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Keratin, type I cytoskeletal 17 (Cytokeratin-17) (CK-17) (Keratin-17) (K17)

 K1C17_MOUSE             Reviewed;         433 AA.
Q9QWL7; A2A4G6; Q61783;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
31-JAN-2018, entry version 139.
RecName: Full=Keratin, type I cytoskeletal 17;
AltName: Full=Cytokeratin-17;
Short=CK-17;
AltName: Full=Keratin-17;
Short=K17;
Name=Krt17; Synonyms=Krt1-17;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DEVELOPMENTAL
STAGE, AND INDUCTION.
STRAIN=129/SvJ;
PubMed=9786956; DOI=10.1083/jcb.143.2.469;
McGowan K.M., Coulombe P.A.;
"Onset of keratin 17 expression coincides with the definition of major
epithelial lineages during skin development.";
J. Cell Biol. 143:469-486(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/10J; TISSUE=Skin;
PubMed=10087197; DOI=10.1006/geno.1998.5721;
Sato H., Koide T., Sagai T., Ishiguro S., Tamai M., Saitou N.,
Shiroishi T.;
"The genomic organization of type I keratin genes in mice.";
Genomics 56:303-309(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 95-101; 164-170; 285-297 AND 377-385, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 229-433, TISSUE SPECIFICITY, AND
INDUCTION.
TISSUE=Skin;
PubMed=2433272;
Knapp B., Rentrop M., Schweizer J., Winter H.;
"Three cDNA sequences of mouse type I keratins: cellular localization
of the mRNAs in normal and hyperproliferative tissues.";
J. Biol. Chem. 262:938-945(1987).
[7]
TISSUE SPECIFICITY.
PubMed=10844551; DOI=10.1046/j.1523-1747.2000.00986.x;
McGowan K.M., Coulombe P.A.;
"Keratin 17 expression in the hard epithelial context of the hair and
nail, and its relevance for the pachyonychia congenita phenotype.";
J. Invest. Dermatol. 114:1101-1107(2000).
[8]
DISRUPTION PHENOTYPE.
PubMed=12050118; DOI=10.1101/gad.979502;
McGowan K.M., Tong X., Colucci-Guyon E., Langa F., Babinet C.,
Coulombe P.A.;
"Keratin 17 null mice exhibit age- and strain-dependent alopecia.";
Genes Dev. 16:1412-1422(2002).
[9]
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-94.
PubMed=14714564; DOI=10.1111/j.0906-6705.2003.00099.x;
Fan W., Yoon K.;
"In vivo alteration of the keratin 17 gene in hair follicles by
oligonucleotide-directed gene targeting.";
Exp. Dermatol. 12:832-842(2003).
[10]
FUNCTION, INTERACTION WITH TRADD, AND SUBCELLULAR LOCATION.
PubMed=16702408; DOI=10.1101/gad.1387406;
Tong X., Coulombe P.A.;
"Keratin 17 modulates hair follicle cycling in a TNFalpha-dependent
fashion.";
Genes Dev. 20:1353-1364(2006).
[11]
FUNCTION, INTERACTION WITH SFN, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF THR-9 AND SER-44.
PubMed=16710422; DOI=10.1038/nature04659;
Kim S., Wong P., Coulombe P.A.;
"A keratin cytoskeletal protein regulates protein synthesis and
epithelial cell growth.";
Nature 441:362-365(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-39, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Pancreas, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
FUNCTION.
PubMed=20871598; DOI=10.1038/ng.665;
Depianto D., Kerns M.L., Dlugosz A.A., Coulombe P.A.;
"Keratin 17 promotes epithelial proliferation and tumor growth by
polarizing the immune response in skin.";
Nat. Genet. 42:910-914(2010).
-!- FUNCTION: Type I keratin involved in the formation and maintenance
of various skin appendages, specifically in determining shape and
orientation of hair (PubMed:14714564, PubMed:16702408). Required
for the correct growth of hair follicles, in particular for the
persistence of the anagen (growth) state (PubMed:16702408).
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 (PubMed:16710422). 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 (PubMed:20871598). 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. {ECO:0000269|PubMed:14714564,
ECO:0000269|PubMed:16702408, ECO:0000269|PubMed:16710422,
ECO:0000269|PubMed:20871598, ECO:0000269|PubMed:9786956}.
-!- SUBUNIT: Heterodimer of a type I and a type II keratin. KRT17
associates with KRT6 isomers (KRT6A or KRT6B) (By similarity).
Interacts with TRADD and SFN. {ECO:0000250,
ECO:0000269|PubMed:16702408, ECO:0000269|PubMed:16710422}.
-!- INTERACTION:
O70456:Sfn; NbExp=3; IntAct=EBI-309015, EBI-1544118;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16702408,
ECO:0000269|PubMed:16710422}.
-!- 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. {ECO:0000269|PubMed:10844551,
ECO:0000269|PubMed:14714564, ECO:0000269|PubMed:2433272}.
-!- 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. {ECO:0000269|PubMed:9786956}.
-!- INDUCTION: Induced in damaged or stressed epidermis and by
interferon-gamma. Up-regulated by LEF1.
{ECO:0000269|PubMed:2433272, ECO:0000269|PubMed:9786956}.
-!- PTM: Phosphorylation at Ser-44 occurs in a growth- and stress-
dependent fashion in skin keratinocytes, it has no effect on
filament organization. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Severe alopecia during the first week
postbirth, correlating with hair fragility, alterations in
follicular histology, and apoptosis in matrix cells.
{ECO:0000269|PubMed:12050118}.
-!- MISCELLANEOUS: There are two types of cytoskeletal and
microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
basic; 56-70 kDa).
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB013608; BAA34229.1; -; mRNA.
EMBL; AL590873; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC132454; AAI32455.1; -; mRNA.
EMBL; BC132456; AAI32457.1; -; mRNA.
EMBL; M13805; AAA39394.1; -; mRNA.
CCDS; CCDS25415.1; -.
PIR; C26135; C26135.
RefSeq; NP_034793.1; NM_010663.3.
UniGene; Mm.14046; -.
ProteinModelPortal; Q9QWL7; -.
SMR; Q9QWL7; -.
BioGrid; 201022; 3.
DIP; DIP-38042N; -.
IntAct; Q9QWL7; 7.
MINT; MINT-1859144; -.
STRING; 10090.ENSMUSP00000079699; -.
iPTMnet; Q9QWL7; -.
PhosphoSitePlus; Q9QWL7; -.
PaxDb; Q9QWL7; -.
PeptideAtlas; Q9QWL7; -.
PRIDE; Q9QWL7; -.
Ensembl; ENSMUST00000080893; ENSMUSP00000079699; ENSMUSG00000035557.
GeneID; 16667; -.
KEGG; mmu:16667; -.
UCSC; uc007lks.1; mouse.
CTD; 3872; -.
MGI; MGI:96691; Krt17.
eggNOG; ENOG410IFTF; Eukaryota.
eggNOG; ENOG410Y9IV; LUCA.
GeneTree; ENSGT00900000140820; -.
HOGENOM; HOG000230975; -.
HOVERGEN; HBG013015; -.
InParanoid; Q9QWL7; -.
KO; K07604; -.
OMA; QYHRTIE; -.
OrthoDB; EOG091G087I; -.
PhylomeDB; Q9QWL7; -.
TreeFam; TF332742; -.
Reactome; R-MMU-6805567; Keratinization.
Reactome; R-MMU-6809371; Formation of the cornified envelope.
ChiTaRS; Krt17; mouse.
PRO; PR:Q9QWL7; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000035557; -.
CleanEx; MM_KRT17; -.
Genevisible; Q9QWL7; MM.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
GO; GO:0042289; F:MHC class II protein binding; ISO:MGI.
GO; GO:0032395; F:MHC class II receptor activity; ISO:MGI.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0031069; P:hair follicle morphogenesis; IMP:UniProtKB.
GO; GO:0045109; P:intermediate filament organization; IGI:MGI.
GO; GO:0031424; P:keratinization; IGI:MGI.
GO; GO:0002009; P:morphogenesis of an epithelium; IGI:MGI.
GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
GO; GO:0051798; P:positive regulation of hair follicle development; IMP:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; ISO:MGI.
InterPro; IPR001664; IF.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR002957; Keratin_I.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
PRINTS; PR01248; TYPE1KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing;
Intermediate filament; Isopeptide bond; Keratin; Methylation;
Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 433 Keratin, type I cytoskeletal 17.
/FTId=PRO_0000063665.
DOMAIN 84 395 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 83 Head.
REGION 84 120 Coil 1A.
REGION 121 138 Linker 1.
REGION 139 230 Coil 1B.
REGION 231 250 Linker 12.
REGION 251 392 Coil 2.
REGION 393 433 Tail.
MOD_RES 12 12 Phosphoserine.
{ECO:0000250|UniProtKB:Q04695}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:Q04695}.
MOD_RES 26 26 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P19001}.
MOD_RES 32 32 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000250|UniProtKB:Q6IFU8}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 44 44 Phosphoserine; by RPS6KA1.
{ECO:0000250|UniProtKB:Q04695}.
MOD_RES 110 110 Phosphothreonine.
{ECO:0000250|UniProtKB:Q04695}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000250|UniProtKB:Q04695}.
CROSSLNK 15 15 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:Q04695}.
CROSSLNK 15 15 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q04695}.
CROSSLNK 278 278 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q04695}.
CROSSLNK 399 399 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:Q04695}.
CROSSLNK 399 399 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q04695}.
CROSSLNK 401 401 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:Q04695}.
CROSSLNK 401 401 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q04695}.
CROSSLNK 420 420 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:Q04695}.
CROSSLNK 420 420 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q04695}.
MUTAGEN 9 9 T->A: Reduces binding to SNF.
{ECO:0000269|PubMed:16710422}.
MUTAGEN 44 44 S->A: Reduces binding to SNF.
{ECO:0000269|PubMed:16710422}.
MUTAGEN 94 94 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.
{ECO:0000269|PubMed:14714564}.
SEQUENCE 433 AA; 48162 MW; 279081DF2ECE105D CRC64;
MTTTIRQFTS SSSIKGSSGL GGGSSRTSCR LSGSLGAGSC RLGSASGLGS ALGSNSYSSC
YSFGTGSGYG GNFGGVDGLL AGGEKATMQN LNDRLASYLD KVRALEEANT ELEVKIRDWY
QKQAPGPARD YSAYYHTIED LKNKILVATV DNASILLQID NARLAADDFR TKFETEQALR
MSVEADINGL RRVLDELTLA RADLEMQIEN LKEELAYLKK NHEEEMNALR GQVGGEINVE
MDAAPGVDLS RILSEMRDQY EKMAEKNRKD AEDWFFSKTE ELNREVATNS ELVQSGKSEI
SELRRTMQAL EIELQSQLSM KASLEGSLAE TENRYCVQLS QIQGLIGSVE EQLAQLRCEM
EQQNQEYKIL LDVKTRLEQE IATYRRLLEG EDAHLTQYKP KEPVTTRQVR TIVEEVQDGK
VISSREQVHQ TTR


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