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Keratin, type I cytoskeletal 20 (Cytokeratin-20) (CK-20) (Cytokeratin-21) (CK-21) (Keratin-20) (K20)

 K1C20_RAT               Reviewed;         429 AA.
P25030;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 2.
23-MAY-2018, entry version 100.
RecName: Full=Keratin, type I cytoskeletal 20;
AltName: Full=Cytokeratin-20;
Short=CK-20;
AltName: Full=Cytokeratin-21;
Short=CK-21;
AltName: Full=Keratin-20;
Short=K20;
Name=Krt20; Synonyms=Krt21;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Intestinal epithelium;
PubMed=1711044;
Chandler J.S., Calnek D., Quaroni A.;
"Identification and characterization of rat intestinal keratins.
Molecular cloning of cDNAs encoding cytokeratins 8, 19, and a new 49-
kDa type I cytokeratin (cytokeratin 21) expressed by differentiated
intestinal epithelial cells.";
J. Biol. Chem. 266:11932-11938(1991).
[2]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=7689500; DOI=10.1111/j.1432-0436.1993.tb00649.x;
Calnek D., Quaroni A.;
"Differential localization by in situ hybridization of distinct
keratin mRNA species during intestinal epithelial cell development and
differentiation.";
Differentiation 53:95-104(1993).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-16 AND SER-26,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Plays a significant role in maintaining keratin filament
organization in intestinal epithelia. When phosphorylated, plays a
role in the secretion of mucin in the small intestine (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
Associates with KRT8 (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed predominantly in the intestinal
epithelium in differentiated villus cells.
{ECO:0000269|PubMed:1711044, ECO:0000269|PubMed:7689500}.
-!- DEVELOPMENTAL STAGE: Becomes apparent upon completion of villus
formation at 20 days gestation (2 days before birth) and is
expressed by the entire epithelium of the villus.
{ECO:0000269|PubMed:7689500}.
-!- PTM: Hyperphosphorylation at Ser-13 occurs during the early stages
of apoptosis but becomes less prominent during the later stages.
Phosphorylation at Ser-13 also increases in response to stress
brought on by cell injury (By similarity). {ECO:0000250}.
-!- PTM: Proteolytically cleaved by caspases during apoptosis.
Cleavage occurs at Asp-233 (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: There are two types of cytoskeletal and
microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
basic; 56-70 kDa).
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M63665; AAA41473.1; -; mRNA.
PIR; A40452; A40452.
RefSeq; NP_775151.1; NM_173128.1.
UniGene; Rn.9887; -.
ProteinModelPortal; P25030; -.
SMR; P25030; -.
iPTMnet; P25030; -.
PhosphoSitePlus; P25030; -.
PRIDE; P25030; -.
GeneID; 286912; -.
KEGG; rno:286912; -.
UCSC; RGD:628646; rat.
CTD; 54474; -.
RGD; 628646; Krt20.
HOVERGEN; HBG013015; -.
InParanoid; P25030; -.
KO; K07604; -.
PhylomeDB; P25030; -.
PRO; PR:P25030; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
GO; GO:0050708; P:regulation of protein secretion; ISS:UniProtKB.
InterPro; IPR001664; IF.
InterPro; IPR018039; IF_conserved.
InterPro; IPR039008; IF_rod_dom.
InterPro; IPR002957; Keratin_I.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
PRINTS; PR01248; TYPE1KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Apoptosis; Coiled coil; Complete proteome; Intermediate filament;
Keratin; Phosphoprotein; Reference proteome.
CHAIN 1 429 Keratin, type I cytoskeletal 20.
/FTId=PRO_0000063676.
DOMAIN 75 386 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 74 Head.
REGION 75 110 Coil 1A.
REGION 111 128 Linker 1.
REGION 129 220 Coil 1B.
REGION 221 243 Linker 12.
REGION 244 382 Coil 2.
REGION 383 429 Tail.
SITE 233 234 Cleavage; by caspases. {ECO:0000250}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
SEQUENCE 429 AA; 49388 MW; 95CCA2ABB0F0028C CRC64;
MDFSRRSFHR SLSSSSQGPA LSTSGSLYRK GTMQRLGLHS VYGGWRHGTR ISVSKTTMSY
GNHLSNGGDL FGGNEKLAMQ NLNDRLASYL EKVRSLEQSN SKLEAQIKQW YETNAPSTIR
DYSSYYAQIK ELQDQIKDAQ IENARCVLQI DNAKLAAEDF RLKFETERGM RITVEADLQG
LSKVYDDLTL QKTDLEIQIE ELNKDLALLK KEHQEEVEVL RRQLGNNVNV EVDAAPGLNL
GEIMNEMRQK YEILAQKNLQ EAKEQFERQT QTLEKQVTVN IEELRGTEVQ VTELRRSYQT
LEIELQSQLS MKESLERTLE ETKARYASQL AAIQEMLSSL EAQLMQIRSD TERQNQEYNI
LLDIKTRLEQ EIATYRRLLE GEDIKTTEYQ LNTLEAKDIK KTRKIKTVVE EVVDGKVVSS
EVKEIEENI


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