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