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Database: UniProt
Entry: A0A091UEW1_PHORB
LinkDB: A0A091UEW1_PHORB
Original site: A0A091UEW1_PHORB 
ID   A0A091UEW1_PHORB        Unreviewed;       354 AA.
AC   A0A091UEW1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=N337_06879 {ECO:0000313|EMBL:KFQ89091.1};
OS   Phoenicopterus ruber ruber.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Phoenicopteriformes; Phoenicopteridae;
OC   Phoenicopterus.
OX   NCBI_TaxID=9218 {ECO:0000313|EMBL:KFQ89091.1, ECO:0000313|Proteomes:UP000053700};
RN   [1] {ECO:0000313|EMBL:KFQ89091.1, ECO:0000313|Proteomes:UP000053700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N337 {ECO:0000313|EMBL:KFQ89091.1};
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}.
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DR   EMBL; KK431397; KFQ89091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091UEW1; -.
DR   Proteomes; UP000053700; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053700}.
FT   DOMAIN          45..354
FT                   /note="IF rod"
FT                   /evidence="ECO:0000259|PROSITE:PS51842"
FT   COILED          155..327
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ89091.1"
FT   NON_TER         354
FT                   /evidence="ECO:0000313|EMBL:KFQ89091.1"
SQ   SEQUENCE   354 AA;  40458 MW;  07B1453643C306BE CRC64;
     QAPSVYGGAG GYGTRISTST SYGQGFGGNF QLNVTGGDVL LSGTEKSTMQ NLNDRLASYL
     EKVRSLEKAN SLIETQIKEW YQKNTADVRH DYSSYFKTIE ELQNKIGDAQ LENARLVLQI
     DNAKLAADDF RLKYENEHLL RQSVENDIQG LLRVRDDLTL TKADLESQIE TVNEEIAFLK
     KNHEEDVDRL RKQVGGSINV EVDAAPSTDL ATIMQNMRQQ YEEMAEKNRQ EAKEQFEKQT
     EELNQEVATN VEQLQAHRRE ITNQRQILQG LELELQSHLN MKKSLEDTLA ETEARYSYEL
     AQIQQAVANL EAQLRQLRAD MEGQNNEYSI LLDIKTRLEM EIATYRRLLE GEDS
//
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