ID   K1C11_PROAT             Reviewed;         467 AA.
AC   Q5K2P6;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Keratin, type 1 cytoskeletal 11;
DE   AltName: Full=Type I keratin 11;
GN   Name=krt11 {ECO:0000312|EMBL:CAH05041.1};
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:CAH05041.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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 the outermost cell layers of skin
CC       epidermis (at protein level). {ECO:0000269|PubMed:15819414}.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC       keratin, I (acidic) and II (neutral to basic) (40-55 and 56-70 kDa,
CC       respectively). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; AJ785785; CAH05041.1; -; mRNA.
DR   AlphaFoldDB; Q5K2P6; -.
DR   SMR; Q5K2P6; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
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..467
FT                   /note="Keratin, type 1 cytoskeletal 11"
FT                   /id="PRO_0000308519"
FT   DOMAIN          101..413
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..100
FT                   /note="Head"
FT                   /evidence="ECO:0000255"
FT   REGION          12..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..137
FT                   /note="Coil 1A"
FT                   /evidence="ECO:0000255"
FT   REGION          138..156
FT                   /note="Linker 1"
FT                   /evidence="ECO:0000255"
FT   REGION          157..248
FT                   /note="Coil 1B"
FT                   /evidence="ECO:0000255"
FT   REGION          249..268
FT                   /note="Linker 12"
FT                   /evidence="ECO:0000255"
FT   REGION          269..416
FT                   /note="Coil 2"
FT                   /evidence="ECO:0000255"
FT   REGION          409..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..463
FT                   /note="Tail"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        410..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   467 AA;  52279 MW;  1B82EACC8268B1F2 CRC64;
     MSYSSFSIAQ GSRVPSLSGT RSSSSYSLKS DLIPQSRRSH SVYGTPGSIR ISSPSMPSAI
     VSSYSSTLSS ALPSSSYGGN SYSSSTSFSS GGTDFLLGTS GKEAMQNLND RLADYLARVR
     SLEDRNRELE QKIREWYEKQ GAGTKRKDFS HYFKIIADLQ NQINAGNMEN ARILLKIDNA
     KLAADDFKQK WEAEQALRLG VEADIHGLRK ILDEMTLART DLEMQIEGHK EEKAYLIKSH
     DEDMKALRSQ LGGQVNVEVD AAPAEDLTKK LEIIRQRYEQ LAEKNRKESE DWFIKKSEEL
     NKNMASSTEA LQTSKTEINE LRRTIQGLEI ELQSQQSMKG ALEGQLADTE HRYSSTLMNL
     QNIINQKEAE LSNIRADIES QASKYKILLD VKTRLENEIS TYRTLLEGDA GRSHSSSHLS
     STVSKDKVPV SSPNVITKVR TIVEEKINGQ VISKKEYEGS PDQLSYY