K1C17_MOUSE
ID K1C17_MOUSE Reviewed; 433 AA.
AC Q9QWL7; A2A4G6; Q61783;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Keratin, type I cytoskeletal 17;
DE AltName: Full=Cytokeratin-17;
DE Short=CK-17;
DE AltName: Full=Keratin-17;
DE Short=K17;
GN Name=Krt17; Synonyms=Krt1-17;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DEVELOPMENTAL STAGE,
RP AND INDUCTION.
RC STRAIN=129/SvJ;
RX PubMed=9786956; DOI=10.1083/jcb.143.2.469;
RA McGowan K.M., Coulombe P.A.;
RT "Onset of keratin 17 expression coincides with the definition of major
RT epithelial lineages during skin development.";
RL J. Cell Biol. 143:469-486(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/10J; TISSUE=Skin;
RX PubMed=10087197; DOI=10.1006/geno.1998.5721;
RA Sato H., Koide T., Sagai T., Ishiguro S., Tamai M., Saitou N.,
RA Shiroishi T.;
RT "The genomic organization of type I keratin genes in mice.";
RL Genomics 56:303-309(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 95-101; 164-170; 285-297 AND 377-385, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 229-433, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Skin;
RX PubMed=2433272; DOI=10.1016/s0021-9258(19)75876-1;
RA Knapp B., Rentrop M., Schweizer J., Winter H.;
RT "Three cDNA sequences of mouse type I keratins: cellular localization of
RT the mRNAs in normal and hyperproliferative tissues.";
RL J. Biol. Chem. 262:938-945(1987).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=10844551; DOI=10.1046/j.1523-1747.2000.00986.x;
RA McGowan K.M., Coulombe P.A.;
RT "Keratin 17 expression in the hard epithelial context of the hair and nail,
RT and its relevance for the pachyonychia congenita phenotype.";
RL J. Invest. Dermatol. 114:1101-1107(2000).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=11408584; DOI=10.1091/mbc.12.6.1775;
RA Peters B., Kirfel J., Bussow H., Vidal M., Magin T.M.;
RT "Complete cytolysis and neonatal lethality in keratin 5 knockout mice
RT reveal its fundamental role in skin integrity and in epidermolysis bullosa
RT simplex.";
RL Mol. Biol. Cell 12:1775-1789(2001).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=12050118; DOI=10.1101/gad.979502;
RA McGowan K.M., Tong X., Colucci-Guyon E., Langa F., Babinet C.,
RA Coulombe P.A.;
RT "Keratin 17 null mice exhibit age- and strain-dependent alopecia.";
RL Genes Dev. 16:1412-1422(2002).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-94.
RX PubMed=14714564; DOI=10.1111/j.0906-6705.2003.00099.x;
RA Fan W., Yoon K.;
RT "In vivo alteration of the keratin 17 gene in hair follicles by
RT oligonucleotide-directed gene targeting.";
RL Exp. Dermatol. 12:832-842(2003).
RN [11]
RP FUNCTION, INTERACTION WITH TRADD, AND SUBCELLULAR LOCATION.
RX PubMed=16702408; DOI=10.1101/gad.1387406;
RA Tong X., Coulombe P.A.;
RT "Keratin 17 modulates hair follicle cycling in a TNFalpha-dependent
RT fashion.";
RL Genes Dev. 20:1353-1364(2006).
RN [12]
RP FUNCTION, INTERACTION WITH SFN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP THR-9 AND SER-44.
RX PubMed=16710422; DOI=10.1038/nature04659;
RA Kim S., Wong P., Coulombe P.A.;
RT "A keratin cytoskeletal protein regulates protein synthesis and epithelial
RT cell growth.";
RL Nature 441:362-365(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-39, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Pancreas, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP FUNCTION.
RX PubMed=20871598; DOI=10.1038/ng.665;
RA Depianto D., Kerns M.L., Dlugosz A.A., Coulombe P.A.;
RT "Keratin 17 promotes epithelial proliferation and tumor growth by
RT polarizing the immune response in skin.";
RL Nat. Genet. 42:910-914(2010).
CC -!- FUNCTION: Type I keratin involved in the formation and maintenance of
CC various skin appendages, specifically in determining shape and
CC orientation of hair (PubMed:14714564, PubMed:16702408). Required for
CC the correct growth of hair follicles, in particular for the persistence
CC of the anagen (growth) state (PubMed:16702408). Modulates the function
CC of TNF-alpha in the specific context of hair cycling. Regulates protein
CC synthesis and epithelial cell growth through binding to the adapter
CC protein SFN and by stimulating Akt/mTOR pathway (PubMed:16710422).
CC Involved in tissue repair. May be a marker of basal cell
CC differentiation in complex epithelia and therefore indicative of a
CC certain type of epithelial 'stem cells'. Acts as a promoter of
CC epithelial proliferation by acting a regulator of immune response in
CC skin: promotes Th1/Th17-dominated immune environment contributing to
CC the development of basaloid skin tumors (PubMed:20871598). May act as
CC an autoantigen in the immunopathogenesis of psoriasis, with certain
CC peptide regions being a major target for autoreactive T-cells and hence
CC causing their proliferation. {ECO:0000269|PubMed:14714564,
CC ECO:0000269|PubMed:16702408, ECO:0000269|PubMed:16710422,
CC ECO:0000269|PubMed:20871598, ECO:0000269|PubMed:9786956}.
CC -!- SUBUNIT: Heterodimer of a type I and a type II keratin. KRT17
CC associates with KRT6 isomers (KRT6A or KRT6B) (By similarity).
CC Interacts with TRADD and SFN. {ECO:0000250,
CC ECO:0000269|PubMed:16702408, ECO:0000269|PubMed:16710422}.
CC -!- INTERACTION:
CC Q9QWL7; O70456: Sfn; NbExp=3; IntAct=EBI-309015, EBI-1544118;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16702408,
CC ECO:0000269|PubMed:16710422}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in outer root sheath and medulla
CC region of hair follicle and in the early differentiating epithelial
CC cells (trichocytes) within the hair bulb region. Weak expression in the
CC matrix cells of hair bulb. Also present in the sweat gland within the
CC skin, vibrissae follicle, salivary gland, tooth and thymus.
CC {ECO:0000269|PubMed:10844551, ECO:0000269|PubMed:14714564,
CC ECO:0000269|PubMed:2433272}.
CC -!- DEVELOPMENTAL STAGE: Expression first occurs in a subset of epithelial
CC cells within the single-layered, undifferentiated ectoderm of embryonic
CC day 10.5 mouse fetuses (PubMed:9786956). In the ensuing 48 hours, K17-
CC expressing cells give rise to placodes, the precursors of ectoderm-
CC derived appendages (hair, glands, and tooth), and to periderm
CC (PubMed:9786956). Expressed in hair follicles and in the basal and
CC suprabasal layers of the interfollicular epidermis at birth
CC (PubMed:11408584). {ECO:0000269|PubMed:11408584,
CC ECO:0000269|PubMed:9786956}.
CC -!- INDUCTION: Induced in damaged or stressed epidermis and by interferon-
CC gamma. Up-regulated by LEF1. {ECO:0000269|PubMed:2433272,
CC ECO:0000269|PubMed:9786956}.
CC -!- PTM: Phosphorylation at Ser-44 occurs in a growth- and stress-dependent
CC fashion in skin keratinocytes, it has no effect on filament
CC organization. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Severe alopecia during the first week postbirth,
CC correlating with hair fragility, alterations in follicular histology,
CC and apoptosis in matrix cells. {ECO:0000269|PubMed:12050118}.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AB013608; BAA34229.1; -; mRNA.
DR EMBL; AL590873; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC132454; AAI32455.1; -; mRNA.
DR EMBL; BC132456; AAI32457.1; -; mRNA.
DR EMBL; M13805; AAA39394.1; -; mRNA.
DR CCDS; CCDS25415.1; -.
DR PIR; C26135; C26135.
DR RefSeq; NP_034793.1; NM_010663.3.
DR AlphaFoldDB; Q9QWL7; -.
DR SMR; Q9QWL7; -.
DR BioGRID; 201022; 13.
DR DIP; DIP-38042N; -.
DR IntAct; Q9QWL7; 7.
DR MINT; Q9QWL7; -.
DR STRING; 10090.ENSMUSP00000079699; -.
DR iPTMnet; Q9QWL7; -.
DR PhosphoSitePlus; Q9QWL7; -.
DR CPTAC; non-CPTAC-3467; -.
DR jPOST; Q9QWL7; -.
DR PaxDb; Q9QWL7; -.
DR PeptideAtlas; Q9QWL7; -.
DR PRIDE; Q9QWL7; -.
DR ProteomicsDB; 268935; -.
DR Antibodypedia; 6491; 1230 antibodies from 46 providers.
DR DNASU; 16667; -.
DR Ensembl; ENSMUST00000080893; ENSMUSP00000079699; ENSMUSG00000035557.
DR GeneID; 16667; -.
DR KEGG; mmu:16667; -.
DR UCSC; uc007lks.1; mouse.
DR CTD; 3872; -.
DR MGI; MGI:96691; Krt17.
DR VEuPathDB; HostDB:ENSMUSG00000035557; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR GeneTree; ENSGT00940000160681; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; Q9QWL7; -.
DR OMA; YYHTIED; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; Q9QWL7; -.
DR TreeFam; TF332742; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 16667; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Krt17; mouse.
DR PRO; PR:Q9QWL7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9QWL7; protein.
DR Bgee; ENSMUSG00000035557; Expressed in lip and 77 other tissues.
DR Genevisible; Q9QWL7; MM.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0031069; P:hair follicle morphogenesis; IMP:UniProtKB.
DR GO; GO:0045109; P:intermediate filament organization; IGI:MGI.
DR GO; GO:0031424; P:keratinization; IGI:MGI.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IGI:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0051798; P:positive regulation of hair follicle development; IMP:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Direct protein sequencing; Intermediate filament;
KW Isopeptide bond; Keratin; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..433
FT /note="Keratin, type I cytoskeletal 17"
FT /id="PRO_0000063665"
FT DOMAIN 84..395
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..83
FT /note="Head"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..120
FT /note="Coil 1A"
FT REGION 121..138
FT /note="Linker 1"
FT REGION 139..230
FT /note="Coil 1B"
FT REGION 231..250
FT /note="Linker 12"
FT REGION 251..392
FT /note="Coil 2"
FT REGION 393..433
FT /note="Tail"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61414"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IFU8"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 44
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IFV3"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 278
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 399
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 399
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 401
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 401
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 420
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 420
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MUTAGEN 9
FT /note="T->A: Reduces binding to SNF."
FT /evidence="ECO:0000269|PubMed:16710422"
FT MUTAGEN 44
FT /note="S->A: Reduces binding to SNF."
FT /evidence="ECO:0000269|PubMed:16710422"
FT MUTAGEN 94
FT /note="R->P: Causes twisted hair shafts, broken hair
FT follicles at sebaceous gland level and occasional rupture
FT of the hair bulb or epidermal cyst-like changes."
FT /evidence="ECO:0000269|PubMed:14714564"
SQ 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
