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Protein

Keratin, type II cytoskeletal 8

Gene

Krt8

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

Functioni

Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle.1 Publication

Miscellaneous

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei342Stutter1

GO - Molecular functioni

  • protein complex binding Source: RGD
  • scaffold protein binding Source: Ensembl
  • structural molecule activity Source: InterPro

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-RNO-6805567. Keratinization.
R-RNO-6809371. Formation of the cornified envelope.

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type II cytoskeletal 8
Alternative name(s):
Cytokeratin endo A
Cytokeratin-8
Short name:
CK-8
Keratin-8
Short name:
K8
Type-II keratin Kb8
Gene namesi
Name:Krt8
Synonyms:Krt2-8
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi2984. Krt8.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Intermediate filament, Keratin, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000637421 – 483Keratin, type II cytoskeletal 8Add BLAST483

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9Phosphoserine; by PKC/PRKCE1 Publication1
Cross-linki11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei13Phosphoserine1 Publication1
Modified residuei15PhosphoserineBy similarity1
Modified residuei21PhosphoserineCombined sources1
Modified residuei22PhosphoserineBy similarity1
Modified residuei23Omega-N-methylarginineBy similarity1
Modified residuei24PhosphoserineCombined sources1
Modified residuei24Phosphoserine; by PKC/PRKCECombined sources1 Publication1
Modified residuei26PhosphothreonineCombined sources1
Modified residuei27PhosphoserineCombined sources1
Modified residuei32Omega-N-methylarginineBy similarity1
Modified residuei34Phosphoserine1 Publication1
Modified residuei37Phosphoserine1 Publication1
Modified residuei39PhosphoserineBy similarity1
Modified residuei40Omega-N-methylarginineBy similarity1
Modified residuei43PhosphoserineCombined sources1 Publication1
Modified residuei44PhosphoserineCombined sources1
Modified residuei47PhosphoserineCombined sources1
Modified residuei49Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei49Omega-N-methylarginine; alternateBy similarity1
Modified residuei51PhosphoserineCombined sources1 Publication1
Modified residuei101N6-malonyllysineBy similarity1
Cross-linki122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki197Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki197Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei207N6-acetyllysineBy similarity1
Modified residuei253PhosphoserineCombined sources1
Modified residuei258PhosphoserineCombined sources1
Modified residuei274PhosphoserineBy similarity1
Cross-linki285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei295N6-acetyllysine; alternateBy similarity1
Cross-linki295Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki304Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei325N6-acetyllysine; alternateBy similarity1
Cross-linki325Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki393Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei400PhosphoserineBy similarity1
Modified residuei404PhosphoserineBy similarity1
Modified residuei410PhosphoserineBy similarity1
Modified residuei417Phosphoserine1 Publication1
Modified residuei424Phosphoserine1 Publication1
Modified residuei426Phosphoserine1 Publication1
Modified residuei432PhosphoserineCombined sources1
Cross-linki472Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki472Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei475PhosphoserineCombined sources1
Modified residuei477PhosphoserineBy similarity1
Modified residuei478PhosphoserineCombined sources1
Modified residuei482PhosphoserineCombined sources1

Post-translational modificationi

O-glycosylated. O-GlcNAcylation at multiple sites increases solubility, and decreases stability by inducing proteasomal degradation (By similarity).By similarity
O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ10758.
PRIDEiQ10758.

PTM databases

iPTMnetiQ10758.
PhosphoSitePlusiQ10758.

Expressioni

Tissue specificityi

Expressed in cardiac and striated muscle. Expressed at Z-lines within the muscle fibers and at Z-line and M-line domains at costameres at the sarcolemmal membrane (at protein level). Observed in coagulating gland, bladder, salivary gland, kidney, spleen, thymus, lung and heart. Also observed in ventral prostate, seminal vesicle and liver where expression increases following castration.2 Publications

Gene expression databases

BgeeiENSRNOG00000009779.
GenevisibleiQ10758. RN.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. KRT8 associates with KRT18. Associates with KRT20. Interacts with PNN. When associated with KRT19, interacts with DMD. Interacts with TCHP. Interacts with APEX1 (By similarity). Interacts with GPER1 (By similarity). Interacts with EPPK1 (By similarity).By similarity

GO - Molecular functioni

  • protein complex binding Source: RGD
  • scaffold protein binding Source: Ensembl

Protein-protein interaction databases

BioGridi247655. 1 interactor.
IntActiQ10758. 4 interactors.
MINTiMINT-4596966.
STRINGi10116.ENSRNOP00000029068.

Structurei

3D structure databases

ProteinModelPortaliQ10758.
SMRiQ10758.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini91 – 402IF rodPROSITE-ProRule annotationAdd BLAST312

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 90HeadAdd BLAST90
Regioni91 – 126Coil 1AAdd BLAST36
Regioni127 – 143Linker 1Add BLAST17
Regioni144 – 235Coil 1BAdd BLAST92
Regioni236 – 259Linker 12Add BLAST24
Regioni260 – 398Coil 2Add BLAST139
Regioni261 – 382Necessary for interaction with PNNBy similarityAdd BLAST122
Regioni399 – 483TailAdd BLAST85

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi9 – 51Ser-richAdd BLAST43

Sequence similaritiesi

Belongs to the intermediate filament family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG4R. Eukaryota.
ENOG410YY6B. LUCA.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiQ10758.
KOiK07605.
OMAiIENAVCW.
OrthoDBiEOG091G09KR.
PhylomeDBiQ10758.
TreeFamiTF317854.

Family and domain databases

InterProiView protein in InterPro
IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR032444. Keratin_2_head.
IPR003054. Keratin_II.
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiView protein in Pfam
PF00038. Filament. 1 hit.
PF16208. Keratin_2_head. 1 hit.
PRINTSiPR01276. TYPE2KERATIN.
SMARTiView protein in SMART
SM01391. Filament. 1 hit.
PROSITEiView protein in PROSITE
PS00226. IF_ROD_1. 1 hit.
PS51842. IF_ROD_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q10758-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVRVTQKSY KMSTSGPRAF SSRSFTSGPG ARISSSSFSR VGSSSSSFRG
60 70 80 90 100
SLGGFGGAGV GGITAVTVNQ SLLNPLKLEV DPNIQAVRTQ EKEQIKTLNN
110 120 130 140 150
KFASFIDKVR FLEQQNKMLE TKWSLLQQQK TSRSNMDNMF ESYINNLRRQ
160 170 180 190 200
LEALGQEKLK LEVELGNMQG LVEDFKNKYE DEINKRTEME NEFVLIKKDV
210 220 230 240 250
DEAYMNKVEL ESRLEGLTDE INFLRQIHEE EIRELQSQIS DTSVVLSMDN
260 270 280 290 300
SRSLDMDSII AEVRAQYEEI ANRSRAEAET MYQIKYEELQ TLAGKHGDDL
310 320 330 340 350
RRSKTEISEM NRNISRLQAE IDALKGQRAT LEAAIADAEQ RGELAVKDAN
360 370 380 390 400
AKLEDLKNAL QKAKQDMARQ LREYQELMNV KLALDIEIAT YRKLLEGEES
410 420 430 440 450
RLESGMQNMS IHTKTTSGYA GGLSSSYGGL TSPGFSYGMS SFQPGFGSVG
460 470 480
GSSTYSRTKA VVVKKIETRD GKLVSESSDI MSK
Length:483
Mass (Da):54,019
Last modified:January 23, 2007 - v3
Checksum:iF52521FFFD972C2A
GO

Sequence cautioni

Q10758: The sequence AAA19668 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63482 mRNA. Translation: AAA19667.1.
M63482 mRNA. Translation: AAA19668.1. Different initiation.
S76054 mRNA. No translation available.
AY464139 mRNA. Translation: AAR36875.1.
BC091106 mRNA. Translation: AAH91106.1.
BC097497 mRNA. Translation: AAH97497.1.
RefSeqiNP_955402.1. NM_199370.1.
UniGeneiRn.11083.

Genome annotation databases

EnsembliENSRNOT00000038480; ENSRNOP00000029068; ENSRNOG00000009779.
GeneIDi25626.
KEGGirno:25626.
UCSCiRGD:2984. rat.

Similar proteinsi

Entry informationi

Entry nameiK2C8_RAT
AccessioniPrimary (citable) accession number: Q10758
Secondary accession number(s): Q5WPB3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 145 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families