K1C17_BOVIN
ID K1C17_BOVIN Reviewed; 441 AA.
AC A1L595; A5PJJ6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
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:ABM06133.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:ABM06133.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2] {ECO:0000312|EMBL:AAI42138.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI42138.1};
RC TISSUE=Fetal skin {ECO:0000312|EMBL:AAI42138.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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-42 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}.
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DR EMBL; BT029882; ABM06133.1; -; mRNA.
DR EMBL; BC142137; AAI42138.1; -; mRNA.
DR RefSeq; NP_001098792.1; NM_001105322.1.
DR RefSeq; XP_005220728.1; XM_005220671.2.
DR AlphaFoldDB; A1L595; -.
DR SMR; A1L595; -.
DR STRING; 9913.ENSBTAP00000008948; -.
DR PaxDb; A1L595; -.
DR PeptideAtlas; A1L595; -.
DR PRIDE; A1L595; -.
DR GeneID; 281889; -.
DR KEGG; bta:281889; -.
DR CTD; 3872; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; A1L595; -.
DR OrthoDB; 798081at2759; -.
DR TreeFam; TF332742; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISS: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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Intermediate filament; Isopeptide bond; Keratin;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..441
FT /note="Keratin, type I cytoskeletal 17"
FT /id="PRO_0000310577"
FT DOMAIN 92..403
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..91
FT /note="Head"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..128
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 129..146
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 147..238
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 239..258
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 259..400
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 401..441
FT /note="Tail"
FT /evidence="ECO:0000255"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61414"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IFU8"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 42
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 118
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IFV3"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 407
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 407
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 409
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 409
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CONFLICT 66
FT /note="G -> S (in Ref. 2; AAI42138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 48712 MW; A02369EA56B935E6 CRC64;
MTTTIRHFSS GSIKGSSGLA GGSSRSCRVS GSLGGGSCRL GSAGGLGSGL GGSSYSSCYS
FGSGGGYGSG GYVSGGYGGG FGGVDGLLVG GEKATMQNLN DRLASYLDKV RALEEANTEL
ELKIRDWYQK QAPGPAPDYS SYFKTIEDLR NKIHTATVDN ANLLLQIDNA RLAADDFRTK
FETEQALRVS VEADINGLRR VLDELTLARA DLEMQIENLK EELAYLRKNH EEEMKALRGQ
VGGEINVEMD AAPGVDLSRI LNEMRDQYEK MAEKNRKDAE DWFFSKTEEL NREVATNSEL
VQSGKSEISE LRRTLQALEI ELQSQLSMKA SLEGSLAETE NRYCMQLSQI QGLIGSVEEQ
LAQLRCEMEQ QNQEYKILLD VKTRLEQEIA TYRRLLEGED AHLTQYKTKE PVTTRQVRTI
VEEVQDGRVI SSREQVHQTS H
