K1C14_MOUSE
ID K1C14_MOUSE Reviewed; 484 AA.
AC Q61781; A2A4G4; Q91VQ4; Q99LE0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Keratin, type I cytoskeletal 14;
DE AltName: Full=Cytokeratin-14;
DE Short=CK-14;
DE AltName: Full=Keratin-14;
DE Short=K14;
GN Name=Krt14; Synonyms=Krt1-14;
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 [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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, and Pancreas;
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 [3]
RP SUBUNIT, AND DISULFIDE BOND.
RX PubMed=22705788; DOI=10.1038/nsmb.2330;
RA Lee C.H., Kim M.S., Chung B.M., Leahy D.J., Coulombe P.A.;
RT "Structural basis for heteromeric assembly and perinuclear organization of
RT keratin filaments.";
RL Nat. Struct. Mol. Biol. 19:707-715(2012).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 123-131; 201-207; 218-228; 322-334 AND 414-422, 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 126-484, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
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 IDENTIFICATION IN A COMPLEX WITH KRT5, INTERACTION WITH KRT5, AND TISSUE
RP SPECIFICITY.
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 [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=12657653; DOI=10.1074/jbc.m211184200;
RA Ravindranath R.M., Basilrose R.M. Sr., Ravindranath N.H., Vaitheesvaran B.;
RT "Amelogenin interacts with cytokeratin-5 in ameloblasts during enamel
RT growth.";
RL J. Biol. Chem. 278:20293-20302(2003).
RN [9]
RP INTERACTION WITH TRADD.
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 [10]
RP INTERACTION WITH EPPK1.
RX PubMed=18285451; DOI=10.1242/jcs.013755;
RA Spazierer D., Raberger J., Gross K., Fuchs P., Wiche G.;
RT "Stress-induced recruitment of epiplakin to keratin networks increases
RT their resistance to hyperphosphorylation-induced disruption.";
RL J. Cell Sci. 121:825-833(2008).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=19267394; DOI=10.1002/humu.20981;
RA Roth W., Reuter U., Wohlenberg C., Bruckner-Tuderman L., Magin T.M.;
RT "Cytokines as genetic modifiers in K5-/- mice and in human epidermolysis
RT bullosa simplex.";
RL Hum. Mutat. 30:832-841(2009).
RN [12]
RP IDENTIFICATION IN A COMPLEX WITH KRT5, AND INTERACTION WITH KRT5 AND 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).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=26758872; DOI=10.1093/hmg/ddw001;
RA Allen E.H., Courtney D.G., Atkinson S.D., Moore J.E., Mairs L.,
RA Poulsen E.T., Schiroli D., Maurizi E., Cole C., Hickerson R.P., James J.,
RA Murgatroyd H., Smith F.J., MacEwen C., Enghild J.J., Nesbit M.A.,
RA Leslie Pedrioli D.M., McLean W.H., Moore C.B.;
RT "Keratin 12 missense mutation induces the unfolded protein response and
RT apoptosis in Meesmann epithelial corneal dystrophy.";
RL Hum. Mol. Genet. 25:1176-1191(2016).
CC -!- FUNCTION: The nonhelical tail domain is involved in promoting KRT5-
CC KRT14 filaments to self-organize into large bundles and enhances the
CC mechanical properties involved in resilience of keratin intermediate
CC filaments in vitro. {ECO:0000250|UniProtKB:P02533}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins
CC (PubMed:22705788). Forms a disulfide-linked heterodimer (via 2B
CC domains) with KRT5 (via 2B domains) (PubMed:22705788, PubMed:24940650).
CC Forms a heterodimer with KRT1; the interaction is more abundant in the
CC absence of KRT5 (PubMed:11408584). Interacts with PLEC isoform 1C, when
CC in a heterodimer with KRT5 (PubMed:24940650). Interacts with TRADD and
CC with keratin filaments (PubMed:16702408). Associates with other type I
CC keratins (By similarity). Interacts with EPPK1 (PubMed:18285451).
CC Interacts with KLHL24 (By similarity). {ECO:0000250|UniProtKB:P02533,
CC ECO:0000269|PubMed:11408584, ECO:0000269|PubMed:16702408,
CC ECO:0000269|PubMed:18285451, ECO:0000269|PubMed:22705788,
CC ECO:0000269|PubMed:24940650}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P02533}. Nucleus
CC {ECO:0000250|UniProtKB:P02533}. Note=Expressed in both as a filamentous
CC pattern. {ECO:0000250|UniProtKB:P02533}.
CC -!- TISSUE SPECIFICITY: Expressed in the corneal epithelium (at protein
CC level) (PubMed:26758872). Expressed in the basal layer of the epidermis
CC and the outer root sheath of hair follicles (at protein level)
CC (PubMed:11408584). Expressed in the epithelial basal layer in the tail
CC epidermis (PubMed:2433272). Expressed in the parabasal cell row, basal
CC cell layer, and suprabasal epithelial layer of the tongue
CC (PubMed:2433272). {ECO:0000269|PubMed:11408584,
CC ECO:0000269|PubMed:2433272, ECO:0000269|PubMed:26758872}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the epithelial cells of the tongue
CC and palate at 17 dpc (PubMed:2433272). Expressed in ameloblasts at the
CC periphery and at the incisal region of mandibular molars at P3
CC (PubMed:12657653). Expressed at the Tomes' processes of ameloblasts at
CC the incisal region at P5 (PubMed:12657653). Expression at the incisal
CC region decreased at P7 and P9 (PubMed:12657653).
CC {ECO:0000269|PubMed:12657653, ECO:0000269|PubMed:2433272}.
CC -!- PTM: A disulfide bond is formed between rather than within filaments
CC and promotes the formation of a keratin filament cage around the
CC nucleus. {ECO:0000269|PubMed:22705788}.
CC -!- PTM: Ubiquitinated by the BCR(KLHL24) E3 ubiquitin ligase complex.
CC {ECO:0000250|UniProtKB:P02533}.
CC -!- DISRUPTION PHENOTYPE: Increase in CXCL16 abundance in the epidermis at
CC 2 days of age. {ECO:0000269|PubMed:19267394}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH03325.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590873; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003325; AAH03325.1; ALT_INIT; mRNA.
DR EMBL; BC011074; AAH11074.1; -; mRNA.
DR EMBL; M13806; AAA39392.1; -; mRNA.
DR CCDS; CCDS25413.1; -.
DR PIR; B26135; B26135.
DR RefSeq; NP_001300886.1; NM_001313957.1.
DR RefSeq; NP_058654.1; NM_016958.2.
DR AlphaFoldDB; Q61781; -.
DR SMR; Q61781; -.
DR BioGRID; 201019; 14.
DR ComplexPortal; CPX-5867; Keratin-5 - Keratin-14 dimer complex.
DR IntAct; Q61781; 2.
DR MINT; Q61781; -.
DR STRING; 10090.ENSMUSP00000007272; -.
DR iPTMnet; Q61781; -.
DR PhosphoSitePlus; Q61781; -.
DR CPTAC; non-CPTAC-3833; -.
DR jPOST; Q61781; -.
DR MaxQB; Q61781; -.
DR PaxDb; Q61781; -.
DR PeptideAtlas; Q61781; -.
DR PRIDE; Q61781; -.
DR ProteomicsDB; 269442; -.
DR Antibodypedia; 3600; 1290 antibodies from 49 providers.
DR DNASU; 16664; -.
DR Ensembl; ENSMUST00000007272; ENSMUSP00000007272; ENSMUSG00000045545.
DR GeneID; 16664; -.
DR KEGG; mmu:16664; -.
DR UCSC; uc007lko.1; mouse.
DR CTD; 3861; -.
DR MGI; MGI:96688; Krt14.
DR VEuPathDB; HostDB:ENSMUSG00000045545; -.
DR eggNOG; ENOG502R8V7; Eukaryota.
DR GeneTree; ENSGT00940000154602; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; Q61781; -.
DR OMA; YWATIND; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; Q61781; -.
DR TreeFam; TF332742; -.
DR Reactome; R-MMU-446107; Type I hemidesmosome assembly.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 16664; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q61781; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q61781; protein.
DR Bgee; ENSMUSG00000045545; Expressed in tail skin and 112 other tissues.
DR Genevisible; Q61781; MM.
DR GO; GO:0045178; C:basal part of cell; IDA:UniProtKB.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; ISO:MGI.
DR GO; GO:0045095; C:keratin filament; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990254; F:keratin filament binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:MGI.
DR GO; GO:0042633; P:hair cycle; ISO:MGI.
DR GO; GO:0045110; P:intermediate filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0030216; P:keratinocyte differentiation; IDA:MGI.
DR GO; GO:0048863; P:stem cell differentiation; IDA:MGI.
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; Disulfide bond;
KW Intermediate filament; Keratin; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..484
FT /note="Keratin, type I cytoskeletal 14"
FT /id="PRO_0000063654"
FT DOMAIN 121..432
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..120
FT /note="Head"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..156
FT /note="Coil 1A"
FT REGION 157..174
FT /note="Linker 1"
FT REGION 175..266
FT /note="Coil 1B"
FT REGION 267..289
FT /note="Linker 12"
FT REGION 290..428
FT /note="Coil 2"
FT REGION 429..484
FT /note="Tail"
FT REGION 431..484
FT /note="Interaction with Type I keratins and keratin
FT filaments"
FT /evidence="ECO:0000250"
FT REGION 435..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 370
FT /note="Stutter"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT DISULFID 373
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:22705788"
SQ SEQUENCE 484 AA; 52867 MW; A9B6BA66B2F46668 CRC64;
MATCSRQFTS SSSMKGSCGI GGGSSRMSSI LAGGSCRAPS TYGGMSVTSS RFSSGGACGI
GGGYGGSFSS SSFGGGLGSG FGGRFDGFGG GFGGGLGGGF GGGLGGGLGG GIGDGLLVGS
EKVTMQNLND RLATYLDKVR ALEEANTELE VKIRDWYQRQ RPTEIKDYSP YFKTIEDLKS
KILAATVDNA NVLLQIDNAR LAADDFRTKF ETEQSLRMSV EADINGLRRV LDELTLARAD
LEMQIESLKE ELAYLKKNHE EEMASMRGQV GGDVNVEMDA APGVDLSRIL NEMRDQYEKM
AEKNRKDAEE WFFSKTEELN REVATNSELV QSGKSEISEL RRTMQNLEIE LQSQLSMKAS
LENNLEETKG RYCMQLAQIQ EMIGSVEEQL AQLRCEMEQQ NQEYKILLDV KTRLEQEIAT
YRRLLEGEDA HLSSSQFSSS SQFSSGSQSS RDVTSTNRQI RTKVMDVHDG KVVSTHEQVL
RTKN
