ID   K1C1_XENLA              Reviewed;         429 AA.
AC   P08777;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Keratin, type I cytoskeletal 47 kDa;
GN   Name=xk81a1;
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 [GENOMIC DNA].
RX   PubMed=2430981; DOI=10.1083/jcb.103.5.1957;
RA   Miyatani S., Winkles J.A., Sargent T.D., Dawid I.B.;
RT   "Stage-specific keratins in Xenopus laevis embryos and tadpoles: the XK81
RT   gene family.";
RL   J. Cell Biol. 103:1957-1965(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2410923; DOI=10.1073/pnas.82.16.5413;
RA   Jonas E., Sargent T.D., Dawid I.B.;
RT   "Epidermal keratin gene expressed in embryos of Xenopus laevis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:5413-5417(1985).
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
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; X04804; CAA28496.1; -; Genomic_DNA.
DR   EMBL; X04668; CAA28374.1; -; Genomic_DNA.
DR   EMBL; M11940; AAA49894.1; -; mRNA.
DR   PIR; A25145; A25145.
DR   AlphaFoldDB; P08777; -.
DR   SMR; P08777; -.
DR   PRIDE; P08777; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR23239; PTHR23239; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
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; Intermediate filament; Keratin; Reference proteome.
FT   CHAIN           1..429
FT                   /note="Keratin, type I cytoskeletal 47 kDa"
FT                   /id="PRO_0000063680"
FT   DOMAIN          70..385
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..69
FT                   /note="Head"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..105
FT                   /note="Coil 1A"
FT   REGION          106..127
FT                   /note="Linker 1"
FT   REGION          128..219
FT                   /note="Coil 1B"
FT   REGION          220..242
FT                   /note="Linker 12"
FT   REGION          243..381
FT                   /note="Coil 2"
FT   REGION          382..429
FT                   /note="Tail"
FT   REGION          389..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            323
FT                   /note="Stutter"
SQ   SEQUENCE   429 AA;  47241 MW;  4248E12440B45D2D CRC64;
     MTSYRSSSAS YYSGSSSKGG FGSRSLAGSN SYGGSSFGAG FSSGVGSGFS SSGGNFAMAE
     AASSSFGGNE KHAMQNLNDR LASYLEKVRA LEATNSDLEG KIRNWYDKQS DAGIGAGSKD
     YSKYFEIIAE LRNKIRAATI DNATVTLQID NARLAADDFR LKFENELALR QSVEGDSNGL
     RRVLDELILA RGDFELQIES LTEELAYLKK NHEEEMSHAK SQSAGKVSVE MDAALGVDLT
     SILNNMRADY EILAEKNRRD AELWFNQKSG ELKKEISVGV EQVQASKSEI TELKRSLQSL
     EIELQSQLAM KQSVEGNLNE LQGFYSSQLQ QIQNTIGSLE EQLLQIRSDM EHQNTEYKLL
     LDIKTRLEME IQTYRRLLEG ELGQVTTVAN TSSVESKTES SSTSTTRTRM VKTIVEEVVD
     GKVVSSRVE