ID K1C17_PANTR Reviewed; 432 AA.
AC A5A6M0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 08-NOV-2023, entry version 81.
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 {ECO:0000312|EMBL:BAF62393.1};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1] {ECO:0000312|EMBL:BAF62393.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin {ECO:0000312|EMBL:BAF62393.1};
RX PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT large potential divergence of the transcriptome.";
RL Gene 399:1-10(2007).
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. Required for the correct growth of hair follicles,
CC in particular for the persistence of the anagen (growth) state.
CC Modulates the function of TNF-alpha in the specific context of hair
CC cycling. Regulates protein synthesis and epithelial cell growth through
CC binding to the adapter protein SFN and by stimulating Akt/mTOR pathway.
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. May act as an autoantigen in
CC the immunopathogenesis of psoriasis, with certain peptide regions being
CC a major target for autoreactive T-cells and hence causing their
CC proliferation. {ECO:0000250|UniProtKB:Q04695,
CC ECO:0000250|UniProtKB:Q9QWL7}.
CC -!- SUBUNIT: Heterodimer of a type I and a type II keratin. KRT17
CC associates with KRT6 isomers (KRT6A or KRT6B). Interacts with TRADD and
CC SFN (By similarity). {ECO:0000250|UniProtKB:Q9QWL7, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QWL7}.
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 -!- 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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB222148; BAF62393.1; -; mRNA.
DR RefSeq; NP_001138309.1; NM_001144837.2.
DR AlphaFoldDB; A5A6M0; -.
DR SMR; A5A6M0; -.
DR STRING; 9598.ENSPTRP00000015625; -.
DR PaxDb; 9598-ENSPTRP00000015625; -.
DR GeneID; 468261; -.
DR KEGG; ptr:468261; -.
DR CTD; 3872; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR InParanoid; A5A6M0; -.
DR OrthoDB; 4640531at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.500; Single helix bin; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; INTERMEDIATE FILAMENT; 1.
DR PANTHER; PTHR23239:SF180; KERATIN, TYPE I CYTOSKELETAL 17; 1.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR SUPFAM; SSF46579; Prefoldin; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Intermediate filament; Isopeptide bond; Keratin;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..432
FT /note="Keratin, type I cytoskeletal 17"
FT /id="PRO_0000310578"
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 /evidence="ECO:0000255"
FT REGION 121..138
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 139..230
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 231..250
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 251..392
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 393..432
FT /note="Tail"
FT /evidence="ECO:0000255"
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:0000250|UniProtKB:Q04695"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
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 400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
SQ SEQUENCE 432 AA; 48121 MW; 3C94DB366BAC86C2 CRC64;
MTTTIRQFTS SSSIKGSSGL GGGSSRTSCR LSGGLGAGSC RLGSAGGLGS TLGGSSYSSC
YSFGSGGGYG SSFGGVDGLL AGGEKATMQN LNDRLASYLD KVRALEEANT ELEVKIRDWY
QRQAPGPARD YSQYYRTIEE LQNKILTATV DNANILLQID NARLAADDFR TKFETEQALR
LSVEADINGL RRVLDELTLA RADLEMQIEN LKEELAYLKK NHEEEMNALR GQVGGEINVE
MDAAPGVDLS RILNEMRDQY EKMAEKNRKD AEDWFFSKTE ELNREVATNS ELVQSGESEI
SELRRTMQAL EIELQSQLSM KASLEGNLAE TENRYCVQLS QIQGLIGSVE EQLAQLRCEM
EQQNQEYKIL LDVKTRLEQE IATYRRLLEG EDAHLTQYKK EPVTTRQVRT IVEEVQDGKV
ISSREQVHQT TR
//
