ID   K2C1_XENLA              Reviewed;         425 AA.
AC   P04266;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Keratin, type II cytoskeletal I;
DE   AltName: Full=Clone PUF23;
DE   Flags: Fragment;
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].
RX   PubMed=2413219; DOI=10.1016/0022-2836(85)90315-8;
RA   Hoffmann W., Franz J.K., Franke W.W.;
RT   "Amino acid sequence microheterogeneities of basic (type II) cytokeratins
RT   of Xenopus laevis epidermis and evolutionary conservativity of helical and
RT   non-helical domains.";
RL   J. Mol. Biol. 184:713-724(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; X02894; CAA26653.1; -; mRNA.
DR   PIR; A02953; KRXL2A.
DR   AlphaFoldDB; P04266; -.
DR   SMR; P04266; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR003054; Keratin_II.
DR   Pfam; PF00038; Filament; 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; Intermediate filament; Keratin; Reference proteome.
FT   CHAIN           <1..425
FT                   /note="Keratin, type II cytoskeletal I"
FT                   /id="PRO_0000063718"
FT   DOMAIN          <1..296
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          <1..16
FT                   /note="Coil 1A"
FT   REGION          17..37
FT                   /note="Linker 1"
FT   REGION          38..129
FT                   /note="Coil 1B"
FT   REGION          130..153
FT                   /note="Linker 12"
FT   REGION          154..292
FT                   /note="Coil 2"
FT   REGION          293..425
FT                   /note="Tail"
FT   SITE            236
FT                   /note="Stutter"
FT   NON_TER         1
SQ   SEQUENCE   425 AA;  45725 MW;  D58D15DEC8C1C4E3 CRC64;
     FLEQQNKVLE TKWKLLQEQG TKGTTKRANL DPLFEKYIAD LKKYLDNLIS EKGRLQQELK
     NLQLLVEDYK KKYEDEINKR TKAENDFVLL KKDVDAAYMV KTELEAKVDT LTSEINFLRT
     RDAAELSQVH DQVTDTSVVL TMDNNRDLNL DSIIKEVKCQ YEQIAQRSKL EAEALYDQKY
     KQLQQTVEGH GDSIKNSKTE ISDLNRKIQR LKAEIENVKK QIASLNQSIA GAEERGNLSL
     KDAEKKLKDL EDAERKLKAD MARQLKEYQE LMSAKLALNL EISTYRYMLE GEEGRISGQI
     VNKVSISVLS GGSSVYTALG GAAGGMGGGG GGGMGSGHGG GYGGMVFGGG MGCGMGDGMG
     GGGMGGGMGS GHGGGYGHGG AVCFGAGGMG YEGGSMHGGG SSYGHSGGKT SVAIASTTST
     TKKTY