K2C8_RAT
ID K2C8_RAT Reviewed; 483 AA.
AC Q10758; Q5WPB3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Keratin, type II cytoskeletal 8;
DE AltName: Full=Cytokeratin endo A;
DE AltName: Full=Cytokeratin-8;
DE Short=CK-8;
DE AltName: Full=Keratin-8;
DE Short=K8;
DE AltName: Full=Type-II keratin Kb8;
GN Name=Krt8; Synonyms=Krt2-8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Prostate;
RX PubMed=1370816; DOI=10.1016/s0021-9258(18)45878-4;
RA Hsieh J.-T., Zhau H.E., Wang X.-H., Liew C.-C., Chung L.W.K.;
RT "Regulation of basal and luminal cell-specific cytokeratin expression in
RT rat accessory sex organs. Evidence for a new class of androgen-repressed
RT genes and insight into their pairwise control.";
RL J. Biol. Chem. 267:2303-2310(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Prostate;
RX PubMed=7525090;
RA Wang X., Hsieh J.-T., Zhau H.E.;
RT "Cloning and characterization of a specific cytokeratin-8 cDNA from rat
RT prostatic epithelium.";
RL Zhongguo Yi Xue Ke Xue Yuan Xue Bao 16:1-7(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DMD, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Heart muscle;
RX PubMed=15247274; DOI=10.1074/jbc.m400128200;
RA Ursitti J.A., Lee P.C., Resneck W.G., McNally M.M., Bowman A.L.,
RA O'Neill A., Stone M.R., Bloch R.J.;
RT "Cloning and characterization of cytokeratins 8 and 19 in adult rat
RT striated muscle. Interaction with the dystrophin glycoprotein complex.";
RL J. Biol. Chem. 279:41830-41838(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 9-18; 24-75 AND 415-452, AND PHOSPHORYLATION AT SER-9;
RP SER-13; SER-24; SER-34; SER-37; SER-43; SER-51; SER-417; SER-424 AND
RP SER-426.
RC TISSUE=Liver;
RX PubMed=8660345; DOI=10.1006/bbrc.1996.0546;
RA Ando S., Tokui T., Yano T., Inagaki M.;
RT "Keratin 8 phosphorylation in vitro by cAMP-dependent protein kinase occurs
RT within the amino- and carboxyl-terminal end domains.";
RL Biochem. Biophys. Res. Commun. 221:67-71(1996).
RN [6]
RP PROTEIN SEQUENCE OF 265-273, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=16128803; DOI=10.1111/j.1742-4658.2005.04847.x;
RA Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K.,
RA Watanabe Y., Furukawa K., Horigome T.;
RT "Proteome analysis of a rat liver nuclear insoluble protein fraction and
RT localization of a novel protein, ISP36, to compartments in the
RT interchromatin space.";
RL FEBS J. 272:4327-4338(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16396499; DOI=10.1021/pr0503073;
RA Moser K., White F.M.;
RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT MS/MS.";
RL J. Proteome Res. 5:98-104(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-24; THR-26; SER-27;
RP SER-43; SER-44; SER-47; SER-51; SER-253; SER-258; SER-432; SER-475; SER-478
RP AND SER-482, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Together with KRT19, helps to link the contractile apparatus
CC to dystrophin at the costameres of striated muscle.
CC {ECO:0000269|PubMed:15247274}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins (By
CC similarity). Forms a heterodimer with KRT18 (By similarity). Associates
CC with KRT20 (By similarity). Interacts with PNN (By similarity). When
CC associated with KRT19, interacts with DMD (PubMed:15247274). Interacts
CC with TCHP (By similarity). Interacts with APEX1 (By similarity).
CC Interacts with GPER1 (By similarity). Interacts with EPPK1 (By
CC similarity). {ECO:0000250|UniProtKB:P05787,
CC ECO:0000250|UniProtKB:P11679, ECO:0000269|PubMed:15247274}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16128803}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:16128803}. Nucleus matrix
CC {ECO:0000269|PubMed:16128803}.
CC -!- TISSUE SPECIFICITY: Expressed in cardiac and striated muscle. Expressed
CC at Z-lines within the muscle fibers and at Z-line and M-line domains at
CC costameres at the sarcolemmal membrane (at protein level). Observed in
CC coagulating gland, bladder, salivary gland, kidney, spleen, thymus,
CC lung and heart. Also observed in ventral prostate, seminal vesicle and
CC liver where expression increases following castration.
CC {ECO:0000269|PubMed:1370816, ECO:0000269|PubMed:15247274}.
CC -!- PTM: O-glycosylated. O-GlcNAcylation at multiple sites increases
CC solubility, and decreases stability by inducing proteasomal degradation
CC (By similarity). {ECO:0000250}.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {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 -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA19668.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M63482; AAA19667.1; -; mRNA.
DR EMBL; M63482; AAA19668.1; ALT_INIT; mRNA.
DR EMBL; S76054; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY464139; AAR36875.1; -; mRNA.
DR EMBL; BC091106; AAH91106.1; -; mRNA.
DR EMBL; BC097497; AAH97497.1; -; mRNA.
DR RefSeq; NP_955402.1; NM_199370.1.
DR AlphaFoldDB; Q10758; -.
DR SMR; Q10758; -.
DR BioGRID; 247655; 3.
DR IntAct; Q10758; 8.
DR MINT; Q10758; -.
DR STRING; 10116.ENSRNOP00000029068; -.
DR iPTMnet; Q10758; -.
DR PhosphoSitePlus; Q10758; -.
DR jPOST; Q10758; -.
DR PaxDb; Q10758; -.
DR PRIDE; Q10758; -.
DR Ensembl; ENSRNOT00000038480; ENSRNOP00000029068; ENSRNOG00000009779.
DR GeneID; 25626; -.
DR KEGG; rno:25626; -.
DR UCSC; RGD:2984; rat.
DR CTD; 3856; -.
DR RGD; 2984; Krt8.
DR eggNOG; ENOG502QURK; Eukaryota.
DR GeneTree; ENSGT00940000153339; -.
DR HOGENOM; CLU_012560_5_4_1; -.
DR InParanoid; Q10758; -.
DR OMA; IDKIQFP; -.
DR OrthoDB; 824246at2759; -.
DR PhylomeDB; Q10758; -.
DR TreeFam; TF317854; -.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q10758; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000009779; Expressed in jejunum and 17 other tissues.
DR Genevisible; Q10758; RN.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISO:RGD.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0043034; C:costamere; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; ISO:RGD.
DR GO; GO:0045095; C:keratin filament; IDA:RGD.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR GO; GO:0060706; P:cell differentiation involved in embryonic placenta development; ISO:RGD.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0097284; P:hepatocyte apoptotic process; ISO:RGD.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR GO; GO:0051599; P:response to hydrostatic pressure; IDA:RGD.
DR GO; GO:0051707; P:response to other organism; ISO:RGD.
DR GO; GO:0045214; P:sarcomere organization; IDA:UniProtKB.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:RGD.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Glycoprotein; Intermediate filament; Isopeptide bond; Keratin; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..483
FT /note="Keratin, type II cytoskeletal 8"
FT /id="PRO_0000063742"
FT DOMAIN 91..402
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..90
FT /note="Head"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..126
FT /note="Coil 1A"
FT REGION 127..143
FT /note="Linker 1"
FT REGION 144..235
FT /note="Coil 1B"
FT REGION 236..259
FT /note="Linker 12"
FT REGION 260..398
FT /note="Coil 2"
FT REGION 261..382
FT /note="Necessary for interaction with PNN"
FT /evidence="ECO:0000250"
FT REGION 399..483
FT /note="Tail"
FT SITE 342
FT /note="Stutter"
FT MOD_RES 9
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000305|PubMed:8660345"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8660345"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 23
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 24
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000305|PubMed:8660345,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8660345"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8660345"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 40
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8660345,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 49
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 49
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8660345,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 101
FT /note="N6-malonyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 207
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 295
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 325
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8660345"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8660345"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8660345"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 285
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 304
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 325
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 393
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 472
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 472
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
SQ 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
