ID A0A091L071_9GRUI Unreviewed; 354 AA.
AC A0A091L071;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Keratin, type I cytoskeletal 20 {ECO:0000256|ARBA:ARBA00040318};
DE AltName: Full=Cytokeratin-20 {ECO:0000256|ARBA:ARBA00041717};
DE AltName: Full=Keratin-20 {ECO:0000256|ARBA:ARBA00042487};
DE Flags: Fragment;
GN ORFNames=N324_07006 {ECO:0000313|EMBL:KFP45103.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP45103.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP45103.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP45103.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a significant role in maintaining keratin filament
CC organization in intestinal epithelia. When phosphorylated, plays a role
CC in the secretion of mucin in the small intestine.
CC {ECO:0000256|ARBA:ARBA00037685}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Associates with KRT8. {ECO:0000256|ARBA:ARBA00038712}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000256|RuleBase:RU000685}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK761556; KFP45103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091L071; -.
DR Proteomes; UP000053330; Unassembled WGS sequence.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; 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; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; INTERMEDIATE FILAMENT; 1.
DR PANTHER; PTHR23239:SF167; KERATIN, TYPE I CYTOSKELETAL 20; 1.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Intermediate filament {ECO:0000256|ARBA:ARBA00022754,
KW ECO:0000256|RuleBase:RU000685}; Keratin {ECO:0000256|ARBA:ARBA00022744};
KW Reference proteome {ECO:0000313|Proteomes:UP000053330}.
FT DOMAIN 45..354
FT /note="IF rod"
FT /evidence="ECO:0000259|PROSITE:PS51842"
FT COILED 42..119
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 155..334
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP45103.1"
FT NON_TER 354
FT /evidence="ECO:0000313|EMBL:KFP45103.1"
SQ SEQUENCE 354 AA; 40422 MW; 14A545E3A9FD4BCD CRC64;
QAPSVYGGAG GSGTRVSTST NYGQGFGGNF QLNITGNDVL LAGNEKSTMQ NLNERLASYL
EKVRSLEKAN SRIEQQIKEW HEKNTADVRH DYSSYFKTIE DLQNKVGAAQ LENARLVLQI
DNAKLAADDF RLKYENELLL RQSVENDING LIRVRDNLTL TKSDLESQIE SVNEELAFLK
RNHEEDVDRL RKQVGGSVNV EVDAAPTVNL ATIMENMRQQ YEEMAEKNRQ EAKEQFEKQT
EELNQEVAIN IEQVQAQRKE ITSRRQICQG VELELQSELN MKKSLEDTLA ETEARYSYQL
TQIQEAVANL EAQLRQLRAD MEAQNNEYSI LLDIKTRLEM EIATYRHLLE GEDT
//
