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 27-MAR-2024, entry version 67.
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 Ensembl; ENSOMYT00000043383.2; ENSOMYP00000039741.2; ENSOMYG00000047933.1.
DR GeneID; 100136068; -.
DR KEGG; omy:100136068; -.
DR CTD; 100136068; -.
DR GeneTree; ENSGT00950000182969; -.
DR OrthoDB; 4640531at2759; -.
DR Proteomes; UP000694395; Chromosome 13.
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 Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.500; Single helix bin; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; INTERMEDIATE FILAMENT; 1.
DR PANTHER; PTHR23239:SF367; KERATIN 15-RELATED; 1.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
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
//
