K1C18_ACIBE
ID K1C18_ACIBE Reviewed; 435 AA.
AC Q7SYF8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Keratin, type I cytoskeletal 18;
DE AltName: Full=Cytokeratin-18;
DE Short=CK-18;
DE AltName: Full=Keratin type Is;
DE AltName: Full=Keratin-18;
DE Short=K18;
GN Name=krt18 {ECO:0000312|EMBL:CAD38124.1};
OS Acipenser baerii (Siberian sturgeon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX NCBI_TaxID=27689;
RN [1] {ECO:0000312|EMBL:CAD38124.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Haberkamp M., Schaffeld M., Markl J.;
RT "Intermediate filament proteins of the siberian sturgeon Acipenser baeri.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved by caspases during epithelial cell
CC apoptosis. {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; AJ493261; CAD38124.1; -; mRNA.
DR AlphaFoldDB; Q7SYF8; -.
DR SMR; Q7SYF8; -.
DR PRIDE; Q7SYF8; -.
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; IPR027695; Keratin-18.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR PANTHER; PTHR23239:SF349; PTHR23239:SF349; 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; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT CHAIN 2..435
FT /note="Keratin, type I cytoskeletal 18"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT /id="PRO_0000289070"
FT DOMAIN 85..396
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..84
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 85..120
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 121..137
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 138..229
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 230..253
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 254..391
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 392..435
FT /note="Tail"
FT /evidence="ECO:0000255"
FT SITE 243..244
FT /note="Cleavage; by caspases"
FT /evidence="ECO:0000250"
SQ SEQUENCE 435 AA; 48486 MW; 2DADCEF184C9E563 CRC64;
MSYRPGSYSV SSMRPVGSVR SSQVMTVQRS MPLASAASVY GGAGGRGSRI SVGGSSSGFG
SGLGSGAGGS YSSMSVSGSG LVGNEKETMI GLNDRLAAYL ETVRNLEQAN SKLEFQIREA
LEKKGPTTRD LSPFEKTLED LRKKVYDMTM DNSRLVLQID NSRLAADDFR VKFESEYSIR
QSVESDIIGL RKVIDDTNMG RMNLESEIES LKEELIFIKQ NHNQEVNDLR NQIAQSGVQV
DVDAPKGQDL AQVLAEVRAQ YESMAQKNRD ELKAWHENKL TEVEVEVIQN TEALQGARTE
VTELRRQMQS LEIELESQRS MKASLEDSLR DTEMRNNMEM ERYNNMILQL EAELGQLRGN
IQMQASEYEA LLNIKMKLEA EIATYRRLLD GEDFRLQDAL VDQSSTKSIK KVTVTQTLVD
GKVVSESTNT KEIGK
