K1C15_MOUSE
ID K1C15_MOUSE Reviewed; 452 AA.
AC Q61414; Q6PEQ0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Keratin, type I cytoskeletal 15;
DE AltName: Full=Cytokeratin-15;
DE Short=CK-15;
DE AltName: Full=Keratin-15;
DE Short=K15;
GN Name=Krt15; Synonyms=Krt1-15;
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].
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=7510260; DOI=10.1016/0378-1119(94)90807-9;
RA Nozaki M., Mori M., Matsushiro A.;
RT "The complete sequence of the gene encoding mouse cytokeratin 15.";
RL Gene 138:197-200(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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]
RP PROTEIN SEQUENCE OF 100-115; 179-185 AND 392-400, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=7539810; DOI=10.1083/jcb.129.5.1329;
RA Lloyd C., Yu Q.C., Cheng J., Turksen K., Degenstein L., Hutton E.,
RA Fuchs E.;
RT "The basal keratin network of stratified squamous epithelia: defining K15
RT function in the absence of K14.";
RL J. Cell Biol. 129:1329-1344(1995).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10623468; DOI=10.1006/excr.1999.4726;
RA Werner S., Munz B.;
RT "Suppression of keratin 15 expression by transforming growth factor beta in
RT vitro and by cutaneous injury in vivo.";
RL Exp. Cell Res. 254:80-90(2000).
RN [6]
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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=14506658; DOI=10.1016/s1083-8791(03)00288-x;
RA Whitaker-Menezes D., Jones S.C., Friedman T.M., Korngold R., Murphy G.F.;
RT "An epithelial target site in experimental graft-versus-host disease and
RT cytokine-mediated cytotoxicity is defined by cytokeratin 15 expression.";
RL Biol. Blood Marrow Transplant. 9:559-570(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-33, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
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 [9]
RP IDENTIFICATION IN A COMPLEX WITH KRT14, AND INTERACTION WITH KRT14 AND
RP PLEC.
RX PubMed=24940650; DOI=10.1038/jid.2014.255;
RA Bouameur J.E., Favre B., Fontao L., Lingasamy P., Begre N., Borradori L.;
RT "Interaction of plectin with keratins 5 and 14: dependence on several
RT plectin domains and keratin quaternary structure.";
RL J. Invest. Dermatol. 134:2776-2783(2014).
CC -!- FUNCTION: In the absence of KRT14, makes a bona fide, but
CC ultrastructurally distinct keratin filament network with KRT5.
CC {ECO:0000269|PubMed:10623468, ECO:0000269|PubMed:7539810}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins
CC (Probable). Forms a heterodimer with KRT14 (PubMed:24940650). Interacts
CC with PLEC isoform 1C, when in a heterodimer with KRT14
CC (PubMed:24940650). Interacts with NOD2 (By similarity).
CC {ECO:0000250|UniProtKB:P19012, ECO:0000269|PubMed:24940650,
CC ECO:0000305|PubMed:24940650}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in the basal cell layer at the
CC tips of rete-like prominences (RLPs) of adult dorsal tongue, outer root
CC sheath (ORS) of hair follicle and skin epidermis (at protein level).
CC {ECO:0000269|PubMed:10623468, ECO:0000269|PubMed:14506658}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the skin at birth (at protein level)
CC (PubMed:11408584). In neonatal mice, additional expression seen in the
CC basal layer of the cornea, forestomach and esophagus (at protein
CC level). {ECO:0000269|PubMed:11408584, ECO:0000269|PubMed:7539810}.
CC -!- INDUCTION: During wound healing expression is suppressed by TGF-beta,
CC TNF-alpha and to a lesser extent by epidermal and keratinocyte growth
CC factors (EGF and KGF respectively). {ECO:0000269|PubMed:10623468}.
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; D16313; BAA03821.1; -; Genomic_DNA.
DR EMBL; BC057934; AAH57934.1; -; mRNA.
DR PIR; I49595; I49595.
DR RefSeq; NP_032495.2; NM_008469.2.
DR AlphaFoldDB; Q61414; -.
DR SMR; Q61414; -.
DR BioGRID; 201020; 13.
DR STRING; 10090.ENSMUSP00000103034; -.
DR iPTMnet; Q61414; -.
DR PhosphoSitePlus; Q61414; -.
DR CPTAC; non-CPTAC-3463; -.
DR jPOST; Q61414; -.
DR PaxDb; Q61414; -.
DR PRIDE; Q61414; -.
DR ProteomicsDB; 269161; -.
DR DNASU; 16665; -.
DR GeneID; 16665; -.
DR KEGG; mmu:16665; -.
DR CTD; 3866; -.
DR MGI; MGI:96689; Krt15.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR InParanoid; Q61414; -.
DR OrthoDB; 798081at2759; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 16665; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Krt15; mouse.
DR PRO; PR:Q61414; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61414; protein.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
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; Direct protein sequencing; Intermediate filament;
KW Isopeptide bond; Keratin; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..452
FT /note="Keratin, type I cytoskeletal 15"
FT /id="PRO_0000063658"
FT DOMAIN 98..410
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..97
FT /note="Head"
FT REGION 98..133
FT /note="Coil 1A"
FT REGION 134..152
FT /note="Linker 1"
FT REGION 153..244
FT /note="Coil 1B"
FT REGION 245..264
FT /note="Linker 12"
FT REGION 265..406
FT /note="Coil 2"
FT REGION 407..452
FT /note="Tail"
FT REGION 413..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 294
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IFV3"
FT MOD_RES 316
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IFV3"
FT CROSSLNK 293
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 443
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 443
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CONFLICT 372..374
FT /note="RCE -> HSQ (in Ref. 1; BAA03821)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="G -> D (in Ref. 1; BAA03821)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="E -> EVSLG (in Ref. 2; AAH57934)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 49138 MW; 4FFBE25AC60E79BF CRC64;
MATTFLQTSS TFGGSSTRGA SLRAGGGSFG GGSLYGGGGS RSISASSARF VSSGAGGGFG
GGMSCGFGGG FGGGFGGGFG GGFGDFGGGD GGLLSGNEKV TMQNLNDRLA SYLDKVRALE
QANTELEVKI RDWYQKQSPA SPDRDYSHYF KTMEEIRDKI LAATIDNSRV VLEIDNARLA
ADDFRLKYEN ELTLRQGVEA DINGLRRVLD ELTLARTDLE MQIEQLNEEL AYLKKNHEEE
MKEFSSQLAG QVNVEMDAAP GVDLTRMLAE MREQYEAIAE KNRRDVEAWF FSKTEELNKE
VASNTEMIQT SKTEITDLRR TLQGLEIELQ SQLSMKAGLE NSLAEVECRY ATQLQQIQGV
ITGLETQLSE LRCEMEAQNQ EYNMLLDIKT RLEQEIATYR NLLEGQDAKM AGIGVREGSS
GGGGSSSSSS NFHISVEESV DGKVVSSRKR EI
