ID K1C20_BOVIN Reviewed; 422 AA.
AC A6QQQ9;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 08-NOV-2023, entry version 76.
DE RecName: Full=Keratin, type I cytoskeletal 20;
DE AltName: Full=Cytokeratin-20;
DE Short=CK-20;
DE AltName: Full=Keratin-20;
DE Short=K20;
GN Name=KRT20 {ECO:0000250|UniProtKB:P35900};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI49956.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI49956.1};
RC TISSUE=Ileum {ECO:0000312|EMBL:AAI49956.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9D312}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Associates with KRT8 (By similarity). {ECO:0000250|UniProtKB:P35900,
CC ECO:0000305}.
CC -!- PTM: Hyperphosphorylation at Ser-13 occurs during the early stages of
CC apoptosis but becomes less prominent during the later stages.
CC Phosphorylation at Ser-13 also increases in response to stress brought
CC on by cell injury (By similarity). {ECO:0000250|UniProtKB:P35900,
CC ECO:0000250|UniProtKB:Q9D312}.
CC -!- PTM: Proteolytically cleaved by caspases during apoptosis. Cleavage
CC occurs at Asp-228 (By similarity). {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI49956.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC149955; AAI49956.1; ALT_INIT; mRNA.
DR RefSeq; NP_001095321.1; NM_001101851.2.
DR AlphaFoldDB; A6QQQ9; -.
DR SMR; A6QQQ9; -.
DR STRING; 9913.ENSBTAP00000010255; -.
DR PaxDb; 9913-ENSBTAP00000054250; -.
DR PeptideAtlas; A6QQQ9; -.
DR GeneID; 505214; -.
DR KEGG; bta:505214; -.
DR CTD; 54474; -.
DR eggNOG; ENOG502QUY3; Eukaryota.
DR HOGENOM; CLU_012560_8_2_1; -.
DR InParanoid; A6QQQ9; -.
DR OrthoDB; 4640531at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
DR GO; GO:0050708; P:regulation of protein secretion; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Apoptosis; Coiled coil; Intermediate filament; Keratin; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..422
FT /note="Keratin, type I cytoskeletal 20"
FT /id="PRO_0000308357"
FT DOMAIN 70..381
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..69
FT /note="Head"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..105
FT /note="Coil 1A"
FT REGION 106..123
FT /note="Linker 1"
FT REGION 124..215
FT /note="Coil 1B"
FT REGION 216..238
FT /note="Linker 12"
FT REGION 239..377
FT /note="Coil 2"
FT REGION 378..422
FT /note="Tail"
FT SITE 228..229
FT /note="Cleavage; by caspases"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and PKC"
FT /evidence="ECO:0000250|UniProtKB:P35900"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D312"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25030"
FT CONFLICT 1
FT /note="M -> V (in Ref. 1; AAI49956)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 48172 MW; 2F0890CBE0400B1C CRC64;
MDFSQRSFHR SLSSSSQSPG LSMSSSIYRR GVAPSVYGGA GGHGTRISTS RHLANYGSVP
AGGNLFAGNE KMTMQNLNDR LASYLERVRS LEQSNSHLEQ QIKHWYETNT PSTGRDHSAY
MGQIKELRDQ IKDAQLQNAR CVLQIDNAKL AMEDFRLKYE AERGICQTVV ADLHGLKRVF
DELTLTKADL EIQIEELTKD LHLLQKEHEE EVRSLRAHLG NNVNVEVDAP PSLNLGAIMN
EMRQKYDAMA QENLQKAKEQ FEIQINDLQQ QVTVSTEELK GTKDQIKEQR HTYQVLELEL
QSLLNMKEAL EHTLEETNAR YGSHLAKIQA RLNSLEGQLV QVRTDTERQI HEYNILLDIK
IRLEQEIATY RRLLEGEDVK EYQLSTLDEK DIKKTRKIKT VVQEVVDGKV VSSEVKEVEE
SV
//
