ID   K1C11_LAMFL             Reviewed;         482 AA.
AC   Q8AWA7;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Keratin, type 1 cytoskeletal 11;
DE   AltName: Full=Type I keratin 11;
OS   Lampetra fluviatilis (European river lamprey) (Petromyzon fluviatilis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Lampetra.
OX   NCBI_TaxID=7748;
RN   [1] {ECO:0000312|EMBL:CAC87097.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Schultess J., Schaffeld M., Markl J.;
RT   "Keratin mRNA sequences from Lampetra fluviatilis.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       {ECO:0000305}.
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; AJ308117; CAC87097.1; -; mRNA.
DR   AlphaFoldDB; Q8AWA7; -.
DR   SMR; Q8AWA7; -.
DR   PRIDE; Q8AWA7; -.
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   2: Evidence at transcript level;
KW   Coiled coil; Intermediate filament; Keratin.
FT   CHAIN           1..482
FT                   /note="Keratin, type 1 cytoskeletal 11"
FT                   /id="PRO_0000308518"
FT   DOMAIN          95..406
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..94
FT                   /note="Head"
FT                   /evidence="ECO:0000255"
FT   REGION          95..130
FT                   /note="Coil 1A"
FT                   /evidence="ECO:0000255"
FT   REGION          131..147
FT                   /note="Linker 1"
FT                   /evidence="ECO:0000255"
FT   REGION          148..239
FT                   /note="Coil 1B"
FT                   /evidence="ECO:0000255"
FT   REGION          240..263
FT                   /note="Linker 12"
FT                   /evidence="ECO:0000255"
FT   REGION          264..402
FT                   /note="Coil 2"
FT                   /evidence="ECO:0000255"
FT   REGION          403..479
FT                   /note="Tail"
FT                   /evidence="ECO:0000255"
FT   REGION          421..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   482 AA;  50969 MW;  AB69A0328EA31525 CRC64;
     MSFSSRSIGG YGGMSTRLGR GSASVYEGGG SSGGYRISQS SMGGGGGYGG GYGGGGGYRG
     GGGYGGGCAI SSSFQSFGAF RGGGAGGGGL SGGNEKAEMQ GLNDRLAEYI EKVRFLENAN
     QELELRIKEL LKGKGPGNKD YSAYYTTMQE LRDKILAQIM ENARVSLEID NARLAADDFR
     SKWETELALR SSVEADINNL RGLLDEYSMA RMGLEGEIES LREELIFMRK NHEEELAALR
     AQLEGSSMSV EVDSTKGKDL HKILAEVRAQ YEAMIAKNRV DQEEAFNKQA QSVQVVAVQH
     SQASQAAKVE VTETRRAMQS LQAELDSLRG LIRSLEDQLQ DTEERNARDL STYTMQIQRL
     EGELSNLRHG INQQLKEYAD LLNMKMKLEA EIATYRRLLE GEDSRMGNIS ANSTSGLITV
     SGGGGGGGGG VSGGGGGGGM SMTMTSSSSS GGGGGSSSSG GGSVVKTTTT KESSSYSTGY
     RS