K1C19_MOUSE
ID K1C19_MOUSE Reviewed; 403 AA.
AC P19001;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Keratin, type I cytoskeletal 19;
DE AltName: Full=Cytokeratin-19;
DE Short=CK-19;
DE AltName: Full=Keratin-19;
DE Short=K19;
GN Name=Krt19; Synonyms=Krt1-19;
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 [MRNA].
RX PubMed=2479589; DOI=10.1016/0378-1119(89)90295-3;
RA Ichinose Y., Hashido K., Miyamoto H., Nagata T., Nozaki M., Morita T.,
RA Matsushiro A.;
RT "Molecular cloning and characterization of cDNA encoding mouse cytokeratin
RT no. 19.";
RL Gene 80:315-323(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=2483396; DOI=10.1016/0378-1119(89)90437-x;
RA Lussier M., Ouellet T., Lampron C., Lapointe L., Royal A.;
RT "Mouse keratin 19: complete amino acid sequence and gene expression during
RT development.";
RL Gene 85:435-444(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1701153; DOI=10.1016/0378-1119(90)90363-v;
RA Lussier M., Filion M., Compton J.G., Nadeau J.H., Lapointe L., Royal A.;
RT "The mouse keratin 19-encoding gene: sequence, structure and chromosomal
RT assignment.";
RL Gene 95:203-213(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67 AND SER-75, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, 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 [6]
RP PHOSPHORYLATION AT TYR-394.
RX PubMed=21049038; DOI=10.1371/journal.pone.0013538;
RA Zhou Q., Snider N.T., Liao J., Li D.H., Hong A., Ku N.O., Cartwright C.A.,
RA Omary M.B.;
RT "Characterization of in vivo keratin 19 phosphorylation on tyrosine-391.";
RL PLoS ONE 5:E13538-E13538(2010).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-24; ARG-32; ARG-43; ARG-51 AND
RP ARG-64, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Involved in the organization of myofibers. Together with
CC KRT8, helps to link the contractile apparatus to dystrophin at the
CC costameres of striated muscle (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Interacts with PNN and the actin-binding domain of DMD (By similarity).
CC {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development with
CC highest levels at 8.5 dpc. Expression decreases by 11.5 dpc and
CC increases again by 17.5 dpc. {ECO:0000269|PubMed:2483396}.
CC -!- DOMAIN: This keratin differs from all other IF proteins in lacking the
CC C-terminal tail domain.
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; M28698; AAA60432.1; -; mRNA.
DR EMBL; M36120; AAA39371.1; -; Genomic_DNA.
DR EMBL; BC034561; AAH34561.1; -; mRNA.
DR EMBL; BC085304; AAH85304.1; -; mRNA.
DR CCDS; CCDS25411.1; -.
DR PIR; JQ0028; JQ0028.
DR RefSeq; NP_032497.1; NM_008471.3.
DR AlphaFoldDB; P19001; -.
DR SMR; P19001; -.
DR BioGRID; 201024; 8.
DR STRING; 10090.ENSMUSP00000007317; -.
DR iPTMnet; P19001; -.
DR PhosphoSitePlus; P19001; -.
DR jPOST; P19001; -.
DR PaxDb; P19001; -.
DR PRIDE; P19001; -.
DR ProteomicsDB; 268936; -.
DR Antibodypedia; 1224; 3385 antibodies from 56 providers.
DR DNASU; 16669; -.
DR Ensembl; ENSMUST00000007317; ENSMUSP00000007317; ENSMUSG00000020911.
DR GeneID; 16669; -.
DR KEGG; mmu:16669; -.
DR UCSC; uc007lkm.2; mouse.
DR CTD; 3880; -.
DR MGI; MGI:96693; Krt19.
DR VEuPathDB; HostDB:ENSMUSG00000020911; -.
DR eggNOG; ENOG502QV0B; Eukaryota.
DR GeneTree; ENSGT00940000155258; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; P19001; -.
DR OMA; QEYLLLM; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; P19001; -.
DR TreeFam; TF332742; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 16669; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Krt19; mouse.
DR PRO; PR:P19001; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P19001; protein.
DR Bgee; ENSMUSG00000020911; Expressed in epithelium of stomach and 178 other tissues.
DR ExpressionAtlas; P19001; baseline and differential.
DR Genevisible; P19001; MM.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0043034; C:costamere; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; ISO:MGI.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:1990357; C:terminal web; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0008307; F:structural constituent of muscle; ISO:MGI.
DR GO; GO:0060706; P:cell differentiation involved in embryonic placenta development; IGI: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:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; ISO: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; Intermediate filament; Keratin; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..403
FT /note="Keratin, type I cytoskeletal 19"
FT /id="PRO_0000063672"
FT DOMAIN 83..394
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..82
FT /note="Head"
FT REGION 83..118
FT /note="Coil 1A"
FT REGION 119..136
FT /note="Linker 1"
FT REGION 137..228
FT /note="Coil 1B"
FT REGION 229..251
FT /note="Linker 12"
FT REGION 247..393
FT /note="Necessary for interaction with PNN"
FT /evidence="ECO:0000250"
FT REGION 252..390
FT /note="Coil 2"
FT REGION 391..403
FT /note="Rod-like helical tail"
FT SITE 270
FT /note="Stutter"
FT SITE 330
FT /note="Stutter"
FT MOD_RES 7
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 24
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 24
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63279"
FT MOD_RES 32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63279"
FT MOD_RES 43
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 51
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63279"
FT MOD_RES 64
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 394
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:21049038"
SQ SEQUENCE 403 AA; 44542 MW; 8CA8A45FFE288BB1 CRC64;
MTSYSYRQTS AMSSFGGTGG GSVRIGSGGV FRAPSIHGGS GGRGVSVSST RFVTSSSGSY
GGVRGGSFSG TLAVSDGLLS GNEKITMQNL NDRLASYLDK VRALEQANGE LEVKIRDWYQ
KQGPGPSRDY NHYFKTIEDL RDKILGATID NSKIVLQIDN ARLAADDFRT KFETEHALRL
SVEADINGLR RVLDELTLAR TDLEMQIESL KEELAYLKKN HEEEITALRS QVGGQVSVEV
DSTPGVDLAK ILSEMRSQYE IMAEKNRKDA EATYLARIEE LNTQVAVHSE QIQISKTEVT
DLRRTLQGLE IELQSQLSMK AALEGTLAET EARYGVQLSQ IQSVISGFEA QLSDVRADIE
RQNQEYKQLM DIKSRLEQEI ATYRSLLEGQ EAHYNNLPTP KAI
