K1C42_MOUSE
ID K1C42_MOUSE Reviewed; 452 AA.
AC Q6IFX2; A7MAW4; Q2M1G8; Q6SEK1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Keratin, type I cytoskeletal 42;
DE AltName: Full=Cytokeratin-42;
DE Short=CK-42;
DE AltName: Full=Keratin-17n;
DE AltName: Full=Keratin-42;
DE Short=K42;
DE AltName: Full=Type I keratin Ka22;
GN Name=Krt42 {ECO:0000312|MGI:MGI:1915489};
GN Synonyms=Ka22 {ECO:0000312|EMBL:DAA04491.1};
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:AAR22526.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAR22526.1};
RX PubMed=15102087; DOI=10.1111/j.0022-202x.2004.22422.x;
RA Tong X., Coulombe P.A.;
RT "A novel mouse type I intermediate filament gene, keratin 17n (K17n),
RT exhibits preferred expression in nail tissue.";
RL J. Invest. Dermatol. 122:965-970(2004).
RN [2]
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 [3] {ECO:0000312|EMBL:AAI48205.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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] {ECO:0000312|EMBL:CAM17782.1}
RP PROTEIN SEQUENCE OF 114-125; 174-180 AND 387-395, 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 [5] {ECO:0000305, ECO:0000312|EMBL:DAA04491.1}
RP IDENTIFICATION.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
CC -!- SUBUNIT: Heterodimer of a type I and a type II keratin. Colocalizes
CC with KRT8/KRT18 filament network. {ECO:0000269|PubMed:15102087,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15102087}.
CC -!- TISSUE SPECIFICITY: Expressed in nail matrix and nail bed epithelium
CC (at protein level). Also expressed in tongue and digits with weak
CC expression in vibrissae and in both filiform and fungiform papillae of
CC oral mucosa. {ECO:0000269|PubMed:15102087}.
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; AY459292; AAR22526.1; -; mRNA.
DR EMBL; AL590873; CAM17782.1; -; Genomic_DNA.
DR EMBL; BC112371; AAI12372.1; -; mRNA.
DR EMBL; BC148204; AAI48205.1; -; mRNA.
DR EMBL; BK004025; DAA04491.1; -; mRNA.
DR CCDS; CCDS25416.1; -.
DR RefSeq; NP_997648.2; NM_212483.2.
DR AlphaFoldDB; Q6IFX2; -.
DR SMR; Q6IFX2; -.
DR BioGRID; 212755; 9.
DR STRING; 10090.ENSMUSP00000017270; -.
DR iPTMnet; Q6IFX2; -.
DR PhosphoSitePlus; Q6IFX2; -.
DR CPTAC; non-CPTAC-3921; -.
DR jPOST; Q6IFX2; -.
DR PaxDb; Q6IFX2; -.
DR PeptideAtlas; Q6IFX2; -.
DR PRIDE; Q6IFX2; -.
DR ProteomicsDB; 268939; -.
DR DNASU; 68239; -.
DR Ensembl; ENSMUST00000017270; ENSMUSP00000017270; ENSMUSG00000053654.
DR GeneID; 68239; -.
DR KEGG; mmu:68239; -.
DR UCSC; uc007lku.1; mouse.
DR CTD; 68239; -.
DR MGI; MGI:1915489; Krt42.
DR VEuPathDB; HostDB:ENSMUSG00000053654; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR GeneTree; ENSGT00940000163247; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; Q6IFX2; -.
DR OMA; CVPGGGF; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; Q6IFX2; -.
DR TreeFam; TF332742; -.
DR BioGRID-ORCS; 68239; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q6IFX2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6IFX2; protein.
DR Bgee; ENSMUSG00000053654; Expressed in epithelium of stomach and 168 other tissues.
DR Genevisible; Q6IFX2; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
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; Cytoplasm; Direct protein sequencing; Intermediate filament;
KW Keratin; Reference proteome.
FT CHAIN 1..452
FT /note="Keratin, type I cytoskeletal 42"
FT /id="PRO_0000311714"
FT DOMAIN 94..405
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 4..93
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 94..129
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 130..147
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 148..239
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 240..262
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 263..401
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 402..452
FT /note="Tail"
FT /evidence="ECO:0000255"
FT CONFLICT 2
FT /note="A -> D (in Ref. 1; AAR22526 and 3; AAI48205)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="A -> S (in Ref. 3; AAI12372/AAI48205)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="A -> V (in Ref. 3; AAI12372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 50133 MW; 4FFE727CEDF69E27 CRC64;
MASTTSVRQF STSGSVKGLC APGMGFSRMS SVRVGGACRA PSLLGGGSCG NMSVTSSRFS
AGLGGGYGGG YTCSLGGGFG SSFGVSDALL GGSEKETMQN LNDRLATYLD RVRALEEANA
DLEVKIREWY KKQGPGPARD YSPYFKTIED LRNKILAATI DNASIVLQID NARLAADDFR
TKYETELNLR MSVEADINGL RRVLDELTLA RADLEMQIES LKEELAYLRK NHEEEMNALR
GQVGGDVNVE MDAAPGVDLS RILNEMRDQY EKMAEKNRKD AEEWFFTKTE ELNREVATNT
EALQSSRTEI TELRRSVQNL EIELQSQLSM KASLENSLAE TEARYGAQLA QLQGLISSVE
QQLCELRCDM ERQNHEYQVL LDVKTRLEQE IATYRRLLEG EDAHLATQYS SSLASQPSRE
GMVTSRQVRT IVEEVQDGKV VSSREQVHRS TH
