   REGION          262..403
FT                   /note="Coil 2"
FT                   /evidence="ECO:0000255"
FT   REGION          404..441
FT                   /note="Tail"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:CAH05045.1"
SQ   SEQUENCE   441 AA;  48902 MW;  CFF6C73A2D0ECE56 CRC64;
     LLLLGHASTS TRGFSGNSFK SDLIPQSRRS HSVYGTPGSI RISSPSVPSA IVSSYSSTLS
     SALPSSSYGG NSFSSSTSFS SGGSDLLLGT SGKEAMQNLN DRLASYLDKV RSLEGKNHEL
     ELKIKDWYSQ VIPGTGGPDA RDYGHLEKEI EDLQNKVNNC RVDTATILLH IDNAKLAADD
     FRNKYENEQS LRLGVEADIN GLKRVLDELA LAKADTDMQI EGLRDELDYL KKNHEEDMKA
     ASSGIAGQVN VELDAAPGTN LLDELDACRR DHEAMLDQMR REAERWYNEK AKDVKDKAGE
     AQETLVSHTS EISDLKRSIQ SLEIELQTQL ARKSSLESTL AGTESQYGMR IQEIQMKINV
     FEDQISDLRA KMEFQSQEYQ MLLDVKQRLE AEIATYRMLL DSEDSKGSII NHKILTAIEK
     LVDGIVLSTE VLEKQIPVLS Y