Keratin, type I cytoskeletal 17 - Mus musculus (Mouse)

Contribute

Send feedback

Read comments (?) or add your own

Q9QWL7 (K1C17_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Keratin, type I cytoskeletal 17

Alternative name(s):
Cytokeratin-17
Short name=CK-17
Keratin-17
Short name=K17

Gene names

Name:	Krt17
Synonyms:	Krt1-17

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role 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". 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. Ref.1 Ref.8 Ref.9 Ref.10
Subunit structure	Heterodimer of a type I and a type II keratin. KRT17 associates with KRT6 isomers By similarity. Interacts with TRADD and SFN. Ref.9 Ref.10
Subcellular location	Cytoplasm Ref.9 Ref.10.
Tissue specificity	Expressed strongly in outer root sheath and medulla region of hair follicle and in the early differentiating epithelial cells (trichocytes) within the hair bulb region. Weak expression in the matrix cells of hair bulb. Also present in the sweat gland within the skin, vibrissae follicle, salivary gland, tooth and thymus. Ref.6 Ref.7 Ref.8
Developmental stage	Expression first occurs in a subset of epithelial cells within the single-layered, undifferentiated ectoderm of embryonic day 10.5 mouse fetuses. In the ensuing 48 hours, K17-expressing cells give rise to placodes, the precursors of ectoderm-derived appendages (hair, glands, and tooth), and to periderm. Ref.1
Induction	Induced in damaged or stressed epidermis and by interferon-gamma. Up-regulated by LEF1. Ref.1 Ref.6
Miscellaneous	There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
Sequence similarities	Belongs to the intermediate filament family.

Ontologies

Keywords
Cellular component	Cytoplasm Intermediate filament Keratin
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	intermediate filament organization Inferred from genetic interaction PubMed 15601842. Source: MGI keratinization Inferred from genetic interaction PubMed 15601842. Source: MGI morphogenesis of an epithelium Inferred from genetic interaction PubMed 15601842. Source: MGI positive regulation of cell growth Inferred from mutant phenotype Ref.10. Source: UniProtKB positive regulation of hair follicle development Inferred from mutant phenotype Ref.9. Source: UniProtKB positive regulation of translation Inferred from mutant phenotype Ref.10. Source: UniProtKB
Cellular_component	cell periphery Inferred from direct assay PubMed 16682203. Source: MGI cytoplasm Inferred from direct assay Ref.9. Source: UniProtKB intermediate filament Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	MHC class II receptor activity Inferred from electronic annotation. Source: Compara structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Sfn	O70456	3	EBI-309015,EBI-1544118

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 433

433

Keratin, type I cytoskeletal 17

PRO_0000063665

Regions

Region

1 – 83

Head

Region

84 – 392

309

Rod

Region

84 – 120

Coil 1A

Region

121 – 138

Linker 1

Region

139 – 230

Coil 1B

Region

231 – 250

Linker 12

Region

251 – 392

142

Coil 2

Region

393 – 433

Tail

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

319

Phosphoserine Ref.11

Experimental info

Mutagenesis

T → A: Reduces binding to SNF. Ref.10

Mutagenesis

S → A: Reduces binding to SNF. Ref.10

Mutagenesis

R → P: Causes twisted hair shafts, broken hair follicles at sebaceous gland level and occasional rupture of the hair bulb or epidermal cyst-like changes. Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

Q9QWL7 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 279081DF2ECE105D
Show »

FASTA

433

48,162

        10         20         30         40         50         60 
MTTTIRQFTS SSSIKGSSGL GGGSSRTSCR LSGSLGAGSC RLGSASGLGS ALGSNSYSSC 

        70         80         90        100        110        120 
YSFGTGSGYG GNFGGVDGLL AGGEKATMQN LNDRLASYLD KVRALEEANT ELEVKIRDWY 

       130        140        150        160        170        180 
QKQAPGPARD YSAYYHTIED LKNKILVATV DNASILLQID NARLAADDFR TKFETEQALR 

       190        200        210        220        230        240 
MSVEADINGL RRVLDELTLA RADLEMQIEN LKEELAYLKK NHEEEMNALR GQVGGEINVE 

       250        260        270        280        290        300 
MDAAPGVDLS RILSEMRDQY EKMAEKNRKD AEDWFFSKTE ELNREVATNS ELVQSGKSEI 

       310        320        330        340        350        360 
SELRRTMQAL EIELQSQLSM KASLEGSLAE TENRYCVQLS QIQGLIGSVE EQLAQLRCEM 

       370        380        390        400        410        420 
EQQNQEYKIL LDVKTRLEQE IATYRRLLEG EDAHLTQYKP KEPVTTRQVR TIVEEVQDGK 

       430 
VISSREQVHQ TTR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Onset of keratin 17 expression coincides with the definition of major epithelial lineages during skin development." McGowan K.M., Coulombe P.A. J. Cell Biol. 143:469-486(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DEVELOPMENTAL STAGE, INDUCTION. Strain: 129/SvJ.
[2]	"The genomic organization of type I keratin genes in mice." Sato H., Koide T., Sagai T., Ishiguro S., Tamai M., Saitou N., Shiroishi T. Genomics 56:303-309(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/10J. Tissue: Skin.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"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: Lung.
[5]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 95-101; 164-170; 285-297 AND 377-385, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[6]	"Three cDNA sequences of mouse type I keratins: cellular localization of the mRNAs in normal and hyperproliferative tissues." Knapp B., Rentrop M., Schweizer J., Winter H. J. Biol. Chem. 262:938-945(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 229-433, TISSUE SPECIFICITY, INDUCTION. Tissue: Skin.
[7]	"Keratin 17 expression in the hard epithelial context of the hair and nail, and its relevance for the pachyonychia congenita phenotype." McGowan K.M., Coulombe P.A. J. Invest. Dermatol. 114:1101-1107(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"In vivo alteration of the keratin 17 gene in hair follicles by oligonucleotide-directed gene targeting." Fan W., Yoon K. Exp. Dermatol. 12:832-842(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-94.
[9]	"Keratin 17 modulates hair follicle cycling in a TNFalpha-dependent fashion." Tong X., Coulombe P.A. Genes Dev. 20:1353-1364(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TRADD, SUBCELLULAR LOCATION.
[10]	"A keratin cytoskeletal protein regulates protein synthesis and epithelial cell growth." Kim S., Wong P., Coulombe P.A. Nature 441:362-365(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SFN, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-9 AND SER-44.
[11]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB013608 mRNA. Translation: BAA34229.1. AL590873 Genomic DNA. Translation: CAM17780.1. BC132454 mRNA. Translation: AAI32455.1. BC132456 mRNA. Translation: AAI32457.1. M13805 mRNA. Translation: AAA39394.1.
IPI	IPI00230365.
PIR	C26135.
RefSeq	NP_034793.1. NM_010663.2.
UniGene	Mm.14046.
3D structure databases
ProteinModelPortal	Q9QWL7.
SMR	Q9QWL7. Positions 134-232, 248-390.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9QWL7. 3 interactions.
PTM databases
PhosphoSite	Q9QWL7.
Proteomic databases
PaxDb	Q9QWL7.
PRIDE	Q9QWL7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000080893; ENSMUSP00000079699; ENSMUSG00000035557.
GeneID	16667.
KEGG	mmu:16667.
UCSC	uc007lks.1. mouse.
Organism-specific databases
CTD	3872.
MGI	MGI:96691. Krt17.
Phylogenomic databases
eggNOG	NOG148784.
GeneTree	ENSGT00610000085921.
HOGENOM	HOG000230975.
HOVERGEN	HBG013015.
InParanoid	Q9QWL7.
KO	K07604.
OMA	YYHTIED.
OrthoDB	EOG483D4W.
Gene expression databases
Bgee	Q9QWL7.
CleanEx	MM_KRT17.
Genevestigator	Q9QWL7.
GermOnline	ENSMUSG00000035557. Mus musculus.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR002957. Keratin_I. IPR009053. Prefoldin. [Graphical view]
PANTHER	PTHR23239. PTHR23239. 1 hit.
Pfam	PF00038. Filament. 1 hit. [Graphical view]
PRINTS	PR01248. TYPE1KERATIN.
SUPFAM	SSF46579. Prefoldin. 1 hit.
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	KRT17. mouse.
NextBio	290383.
SOURCE	Search...

Entry information

Entry name

K1C17_MOUSE

Accession

Primary (citable) accession number: Q9QWL7
Secondary accession number(s): A2A4G6, Q61783

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 101 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents