K2C8_POTTR
ID K2C8_POTTR Reviewed; 310 AA.
AC Q28810;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Keratin, type II cytoskeletal 8;
DE AltName: Full=Cytokeratin-8;
DE Short=CK-8;
DE AltName: Full=Keratin-8;
DE Short=K8;
DE AltName: Full=Type-II keratin Kb8;
DE Flags: Fragment;
GN Name=KRT8 {ECO:0000250|UniProtKB:P05787};
OS Potorous tridactylus (Potoroo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Potoroidae; Potorous.
OX NCBI_TaxID=9310;
RN [1] {ECO:0000312|EMBL:CAA50316.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7507169; DOI=10.1016/s0022-2836(05)80013-0;
RA Boettger V., Lane E.B.;
RT "A monoclonal antibody epitope on keratin 8 identified using a phage
RT peptide library.";
RL J. Mol. Biol. 235:61-67(1994).
CC -!- FUNCTION: Together with KRT19, helps to link the contractile apparatus
CC to dystrophin at the costameres of striated muscle.
CC {ECO:0000250|UniProtKB:P05787}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins (By
CC similarity). Forms a heterodimer with KRT18 (By similarity). Associates
CC with KRT20 (By similarity). Interacts with PNN (By similarity). When
CC associated with KRT19, interacts with DMD (By similarity). Interacts
CC with APEX1 (By similarity). Interacts with GPER1 (By similarity).
CC Interacts with EPPK1 (By similarity). {ECO:0000250|UniProtKB:P05787,
CC ECO:0000250|UniProtKB:P11679, ECO:0000250|UniProtKB:Q10758}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q10758}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q10758}. Nucleus matrix
CC {ECO:0000250|UniProtKB:Q10758}.
CC -!- PTM: O-glycosylated. O-GlcNAcylation at multiple sites increases
CC solubility, and decreases stability by inducing proteasomal degradation
CC (By similarity). {ECO:0000250}.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {ECO:0000250}.
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; X70987; CAA50316.1; -; mRNA.
DR PIR; S43865; S43865.
DR AlphaFoldDB; Q28810; -.
DR SMR; Q28810; -.
DR PRIDE; Q28810; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Cytoplasm; Glycoprotein; Intermediate filament;
KW Isopeptide bond; Keratin; Methylation; Nucleus; Phosphoprotein;
KW Ubl conjugation.
FT CHAIN <1..310
FT /note="Keratin, type II cytoskeletal 8"
FT /evidence="ECO:0000305"
FT /id="PRO_0000228675"
FT DOMAIN 92..>310
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..127
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 128..144
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 145..236
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 237..260
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 261..310
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 17
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 26
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 34
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 42
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 42
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 102
FT /note="N6-malonyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 208
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 229
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 296
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 296
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:CAA50316.1"
FT NON_TER 310
FT /evidence="ECO:0000312|EMBL:CAA50316.1"
SQ SEQUENCE 310 AA; 35170 MW; 31D37E0BC63BFA85 CRC64;
QRTLKVSSSG PRSFSSRSFS SGPSSRISSS SYSRVGSNSS FRSGVGFGPN YGMGLGSSIG
VGGITAVSVN QSLLNPLKLE LDPSIQAVRT QEKEQIKTLN NKFASFIDKV RFLEQQNKIL
ETKWSFLQQQ KTSQSNLDGL FEKYITNLRR QLDSMGQEKL KLEVELGNMQ GLVEDFKKKY
EDEINKRTEM ENEFVLIKKD VDEAYMNKVE LESRLEGLTD EINFLRHLYE EEIKEMQSQI
SDTSVVVSMD NSRSLDLDGI IADVRAQYEE IANRSRAEAE TMYQIKYEEL QLLAGKHGDD
LRHTKTEISE
