K2C6A_RAT
ID K2C6A_RAT Reviewed; 552 AA.
AC Q4FZU2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Keratin, type II cytoskeletal 6A;
DE AltName: Full=Cytokeratin-6A;
DE Short=CK-6A;
DE AltName: Full=Keratin-6A;
DE Short=K6A;
DE AltName: Full=Type-II keratin Kb6;
GN Name=Krt6a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 163-169; 316-336; 349-358; 445-455 AND 523-548, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Diao W., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
CC -!- FUNCTION: Epidermis-specific type I keratin involved in wound healing.
CC Involved in the activation of follicular keratinocytes after wounding,
CC while it does not play a major role in keratinocyte proliferation or
CC migration. Participates in the regulation of epithelial migration by
CC inhibiting the activity of SRC during wound repair.
CC {ECO:0000250|UniProtKB:P50446}.
CC -!- SUBUNIT: Heterodimer of a type I and a type II keratin. KRT6 isomers
CC associate with KRT16 and/or KRT17. Interacts with TCHP.
CC {ECO:0000250|UniProtKB:P50446}.
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 -!- MISCELLANEOUS: There are at least six isoforms of human type II
CC keratin-6 (K6), K6A being the most abundant representing about 77% of
CC all forms found in epithelia.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; BC099121; AAH99121.1; -; mRNA.
DR RefSeq; NP_001094477.1; NM_001101007.1.
DR AlphaFoldDB; Q4FZU2; -.
DR SMR; Q4FZU2; -.
DR BioGRID; 598219; 1.
DR iPTMnet; Q4FZU2; -.
DR PhosphoSitePlus; Q4FZU2; -.
DR jPOST; Q4FZU2; -.
DR PRIDE; Q4FZU2; -.
DR Ensembl; ENSRNOT00000102479; ENSRNOP00000087976; ENSRNOG00000070470.
DR GeneID; 683313; -.
DR KEGG; rno:683313; -.
DR RGD; 1588056; LOC683313.
DR GeneTree; ENSGT00940000154600; -.
DR InParanoid; Q4FZU2; -.
DR PhylomeDB; Q4FZU2; -.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q4FZU2; -.
DR Proteomes; UP000002494; Chromosome 7.
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:0045104; P:intermediate filament cytoskeleton organization; ISO:RGD.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR GO; GO:0002009; P:morphogenesis of an epithelium; ISS:UniProtKB.
DR GO; GO:0042060; P:wound healing; ISS:UniProtKB.
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; Direct protein sequencing; Intermediate filament; Keratin;
KW Reference proteome.
FT CHAIN 1..552
FT /note="Keratin, type II cytoskeletal 6A"
FT /id="PRO_0000288714"
FT DOMAIN 152..465
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..151
FT /note="Head"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..187
FT /note="Coil 1A"
FT REGION 188..206
FT /note="Linker 1"
FT REGION 207..298
FT /note="Coil 1B"
FT REGION 299..322
FT /note="Linker 12"
FT REGION 323..461
FT /note="Coil 2"
FT REGION 462..552
FT /note="Tail"
FT REGION 524..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 403
FT /note="Stutter"
SQ SEQUENCE 552 AA; 59249 MW; DF5AC8C3DC073AB7 CRC64;
MSTKTVIRSQ TSHRGFSAGS ARLPGLNRSG FSSVSVCRSR GSGGSRAVCG GAGFGSRSLC
GVGSSQRISI GGGSCGIGGG YGGRFGGSFG YGGGAGGSLG FGAGAGFGGG YGGAGFPVCP
PGGIQEVTIN QSLLTPMNLQ IDPTIQRVRT EEREQIKTLN NKFASFIDKV RFLEQQNKVL
DTKWALLQEQ GTKTVRQGLE TLFEQYINDL RKELDNILGQ RGRLDSELRN MQGTVEDYKS
KYEDEINRRT AAENEFVTLK KDVDAAYMNK VELQAKADSL TDEINFLRAL YEAELSQMQT
HISDTSVVLS MDNNRSLDLD SIIAEVKAQY EEIAKRSRAE AESWYQTKYE ELQITAGRHG
DDLRNTKQEI SEINRMIQRL RSEIDHVKKQ IANLQAAIAE AEQRGEMALK DARGKLEGLE
DALQKAKQDM ARLLKEYQDL MNVKLALDVE IATYRTLLEG EECRLNGEGV GPVNISVVQS
TVSSSYGSAG GASSSIGLGG SSSFSYGGSH SIGGGFSAGS GRGISSGLSS SGGSSSTIKY
TTTSSTRKSY RP
