K1C13_MOUSE
ID K1C13_MOUSE Reviewed; 437 AA.
AC P08730; Q3V176; Q6PAI1;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Keratin, type I cytoskeletal 13;
DE AltName: Full=47 kDa cytokeratin;
DE AltName: Full=Cytokeratin-13;
DE Short=CK-13;
DE AltName: Full=Keratin-13;
DE Short=K13;
GN Name=Krt13; Synonyms=Krt1-13;
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;
RX PubMed=7535287; DOI=10.1006/geno.1994.1620;
RA Filion M., Sarafian V., Lussier M., Belanger C., Lapointe L., Royal A.;
RT "Arrangement of a cluster of three mouse type I keratin genes expressed
RT sequentially during esophageal-type epithelial cell differentiation.";
RL Genomics 24:303-310(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-157, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=1695590; DOI=10.1111/j.1432-0436.1990.tb00436.x;
RA Winter H., Rentrop M., Nischt R., Schweizer J.;
RT "Tissue-specific expression of murine keratin K13 in internal stratified
RT squamous epithelia and its aberrant expression during two-stage mouse skin
RT carcinogenesis is associated with the methylation state of a distinct CpG
RT site in the remote 5'-flanking region of the gene.";
RL Differentiation 43:105-114(1990).
RN [5]
RP PROTEIN SEQUENCE OF 107-113; 177-183; 194-204 AND 390-398, 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 126-437 (ISOFORM 1).
RX PubMed=2418416; DOI=10.1093/nar/14.2.751;
RA Knapp B., Rentrop M., Schweizer J., Winter H.;
RT "Nonepidermal members of the keratin multigene family: cDNA sequences and
RT in situ localization of the mRNAs.";
RL Nucleic Acids Res. 14:751-763(1986).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Liver;
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 [8]
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).
RN [9]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=32758484; DOI=10.1016/j.ydbio.2020.07.016;
RA Simonson L., Vold S., Mowers C., Massey R.J., Ong I.M., Longley B.J.,
RA Chang H.;
RT "Keratin 13 deficiency causes white sponge nevus in mice.";
RL Dev. Biol. 468:146-153(2020).
CC -!- FUNCTION: Type 1 keratin (Probable). Maintains postnatal tongue mucosal
CC cell homeostasis and tissue organization in response to mechanical
CC stress, potentially via regulation of the G1/S phase cyclins CCNE1 and
CC CCNE2 (PubMed:32758484). {ECO:0000269|PubMed:32758484, ECO:0000305}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P08730-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P08730-2; Sequence=VSP_016378;
CC -!- TISSUE SPECIFICITY: Expressed in tongue epithelia (at protein level)
CC (PubMed:1695590). Expressed in upper suprabasal layers of the corneal
CC epithelium (at protein level) (PubMed:26758872).
CC {ECO:0000269|PubMed:1695590, ECO:0000269|PubMed:26758872}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the oral mucosa, including the
CC palate, dorsal tongue, ventral tongue, and the floor of the mouth at
CC 17.5 dpc (PubMed:32758484). Expressed in basal cells and differentiated
CC keratinocytes at the ventral surface and the oral interpapillary cell
CC column on the dorsal surface of the tongue at birth (PubMed:32758484).
CC Ubiquitously expressed in basal cells and differentiated keratinocytes
CC on the ventral tongue epithelium, however expression was limited to the
CC cells in the interpapillary region and keratinized layer on the dorsal
CC tongue at postnatal day 20 (P20) (PubMed:32758484). Also expressed in
CC the buccal mucosa and esophagus at P20 (PubMed:32758484).
CC {ECO:0000269|PubMed:32758484}.
CC -!- PTM: O-glycosylated; glycans consist of single N-acetylglucosamine
CC residues. {ECO:0000250|UniProtKB:P13646}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice maintain a normal body weight and
CC developmental phenotype (PubMed:32758484). Tongue histological
CC abnormalities are evident at P20 including the loss of two lingual
CC vessel branches at the ventral side of the tongue which appears white
CC and wrinkled, especially on the ventral surface at three weeks of age
CC (PubMed:32758484). Loss of column-like basal cell organization and
CC increase in nuclear atypia and vacuolization in both the basal and
CC suprabasal layers of the tongue (PubMed:32758484). Loss of keratohyalin
CC granules, abnormal presence of cuboidal cells in the suprabasal layers
CC and loss of organization of the outermost keratin layer leading to a
CC foamy appearance (PubMed:32758484). Increase in intracellular gaps,
CC however desmosomes still formed but were found broken and intermediate
CC filaments running from the desmosomes to the cytoplasm were missing or
CC reduced (PubMed:32758484). Cytoplasmic vacuolization is evident in all
CC cell layers and large lipid droplets are found in granular cells in the
CC tongue epithelia (PubMed:32758484). Severe abnormalities in buccal
CC mucosa and esophagus including thickened epithelium, immature
CC suprabasal cells, loss of keratohyalin granules and a disorganized
CC keratin layer at P20 (PubMed:32758484). Disrupted proliferation and
CC differentiation in tongue epithelial cells at P20, as indicated by
CC disordered expression of the transcription factor Tp63/P63, the basal
CC progenitor cell marker Krt5, and the differentiated epithelial cell
CC marker Loricrin (PubMed:32758484). Increase in proliferating cells in
CC the upper layers of the tongue epithelium at P20 (PubMed:32758484).
CC Normal tongue morphology, structural architecture and epithelial cell
CC proliferation at birth (PubMed:32758484). Differential expression of
CC 125 genes in the tongue at P0, enriched in keratinization,
CC proinflammatory responses, stress-activated protein kinase signaling
CC and threonine/lipid metabolic processes (PubMed:32758484). Differential
CC expression of 2907 genes in the ventral tongue at P20 involved in a
CC range of processes, however primarily in cell cycle regulatory pathways
CC (PubMed:32758484). Increase in the expression of CCNE1 and CCNE2 in
CC response to in vitro mechanical stress of the tongue (PubMed:32758484).
CC {ECO:0000269|PubMed:32758484}.
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; U13921; AAC52150.1; -; Genomic_DNA.
DR EMBL; AK132640; BAE21276.1; -; mRNA.
DR EMBL; BC060286; AAH60286.1; -; mRNA.
DR EMBL; X53320; CAA37407.1; -; Genomic_DNA.
DR EMBL; X03492; CAA27208.1; -; mRNA.
DR CCDS; CCDS25409.1; -. [P08730-1]
DR PIR; A55682; A55682.
DR RefSeq; NP_001300878.1; NM_001313949.1.
DR RefSeq; NP_034792.1; NM_010662.2. [P08730-1]
DR AlphaFoldDB; P08730; -.
DR SMR; P08730; -.
DR BioGRID; 201018; 11.
DR IntAct; P08730; 2.
DR MINT; P08730; -.
DR STRING; 10090.ENSMUSP00000007275; -.
DR iPTMnet; P08730; -.
DR PhosphoSitePlus; P08730; -.
DR jPOST; P08730; -.
DR PaxDb; P08730; -.
DR PeptideAtlas; P08730; -.
DR PRIDE; P08730; -.
DR ProteomicsDB; 269048; -. [P08730-1]
DR ProteomicsDB; 269049; -. [P08730-2]
DR DNASU; 16663; -.
DR Ensembl; ENSMUST00000007275; ENSMUSP00000007275; ENSMUSG00000044041. [P08730-1]
DR GeneID; 16663; -.
DR KEGG; mmu:16663; -.
DR UCSC; uc007lkj.1; mouse. [P08730-1]
DR CTD; 3860; -.
DR MGI; MGI:101925; Krt13.
DR VEuPathDB; HostDB:ENSMUSG00000044041; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR GeneTree; ENSGT00940000154403; -.
DR HOGENOM; CLU_012560_8_3_1; -.
DR InParanoid; P08730; -.
DR OMA; DAKMTGF; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; P08730; -.
DR TreeFam; TF332742; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 16663; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Krt13; mouse.
DR PRO; PR:P08730; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P08730; protein.
DR Bgee; ENSMUSG00000044041; Expressed in superior surface of tongue and 103 other tissues.
DR Genevisible; P08730; MM.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0045095; C:keratin filament; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0043555; P:regulation of translation in response to stress; IMP:UniProtKB.
DR GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR GO; GO:0043587; P:tongue morphogenesis; IEA:Ensembl.
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 Alternative splicing; Coiled coil; Direct protein sequencing; Glycoprotein;
KW Intermediate filament; Keratin; Methylation; Reference proteome.
FT CHAIN 1..437
FT /note="Keratin, type I cytoskeletal 13"
FT /id="PRO_0000063648"
FT DOMAIN 96..408
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..95
FT /note="Head"
FT REGION 96..131
FT /note="Coil 1A"
FT REGION 132..150
FT /note="Linker 1"
FT REGION 151..242
FT /note="Coil 1B"
FT REGION 243..265
FT /note="Linker 12"
FT REGION 266..404
FT /note="Coil 2"
FT REGION 405..437
FT /note="Tail"
FT REGION 408..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P13646"
FT MOD_RES 35
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P13646"
FT VAR_SEQ 300..425
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016378"
SQ SEQUENCE 437 AA; 47754 MW; 924128DBAC317E2F CRC64;
MSCRFQSSSM SYGGGFGAGS CQLGGGRNIS SCSSRFVTGG SAGGYGGGMS CGFGGGAGGG
FGGGFGGGFG GSYGGGFGGG FGDFGGVDGG LLSGNEKITM QNLNDRLASY LDKVRALEAA
NADLEVKIRD WHLKQSPASP ERDYSAYYKT IEELRIKILE ATTDNNRIIL EIDNARLAAD
DFRLKYENEL TLRQSVEADI NGLRRVLDEL TLAKTDLEMQ IESLNEELAY LKKNHEEEMK
EFSNQVVGQV NVEMDATPGI DLTRVLAEMR EQYEALAEKN RRDAEEWFQT KSAELNKEVS
SNAEMIQTSK TEITELRRTL QGLEIELQSQ LSMKAGLEST LAETECRYAL QLQQIQGLIS
SIEAQLSELR SEMECQNQEY KMLLDIKTRL EQEIATYRSL LEGQDAKMTG FNSGGNNTTT
SNGSPSSNSG RPDFRKY
