K2C6A_HUMAN
ID K2C6A_HUMAN Reviewed; 564 AA.
AC P02538; A4QPC1; P48667; Q08AR4; Q6NT67; Q96CL4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Keratin, type II cytoskeletal 6A;
DE AltName: Full=Cytokeratin-6A;
DE Short=CK-6A;
DE AltName: Full=Cytokeratin-6D;
DE Short=CK-6D;
DE AltName: Full=Keratin-6A;
DE Short=K6A;
DE AltName: Full=Type-II keratin Kb6;
DE AltName: Allergen=Hom s 5;
GN Name=KRT6A; Synonyms=K6A, KRT6D;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Skin;
RX PubMed=7543104; DOI=10.1074/jbc.270.31.18581;
RA Takahashi K., Paladini R.D., Coulombe P.A.;
RT "Cloning and characterization of multiple human genes and cDNAs encoding
RT highly related type II keratin 6 isoforms.";
RL J. Biol. Chem. 270:18581-18592(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-21.
RC TISSUE=Brain, Ovary, and Pancreas;
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 [4]
RP PROTEIN SEQUENCE OF 2-9; 31-40; 43-86; 169-204; 208-232; 241-347; 350-369;
RP 379-386; 425-436; 447-475 AND 534-550, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N., Lilla S., Lange E.,
RA Sumpton D.P.;
RL Submitted (MAR-2008) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 208-564.
RX PubMed=6191871; DOI=10.1016/0092-8674(83)90034-x;
RA Hanukoglu I., Fuchs E.;
RT "The cDNA sequence of a type II cytoskeletal keratin reveals constant and
RT variable structural domains among keratins.";
RL Cell 33:915-924(1983).
RN [6]
RP INTERACTION WITH TCHP.
RX PubMed=15731013; DOI=10.1242/jcs.01667;
RA Nishizawa M., Izawa I., Inoko A., Hayashi Y., Nagata K., Yokoyama T.,
RA Usukura J., Inagaki M.;
RT "Identification of trichoplein, a novel keratin filament-binding protein.";
RL J. Cell Sci. 118:1081-1090(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP INVOLVEMENT IN PC3.
RX PubMed=22668561; DOI=10.1684/ejd.2012.1773;
RA Du Z.F., Xu C.M., Zhao Y., Liu W.T., Chen X.L., Chen C.Y., Fang H.,
RA Ke H.P., Zhang X.N.;
RT "Two novel de novo mutations of KRT6A and KRT16 genes in two Chinese
RT pachyonychia congenita pedigrees with fissured tongue or diffuse plantar
RT keratoderma.";
RL Eur. J. Dermatol. 22:476-480(2012).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=26758872; DOI=10.1093/hmg/ddw001;
RA Allen E.H., Courtney D.G., Atkinson S.D., Moore J.E., Mairs L.,
RA Poulsen E.T., Schiroli D., Maurizi E., Cole C., Hickerson R.P., James J.,
RA Murgatroyd H., Smith F.J., MacEwen C., Enghild J.J., Nesbit M.A.,
RA Leslie Pedrioli D.M., McLean W.H., Moore C.B.;
RT "Keratin 12 missense mutation induces the unfolded protein response and
RT apoptosis in Meesmann epithelial corneal dystrophy.";
RL Hum. Mol. Genet. 25:1176-1191(2016).
RN [11]
RP VARIANT PC3 ASN-171 DEL.
RX PubMed=7545493; DOI=10.1038/ng0795-363;
RA Bowden P.E., Haley J.L., Kansky A., Rothnagel J.A., Jones D.O.,
RA Turner R.J.;
RT "Mutation of a type II keratin gene (K6a) in pachyonychia congenita.";
RL Nat. Genet. 10:363-365(1995).
RN [12]
RP VARIANTS PC3 LYS-171 AND SER-174.
RX PubMed=10232400; DOI=10.1111/j.1600-0625.1999.tb00356.x;
RA Smith F.J., McKenna K.E., Irvine A.D., Bingham E.A., Coleman C.M.,
RA Uitto J., McLean W.H.;
RT "A mutation detection strategy for the human keratin 6A gene and novel
RT missense mutations in two cases of pachyonychia congenita type 1.";
RL Exp. Dermatol. 8:109-114(1999).
RN [13]
RP VARIANTS PC3 VAL-174; ARG-469 AND LYS-472.
RX PubMed=11886499; DOI=10.1046/j.0022-202x.2001.01565.x;
RA Terrinoni A., Smith F.J.D., Didona B., Canzona F., Paradisi M., Huber M.,
RA Hohl D., David A., Verloes A., Leigh I.M., Munro C.S., Melino G.,
RA McLean W.H.I.;
RT "Novel and recurrent mutations in the genes encoding keratins K6a, K16 and
RT K17 in 13 cases of pachyonychia congenita.";
RL J. Invest. Dermatol. 117:1391-1396(2001).
RN [14]
RP VARIANT PC3 SER-462.
RX PubMed=15387942;
RA Kang X.J., Sun M., Yang W., Yu M., Ju Q., Lo W.H., Xia L.Q., Zhang X.;
RT "[A de nono I462S mutation in the KRT6A gene is associated with
RT pachyonychia congenita type I].";
RL Zhonghua Yi Xue Za Zhi 84:1344-1347(2004).
RN [15]
RP VARIANT PC3 PRO-464.
RX PubMed=15840119; DOI=10.1111/j.1365-2133.2005.06473.x;
RA Garcia-Rio I., Penas P.F., Garcia-Diez A., McLean W.H., Smith F.J.;
RT "A severe case of pachyonychia congenita type I due to a novel proline
RT mutation in keratin 6a.";
RL Br. J. Dermatol. 152:800-802(2005).
RN [16]
RP VARIANTS PC3 ASN-167; PHE-170; LYS-171; ASN-171 DEL; SER-171; SER-174;
RP PRO-176; ASN-462; PRO-468 AND PRO-469.
RX PubMed=16250206; DOI=10.1111/j.1087-0024.2005.10204.x;
RA Smith F.J., Liao H., Cassidy A.J., Stewart A., Hamill K.J., Wood P.,
RA Joval I., van Steensel M.A., Bjoerck E., Callif-Daley F., Pals G.,
RA Collins P., Leachman S.A., Munro C.S., McLean W.H.;
RT "The genetic basis of pachyonychia congenita.";
RL J. Investig. Dermatol. Symp. Proc. 10:21-30(2005).
RN [17]
RP VARIANTS PC3 PRO-164; ASP-171; SER-171; TYR-171; ASN-172 DEL; CYS-174;
RP ARG-469; PRO-469 AND LYS-472.
RX PubMed=17719747; DOI=10.1016/j.jdermsci.2007.07.003;
RA Liao H., Sayers J.M., Wilson N.J., Irvine A.D., Mellerio J.E., Baselga E.,
RA Bayliss S.J., Uliana V., Fimiani M., Lane E.B., McLean W.H., Leachman S.A.,
RA Smith F.J.;
RT "A spectrum of mutations in keratins K6a, K16 and K17 causing pachyonychia
RT congenita.";
RL J. Dermatol. Sci. 48:199-205(2007).
RN [18]
RP VARIANT PC3 GLN-468.
RX PubMed=17309457; DOI=10.1111/j.1468-3083.2006.01930.x;
RA Zhou H.L., Yang S., Gao M., Zhao X.Y., Zhu Y.G., Li W., Ren Y.Q.,
RA Liang Y.H., Du W.H., Zhang X.J.;
RT "A novel missense mutation L468Q of keratin 6a in pachyonychia congenita
RT type 1.";
RL J. Eur. Acad. Dermatol. Venereol. 21:351-355(2007).
RN [19]
RP VARIANTS PC3 ASP-171 AND HIS-465.
RX PubMed=18489596; DOI=10.1111/j.1365-2133.2008.08603.x;
RA Bai Z.L., Feng Y.G., Tan S.S., Wang X.Y., Xiao S.X., Wang H., Jia H.Q.,
RA Wu J.W., He D.L., Kang R.H.;
RT "Mutations of KRT6A are more frequent than those of KRT16 in pachyonychia
RT congenita type 1: report of a novel and a recently reported mutation in two
RT unrelated Chinese families.";
RL Br. J. Dermatol. 159:238-240(2008).
RN [20]
RP VARIANTS PC3 PRO-166; LYS-171; ASN-172 DEL; SER-174; ASN-178; PRO-463 AND
RP SER-465.
RX PubMed=19416275; DOI=10.1111/j.1365-2133.2009.09062.x;
RA Lv Y.M., Yang S., Zhang Z., Cui Y., Quan C., Zhou F.S., Fang Q.Y., Du W.H.,
RA Zhang F.R., Chang J.M., Tao X.P., Zhang A.L., Kang R.H., Du W.D.,
RA Zhang X.J.;
RT "Novel and recurrent keratin 6A (KRT6A) mutations in Chinese patients with
RT pachyonychia congenita type 1.";
RL Br. J. Dermatol. 160:1327-1329(2009).
RN [21]
RP VARIANTS PC3 SER-171; LYS-171; ASN-172 DEL AND PRO-468.
RX PubMed=21326300; DOI=10.1038/jid.2011.20;
RA Wilson N.J., Leachman S.A., Hansen C.D., McMullan A.C., Milstone L.M.,
RA Schwartz M.E., McLean W.H., Hull P.R., Smith F.J.;
RT "A large mutational study in pachyonychia congenita.";
RL J. Invest. Dermatol. 131:1018-1024(2011).
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 (By similarity). Interacts with TCHP
CC (PubMed:15731013). {ECO:0000250|UniProtKB:P50446,
CC ECO:0000269|PubMed:15731013}.
CC -!- INTERACTION:
CC P02538; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-702198, EBI-745073;
CC P02538; Q15834: CCDC85B; NbExp=2; IntAct=EBI-702198, EBI-739674;
CC P02538; P55040: GEM; NbExp=3; IntAct=EBI-702198, EBI-744104;
CC P02538; Q08379: GOLGA2; NbExp=7; IntAct=EBI-702198, EBI-618309;
CC P02538; O14964: HGS; NbExp=6; IntAct=EBI-702198, EBI-740220;
CC P02538; F5H3M2: KIFC3; NbExp=4; IntAct=EBI-702198, EBI-11953930;
CC P02538; Q9BVG8: KIFC3; NbExp=5; IntAct=EBI-702198, EBI-2125614;
CC P02538; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-702198, EBI-14069005;
CC P02538; A1A4E9: KRT13; NbExp=5; IntAct=EBI-702198, EBI-10171552;
CC P02538; P13646: KRT13; NbExp=8; IntAct=EBI-702198, EBI-1223876;
CC P02538; P19012: KRT15; NbExp=15; IntAct=EBI-702198, EBI-739566;
CC P02538; P08779: KRT16; NbExp=3; IntAct=EBI-702198, EBI-356410;
CC P02538; P05783: KRT18; NbExp=3; IntAct=EBI-702198, EBI-297888;
CC P02538; P08727: KRT19; NbExp=5; IntAct=EBI-702198, EBI-742756;
CC P02538; Q7Z3Z0: KRT25; NbExp=3; IntAct=EBI-702198, EBI-11980019;
CC P02538; Q7Z3Y9: KRT26; NbExp=3; IntAct=EBI-702198, EBI-12084444;
CC P02538; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-702198, EBI-3044087;
CC P02538; Q7Z3Y7: KRT28; NbExp=5; IntAct=EBI-702198, EBI-11980489;
CC P02538; Q15323: KRT31; NbExp=12; IntAct=EBI-702198, EBI-948001;
CC P02538; O76011: KRT34; NbExp=3; IntAct=EBI-702198, EBI-1047093;
CC P02538; Q92764: KRT35; NbExp=3; IntAct=EBI-702198, EBI-1058674;
CC P02538; O76013-2: KRT36; NbExp=3; IntAct=EBI-702198, EBI-11958506;
CC P02538; O76015: KRT38; NbExp=14; IntAct=EBI-702198, EBI-1047263;
CC P02538; Q6A162: KRT40; NbExp=14; IntAct=EBI-702198, EBI-10171697;
CC P02538; P61601: NCALD; NbExp=3; IntAct=EBI-702198, EBI-749635;
CC P02538; P37198: NUP62; NbExp=3; IntAct=EBI-702198, EBI-347978;
CC P02538; P07237: P4HB; NbExp=3; IntAct=EBI-702198, EBI-395883;
CC P02538; O43765: SGTA; NbExp=3; IntAct=EBI-702198, EBI-347996;
CC P02538; Q9UBB9: TFIP11; NbExp=10; IntAct=EBI-702198, EBI-1105213;
CC P02538; P36406: TRIM23; NbExp=8; IntAct=EBI-702198, EBI-740098;
CC P02538; Q9BYV2: TRIM54; NbExp=11; IntAct=EBI-702198, EBI-2130429;
CC P02538; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-702198, EBI-6116822;
CC P02538; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-702198, EBI-947187;
CC -!- TISSUE SPECIFICITY: Expressed in the corneal epithelium (at protein
CC level). {ECO:0000269|PubMed:26758872}.
CC -!- DISEASE: Pachyonychia congenita 3 (PC3) [MIM:615726]: An autosomal
CC dominant genodermatosis characterized by hypertrophic nail dystrophy,
CC painful and highly debilitating plantar keratoderma, oral
CC leukokeratosis, and a variety of epidermal cysts.
CC {ECO:0000269|PubMed:10232400, ECO:0000269|PubMed:11886499,
CC ECO:0000269|PubMed:15387942, ECO:0000269|PubMed:15840119,
CC ECO:0000269|PubMed:16250206, ECO:0000269|PubMed:17309457,
CC ECO:0000269|PubMed:17719747, ECO:0000269|PubMed:18489596,
CC ECO:0000269|PubMed:19416275, ECO:0000269|PubMed:21326300,
CC ECO:0000269|PubMed:22668561, ECO:0000269|PubMed:7545493}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE from
CC atopic dermatitis (AD) patients. Identified as an IgE autoantigen in
CC atopic dermatitis (AD) patients with severe skin manifestations.
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 -!- 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}.
CC -!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
CC URL="http://www.interfil.org";
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DR EMBL; L42583; AAC41767.1; -; Genomic_DNA.
DR EMBL; L42575; AAC41767.1; JOINED; Genomic_DNA.
DR EMBL; L42576; AAC41767.1; JOINED; Genomic_DNA.
DR EMBL; L42577; AAC41767.1; JOINED; Genomic_DNA.
DR EMBL; L42578; AAC41767.1; JOINED; Genomic_DNA.
DR EMBL; L42579; AAC41767.1; JOINED; Genomic_DNA.
DR EMBL; L42580; AAC41767.1; JOINED; Genomic_DNA.
DR EMBL; L42581; AAC41767.1; JOINED; Genomic_DNA.
DR EMBL; AH005420; AAB60696.1; -; Genomic_DNA.
DR EMBL; BT006899; AAP35545.1; -; mRNA.
DR EMBL; BC008807; AAH08807.1; -; mRNA.
DR EMBL; BC014152; AAH14152.1; -; mRNA.
DR EMBL; BC069269; AAH69269.1; -; mRNA.
DR EMBL; BC125058; AAI25059.1; -; mRNA.
DR EMBL; BC139753; AAI39754.1; -; mRNA.
DR EMBL; V01516; CAA24760.1; -; Genomic_DNA.
DR CCDS; CCDS41786.1; -.
DR PIR; A57398; KRHUEA.
DR PIR; I61769; I61769.
DR RefSeq; NP_005545.1; NM_005554.3.
DR PDB; 5KI0; NMR; -; A=533-551.
DR PDBsum; 5KI0; -.
DR AlphaFoldDB; P02538; -.
DR SMR; P02538; -.
DR BioGRID; 110051; 99.
DR DIP; DIP-533N; -.
DR IntAct; P02538; 66.
DR MINT; P02538; -.
DR STRING; 9606.ENSP00000369317; -.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR Allergome; 3326; Hom s 5.0101.
DR Allergome; 415; Hom s 5.
DR GlyGen; P02538; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P02538; -.
DR PhosphoSitePlus; P02538; -.
DR SwissPalm; P02538; -.
DR BioMuta; KRT6A; -.
DR DMDM; 1346344; -.
DR jPOST; P02538; -.
DR MassIVE; P02538; -.
DR PaxDb; P02538; -.
DR PeptideAtlas; P02538; -.
DR PRIDE; P02538; -.
DR ProteomicsDB; 51529; -.
DR TopDownProteomics; P02538; -.
DR Antibodypedia; 7850; 682 antibodies from 36 providers.
DR DNASU; 3853; -.
DR Ensembl; ENST00000330722.7; ENSP00000369317.3; ENSG00000205420.11.
DR GeneID; 3853; -.
DR KEGG; hsa:3853; -.
DR MANE-Select; ENST00000330722.7; ENSP00000369317.3; NM_005554.4; NP_005545.1.
DR UCSC; uc001sam.4; human.
DR CTD; 3853; -.
DR DisGeNET; 3853; -.
DR GeneCards; KRT6A; -.
DR GeneReviews; KRT6A; -.
DR HGNC; HGNC:6443; KRT6A.
DR HPA; ENSG00000205420; Group enriched (esophagus, vagina).
DR MalaCards; KRT6A; -.
DR MIM; 148041; gene.
DR MIM; 615726; phenotype.
DR neXtProt; NX_P02538; -.
DR OpenTargets; ENSG00000205420; -.
DR Orphanet; 2309; Pachyonychia congenita.
DR PharmGKB; PA30231; -.
DR VEuPathDB; HostDB:ENSG00000205420; -.
DR eggNOG; ENOG502QURK; Eukaryota.
DR GeneTree; ENSGT00940000154600; -.
DR HOGENOM; CLU_012560_6_1_1; -.
DR InParanoid; P02538; -.
DR OMA; RWVHDAM; -.
DR OrthoDB; 824246at2759; -.
DR PhylomeDB; P02538; -.
DR TreeFam; TF317854; -.
DR PathwayCommons; P02538; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; P02538; -.
DR BioGRID-ORCS; 3853; 34 hits in 1003 CRISPR screens.
DR ChiTaRS; KRT6A; human.
DR GeneWiki; Keratin_6A; -.
DR GenomeRNAi; 3853; -.
DR Pharos; P02538; Tbio.
DR PRO; PR:P02538; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P02538; protein.
DR Bgee; ENSG00000205420; Expressed in gingival epithelium and 113 other tissues.
DR ExpressionAtlas; P02538; baseline and differential.
DR Genevisible; P02538; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
DR GO; GO:0051838; P:cytolysis by host of symbiont cells; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
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:0001899; P:negative regulation of cytolysis by symbiont of host cells; IDA:UniProtKB.
DR GO; GO:2000536; P:negative regulation of entry of bacterium into host cell; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; NAS: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 3D-structure; Acetylation; Allergen; Coiled coil;
KW Direct protein sequencing; Disease variant; Ectodermal dysplasia;
KW Intermediate filament; Keratin; Palmoplantar keratoderma;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..564
FT /note="Keratin, type II cytoskeletal 6A"
FT /id="PRO_0000063731"
FT DOMAIN 163..476
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..162
FT /note="Head"
FT REGION 163..198
FT /note="Coil 1A"
FT REGION 199..217
FT /note="Linker 1"
FT REGION 218..309
FT /note="Coil 1B"
FT REGION 310..333
FT /note="Linker 12"
FT REGION 334..472
FT /note="Coil 2"
FT REGION 473..564
FT /note="Tail"
FT SITE 414
FT /note="Stutter"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4"
FT VARIANT 21
FT /note="N -> S (in dbSNP:rs17845411)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_021264"
FT VARIANT 111
FT /note="G -> D (in dbSNP:rs681063)"
FT /id="VAR_035030"
FT VARIANT 164
FT /note="R -> P (in PC3; dbSNP:rs62635293)"
FT /evidence="ECO:0000269|PubMed:17719747"
FT /id="VAR_072446"
FT VARIANT 166
FT /note="Q -> P (in PC3; dbSNP:rs267607460)"
FT /evidence="ECO:0000269|PubMed:19416275"
FT /id="VAR_072447"
FT VARIANT 167
FT /note="I -> N (in PC3; dbSNP:rs57126929)"
FT /evidence="ECO:0000269|PubMed:16250206"
FT /id="VAR_072448"
FT VARIANT 170
FT /note="L -> F (in PC3; dbSNP:rs57448541)"
FT /evidence="ECO:0000269|PubMed:16250206"
FT /id="VAR_072449"
FT VARIANT 171
FT /note="N -> D (in PC3; dbSNP:rs62635294)"
FT /evidence="ECO:0000269|PubMed:17719747,
FT ECO:0000269|PubMed:18489596"
FT /id="VAR_072450"
FT VARIANT 171
FT /note="N -> K (in PC3; dbSNP:rs59685571)"
FT /evidence="ECO:0000269|PubMed:10232400,
FT ECO:0000269|PubMed:16250206, ECO:0000269|PubMed:19416275,
FT ECO:0000269|PubMed:21326300"
FT /id="VAR_072451"
FT VARIANT 171
FT /note="N -> S (in PC3; dbSNP:rs58556099)"
FT /evidence="ECO:0000269|PubMed:16250206,
FT ECO:0000269|PubMed:17719747, ECO:0000269|PubMed:21326300"
FT /id="VAR_072452"
FT VARIANT 171
FT /note="N -> Y (in PC3; dbSNP:rs62635294)"
FT /evidence="ECO:0000269|PubMed:17719747"
FT /id="VAR_072453"
FT VARIANT 171
FT /note="Missing (in PC3)"
FT /evidence="ECO:0000269|PubMed:16250206,
FT ECO:0000269|PubMed:7545493"
FT /id="VAR_003878"
FT VARIANT 172
FT /note="Missing (in PC3)"
FT /evidence="ECO:0000269|PubMed:17719747,
FT ECO:0000269|PubMed:19416275, ECO:0000269|PubMed:21326300"
FT /id="VAR_072454"
FT VARIANT 174
FT /note="F -> C (in PC3; dbSNP:rs61145796)"
FT /evidence="ECO:0000269|PubMed:17719747"
FT /id="VAR_072455"
FT VARIANT 174
FT /note="F -> S (in PC3; dbSNP:rs61145796)"
FT /evidence="ECO:0000269|PubMed:10232400,
FT ECO:0000269|PubMed:16250206, ECO:0000269|PubMed:19416275"
FT /id="VAR_072456"
FT VARIANT 174
FT /note="F -> V (in PC3; dbSNP:rs28933087)"
FT /evidence="ECO:0000269|PubMed:11886499"
FT /id="VAR_017075"
FT VARIANT 176
FT /note="S -> P (in PC3; dbSNP:rs59642296)"
FT /evidence="ECO:0000269|PubMed:16250206"
FT /id="VAR_072457"
FT VARIANT 178
FT /note="I -> N (in PC3; dbSNP:rs267607461)"
FT /evidence="ECO:0000269|PubMed:19416275"
FT /id="VAR_072458"
FT VARIANT 462
FT /note="I -> N (in PC3; dbSNP:rs57629991)"
FT /evidence="ECO:0000269|PubMed:16250206"
FT /id="VAR_072459"
FT VARIANT 462
FT /note="I -> S (in PC3; dbSNP:rs57629991)"
FT /evidence="ECO:0000269|PubMed:15387942"
FT /id="VAR_072460"
FT VARIANT 463
FT /note="A -> P (in PC3; dbSNP:rs267607462)"
FT /evidence="ECO:0000269|PubMed:19416275"
FT /id="VAR_072461"
FT VARIANT 464
FT /note="T -> P (in PC3; dbSNP:rs61293647)"
FT /evidence="ECO:0000269|PubMed:15840119"
FT /id="VAR_072462"
FT VARIANT 465
FT /note="Y -> H (in PC3; dbSNP:rs267607463)"
FT /evidence="ECO:0000269|PubMed:18489596"
FT /id="VAR_072463"
FT VARIANT 465
FT /note="Y -> S (in PC3)"
FT /evidence="ECO:0000269|PubMed:19416275"
FT /id="VAR_072464"
FT VARIANT 468
FT /note="L -> P (in PC3; dbSNP:rs59018888)"
FT /evidence="ECO:0000269|PubMed:16250206,
FT ECO:0000269|PubMed:21326300"
FT /id="VAR_072465"
FT VARIANT 468
FT /note="L -> Q (in PC3; dbSNP:rs59018888)"
FT /evidence="ECO:0000269|PubMed:17309457"
FT /id="VAR_072466"
FT VARIANT 469
FT /note="L -> P (in PC3; dbSNP:rs57052654)"
FT /evidence="ECO:0000269|PubMed:16250206,
FT ECO:0000269|PubMed:17719747"
FT /id="VAR_072467"
FT VARIANT 469
FT /note="L -> R (in PC3; dbSNP:rs57052654)"
FT /evidence="ECO:0000269|PubMed:11886499,
FT ECO:0000269|PubMed:17719747"
FT /id="VAR_017076"
FT VARIANT 472
FT /note="E -> K (in PC3; dbSNP:rs60554162)"
FT /evidence="ECO:0000269|PubMed:11886499,
FT ECO:0000269|PubMed:17719747"
FT /id="VAR_017077"
FT CONFLICT 192
FT /note="E -> D (in Ref. 1; AAB60696)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="G -> N (in Ref. 1; AAB60696)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="F -> L (in Ref. 1; AAB60696)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="I -> S (in Ref. 5; CAA24760)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="N -> S (in Ref. 1; AAB60696)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="R -> W (in Ref. 3; AAH69269)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="I -> V (in Ref. 1; AAB60696)"
FT /evidence="ECO:0000305"
FT HELIX 539..541
FT /evidence="ECO:0007829|PDB:5KI0"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:5KI0"
SQ SEQUENCE 564 AA; 60045 MW; 26708916C7DC923A CRC64;
MASTSTTIRS HSSSRRGFSA NSARLPGVSR SGFSSVSVSR SRGSGGLGGA CGGAGFGSRS
LYGLGGSKRI SIGGGSCAIS GGYGSRAGGS YGFGGAGSGF GFGGGAGIGF GLGGGAGLAG
GFGGPGFPVC PPGGIQEVTV NQSLLTPLNL QIDPTIQRVR AEEREQIKTL NNKFASFIDK
VRFLEQQNKV LETKWTLLQE QGTKTVRQNL EPLFEQYINN LRRQLDSIVG ERGRLDSELR
GMQDLVEDFK NKYEDEINKR TAAENEFVTL KKDVDAAYMN KVELQAKADT LTDEINFLRA
LYDAELSQMQ THISDTSVVL SMDNNRNLDL DSIIAEVKAQ YEEIAQRSRA EAESWYQTKY
EELQVTAGRH GDDLRNTKQE IAEINRMIQR LRSEIDHVKK QCANLQAAIA DAEQRGEMAL
KDAKNKLEGL EDALQKAKQD LARLLKEYQE LMNVKLALDV EIATYRKLLE GEECRLNGEG
VGQVNISVVQ STVSSGYGGA SGVGSGLGLG GGSSYSYGSG LGVGGGFSSS SGRAIGGGLS
SVGGGSSTIK YTTTSSSSRK SYKH
