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Keratin, type II cytoskeletal 8 (Cytokeratin endo A) (Cytokeratin-8) (CK-8) (Keratin-8) (K8) (Type-II keratin Kb8)

 K2C8_RAT                Reviewed;         483 AA.
Q10758; Q5WPB3;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 150.
RecName: Full=Keratin, type II cytoskeletal 8;
AltName: Full=Cytokeratin endo A;
AltName: Full=Cytokeratin-8;
Short=CK-8;
AltName: Full=Keratin-8;
Short=K8;
AltName: Full=Type-II keratin Kb8;
Name=Krt8; Synonyms=Krt2-8;
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=Prostate;
PubMed=1370816;
Hsieh J.-T., Zhau H.E., Wang X.-H., Liew C.-C., Chung L.W.K.;
"Regulation of basal and luminal cell-specific cytokeratin expression
in rat accessory sex organs. Evidence for a new class of androgen-
repressed genes and insight into their pairwise control.";
J. Biol. Chem. 267:2303-2310(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Prostate;
PubMed=7525090;
Wang X., Hsieh J.-T., Zhau H.E.;
"Cloning and characterization of a specific cytokeratin-8 cDNA from
rat prostatic epithelium.";
Zhongguo Yi Xue Ke Xue Yuan Xue Bao 16:1-7(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DMD, AND TISSUE
SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Heart muscle;
PubMed=15247274; DOI=10.1074/jbc.M400128200;
Ursitti J.A., Lee P.C., Resneck W.G., McNally M.M., Bowman A.L.,
O'Neill A., Stone M.R., Bloch R.J.;
"Cloning and characterization of cytokeratins 8 and 19 in adult rat
striated muscle. Interaction with the dystrophin glycoprotein
complex.";
J. Biol. Chem. 279:41830-41838(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, and Thymus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 9-18; 24-75 AND 415-452, AND PHOSPHORYLATION AT
SER-9; SER-13; SER-24; SER-34; SER-37; SER-43; SER-51; SER-417;
SER-424 AND SER-426.
TISSUE=Liver;
PubMed=8660345; DOI=10.1006/bbrc.1996.0546;
Ando S., Tokui T., Yano T., Inagaki M.;
"Keratin 8 phosphorylation in vitro by cAMP-dependent protein kinase
occurs within the amino- and carboxyl-terminal end domains.";
Biochem. Biophys. Res. Commun. 221:67-71(1996).
[6]
PROTEIN SEQUENCE OF 265-273, AND SUBCELLULAR LOCATION.
TISSUE=Liver;
PubMed=16128803; DOI=10.1111/j.1742-4658.2005.04847.x;
Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K.,
Watanabe Y., Furukawa K., Horigome T.;
"Proteome analysis of a rat liver nuclear insoluble protein fraction
and localization of a novel protein, ISP36, to compartments in the
interchromatin space.";
FEBS J. 272:4327-4338(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16396499; DOI=10.1021/pr0503073;
Moser K., White F.M.;
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
MS/MS.";
J. Proteome Res. 5:98-104(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-24; THR-26;
SER-27; SER-43; SER-44; SER-47; SER-51; SER-253; SER-258; SER-432;
SER-475; SER-478 AND SER-482, 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: Together with KRT19, helps to link the contractile
apparatus to dystrophin at the costameres of striated muscle.
{ECO:0000269|PubMed:15247274}.
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
KRT8 associates with KRT18. Associates with KRT20. Interacts with
PNN. When associated with KRT19, interacts with DMD. Interacts
with TCHP. Interacts with APEX1 (By similarity). Interacts with
GPER1 (By similarity). Interacts with EPPK1 (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:P11679}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16128803}.
Nucleus, nucleoplasm {ECO:0000269|PubMed:16128803}. Nucleus matrix
{ECO:0000269|PubMed:16128803}.
-!- TISSUE SPECIFICITY: Expressed in cardiac and striated muscle.
Expressed at Z-lines within the muscle fibers and at Z-line and M-
line domains at costameres at the sarcolemmal membrane (at protein
level). Observed in coagulating gland, bladder, salivary gland,
kidney, spleen, thymus, lung and heart. Also observed in ventral
prostate, seminal vesicle and liver where expression increases
following castration. {ECO:0000269|PubMed:1370816,
ECO:0000269|PubMed:15247274}.
-!- PTM: O-glycosylated. O-GlcNAcylation at multiple sites increases
solubility, and decreases stability by inducing proteasomal
degradation (By similarity). {ECO:0000250}.
-!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent
manner. {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}.
-!- SEQUENCE CAUTION:
Sequence=AAA19668.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M63482; AAA19667.1; -; mRNA.
EMBL; M63482; AAA19668.1; ALT_INIT; mRNA.
EMBL; S76054; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AY464139; AAR36875.1; -; mRNA.
EMBL; BC091106; AAH91106.1; -; mRNA.
EMBL; BC097497; AAH97497.1; -; mRNA.
RefSeq; NP_955402.1; NM_199370.1.
UniGene; Rn.11083; -.
ProteinModelPortal; Q10758; -.
SMR; Q10758; -.
BioGrid; 247655; 1.
IntAct; Q10758; 4.
MINT; Q10758; -.
STRING; 10116.ENSRNOP00000029068; -.
iPTMnet; Q10758; -.
PhosphoSitePlus; Q10758; -.
PaxDb; Q10758; -.
PRIDE; Q10758; -.
Ensembl; ENSRNOT00000038480; ENSRNOP00000029068; ENSRNOG00000009779.
GeneID; 25626; -.
KEGG; rno:25626; -.
UCSC; RGD:2984; rat.
CTD; 3856; -.
RGD; 2984; Krt8.
eggNOG; ENOG410IG4R; Eukaryota.
eggNOG; ENOG410YY6B; LUCA.
GeneTree; ENSGT00760000118796; -.
HOGENOM; HOG000230976; -.
HOVERGEN; HBG013015; -.
InParanoid; Q10758; -.
KO; K07605; -.
OMA; IENAVCW; -.
OrthoDB; EOG091G09KR; -.
PhylomeDB; Q10758; -.
TreeFam; TF317854; -.
Reactome; R-RNO-6805567; Keratinization.
Reactome; R-RNO-6809371; Formation of the cornified envelope.
PRO; PR:Q10758; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000009779; -.
Genevisible; Q10758; RN.
GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0043034; C:costamere; IDA:RGD.
GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:UniProtKB.
GO; GO:0045095; C:keratin filament; IDA:RGD.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
GO; GO:0030018; C:Z disc; IDA:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0060706; P:cell differentiation involved in embryonic placenta development; IEA:Ensembl.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
GO; GO:0051599; P:response to hydrostatic pressure; IDA:RGD.
GO; GO:0051707; P:response to other organism; IEA:Ensembl.
GO; GO:0045214; P:sarcomere organization; IDA:UniProtKB.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
InterPro; IPR001664; IF.
InterPro; IPR018039; IF_conserved.
InterPro; IPR039008; IF_rod_dom.
InterPro; IPR032444; Keratin_2_head.
InterPro; IPR003054; Keratin_II.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF16208; Keratin_2_head; 1.
PRINTS; PR01276; TYPE2KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm;
Direct protein sequencing; Glycoprotein; Intermediate filament;
Isopeptide bond; Keratin; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1 483 Keratin, type II cytoskeletal 8.
/FTId=PRO_0000063742.
DOMAIN 91 402 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 90 Head.
REGION 91 126 Coil 1A.
REGION 127 143 Linker 1.
REGION 144 235 Coil 1B.
REGION 236 259 Linker 12.
REGION 260 398 Coil 2.
REGION 261 382 Necessary for interaction with PNN.
{ECO:0000250}.
REGION 399 483 Tail.
COMPBIAS 9 51 Ser-rich.
SITE 342 342 Stutter.
MOD_RES 9 9 Phosphoserine; by PKC/PRKCE.
{ECO:0000305|PubMed:8660345}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000269|PubMed:8660345}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 23 23 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 24 24 Phosphoserine; by PKC/PRKCE.
{ECO:0000244|PubMed:22673903,
ECO:0000305|PubMed:8660345}.
MOD_RES 26 26 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 32 32 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000269|PubMed:8660345}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000269|PubMed:8660345}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 40 40 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:8660345}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 49 49 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 49 49 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 51 51 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:8660345}.
MOD_RES 101 101 N6-malonyllysine. {ECO:0000250}.
MOD_RES 207 207 N6-acetyllysine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 253 253 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 274 274 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 295 295 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 325 325 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 400 400 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 404 404 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 417 417 Phosphoserine.
{ECO:0000269|PubMed:8660345}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000269|PubMed:8660345}.
MOD_RES 426 426 Phosphoserine.
{ECO:0000269|PubMed:8660345}.
MOD_RES 432 432 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 475 475 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 477 477 Phosphoserine.
{ECO:0000250|UniProtKB:P05787}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 482 482 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 130 130 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 197 197 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 197 197 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 285 285 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 295 295 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 304 304 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 325 325 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 393 393 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 472 472 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P05787}.
CROSSLNK 472 472 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P05787}.
SEQUENCE 483 AA; 54019 MW; F52521FFFD972C2A CRC64;
MSVRVTQKSY KMSTSGPRAF SSRSFTSGPG ARISSSSFSR VGSSSSSFRG SLGGFGGAGV
GGITAVTVNQ SLLNPLKLEV DPNIQAVRTQ EKEQIKTLNN KFASFIDKVR FLEQQNKMLE
TKWSLLQQQK TSRSNMDNMF ESYINNLRRQ LEALGQEKLK LEVELGNMQG LVEDFKNKYE
DEINKRTEME NEFVLIKKDV DEAYMNKVEL ESRLEGLTDE INFLRQIHEE EIRELQSQIS
DTSVVLSMDN SRSLDMDSII AEVRAQYEEI ANRSRAEAET MYQIKYEELQ TLAGKHGDDL
RRSKTEISEM NRNISRLQAE IDALKGQRAT LEAAIADAEQ RGELAVKDAN AKLEDLKNAL
QKAKQDMARQ LREYQELMNV KLALDIEIAT YRKLLEGEES RLESGMQNMS IHTKTTSGYA
GGLSSSYGGL TSPGFSYGMS SFQPGFGSVG GSSTYSRTKA VVVKKIETRD GKLVSESSDI
MSK


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Genprice Inc, Invoices and accounting
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