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Keratin, type II cytoskeletal 6A (Cytokeratin-6A) (CK-6A) (Keratin-6-alpha) (mK6-alpha) (Keratin-6A) (K6A)

 K2C6A_MOUSE             Reviewed;         553 AA.
P50446; Q9Z332;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 144.
RecName: Full=Keratin, type II cytoskeletal 6A;
AltName: Full=Cytokeratin-6A;
Short=CK-6A;
AltName: Full=Keratin-6-alpha;
Short=mK6-alpha;
AltName: Full=Keratin-6A;
Short=K6A;
Name=Krt6a; Synonyms=Ker2, Krt2-6, Krt2-6a, Krt6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Epidermis;
PubMed=6207530; DOI=10.1073/pnas.81.18.5709;
Steinert P.M., Parry D.A.D., Racoosin E.L., Idler W.W., Steven A.C.,
Trus B.L., Roop D.R.;
"The complete cDNA and deduced amino acid sequence of a type II mouse
epidermal keratin of 60,000 Da: analysis of sequence differences
between type I and type II keratins.";
Proc. Natl. Acad. Sci. U.S.A. 81:5709-5713(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=129/Sv; TISSUE=Skin;
PubMed=9790766; DOI=10.1006/geno.1998.5476;
Takahashi K., Yan B., Yamanishi K., Imamura S., Coulombe P.A.;
"The two functional keratin 6 genes of mouse are differentially
regulated and evolved independently from their human orthologs.";
Genomics 53:170-183(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Jaw, and Limb;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE OF 528-553.
PubMed=1713533; DOI=10.1093/carcin/12.8.1519;
Finch J., Andrews K., Krieg P., Furstenberger G., Slaga T.,
Ootsuyama A., Tanooka H., Bowden G.T.;
"Identification of a cloned sequence activated during multi-stage
carcinogenesis in mouse skin.";
Carcinogenesis 12:1519-1522(1991).
[5]
SUBUNIT, AND INDUCTION.
PubMed=8636216; DOI=10.1083/jcb.132.3.381;
Paladini R.D., Takahashi K., Bravo N.S., Coulombe P.A.;
"Onset of re-epithelialization after skin injury correlates with a
reorganization of keratin filaments in wound edge keratinocytes:
defining a potential role for keratin 16.";
J. Cell Biol. 132:381-397(1996).
[6]
TISSUE SPECIFICITY.
PubMed=11069616; DOI=10.1046/j.1523-1747.2000.00132.x;
Mahony D., Karunaratne S., Cam G., Rothnagel J.A.;
"Analysis of mouse keratin 6a regulatory sequences in transgenic mice
reveals constitutive, tissue-specific expression by a keratin 6a
minigene.";
J. Invest. Dermatol. 115:795-804(2000).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
PubMed=10866680; DOI=10.1128/MCB.20.14.5248-5255.2000;
Wojcik S.M., Bundman D.S., Roop D.R.;
"Delayed wound healing in keratin 6a knockout mice.";
Mol. Cell. Biol. 20:5248-5255(2000).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Liver, Lung, Pancreas, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION.
PubMed=22529101; DOI=10.1083/jcb.201107078;
Rotty J.D., Coulombe P.A.;
"A wound-induced keratin inhibits Src activity during keratinocyte
migration and tissue repair.";
J. Cell Biol. 197:381-389(2012).
-!- FUNCTION: Epidermis-specific type I keratin involved in wound
healing (PubMed:10866680). Involved in the activation of
follicular keratinocytes after wounding, while it does not play a
major role in keratinocyte proliferation or migration
(PubMed:10866680). Participates in the regulation of epithelial
migration by inhibiting the activity of SRC during wound repair
(PubMed:22529101). {ECO:0000269|PubMed:10866680,
ECO:0000269|PubMed:22529101}.
-!- SUBUNIT: Heterodimer of a type I and a type II keratin. KRT6
isomers associate with KRT16 and/or KRT17 (PubMed:8636216).
Interacts with TCHP (By similarity). {ECO:0000250,
ECO:0000269|PubMed:8636216}.
-!- TISSUE SPECIFICITY: Predominates in the adult trunk skin, tongue,
trachea/esophagus and eye. In adult skin, localization is
restricted to hair follicles, where it is localized predominantly
in the outer root sheath. {ECO:0000269|PubMed:11069616,
ECO:0000269|PubMed:9790766}.
-!- INDUCTION: With the exception of specific body sites, expression
is induced under conditions of epithelial hyperproliferation such
as wound healing, certain skin diseases, cancer, and by treatment
of the skin with the phorbol ester PMA. Upon wounding, induced in
the outer root sheath and the interfollicular epidermis including
the basal cell layer (PubMed:10866680).
{ECO:0000269|PubMed:10866680, ECO:0000269|PubMed:8636216,
ECO:0000269|PubMed:9790766}.
-!- DISRUPTION PHENOTYPE: Wound healing defects. Delay in
reepithelialization from the hair follicle while the healing of
full-thickness skin wounds is not impaired.
{ECO:0000269|PubMed:10866680}.
-!- MISCELLANEOUS: There are two types of cytoskeletal and
microfibrillar keratin, I (acidic) and II (neutral to basic) (40-
55 and 56-70 kDa, respectively).
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; K02108; AAA39395.1; -; mRNA.
EMBL; AB012033; BAA34178.1; -; Genomic_DNA.
EMBL; BC080820; AAH80820.1; -; mRNA.
CCDS; CCDS27860.1; -.
PIR; I59009; I59009.
RefSeq; NP_032502.3; NM_008476.3.
UniGene; Mm.302399; -.
ProteinModelPortal; P50446; -.
SMR; P50446; -.
BioGrid; 201035; 6.
IntAct; P50446; 2.
MINT; P50446; -.
STRING; 10090.ENSMUSP00000023788; -.
iPTMnet; P50446; -.
PhosphoSitePlus; P50446; -.
PaxDb; P50446; -.
PeptideAtlas; P50446; -.
PRIDE; P50446; -.
Ensembl; ENSMUST00000023788; ENSMUSP00000023788; ENSMUSG00000058354.
GeneID; 16687; -.
KEGG; mmu:16687; -.
UCSC; uc007xtv.1; mouse.
CTD; 3853; -.
MGI; MGI:1100845; Krt6a.
eggNOG; ENOG410IG4R; Eukaryota.
eggNOG; ENOG410YY6B; LUCA.
GeneTree; ENSGT00760000118796; -.
HOGENOM; HOG000230976; -.
HOVERGEN; HBG013015; -.
InParanoid; P50446; -.
KO; K07605; -.
OMA; MQDQVED; -.
OrthoDB; EOG091G09KR; -.
PhylomeDB; P50446; -.
TreeFam; TF317854; -.
Reactome; R-MMU-6805567; Keratinization.
Reactome; R-MMU-6809371; Formation of the cornified envelope.
ChiTaRS; Krt6a; mouse.
PRO; PR:P50446; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000058354; -.
CleanEx; MM_KRT6A; -.
Genevisible; P50446; MM.
GO; GO:0045095; C:keratin filament; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IMP:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
GO; GO:0045109; P:intermediate filament organization; IGI:MGI.
GO; GO:0031424; P:keratinization; IGI:MGI.
GO; GO:0002009; P:morphogenesis of an epithelium; IMP:UniProtKB.
GO; GO:0044140; P:negative regulation of growth of symbiont on or near host surface; IMP:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
GO; GO:0042060; P:wound healing; IMP:UniProtKB.
InterPro; IPR001664; IF.
InterPro; IPR018039; IF_conserved.
InterPro; IPR039008; IF_rod_dom.
InterPro; IPR032444; Keratin_2_head.
InterPro; IPR003054; Keratin_II.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF16208; Keratin_2_head; 1.
PRINTS; PR01276; TYPE2KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Intermediate filament; Keratin;
Reference proteome.
CHAIN 1 553 Keratin, type II cytoskeletal 6A.
/FTId=PRO_0000063736.
DOMAIN 152 465 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 151 Head.
REGION 152 187 Coil 1A.
REGION 188 206 Linker 1.
REGION 207 298 Coil 1B.
REGION 299 322 Linker 12.
REGION 323 461 Coil 2.
REGION 462 553 Tail.
SITE 403 403 Stutter.
CONFLICT 24 24 P -> L (in Ref. 1; AAA39395).
{ECO:0000305}.
CONFLICT 121 121 P -> L (in Ref. 1; AAA39395).
{ECO:0000305}.
CONFLICT 173 173 L -> M (in Ref. 1; AAA39395).
{ECO:0000305}.
CONFLICT 180 180 L -> M (in Ref. 1; AAA39395).
{ECO:0000305}.
CONFLICT 191 191 G -> D (in Ref. 1; AAA39395).
{ECO:0000305}.
CONFLICT 199 199 L -> M (in Ref. 1; AAA39395).
{ECO:0000305}.
CONFLICT 224 225 LD -> MN (in Ref. 1; AAA39395).
{ECO:0000305}.
CONFLICT 233 240 DTVEDYKS -> ELVEELRN (in Ref. 1;
AAA39395). {ECO:0000305}.
CONFLICT 251 251 A -> D (in Ref. 1; AAA39395).
{ECO:0000305}.
CONFLICT 312 312 D -> V (in Ref. 1; AAA39395).
{ECO:0000305}.
CONFLICT 318 318 D -> V (in Ref. 1; AAA39395).
{ECO:0000305}.
CONFLICT 330 332 YED -> FEV (in Ref. 1; AAA39395).
{ECO:0000305}.
CONFLICT 344 344 W -> L (in Ref. 1; AAA39395).
{ECO:0000305}.
CONFLICT 432 432 R -> M (in Ref. 1; AAA39395).
{ECO:0000305}.
CONFLICT 438 438 Q -> H (in Ref. 1; AAA39395).
{ECO:0000305}.
CONFLICT 498 498 L -> M (in Ref. 1; AAA39395).
{ECO:0000305}.
SEQUENCE 553 AA; 59335 MW; C4DF69569E738DAF CRC64;
MSTKTTIKSQ TSHRGYSASS ARVPGLNRSG FSSVSVCRSR GSGGSSAMCG GAGFGSRSLY
GVGSSKRISI GGGSCGIGGG YGSRFGGSFG IGGGAGSGFG FGGGAGFGGG YGGAGFPVCP
PGGIQEVTIN QSLLTPLNLQ IDPTIQRVRT EEREQIKTLN NKFASFIDKV RFLEQQNKVL
DTKWALLQEQ GTKTVRQNLE PMFEQYISNL RRQLDSIIGE RGRLDSELRN MQDTVEDYKS
KYEDEINKRT AAENEFVTLK KDVDAAYMNK VELQAKADSL TDDINFLRAL YEAELSQMQT
HISDTSVVLS MDNNRSLDLD SIIAEVKAQY EDIAQRSRAE AESWYQTKYE ELQVTAGRHG
DDLRNTKQEI AEINRMIQRL RSEIDHVKKQ CANLQAAIAD AEQRGEMALK DARGKLEGLE
DALQKAKQDM ARLLKEYQEL MNVKLALDVE IATYRKLLEG EECRLNGEGV GPVNISVVQS
TVSSGYGSAG GASSSLGLGG GSSYSYSSSH GLGGGFSAGS GRAIGGGLSS SGGLSSSTIK
YTTTSSSKKS YRQ


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