ID K1C18_CARAU Reviewed; 435 AA. AC Q07427; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 72. 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; GN Name=krt18; OS Carassius auratus (Goldfish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Cyprininae; Carassius. OX NCBI_TaxID=7957; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC38007.1} RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Optic nerve {ECO:0000312|EMBL:AAC38007.1}; RX PubMed=7515399; DOI=10.1002/cne.903400211; RA Druger R.K., Glasgow E., Fuchs C., Levine E.M., Matthews J.P., Park C.Y., RA Schechter N.; RT "Complex expression of keratins in goldfish optic nerve."; RL J. Comp. Neurol. 340:269-280(1994). 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: Abundantly expressed in an even distribution CC throughout the optic nerve, localizing specifically to the astrocyte CC domains. Moderately expressed in spinal cord, brain, liver and oocytes. CC {ECO:0000269|PubMed:7515399}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L09744; AAC38007.1; -; mRNA. DR AlphaFoldDB; Q07427; -. DR SMR; Q07427; -. DR Proteomes; UP000515129; Genome assembly. DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. 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; IPR018039; IF_conserved. DR InterPro; IPR039008; IF_rod_dom. DR InterPro; IPR002957; Keratin_I. DR PANTHER; PTHR23239; INTERMEDIATE FILAMENT; 1. DR PANTHER; PTHR23239:SF377; KERATIN, TYPE I CYTOSKELETAL 18-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; 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; KW Reference proteome. 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_0000289071" FT DOMAIN 89..399 FT /note="IF rod" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2..88 FT /note="Head" FT /evidence="ECO:0000255" FT REGION 89..123 FT /note="Coil 1A" FT /evidence="ECO:0000255" FT REGION 124..140 FT /note="Linker 1" FT /evidence="ECO:0000255" FT REGION 141..232 FT /note="Coil 1B" FT /evidence="ECO:0000255" FT REGION 233..256 FT /note="Linker 12" FT /evidence="ECO:0000255" FT REGION 257..394 FT /note="Coil 2" FT /evidence="ECO:0000255" FT REGION 395..435 FT /note="Tail" FT /evidence="ECO:0000255" FT SITE 246..247 FT /note="Cleavage; by caspases" FT /evidence="ECO:0000250" FT SITE 339 FT /note="Stutter" FT /evidence="ECO:0000255" SQ SEQUENCE 435 AA; 49179 MW; C5346F321732ABA7 CRC64; MSLRSSYSVR SSTSQVPVSQ MSQMSQMSIK RTTNVPTYRA ARSTAAAGQG TRISSASYSG VRSGVGLPSM SSSIHVSATG ATGDIMGNEK MAMQNLNDRL ASYLRSETLE QANSKLELKI REALEKKGPE VCDYSRFQPI IDDLRRKIFD ATSNNARLVL QIDNARLAAD DFRVKYDSEL SIRQGVEADI AGLRKVIDDT NMNRMNLESE IEALKEELIF LKKNHDNEVM ELRNQISHSG VQVDVDAPKG QDLAKIMEEI RSKYEKMALK NQEELKAWHE SQITEVQVQV IQNTEALEGA RTEVNELRRQ IQTLEIELES QRNLKGSLEA TLRDTEMRYN MEIESLNAVT MQLEAELTQL RNNIQHQTQE YEALLNLKMK LEAEIATYRR LLDGGDFKLQ DALEEQKRVK VMTVTQTLVD GKVVSSSTET KEKKF //