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Protein

Keratin, type I cytoskeletal 18

Gene

krt18

Organism
Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

When phosphorylated, plays a role in filament reorganization.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei279 – 2791StutterSequence analysis
Sitei340 – 3401StutterSequence analysis

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type I cytoskeletal 18
Alternative name(s):
Cytokeratin-18
Short name:
CK-18
Keratin-18
Short name:
K18
Simple type I keratin
Gene namesi
Name:krt18
OrganismiOncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Taxonomic identifieri8022 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiProtacanthopterygiiSalmoniformesSalmonidaeSalmoninaeOncorhynchus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 438437Keratin, type I cytoskeletal 18By similarityPRO_0000289073Add
BLAST

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiO57607.

Expressioni

Tissue specificityi

Expressed in all tissues examined, including epidermal keratinocytes, tongue mucosa, corneal epithelium, Meninges cells, epidermal goblet and Merkel cells, gill mucosa, basal cells of gill secondary lamellae, hepatocytes and bile canaliculi, bile duct, intestinal mucosa, blood vessel endothelial and muscle cells, interstitial cells, fibroblasts, scale-associated cells, ovary stroma and follicle, optic nerve glia, eye ciliary body, chondrocytes and kidney tubules.1 Publication

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. Keratin-18 associates with keratin-8 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliO57607.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 8887HeadSequence analysisAdd
BLAST
Regioni89 – 395307RodSequence analysisAdd
BLAST
Regioni89 – 12436Coil 1ASequence analysisAdd
BLAST
Regioni125 – 14117Linker 1Sequence analysisAdd
BLAST
Regioni142 – 23392Coil 1BSequence analysisAdd
BLAST
Regioni234 – 25724Linker 12Sequence analysisAdd
BLAST
Regioni258 – 395138Coil 2Sequence analysisAdd
BLAST
Regioni396 – 43843TailSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi35 – 6834Gly-richSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Sequence analysis

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOVERGENiHBG013015.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O57607-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVKRSSVRG PGSGYGYSIT HNSTAPTYRA ASTYGGAGGQ GTRISSVSYS
60 70 80 90 100
GVRSGMGGMG VGMGGSGGSM SSSIQVSTSG DTAHIMGNEK FAMQNLNDRL
110 120 130 140 150
ASYLEMVRNL EQANGKLELK IREAMEKRGP DVNDYSRYNA ILDDLRKKVF
160 170 180 190 200
DATTDNARMC LQIDNARLAA DDFRVKFESE LSIRQSVEAD IVGLRKVIDD
210 220 230 240 250
TNMGRMNLES EIEALKEELI FLKKNHDNEV MEMRNMISQS GVQVDVDAPK
260 270 280 290 300
GQDLAAIMAE VRAKYEKEAL KNQEELKAWH ETRITEVQSV VSQNTEALQG
310 320 330 340 350
AHTEINDLRR QLQTLEIELD SQKSLKGSLE GTLRDTEMRY NMEMESLNKI
360 370 380 390 400
LVGLESELTN LRSNIQQQTQ EYEHLLNIKM KLEAEIATYR RLLDGGDFKL
410 420 430
QDALEDQRTV KTKVMTVTQT LVDGKVVSSS TETKERNL
Length:438
Mass (Da):48,779
Last modified:June 1, 1998 - v1
Checksum:i06EF8C4EEEAD841B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14289 mRNA. Translation: CAA74664.1.
RefSeqiNP_001118196.1. NM_001124724.1.
UniGeneiOmy.34894.

Genome annotation databases

GeneIDi100136778.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14289 mRNA. Translation: CAA74664.1.
RefSeqiNP_001118196.1. NM_001124724.1.
UniGeneiOmy.34894.

3D structure databases

ProteinModelPortaliO57607.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO57607.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100136778.

Phylogenomic databases

HOVERGENiHBG013015.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Tracing keratin evolution: catalog, expression patterns and primary structure of shark (Scyliorhinus stellaris) keratins."
    Schaffeld M., Lobbecke A., Lieb B., Markl J.
    Eur. J. Cell Biol. 77:69-80(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: SpleenImported.
  2. "Type I keratin cDNAs from the rainbow trout: independent radiation of keratins in fish."
    Schaffeld M., Hoffling S., Haberkamp M., Conrad M., Markl J.
    Differentiation 70:282-291(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Spleen1 Publication.

Entry informationi

Entry nameiK1C18_ONCMY
AccessioniPrimary (citable) accession number: O57607
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).Curated

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.