K1C19_BOVIN
ID K1C19_BOVIN Reviewed; 399 AA.
AC P08728; Q1JQB4;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 146.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Urinary bladder urothelium;
RX PubMed=2428612; DOI=10.1002/j.1460-2075.1986.tb04438.x;
RA Bader B.L., Magin T.M., Hatzfeld M., Franke W.W.;
RT "Amino acid sequence and gene organization of cytokeratin no. 19, an
RT exceptional tail-less intermediate filament protein.";
RL EMBO J. 5:1865-1875(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; X04152; CAA27770.1; -; Genomic_DNA.
DR EMBL; X04198; CAA27770.1; JOINED; Genomic_DNA.
DR EMBL; BC116088; AAI16089.1; -; mRNA.
DR PIR; A25470; A25470.
DR RefSeq; NP_001015600.1; NM_001015600.3.
DR AlphaFoldDB; P08728; -.
DR SMR; P08728; -.
DR STRING; 9913.ENSBTAP00000006450; -.
DR PaxDb; P08728; -.
DR PeptideAtlas; P08728; -.
DR PRIDE; P08728; -.
DR Ensembl; ENSBTAT00000006450; ENSBTAP00000006450; ENSBTAG00000004905.
DR GeneID; 514812; -.
DR KEGG; bta:514812; -.
DR CTD; 3880; -.
DR VEuPathDB; HostDB:ENSBTAG00000004905; -.
DR VGNC; VGNC:30720; KRT19.
DR eggNOG; ENOG502QV0B; Eukaryota.
DR GeneTree; ENSGT00940000155258; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; P08728; -.
DR OMA; QEYLLLM; -.
DR OrthoDB; 798081at2759; -.
DR TreeFam; TF332742; -.
DR Reactome; R-BTA-6805567; Keratinization.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000004905; Expressed in placenta and 102 other tissues.
DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0043034; C:costamere; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:1990357; C:terminal web; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0008307; F:structural constituent of muscle; IEA:Ensembl.
DR GO; GO:0060706; P:cell differentiation involved in embryonic placenta development; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; 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 2: Evidence at transcript level;
KW Coiled coil; Intermediate filament; Keratin; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..399
FT /note="Keratin, type I cytoskeletal 19"
FT /id="PRO_0000063670"
FT DOMAIN 79..390
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..78
FT /note="Head"
FT REGION 79..114
FT /note="Coil 1A"
FT REGION 115..132
FT /note="Linker 1"
FT REGION 133..224
FT /note="Coil 1B"
FT REGION 225..247
FT /note="Linker 12"
FT REGION 243..389
FT /note="Necessary for interaction with PNN"
FT /evidence="ECO:0000250"
FT REGION 248..386
FT /note="Coil 2"
FT REGION 387..399
FT /note="Rod-like helical tail"
FT SITE 266
FT /note="Stutter"
FT SITE 326
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:0000250|UniProtKB:P08727"
FT MOD_RES 32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
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:0000250|UniProtKB:P08727"
FT MOD_RES 51
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63279"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19001"
FT MOD_RES 322
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
SQ SEQUENCE 399 AA; 43885 MW; 8F2E12149A7B99F2 CRC64;
MTSYSYRQSS STSSFGGMGG GSMRFGAGGA FRAPSIHGGS GGRGVSVSSA RFVSSSSGGY
GGGYGGALAT SDGLLAGNEK LTMQNLNDRL ASYLEKVRAL EEANGDLEVK IRDWYQKQGP
GPARDYSHYF KTIEDLRDQI LGATIENSKI VLQIDNARLA ADDFRTKFET EQALRMSVEA
DINGLRRVLD ELTLARTDLE MQIEGLKEEL AYLKKNHEEE MSVLKGQVGG QVSVEVDSAP
GIDLAKILSD MRSQYEVIAE KNRKDAEAWF ISQTEELNRE VAGHTEQLQI SKTEVTDLRR
TLQGLEIELQ SQLSMKAALE GTLAETEARF GAQLAQIQAL ISGIEAQLSD VRADTERQNQ
EYQHLMDIKT RLEQEIATYR NLLEGQDAYF NDLSLAKAL
