ID   K2C8_XENLA              Reviewed;         502 AA.
AC   P08776;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Keratin, type II cytoskeletal 8;
DE   AltName: Full=Cytokeratin-8;
DE            Short=CK-8;
DE   AltName: Full=Keratin-8;
DE            Short=K8;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=2428034; DOI=10.1073/pnas.83.17.6475;
RA   Franz J.K., Franke W.W.;
RT   "Cloning of cDNA and amino acid sequence of a cytokeratin expressed in
RT   oocytes of Xenopus laevis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:6475-6479(1986).
CC   -!- FUNCTION: Together with KRT19, helps to link the contractile apparatus
CC       to dystrophin at the costameres of striated muscle. {ECO:0000250}.
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       Keratin-8 associates with keratin-18 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm
CC       {ECO:0000250}. Nucleus matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in oocytes, eggs, embryos, liver and
CC       intestinal mucosa. {ECO:0000269|PubMed:2428034}.
CC   -!- DEVELOPMENTAL STAGE: Synthesized in the oocyte in early and late
CC       embryonic stages. {ECO:0000269|PubMed:2428034}.
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}.
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DR   EMBL; M13811; AAA49891.1; -; mRNA.
DR   PIR; A23547; A23547.
DR   AlphaFoldDB; P08776; -.
DR   SMR; P08776; -.
DR   PRIDE; P08776; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Intermediate filament; Keratin; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..502
FT                   /note="Keratin, type II cytoskeletal 8"
FT                   /id="PRO_0000063743"
FT   DOMAIN          99..410
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..98
FT                   /note="Head"
FT   REGION          99..134
FT                   /note="Coil 1A"
FT   REGION          135..151
FT                   /note="Linker 1"
FT   REGION          152..243
FT                   /note="Coil 1B"
FT   REGION          244..267
FT                   /note="Linker 12"
FT   REGION          268..406
FT                   /note="Coil 2"
FT   REGION          269..390
FT                   /note="Necessary for interaction with PNN"
FT                   /evidence="ECO:0000250"
FT   REGION          407..502
FT                   /note="Tail"
FT   SITE            350
FT                   /note="Stutter"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         40
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         425
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         428
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         436
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         444
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  55679 MW;  96249824FBE131F0 CRC64;
     MSVRSTKVTY RTSSAAPRSG GFSSFSYSGA PMASRASSAS FSLGSSYGGA SRFGSGYRSG
     FGGAGVGSAG ITSVSVNQSL LAPLNLEIDP SIQQVRTEEK EQIKTLNNKF ASFIDKVRFL
     EQQNKMLETK WNLLQNQKTT RSNMDGMFEA YISNLRRQLD GLGQDKMRLE SELGNMQGLV
     EDFKNKYEDE INRRTELENE FVLLKKDVDE AYMNKVQLEA RLEALTDEIN FLRQLYEEEL
     REMQSQISDT SVVLSMDNNR SLDLDGIIAE VRAQYEDVAN KSRLEVENMY QVKYQELQTS
     AGRYGDDLKN TKTEISELTR YTTRLQSEID ALKAQRANLE AQIAEAEERG ELALKDARNK
     LAELEAALQK AKQDMSRQLR DYQELMNVKL ALDIEIATYR KLLEGEESRL ESGFQNLSIQ
     TKTVSGVSSG FGGGISSGFS NGVSSGFGGG YGGGYGGGYS YSSNVSSYIG DTKTSKRRLL
     VKTVETKDGR VLSESSDVFS KP