K2C8_MESAU
ID K2C8_MESAU Reviewed; 110 AA.
AC P86247;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Keratin, type II cytoskeletal 8 {ECO:0000250|UniProtKB:P05787};
DE AltName: Full=Cytokeratin-8 {ECO:0000250|UniProtKB:P05787};
DE Short=CK-8 {ECO:0000250|UniProtKB:P05787};
DE AltName: Full=Keratin-8 {ECO:0000250|UniProtKB:P05787};
DE Short=K8 {ECO:0000250|UniProtKB:P05787};
DE Flags: Fragments;
GN Name=KRT8 {ECO:0000250|UniProtKB:P05787};
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: 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. When associated with
CC KRT19, interacts with DMD (By similarity). Interacts with TCHP (By
CC similarity). Interacts with APEX1 (By similarity). Interacts with GPER1
CC (By similarity). Interacts with EPPK1 (By similarity).
CC {ECO:0000250|UniProtKB:P05787, ECO:0000250|UniProtKB:P11679,
CC 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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR AlphaFoldDB; P86247; -.
DR SMR; P86247; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
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 Pfam; PF00038; Filament; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Glycoprotein; Intermediate filament;
KW Isopeptide bond; Keratin; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN <1..>110
FT /note="Keratin, type II cytoskeletal 8"
FT /id="PRO_0000394419"
FT DOMAIN <1..>110
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION <1..>12
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION <13..25
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 26..39
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 40..>79
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION <80..86
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 87..>110
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 88..99
FT /note="Necessary for interaction with PNN"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 12
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT NON_CONS 12..13
FT /evidence="ECO:0000305"
FT NON_CONS 21..22
FT /evidence="ECO:0000305"
FT NON_CONS 29..30
FT /evidence="ECO:0000305"
FT NON_CONS 44..45
FT /evidence="ECO:0000305"
FT NON_CONS 79..80
FT /evidence="ECO:0000305"
FT NON_CONS 91..92
FT /evidence="ECO:0000305"
FT NON_CONS 98..99
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 110
SQ SEQUENCE 110 AA; 12975 MW; F1BA9D70B802B966 CRC64;
MSTSGPRAFS SRFASFIDKV RWSLLQQQKS NMDNMFESYI NNLRDVDEAY MNKVELESRL
EGLTDEINFL RQIHEEEIRS LDMDSIIAEV RHGDDLRRLA LDIEIATYRK
