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Database: UniProt
Entry: A0A099ZIY6_TINGU
LinkDB: A0A099ZIY6_TINGU
Original site: A0A099ZIY6_TINGU 
ID   A0A099ZIY6_TINGU        Unreviewed;       358 AA.
AC   A0A099ZIY6;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=N309_02232 {ECO:0000313|EMBL:KGL81751.1};
OS   Tinamus guttatus (White-throated tinamou).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX   NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL81751.1, ECO:0000313|Proteomes:UP000053641};
RN   [1] {ECO:0000313|EMBL:KGL81751.1, ECO:0000313|Proteomes:UP000053641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL81751.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-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; KL894503; KGL81751.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099ZIY6; -.
DR   STRING; 94827.A0A099ZIY6; -.
DR   Proteomes; UP000053641; 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:UP000053641}.
FT   DOMAIN          50..358
FT                   /note="IF rod"
FT                   /evidence="ECO:0000259|PROSITE:PS51842"
FT   COILED          54..124
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          160..187
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          219..332
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL81751.1"
FT   NON_TER         358
FT                   /evidence="ECO:0000313|EMBL:KGL81751.1"
SQ   SEQUENCE   358 AA;  40508 MW;  5875BD84C9D5259E CRC64;
     FQAPSVYGGA GGYGTRISSS TNYGQGFGGR FNNSFQLSVT GNEDLLSGNE KATMQNLNDR
     LASYLEKVRA LEKANSHIEQ QIKEYYEKNS SAVSRDHSPY FTIIEELRTK IGAAQLENAR
     LVLQIDNAKL AADDFRIKFE NEHLLLQSVQ SDINGLLRVR DDLTLTKADL ESQIEGVNEE
     ILFLKKSHEE EVYSLHKQVG GSVNVEVDAA PGINLASIME KMRLQYEEMA EKNREEAKQR
     FEKQTEQLTQ EVAINIEQLQ SQRTEITERR QIIQGLELEL QSHLNMKKSL EDTLADTEAR
     YSQQLAQIQG AVARLEAQLR QLRADMAGQS SEYAALLDVK TRLEMEIATY RRLLEGDD
//
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