K2C6B_MOUSE
ID K2C6B_MOUSE Reviewed; 562 AA.
AC Q9Z331;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Keratin, type II cytoskeletal 6B;
DE AltName: Full=Cytokeratin-6B;
DE Short=CK-6B;
DE AltName: Full=Keratin-6-beta;
DE Short=mK6-beta;
DE AltName: Full=Keratin-6B;
DE Short=K6B;
GN Name=Krt6b; Synonyms=K6-beta {ECO:0000303|PubMed:9790766}, Krt2-6b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=129/Sv {ECO:0000312|EMBL:BAA34179.1};
RC TISSUE=Skin {ECO:0000269|PubMed:9790766};
RX PubMed=9790766; DOI=10.1006/geno.1998.5476;
RA Takahashi K., Yan B., Yamanishi K., Imamura S., Coulombe P.A.;
RT "The two functional keratin 6 genes of mouse are differentially regulated
RT and evolved independently from their human orthologs.";
RL Genomics 53:170-183(1998).
RN [2]
RP INDUCTION, AND SUBUNIT.
RX PubMed=8636216; DOI=10.1083/jcb.132.3.381;
RA Paladini R.D., Takahashi K., Bravo N.S., Coulombe P.A.;
RT "Onset of re-epithelialization after skin injury correlates with a
RT reorganization of keratin filaments in wound edge keratinocytes: defining a
RT potential role for keratin 16.";
RL J. Cell Biol. 132:381-397(1996).
CC -!- SUBUNIT: Heterodimer of a type I and a type II keratin. KRT6 isomers
CC associate with KRT16 and/or KRT17. {ECO:0000269|PubMed:8636216}.
CC -!- TISSUE SPECIFICITY: Expressed in adult epithelia including the tongue,
CC esophagus/trachea, eye and skin. Localized preferentially to the
CC suprabasal layers of thickened epidermis in injured and chemically
CC treated skin. {ECO:0000269|PubMed:9790766}.
CC -!- INDUCTION: By injury, and treatment of the skin with the phorbol ester
CC PMA. {ECO:0000269|PubMed:8636216, ECO:0000269|PubMed:9790766}.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin, I (acidic) and II (neutral to basic) (40-55 and 56-70 kDa,
CC respectively).
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AB012042; BAA34179.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9Z331; -.
DR SMR; Q9Z331; -.
DR STRING; 10090.ENSMUSP00000023786; -.
DR iPTMnet; Q9Z331; -.
DR PhosphoSitePlus; Q9Z331; -.
DR SwissPalm; Q9Z331; -.
DR CPTAC; non-CPTAC-3462; -.
DR jPOST; Q9Z331; -.
DR MaxQB; Q9Z331; -.
DR PRIDE; Q9Z331; -.
DR ProteomicsDB; 268944; -.
DR MGI; MGI:1333768; Krt6b.
DR eggNOG; ENOG502QURK; Eukaryota.
DR InParanoid; Q9Z331; -.
DR PhylomeDB; Q9Z331; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR ChiTaRS; Krt6b; mouse.
DR PRO; PR:Q9Z331; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z331; protein.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IGI:MGI.
DR GO; GO:0031424; P:keratinization; IGI:MGI.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IGI:MGI.
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 1: Evidence at protein level;
KW Coiled coil; Intermediate filament; Keratin; Reference proteome.
FT CHAIN 1..562
FT /note="Keratin, type II cytoskeletal 6B"
FT /id="PRO_0000063737"
FT DOMAIN 160..473
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..159
FT /note="Head"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..195
FT /note="Coil 1A"
FT REGION 196..214
FT /note="Linker 1"
FT REGION 215..306
FT /note="Coil 1B"
FT REGION 307..330
FT /note="Linker 12"
FT REGION 331..469
FT /note="Coil 2"
FT REGION 470..562
FT /note="Tail"
FT REGION 536..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 411
FT /note="Stutter"
SQ SEQUENCE 562 AA; 60322 MW; 65A2A5A58141DCD1 CRC64;
MSTKTTIKSQ TSHRGYSASS ARVPGLNRSG FSSVSVCRSR GSGGSSAMCG GAGFGSRSLY
GVGSSKRISI GGGSCGIGGG YGSRFGGAYG SRFGGSFGIG GGAGSGFGFG GGVGFGGGYG
GAGFPVCPPG GIQEVTINQN LLTPLNVQID PTIQRVRTEE REQIKTLNNK FASFIDKVRF
LEQQNKVLDT KWALLQEQGT KTVRQNLEPM FEQYISNLRR QLDSIIGERG RLDSELRNMQ
DTVEDYKSKY EDEINKRTKA ENEFVTVKKD VDAAYMTKVE LQAKADSLAD EINFLRVIYE
AELSQMQTHI SDTSVVLSMD NNRSLDLDSI IAEVKAQYED IAQRSRAEAE SWYQTKYEEL
QVTAGRHGDD LRNTKQEIAE INRMIQRLRS EIDHVKKQCA NLQAAIADAE QRGEMALKDA
RGKLEGLEDA LQKAKQEMAR LLKEYQELMN VKLALDVEIA TYRKLLEGEE CRLNGEGVGP
VNISVVQSTV SSGYGSAGGA SSSLGLGGSS SYSYGSSHGL GGGFSAGSGR AIGGGLSSSG
GLSSSTIKYT TSASSSRKSY RH
