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Protein

Keratin, type I cytoskeletal 20

Gene

Krt20

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a significant role in maintaining keratin filament organization in intestinal epithelia. When phosphorylated, plays a role in the secretion of mucin in the small intestine (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type I cytoskeletal 20
Alternative name(s):
Cytokeratin-20
Short name:
CK-20
Cytokeratin-21
Short name:
CK-21
Keratin-20
Short name:
K20
Gene namesi
Name:Krt20
Synonyms:Krt21
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628646. Krt20.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Keratin, type I cytoskeletal 20PRO_0000063676Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131PhosphoserineCombined sources
Modified residuei16 – 161PhosphoserineCombined sources
Modified residuei26 – 261PhosphoserineCombined sources

Post-translational modificationi

Hyperphosphorylation at Ser-13 occurs during the early stages of apoptosis but becomes less prominent during the later stages. Phosphorylation at Ser-13 also increases in response to stress brought on by cell injury (By similarity).By similarity
Proteolytically cleaved by caspases during apoptosis. Cleavage occurs at Asp-233 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei233 – 2342Cleavage; by caspasesBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP25030.

PTM databases

iPTMnetiP25030.

Expressioni

Tissue specificityi

Expressed predominantly in the intestinal epithelium in differentiated villus cells.2 Publications

Developmental stagei

Becomes apparent upon completion of villus formation at 20 days gestation (2 days before birth) and is expressed by the entire epithelium of the villus.1 Publication

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. Associates with KRT8 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP25030.
SMRiP25030. Positions 72-109.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7474HeadAdd
BLAST
Regioni75 – 382308RodAdd
BLAST
Regioni75 – 11036Coil 1AAdd
BLAST
Regioni111 – 12818Linker 1Add
BLAST
Regioni129 – 22092Coil 1BAdd
BLAST
Regioni221 – 24323Linker 12Add
BLAST
Regioni244 – 382139Coil 2Add
BLAST
Regioni383 – 42947TailAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOVERGENiHBG013015.
InParanoidiP25030.
KOiK07604.
PhylomeDBiP25030.

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.

P25030-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFSRRSFHR SLSSSSQGPA LSTSGSLYRK GTMQRLGLHS VYGGWRHGTR
60 70 80 90 100
ISVSKTTMSY GNHLSNGGDL FGGNEKLAMQ NLNDRLASYL EKVRSLEQSN
110 120 130 140 150
SKLEAQIKQW YETNAPSTIR DYSSYYAQIK ELQDQIKDAQ IENARCVLQI
160 170 180 190 200
DNAKLAAEDF RLKFETERGM RITVEADLQG LSKVYDDLTL QKTDLEIQIE
210 220 230 240 250
ELNKDLALLK KEHQEEVEVL RRQLGNNVNV EVDAAPGLNL GEIMNEMRQK
260 270 280 290 300
YEILAQKNLQ EAKEQFERQT QTLEKQVTVN IEELRGTEVQ VTELRRSYQT
310 320 330 340 350
LEIELQSQLS MKESLERTLE ETKARYASQL AAIQEMLSSL EAQLMQIRSD
360 370 380 390 400
TERQNQEYNI LLDIKTRLEQ EIATYRRLLE GEDIKTTEYQ LNTLEAKDIK
410 420
KTRKIKTVVE EVVDGKVVSS EVKEIEENI
Length:429
Mass (Da):49,388
Last modified:September 19, 2002 - v2
Checksum:i95CCA2ABB0F0028C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63665 mRNA. Translation: AAA41473.1.
PIRiA40452.
RefSeqiNP_775151.1. NM_173128.1.
UniGeneiRn.9887.

Genome annotation databases

GeneIDi286912.
KEGGirno:286912.
UCSCiRGD:628646. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63665 mRNA. Translation: AAA41473.1.
PIRiA40452.
RefSeqiNP_775151.1. NM_173128.1.
UniGeneiRn.9887.

3D structure databases

ProteinModelPortaliP25030.
SMRiP25030. Positions 72-109.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiP25030.

Proteomic databases

PRIDEiP25030.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi286912.
KEGGirno:286912.
UCSCiRGD:628646. rat.

Organism-specific databases

CTDi54474.
RGDi628646. Krt20.

Phylogenomic databases

HOVERGENiHBG013015.
InParanoidiP25030.
KOiK07604.
PhylomeDBiP25030.

Miscellaneous databases

NextBioi625022.
PROiP25030.

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

« Hide 'large scale' publications
  1. "Identification and characterization of rat intestinal keratins. Molecular cloning of cDNAs encoding cytokeratins 8, 19, and a new 49-kDa type I cytokeratin (cytokeratin 21) expressed by differentiated intestinal epithelial cells."
    Chandler J.S., Calnek D., Quaroni A.
    J. Biol. Chem. 266:11932-11938(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Intestinal epithelium.
  2. "Differential localization by in situ hybridization of distinct keratin mRNA species during intestinal epithelial cell development and differentiation."
    Calnek D., Quaroni A.
    Differentiation 53:95-104(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-16 AND SER-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiK1C20_RAT
AccessioniPrimary (citable) accession number: P25030
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: September 19, 2002
Last modified: May 11, 2016
This is version 90 of the entry and version 2 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).

Keywords - Technical termi

Complete proteome, Reference proteome

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.