K1C19_MESAU
ID K1C19_MESAU Reviewed; 110 AA.
AC P86246;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Keratin, type I cytoskeletal 19 {ECO:0000250|UniProtKB:P08727};
DE AltName: Full=Cytokeratin-19 {ECO:0000250|UniProtKB:P08727};
DE Short=CK-19 {ECO:0000250|UniProtKB:P08727};
DE AltName: Full=Keratin-19 {ECO:0000250|UniProtKB:P08727};
DE Short=K19 {ECO:0000250|UniProtKB:P08727};
DE Flags: Fragments;
GN Name=KRT19 {ECO:0000250|UniProtKB:P08727};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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).
CC {ECO:0000250|UniProtKB:P08727}.
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|UniProtKB:P08727}.
CC -!- DOMAIN: This keratin differs from all other IF proteins in lacking the
CC C-terminal tail domain. {ECO:0000305}.
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 AlphaFoldDB; P86246; -.
DR SMR; P86246; -.
DR STRING; 10036.XP_005087423.1; -.
DR PRIDE; P86246; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 2.
DR Pfam; PF00038; Filament; 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..>110
FT /note="Keratin, type I cytoskeletal 19"
FT /id="PRO_0000394418"
FT DOMAIN 7..>110
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION <1..>8
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION <9..42
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 43..>45
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION <46..83
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION <85..>110
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION <85..>110
FT /note="Necessary for interaction with PNN"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63279"
FT MOD_RES 8
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT NON_CONS 8..9
FT /evidence="ECO:0000305"
FT NON_CONS 45..46
FT /evidence="ECO:0000305"
FT NON_CONS 54..55
FT /evidence="ECO:0000305"
FT NON_CONS 64..65
FT /evidence="ECO:0000305"
FT NON_CONS 73..74
FT /evidence="ECO:0000305"
FT NON_CONS 84..85
FT /evidence="ECO:0000305"
FT NON_CONS 101..102
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 110
SQ SEQUENCE 110 AA; 12974 MW; C447ECF3636478BF CRC64;
FGSGGVFRIT MQNLNDRLAS YLDKVRALEQ ANGELEVKIR DWYQKIVLQI DNARTKFETE
QALRVLDELT LARKNHEEEI SALRADTERQ NQEYQQLMDI KLEQEIATYR
