ID   K1C13_ONCMY             Reviewed;         492 AA.
AC   Q8JFQ6;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Keratin, type I cytoskeletal 13;
DE   AltName: Full=Cytokeratin-13;
DE            Short=CK-13;
DE   AltName: Full=Keratin-13;
DE            Short=K13;
GN   Name=krt13 {ECO:0000250|UniProtKB:P13646};
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAD20810.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Skin {ECO:0000312|EMBL:CAD20810.1};
RX   PubMed=12190989; DOI=10.1046/j.1432-0436.2002.700606.x;
RA   Schaffeld M., Hoffling S., Haberkamp M., Conrad M., Markl J.;
RT   "Type I keratin cDNAs from the rainbow trout: independent radiation of
RT   keratins in fish.";
RL   Differentiation 70:282-291(2002).
CC   -!- FUNCTION: Type 1 keratin (Probable). May maintain oral mucosal cell
CC       homeostasis and tissue organization in response to mechanical stress
CC       (By similarity). {ECO:0000250|UniProtKB:P08730, ECO:0000305}.
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in epidermis.
CC       {ECO:0000269|PubMed:12190989}.
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; AJ427867; CAD20810.1; -; mRNA.
DR   RefSeq; NP_001117848.1; NM_001124376.1.
DR   AlphaFoldDB; Q8JFQ6; -.
DR   SMR; Q8JFQ6; -.
DR   PRIDE; Q8JFQ6; -.
DR   Ensembl; ENSOMYT00000043383; ENSOMYP00000039741; ENSOMYG00000047933.
DR   GeneID; 100136068; -.
DR   KEGG; omy:100136068; -.
DR   CTD; 100136068; -.
DR   OrthoDB; 798081at2759; -.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0043555; P:regulation of translation in response to stress; ISS:UniProtKB.
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; PS51842; IF_ROD_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Intermediate filament; Keratin.
FT   CHAIN           1..492
FT                   /note="Keratin, type I cytoskeletal 13"
FT                   /id="PRO_0000063650"
FT   DOMAIN          117..428
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..116
FT                   /note="Head"
FT                   /evidence="ECO:0000255"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..152
FT                   /note="Coil 1A"
FT                   /evidence="ECO:0000255"
FT   REGION          154..170
FT                   /note="Linker 1"
FT                   /evidence="ECO:0000255"
FT   REGION          171..262
FT                   /note="Coil 1B"
FT                   /evidence="ECO:0000255"
FT   REGION          263..285
FT                   /note="Linker 12"
FT                   /evidence="ECO:0000255"
FT   REGION          286..424
FT                   /note="Coil 2"
FT                   /evidence="ECO:0000255"
FT   REGION          425..492
FT                   /note="Tail"
FT                   /evidence="ECO:0000255"
FT   REGION          426..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..470
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  51971 MW;  681C089152B01D7A CRC64;
     MSFSRSSMSY SSSGGGGGGG TMSMRSGGGG GMGMGSSRFS SMGGGGGGGG AMRSGSVYGG
     AGGSGVRISS SSFGSGGGGG GGGYGFGMGG GGGGGGGFGM GGGGGGGGAD MNVSANEKAT
     MQNLNDRLST YLEKVRKLEA ANAELELKIR QFMESKTSPS SRDYSAFYAI IADLQDKIQA
     ATRVNGGIYL SIDNAKLAAD DFRTKYENEL AMRQSVEADI AGLKRMLDEM TMARSDLEMQ
     IEGLKEELIY LKKNHEEELL AMRTQMTGQI NVEVDAAPQE DLSRVMAEIR EQYESVSAKN
     QRDLEAWFQT KTETLNKEVA SSTEVLQTSK SEISEIRRTL QALEIELQSQ QSMKGSLENT
     LAETEGRYSM QLGRLQNQVT SLEEQLVSLR SDMERQGQEY KMLLDIKTRL EMEIAEYRRL
     LDGEASGLGA SSSKSVQKSS SSGLSSSVSS STVSSSSSVP SSTTSTTRKV VIVTEEIVDG
     KVVSTSETKH TT