K1C20_MOUSE
ID K1C20_MOUSE Reviewed; 431 AA.
AC Q9D312; Q6PG82;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Keratin, type I cytoskeletal 20;
DE AltName: Full=Cytokeratin-20;
DE Short=CK-20;
DE AltName: Full=Keratin-20;
DE Short=K20;
GN Name=Krt20 {ECO:0000312|EMBL:AAH57172.1, ECO:0000312|MGI:MGI:1914059};
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] {ECO:0000305, ECO:0000312|EMBL:AAL82480.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH KRT8, AND TISSUE
RP SPECIFICITY.
RX PubMed=12857878; DOI=10.1091/mbc.e03-02-0059;
RA Zhou Q., Toivola D.M., Feng N., Greenberg H.B., Franke W.W., Omary M.B.;
RT "Keratin 20 helps maintain intermediate filament organization in intestinal
RT epithelia.";
RL Mol. Biol. Cell 14:2959-2971(2003).
RN [2] {ECO:0000312|EMBL:BAB31280.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB31280.1};
RC TISSUE=Colon {ECO:0000312|EMBL:BAB31280.1};
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 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 [4] {ECO:0000312|EMBL:AAH57172.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH57172.1};
RC TISSUE=Colon {ECO:0000312|EMBL:AAH57172.1};
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 [5] {ECO:0000312|EMBL:CAM21365.1}
RP PROTEIN SEQUENCE OF 79-87 AND 370-378, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT SER-13.
RX PubMed=16608857; DOI=10.1074/jbc.m512284200;
RA Zhou Q., Cadrin M., Herrmann H., Chen C.-H., Chalkley R.J.,
RA Burlingame A.L., Omary M.B.;
RT "Keratin 20 serine 13 phosphorylation is a stress and intestinal goblet
RT cell marker.";
RL J. Biol. Chem. 281:16453-16461(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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 [9]
RP PHOSPHORYLATION AT SER-13 BY MAPKAPK2 AND MAPKAPK3.
RX PubMed=20724476; DOI=10.1074/jbc.m110.132357;
RA Menon M.B., Schwermann J., Singh A.K., Franz-Wachtel M., Pabst O.,
RA Seidler U., Omary M.B., Kotlyarov A., Gaestel M.;
RT "p38 MAP kinase and MAPKAP kinases MK2/3 cooperatively phosphorylate
RT epithelial keratins.";
RL J. Biol. Chem. 285:33242-33251(2010).
CC -!- FUNCTION: Plays a significant role in maintaining keratin filament
CC organization in intestinal epithelia. When phosphorylated, plays a role
CC in the secretion of mucin in the small intestine.
CC {ECO:0000269|PubMed:12857878, ECO:0000269|PubMed:16608857}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Associates with KRT8. {ECO:0000269|PubMed:12857878, ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in the more differentiated
CC suprabasal regions of the small intestine, and at higher levels in the
CC colon, mainly in the upper region and in scattered cells throughout the
CC remaining epithelium. Also expressed in epithelial cells of bladder,
CC ileum and stomach and at lower levels in pancreas and earskin. The
CC phosphorylated form is nearly exclusively expressed in goblet cells of
CC the small intestine and in the lumen-proximal cells of the colon (at
CC protein level). Also expressed in jejunum and duodenum.
CC {ECO:0000269|PubMed:12857878, ECO:0000269|PubMed:16608857}.
CC -!- PTM: Hyperphosphorylation at Ser-13 occurs during the early stages of
CC apoptosis but becomes less prominent during the later stages (By
CC similarity). Phosphorylation at Ser-13 also increases in response to
CC stress brought on by cell injury. {ECO:0000250|UniProtKB:P35900,
CC ECO:0000269|PubMed:16608857, ECO:0000269|PubMed:20724476}.
CC -!- PTM: Proteolytically cleaved by caspases during apoptosis. Cleavage
CC occurs at Asp-235 (By similarity). {ECO:0000250|UniProtKB:P35900}.
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; AF473907; AAL82480.1; -; mRNA.
DR EMBL; AK018567; BAB31280.1; -; mRNA.
DR EMBL; AL591165; CAM21365.1; -; Genomic_DNA.
DR EMBL; BC057172; AAH57172.1; -; mRNA.
DR CCDS; CCDS25381.1; -.
DR RefSeq; NP_075745.1; NM_023256.2.
DR AlphaFoldDB; Q9D312; -.
DR SMR; Q9D312; -.
DR BioGRID; 211731; 1.
DR STRING; 10090.ENSMUSP00000017743; -.
DR iPTMnet; Q9D312; -.
DR PhosphoSitePlus; Q9D312; -.
DR PaxDb; Q9D312; -.
DR PeptideAtlas; Q9D312; -.
DR PRIDE; Q9D312; -.
DR ProteomicsDB; 269050; -.
DR Antibodypedia; 3502; 1407 antibodies from 50 providers.
DR DNASU; 66809; -.
DR Ensembl; ENSMUST00000017743; ENSMUSP00000017743; ENSMUSG00000035775.
DR GeneID; 66809; -.
DR KEGG; mmu:66809; -.
DR UCSC; uc007liu.1; mouse.
DR CTD; 54474; -.
DR MGI; MGI:1914059; Krt20.
DR VEuPathDB; HostDB:ENSMUSG00000035775; -.
DR eggNOG; ENOG502QUY3; Eukaryota.
DR GeneTree; ENSGT00940000161855; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; Q9D312; -.
DR OMA; YSAYYKQ; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; Q9D312; -.
DR TreeFam; TF332742; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 66809; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Krt20; mouse.
DR PRO; PR:Q9D312; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D312; protein.
DR Bgee; ENSMUSG00000035775; Expressed in small intestine Peyer's patch and 86 other tissues.
DR Genevisible; Q9D312; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0009267; P:cellular response to starvation; IDA:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IMP:UniProtKB.
DR GO; GO:0050708; P:regulation of protein secretion; IDA: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 1: Evidence at protein level;
KW Apoptosis; Coiled coil; Direct protein sequencing; Intermediate filament;
KW Keratin; Phosphoprotein; Reference proteome.
FT CHAIN 1..431
FT /note="Keratin, type I cytoskeletal 20"
FT /id="PRO_0000308358"
FT DOMAIN 77..388
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..76
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..112
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 113..130
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 131..222
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 223..245
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 246..384
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 385..431
FT /note="Tail"
FT /evidence="ECO:0000255"
FT SITE 235..236
FT /note="Cleavage; by caspases"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and PKC"
FT /evidence="ECO:0000269|PubMed:16608857,
FT ECO:0000269|PubMed:20724476"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25030"
FT CONFLICT 24
FT /note="S -> N (in Ref. 4; AAH57172)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="R -> Q (in Ref. 4; AAH57172)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="R -> H (in Ref. 4; AAH57172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 49034 MW; 5375E42A8BA0ACB3 CRC64;
MDFSRQSFHR SLSSSSQGPA LSMSGSLYRK GTVQRLGAAP SVYGGAGGHG TRISVSKAVM
SYGGDLSNGS DLFGGNGKLA MQNLNDRLAN YLEKVRSLEQ SNSRLEAQIK QWYETNAPST
IRDYSSYYAQ IKELQNQVKD AQVQNAQCVL RIDNAKLAAE DFRLKFETER GMRIAVEADL
QGLSKVYDNL TLQKTDLEIQ IEELNKDLAL LKKEHQEEVE VLRRQLGNNV NVEVDAAPGL
NLGEIMNEMR QRYEVLAQKN LQEAKEQFER QSQTLQQQVT VNTEELKGFE VQVTELRRTY
QNLEIELQSH LSMKESLERN LEDVKARYAS QLAAIQEMLS SLEAQLMQIR SDTERQNQEH
NILLDIKTRL EQEIATYRRL LEGEDIKTTE YQLSTLEMKD IKKTRKIKTV VEEVVDGKVV
SSEVKEIEES V
