Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Keratin, type I cytoskeletal 17

Gene

Krt17

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

Functioni

Type I keratin involved in the formation and maintenance of various skin appendages, specifically in determining shape and orientation of hair. Required for the correct growth of hair follicles, in particular for the persistence of the anagen (growth) state. Modulates the function of TNF-alpha in the specific context of hair cycling. Regulates protein synthesis and epithelial cell growth through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway. Involved in tissue repair. May be a marker of basal cell differentiation in complex epithelia and therefore indicative of a certain type of epithelial "stem cells". Acts as a promoter of epithelial proliferation by acting a regulator of immune response in skin: promotes Th1/Th17-dominated immune environment contributing to the development of basaloid skin tumors. May act as an autoantigen in the immunopathogenesis of psoriasis, with certain peptide regions being a major target for autoreactive T-cells and hence causing their proliferation.By similarity

GO - Molecular functioni

  • MHC class II receptor activity Source: Ensembl
  • structural constituent of cytoskeleton Source: RGD

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type I cytoskeletal 17
Alternative name(s):
Cytokeratin-17
Short name:
CK-17
Keratin-17
Short name:
K17
Type I keratin Ka17
Gene namesi
Name:Krt17By similarity
Synonyms:Ka17Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi1303181. Krt17.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

  • cell periphery Source: Ensembl
  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: Ensembl
  • intermediate filament Source: RGD
  • keratin filament Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament, Keratin

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 433433Keratin, type I cytoskeletal 17PRO_0000310579Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131PhosphoserineBy similarity
Cross-linki15 – 15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei32 – 321PhosphoserineBy similarity
Modified residuei34 – 341PhosphoserineCombined sources
Modified residuei39 – 391PhosphoserineCombined sources
Modified residuei44 – 441Phosphoserine; by RPS6KA1By similarity
Cross-linki399 – 399Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki420 – 420Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Post-translational modificationi

Phosphorylation at Ser-44 occurs in a growth- and stress-dependent fashion in skin keratinocytes, it has no effect on filament organization.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ6IFU8.
PRIDEiQ6IFU8.

PTM databases

iPTMnetiQ6IFU8.

Expressioni

Gene expression databases

ExpressionAtlasiQ6IFU8. baseline and differential.
GenevisibleiQ6IFU8. RN.

Interactioni

Subunit structurei

Heterodimer of a type I and a type II keratin. KRT17 associates with KRT6 isomers (KRT6A or KRT6B). Interacts with TRADD and SFN (By similarity).By similarityCurated

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005382.

Structurei

3D structure databases

ProteinModelPortaliQ6IFU8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8383HeadAdd
BLAST
Regioni84 – 392309RodSequence analysisAdd
BLAST
Regioni84 – 12037Coil 1ASequence analysisAdd
BLAST
Regioni121 – 13818Linker 1Sequence analysisAdd
BLAST
Regioni139 – 23092Coil 1BSequence analysisAdd
BLAST
Regioni231 – 25020Linker 12Sequence analysisAdd
BLAST
Regioni251 – 392142Coil 2Sequence analysisAdd
BLAST
Regioni393 – 43341TailSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 6253Ser-richSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Sequence analysis

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFTF. Eukaryota.
ENOG410Y9IV. LUCA.
GeneTreeiENSGT00760000118808.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiQ6IFU8.
KOiK07604.
OMAiQYHRTIE.
OrthoDBiEOG7FV3Q8.
PhylomeDBiQ6IFU8.
TreeFamiTF332742.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6IFU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTTIRQFTS SSSIKGSSGL GGGSSRTSCR LSGSLGAGSC RLGSASGLGS
60 70 80 90 100
ALGGNSYSSC YSFGTGSGYG GNFGGVDGLL AGGEKATMQN LNDRLASYLD
110 120 130 140 150
KVRALEEANT ELEVKIRDWY QKQAPGPARD YSAYYQTIED LKNKILVATV
160 170 180 190 200
DNASILLQID NARLAADDFR TKFETEQALR MSVEADINGL RRVLDELTLA
210 220 230 240 250
RADLEMQIEN LKEELAYLKK NHEEEMNALR GQVGGEINVE MDAAPGVDLS
260 270 280 290 300
RILSEMRDQY EKMAEKNRKD AEDWFFSKTE ELNREVATNS ELVQSGKSEI
310 320 330 340 350
SELRRTMQAL EIELQSQLSM KASLEGSLAE TENRYCVQLS QIQGLIGSVE
360 370 380 390 400
EQLAQLRCEM EQQNQEYKIL LDVKTRLEQE IATYRRLLEG EDAHLTQYKP
410 420 430
KEPVTTRQVR TIVEEVQDGK VISSREQVHQ TTR
Length:433
Mass (Da):48,123
Last modified:July 5, 2004 - v1
Checksum:i7CB5C921841382D2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03073469 Genomic DNA. No translation available.
BC100058 mRNA. Translation: AAI00059.1.
BK004050 mRNA. Translation: DAA04484.1.
RefSeqiNP_997710.1. NM_212545.2.
UniGeneiRn.106755.

Genome annotation databases

EnsembliENSRNOT00000005382; ENSRNOP00000005382; ENSRNOG00000026371.
GeneIDi287702.
KEGGirno:287702.
UCSCiRGD:1303181. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03073469 Genomic DNA. No translation available.
BC100058 mRNA. Translation: AAI00059.1.
BK004050 mRNA. Translation: DAA04484.1.
RefSeqiNP_997710.1. NM_212545.2.
UniGeneiRn.106755.

3D structure databases

ProteinModelPortaliQ6IFU8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005382.

PTM databases

iPTMnetiQ6IFU8.

Proteomic databases

PaxDbiQ6IFU8.
PRIDEiQ6IFU8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005382; ENSRNOP00000005382; ENSRNOG00000026371.
GeneIDi287702.
KEGGirno:287702.
UCSCiRGD:1303181. rat.

Organism-specific databases

CTDi3872.
RGDi1303181. Krt17.

Phylogenomic databases

eggNOGiENOG410IFTF. Eukaryota.
ENOG410Y9IV. LUCA.
GeneTreeiENSGT00760000118808.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiQ6IFU8.
KOiK07604.
OMAiQYHRTIE.
OrthoDBiEOG7FV3Q8.
PhylomeDBiQ6IFU8.
TreeFamiTF332742.

Miscellaneous databases

NextBioi626818.
PROiQ6IFU8.

Gene expression databases

ExpressionAtlasiQ6IFU8. baseline and differential.
GenevisibleiQ6IFU8. RN.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway1 Publication.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: ThymusImported.
  3. "Comprehensive analysis of keratin gene clusters in humans and rodents."
    Hesse M., Zimek A., Weber K., Magin T.M.
    Eur. J. Cell Biol. 83:19-26(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.
  4. "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-34 AND SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiK1C17_RAT
AccessioniPrimary (citable) accession number: Q6IFU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 83 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

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.