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 01-APR-2015, entry version 53. 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; 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., RA Park C.Y., 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 CC reorganization. {ECO:0000250}. CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins. CC Keratin-18 associates with keratin-8 (By similarity). CC {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Abundantly expressed in an even distribution CC throughout the optic nerve, localizing specifically to the CC astrocyte domains. Moderately expressed in spinal cord, brain, CC liver and oocytes. {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 CC microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to CC basic; 56-70 kDa). {ECO:0000305}. CC -!- SIMILARITY: Belongs to the intermediate filament family. CC {ECO:0000255}. 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 PRIDE; Q07427; -. DR HOVERGEN; HBG013015; -. DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR InterPro; IPR001664; IF. DR InterPro; IPR018039; Intermediate_filament_CS. DR InterPro; IPR002957; Keratin_I. DR PANTHER; PTHR23239; PTHR23239; 1. DR Pfam; PF00038; Filament; 1. DR PRINTS; PR01248; TYPE1KERATIN. DR PROSITE; PS00226; IF; 1. PE 2: Evidence at transcript level; KW Coiled coil; Intermediate filament; Keratin; Phosphoprotein. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P05783}. FT CHAIN 2 435 Keratin, type I cytoskeletal 18. FT {ECO:0000250|UniProtKB:P05783}. FT /FTId=PRO_0000289071. FT REGION 2 88 Head. {ECO:0000255}. FT REGION 89 394 Rod. {ECO:0000255}. FT REGION 89 123 Coil 1A. {ECO:0000255}. FT REGION 124 140 Linker 1. {ECO:0000255}. FT REGION 141 232 Coil 1B. {ECO:0000255}. FT REGION 233 256 Linker 12. {ECO:0000255}. FT REGION 257 394 Coil 2. {ECO:0000255}. FT REGION 395 435 Tail. {ECO:0000255}. FT SITE 246 247 Cleavage; by caspases. {ECO:0000250}. FT SITE 339 339 Stutter. {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 //