K1C17_RAT
ID K1C17_RAT Reviewed; 433 AA.
AC Q6IFU8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
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;
DE AltName: Full=Type I keratin Ka17;
GN Name=Krt17 {ECO:0000250|UniProtKB:Q04695};
GN Synonyms=Ka17 {ECO:0000312|RGD:1303181};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000312|EMBL:AAI00059.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus {ECO:0000312|EMBL:AAI00059.1};
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 [3] {ECO:0000305, ECO:0000312|EMBL:DAA04484.1}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000312|EMBL:DAA04484.1};
RX PubMed=15085952; DOI=10.1078/0171-9335-00354;
RA Hesse M., Zimek A., Weber K., Magin T.M.;
RT "Comprehensive analysis of keratin gene clusters in humans and rodents.";
RL Eur. J. Cell Biol. 83:19-26(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-39, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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}.
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DR EMBL; AABR03073469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC100058; AAI00059.1; -; mRNA.
DR EMBL; BK004050; DAA04484.1; -; mRNA.
DR RefSeq; NP_997710.1; NM_212545.2.
DR AlphaFoldDB; Q6IFU8; -.
DR SMR; Q6IFU8; -.
DR BioGRID; 252298; 2.
DR IntAct; Q6IFU8; 1.
DR STRING; 10116.ENSRNOP00000005382; -.
DR iPTMnet; Q6IFU8; -.
DR PhosphoSitePlus; Q6IFU8; -.
DR jPOST; Q6IFU8; -.
DR PaxDb; Q6IFU8; -.
DR PRIDE; Q6IFU8; -.
DR Ensembl; ENSRNOT00000005382; ENSRNOP00000005382; ENSRNOG00000026371.
DR GeneID; 287702; -.
DR KEGG; rno:287702; -.
DR UCSC; RGD:1303181; rat.
DR CTD; 3872; -.
DR RGD; 1303181; Krt17.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR GeneTree; ENSGT00940000160681; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; Q6IFU8; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; Q6IFU8; -.
DR TreeFam; TF332742; -.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q6IFU8; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000026371; Expressed in thymus and 8 other tissues.
DR ExpressionAtlas; Q6IFU8; baseline and differential.
DR Genevisible; Q6IFU8; RN.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; TAS:RGD.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:RGD.
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; ISO:RGD.
DR GO; GO:0045103; P:intermediate filament-based process; TAS:RGD.
DR GO; GO:0031424; P:keratinization; ISO:RGD.
DR GO; GO:0002009; P:morphogenesis of an epithelium; ISO:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:RGD.
DR GO; GO:0051798; P:positive regulation of hair follicle development; ISO:RGD.
DR GO; GO:0045727; P:positive regulation of translation; ISO:RGD.
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; Intermediate filament; Isopeptide bond; Keratin;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..433
FT /note="Keratin, type I cytoskeletal 17"
FT /id="PRO_0000310579"
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..433
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 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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"
SQ SEQUENCE 433 AA; 48123 MW; 7CB5C921841382D2 CRC64;
MTTTIRQFTS SSSIKGSSGL GGGSSRTSCR LSGSLGAGSC RLGSASGLGS ALGGNSYSSC
YSFGTGSGYG GNFGGVDGLL AGGEKATMQN LNDRLASYLD KVRALEEANT ELEVKIRDWY
QKQAPGPARD YSAYYQTIED 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
