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Database: UniProt
Entry: A0A091EIM3_FUKDA
LinkDB: A0A091EIM3_FUKDA
Original site: A0A091EIM3_FUKDA 
ID   A0A091EIM3_FUKDA        Unreviewed;       494 AA.
AC   A0A091EIM3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Keratin, type II cytoskeletal 8 {ECO:0000256|ARBA:ARBA00039429};
DE   AltName: Full=Cytokeratin-8 {ECO:0000256|ARBA:ARBA00042964};
DE   AltName: Full=Keratin-8 {ECO:0000256|ARBA:ARBA00042886};
DE   AltName: Full=Type-II keratin Kb8 {ECO:0000256|ARBA:ARBA00043133};
GN   ORFNames=H920_03204 {ECO:0000313|EMBL:KFO35331.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO35331.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO35331.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO35331.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Together with KRT19, helps to link the contractile apparatus
CC       to dystrophin at the costameres of striated muscle.
CC       {ECO:0000256|ARBA:ARBA00037766}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus matrix {ECO:0000256|ARBA:ARBA00004109}.
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DR   EMBL; KN121817; KFO35331.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091EIM3; -.
DR   STRING; 885580.ENSFDAP00000014289; -.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.5.500; Single helix bin; 1.
DR   Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR032444; Keratin_2_head.
DR   InterPro; IPR003054; Keratin_II.
DR   PANTHER; PTHR45616; GATA-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45616:SF26; KERATIN, TYPE II CYTOSKELETAL 8; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF16208; Keratin_2_head; 1.
DR   PRINTS; PR01276; TYPE2KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 3.
DR   PROSITE; PS51842; IF_ROD_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Intermediate filament {ECO:0000256|ARBA:ARBA00022754};
KW   Keratin {ECO:0000256|ARBA:ARBA00022744};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT   DOMAIN          115..424
FT                   /note="IF rod"
FT                   /evidence="ECO:0000259|PROSITE:PS51842"
FT   COILED          168..257
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          337..403
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   494 AA;  56405 MW;  A383842646984ABB CRC64;
     MWFFKKPWSH LPEAAAWLHP SLHHVHEGDP DLQGVHLWPP GFQQPLIHQW PRFPCQLLQL
     LPSGQQQQLP GQPRSGRLWR CCWHGGITAV LVNQSLLNCL DLEVDPNIQA VRLQEKEQIK
     TLNNKFASFI DKVRFLEQQN KMLATKWSLL QQQQTSQSNM DNMFESYNSH LRQQLDTLGQ
     EKLKLEAELG NKQGLVEDFK NKYEDEINKR REIENKFVLI KKDVDEAYMN KVELESRLEL
     TDEINFLRQQ YEEEICELQS QISDTSVVLS MDNSRSLDLD GIITEVKAQY EKTANLSHAE
     ADSMYQIKYE ELQTLAGKHR DDLHCMKSEI SDKNHSISRL QGKIEALKGQ RASLEAAIAD
     AKQRGELAIN DTNAKLAQLE GALQKAKQDM AQQLHEYQKL MNVKLVVDIE TTYHKLLEGE
     ENRLEAGMQN MSIQMKTTSG YSGMVSSPYG GLPIPGFGSL QSPGFTPTKS AVVVKKIKTC
     DRKLVSQTSD VLPK
//
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