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K1C0_XENLA
ID   K1C0_XENLA              Reviewed;         486 AA.
AC   P02537;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Keratin-3, type I cytoskeletal 51 kDa;
DE   AltName: Full=51 kDa cytokeratin;
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=2458965; DOI=10.1016/0014-5793(88)80196-0;
RA   Hoffmann W., Sterrer S., Koenigstorfer A.;
RT   "Amino acid sequence microheterogeneities of a type I cytokeratin of Mr
RT   51,000 from Xenopus laevis epidermis.";
RL   FEBS Lett. 237:178-182(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 339-386.
RX   PubMed=6204859; DOI=10.1002/j.1460-2075.1984.tb01966.x;
RA   Hoffmann W., Franz J.K.;
RT   "Amino acid sequence of the carboxy-terminal part of an acidic type I
RT   cytokeratin of molecular weight 51 000 from Xenopus laevis epidermis as
RT   predicted from the cDNA sequence.";
RL   EMBO J. 3:1301-1306(1984).
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; Y00968; CAA68783.1; -; mRNA.
DR   PIR; S01327; KRXL.
DR   PIR; S04511; S04511.
DR   RefSeq; NP_001081485.1; NM_001088016.1.
DR   AlphaFoldDB; P02537; -.
DR   SMR; P02537; -.
DR   BioGRID; 99202; 1.
DR   PRIDE; P02537; -.
DR   GeneID; 397864; -.
DR   KEGG; xla:397864; -.
DR   CTD; 397864; -.
DR   Xenbase; XB-GENE-22060973; krt57.L.
DR   OrthoDB; 798081at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 397864; Expressed in zone of skin and 11 other tissues.
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..486
FT                   /note="Keratin-3, type I cytoskeletal 51 kDa"
FT                   /id="PRO_0000063679"
FT   DOMAIN          126..442
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..125
FT                   /note="Head"
FT   REGION          126..161
FT                   /note="Coil 1A"
FT   REGION          162..184
FT                   /note="Linker 1"
FT   REGION          185..276
FT                   /note="Coil 1B"
FT   REGION          277..299
FT                   /note="Linker 12"
FT   REGION          300..438
FT                   /note="Coil 2"
FT   REGION          435..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..486
FT                   /note="Tail"
FT   COMPBIAS        443..460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            380
FT                   /note="Stutter"
FT   CONFLICT        352
FT                   /note="R -> T (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   486 AA;  51889 MW;  9B6D026C597109C5 CRC64;
     MSNYSIKQSA KNNYSSSSSG GFRGGHGGNE YFCGVGGEGD FGGMGGFGAC GAGYGGGAGY
     GGGAGGAGYG GGAGGGGAGY GGGFGGGSGA GYGGGFGGGA GGGYGGGFGG GFGGGAGGMD
     IFSTNEKQTM QNLNDRLASY LDKVHALETA NTELERKIKE WYEKQRPGSS SGDGAKDYSK
     YYTMINDLKN QIIAASIENA KFLLQNDNAR LAADDFKMKF ENEQYMRQTV EADINGLRRV
     MDDLTLSKSD LESQLESLSE ELAYLKKNHE DELKGMQVTQ VGQVNVEMNA APSSDLTKIL
     NDMRSQYEDL AKRNRAAAEE QFNRMSTDLK NTLSQGIEQQ KESKSELTEL KRTLQSLEIE
     LQSQLAMKKS LEMTLAEVEG SFCMKLSRLQ EMIVNVEEQI ARLKGESECQ TAEYQQLLDI
     KTRLENEIET YRRLLDGDLS KPKSGGGTST NTGSTSSKGS TRTVKRREII EEVVDGKVVS
     TKVVDM
 
 
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