ID   K1C18_ONCMY             Reviewed;         438 AA.
AC   O57607;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Keratin, type I cytoskeletal 18;
DE   AltName: Full=Cytokeratin-18;
DE            Short=CK-18;
DE   AltName: Full=Keratin-18;
DE            Short=K18;
DE   AltName: Full=Simple type I keratin;
GN   Name=krt18;
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:0000312|EMBL:CAA74664.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen {ECO:0000312|EMBL:CAA74664.1};
RX   PubMed=9840456; DOI=10.1016/s0171-9335(98)80074-5;
RA   Schaffeld M., Lobbecke A., Lieb B., Markl J.;
RT   "Tracing keratin evolution: catalog, expression patterns and primary
RT   structure of shark (Scyliorhinus stellaris) keratins.";
RL   Eur. J. Cell Biol. 77:69-80(1998).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Spleen {ECO:0000269|PubMed:12190989};
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: When phosphorylated, plays a role in filament reorganization.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       Keratin-18 associates with keratin-8 (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined, including
CC       epidermal keratinocytes, tongue mucosa, corneal epithelium, Meninges
CC       cells, epidermal goblet and Merkel cells, gill mucosa, basal cells of
CC       gill secondary lamellae, hepatocytes and bile canaliculi, bile duct,
CC       intestinal mucosa, blood vessel endothelial and muscle cells,
CC       interstitial cells, fibroblasts, scale-associated cells, ovary stroma
CC       and follicle, optic nerve glia, eye ciliary body, chondrocytes and
CC       kidney tubules. {ECO:0000269|PubMed:12190989}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
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       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; Y14289; CAA74664.1; -; mRNA.
DR   RefSeq; NP_001118196.1; NM_001124724.1.
DR   AlphaFoldDB; O57607; -.
DR   SMR; O57607; -.
DR   PRIDE; O57607; -.
DR   GeneID; 100136778; -.
DR   KEGG; omy:100136778; -.
DR   OrthoDB; 711591at2759; -.
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; Phosphoprotein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P05783"
FT   CHAIN           2..438
FT                   /note="Keratin, type I cytoskeletal 18"
FT                   /evidence="ECO:0000250|UniProtKB:P05783"
FT                   /id="PRO_0000289073"
FT   DOMAIN          89..400
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..88
FT                   /note="Head"
FT                   /evidence="ECO:0000255"
FT   REGION          89..124
FT                   /note="Coil 1A"
FT                   /evidence="ECO:0000255"
FT   REGION          125..141
FT                   /note="Linker 1"
FT                   /evidence="ECO:0000255"
FT   REGION          142..233
FT                   /note="Coil 1B"
FT                   /evidence="ECO:0000255"
FT   REGION          234..257
FT                   /note="Linker 12"
FT                   /evidence="ECO:0000255"
FT   REGION          258..395
FT                   /note="Coil 2"
FT                   /evidence="ECO:0000255"
FT   REGION          396..438
FT                   /note="Tail"
FT                   /evidence="ECO:0000255"
FT   SITE            279
FT                   /note="Stutter"
FT                   /evidence="ECO:0000255"
FT   SITE            340
FT                   /note="Stutter"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   438 AA;  48779 MW;  06EF8C4EEEAD841B CRC64;
     MSVKRSSVRG PGSGYGYSIT HNSTAPTYRA ASTYGGAGGQ GTRISSVSYS GVRSGMGGMG
     VGMGGSGGSM SSSIQVSTSG DTAHIMGNEK FAMQNLNDRL ASYLEMVRNL EQANGKLELK
     IREAMEKRGP DVNDYSRYNA ILDDLRKKVF DATTDNARMC LQIDNARLAA DDFRVKFESE
     LSIRQSVEAD IVGLRKVIDD TNMGRMNLES EIEALKEELI FLKKNHDNEV MEMRNMISQS
     GVQVDVDAPK GQDLAAIMAE VRAKYEKEAL KNQEELKAWH ETRITEVQSV VSQNTEALQG
     AHTEINDLRR QLQTLEIELD SQKSLKGSLE GTLRDTEMRY NMEMESLNKI LVGLESELTN
     LRSNIQQQTQ EYEHLLNIKM KLEAEIATYR RLLDGGDFKL QDALEDQRTV KTKVMTVTQT
     LVDGKVVSSS TETKERNL