K1C12_HUMAN
ID K1C12_HUMAN Reviewed; 494 AA.
AC Q99456; B2R9E0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Keratin, type I cytoskeletal 12;
DE AltName: Full=Cytokeratin-12;
DE Short=CK-12;
DE AltName: Full=Keratin-12;
DE Short=K12;
GN Name=KRT12;
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 [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Cornea;
RX PubMed=8759347;
RA Nishida K., Adachi W., Shimizu-Matsumoto A., Kinoshita S., Mizuno K.,
RA Matsubara K., Okubo K.;
RT "A gene expression profile of human corneal epithelium and the isolation of
RT human keratin 12 cDNA.";
RL Invest. Ophthalmol. Vis. Sci. 37:1800-1809(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MECD1 GLY-135; ILE-135;
RP ARG-140 AND ASP-429.
RX PubMed=9399908; DOI=10.1086/301650;
RA Nishida K., Honma Y., Dota A., Kawasaki S., Adachi W., Nakamura T.,
RA Quantock A.J., Hosotani H., Yamamoto S., Okada M., Shimomura Y.,
RA Kinoshita S.;
RT "Isolation and chromosomal localization of a cornea-specific human keratin
RT 12 gene and detection of four mutations in Meesmann corneal epithelial
RT dystrophy.";
RL Am. J. Hum. Genet. 61:1268-1275(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MECD1 THR-129 AND THR-135, AND VARIANT
RP TRP-20.
RX PubMed=10644419; DOI=10.1006/exer.1999.0769;
RA Corden L.D., Swensson O., Swensson B., Smith F.J.D., Rochels R., Uitto J.,
RA McLean W.H.I.;
RT "Molecular genetics of Meesmann's corneal dystrophy: ancestral and novel
RT mutations in keratin 12 (K12) and complete sequence of the human KRT12
RT gene.";
RL Exp. Eye Res. 70:41-49(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 21-31.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
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 FUNCTION, TISSUE SPECIFICITY, AND CHARACTERIZATION OF VARIANT MECD1
RP PRO-132.
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 [9]
RP VARIANTS MECD1 THR-135 AND LEU-143.
RX PubMed=9171831; DOI=10.1038/ng0697-184;
RA Irvine A.D., Corden L.D., Swensson O., Swensson B., Moore J.E.,
RA Frazer D.G., Smith F.J.D., Knowlton R.G., Christophers E., Rochels R.,
RA Uitto J., McLean W.H.I.;
RT "Mutations in cornea-specific keratin K3 or K12 genes cause Meesmann's
RT corneal dystrophy.";
RL Nat. Genet. 16:184-187(1997).
RN [10]
RP VARIANT MECD1 VAL-426.
RX PubMed=10612503; DOI=10.1016/s0002-9394(99)00317-7;
RA Coleman C.M., Hannush S., Covello S.P., Smith F.J., Uitto J., McLean W.H.;
RT "A novel mutation in the helix termination motif of keratin K12 in a US
RT family with Meesmann corneal dystrophy.";
RL Am. J. Ophthalmol. 128:687-691(1999).
RN [11]
RP VARIANT MECD1 PRO-130.
RX PubMed=10781519; DOI=10.1136/bjo.84.5.527;
RA Corden L.D., Swensson O., Swensson B., Rochels R., Wannke B., Thiel H.J.,
RA McLean W.H.I.;
RT "A novel keratin 12 mutation in a German kindred with Meesmann's corneal
RT dystrophy.";
RL Br. J. Ophthalmol. 84:527-530(2000).
RN [12]
RP VARIANT MECD1 PRO-137.
RX PubMed=12543196; DOI=10.1016/s0021-5155(02)00563-4;
RA Takahashi K., Takahashi K., Murakami A., Okisaka S., Kimura T., Kanai A.;
RT "Heterozygous Ala137Pro mutation in keratin 12 gene found in Japanese with
RT Meesmann's corneal dystrophy.";
RL Jpn. J. Ophthalmol. 46:673-674(2002).
RN [13]
RP VARIANTS MECD1 SER-135 AND ILE-SER-ASN-LEU-GLU-ALA-GLN-LEU-LEU-399 INS.
RX PubMed=15148206; DOI=10.1136/bjo.2003.032870;
RA Yoon M.K., Warren J.F., Holsclaw D.S., Gritz D.C., Margolis T.P.;
RT "A novel arginine substitution mutation in 1A domain and a novel 27 bp
RT insertion mutation in 2B domain of keratin 12 gene associated with
RT Meesmann's corneal dystrophy.";
RL Br. J. Ophthalmol. 88:752-756(2004).
RN [14]
RP VARIANT MECD1 CYS-429.
RX PubMed=16227835; DOI=10.1097/01.ico.0000159732.29930.26;
RA Chen Y.T., Tseng S.H., Chao S.C.;
RT "Novel mutations in the helix termination motif of keratin 3 and keratin 12
RT in 2 Taiwanese families with Meesmann corneal dystrophy.";
RL Cornea 24:928-932(2005).
RN [15]
RP VARIANTS MECD1 THR-129 AND SER-426.
RX PubMed=16352477; DOI=10.1080/13816810500374391;
RA Nichini O., Manzi V., Munier F.L., Schorderet D.F.;
RT "Meesmann corneal dystrophy (MECD): report of 2 families and a novel
RT mutation in the cornea specific keratin 12 (KRT12) gene.";
RL Ophthalmic Genet. 26:169-173(2005).
RN [16]
RP VARIANT MECD1 PRO-430.
RX PubMed=17653038;
RA Sullivan L.S., Baylin E.B., Font R., Daiger S.P., Pepose J.S., Clinch T.E.,
RA Nakamura H., Zhao X.C., Yee R.W.;
RT "A novel mutation of the Keratin 12 gene responsible for a severe phenotype
RT of Meesmann's corneal dystrophy.";
RL Mol. Vis. 13:975-980(2007).
RN [17]
RP VARIANTS SER-15 AND TRP-20, AND VARIANT MECD1 LEU-143.
RX PubMed=18245975; DOI=10.1097/ico.0b013e31815652fd;
RA Nielsen K., Orntoft T., Hjortdal J., Rasmussen T., Ehlers N.;
RT "A novel mutation as the basis for asymptomatic meesmann dystrophy in a
RT Danish family.";
RL Cornea 27:100-102(2008).
RN [18]
RP VARIANT MECD1 ARG-433.
RX PubMed=18661274; DOI=10.1007/s10384-007-0518-2;
RA Seto T., Fujiki K., Kishishita H., Fujimaki T., Murakami A., Kanai A.;
RT "A novel mutation in the cornea-specific keratin 12 gene in Meesmann
RT corneal dystrophy.";
RL Jpn. J. Ophthalmol. 52:224-226(2008).
RN [19]
RP VARIANT SER-15, AND VARIANT MECD1 VAL-129.
RX PubMed=20577595;
RA Clausen I., Duncker G.I., Grunauer-Kloevekorn C.;
RT "Identification of a novel mutation in the cornea specific keratin 12 gene
RT causing Meesmann's corneal dystrophy in a German family.";
RL Mol. Vis. 16:954-960(2010).
RN [20]
RP VARIANT MECD1 PRO-132.
RX PubMed=23222558; DOI=10.1038/eye.2012.261;
RA Hassan H., Thaung C., Ebenezer N.D., Larkin G., Hardcastle A.J., Tuft S.J.;
RT "Severe Meesmann's epithelial corneal dystrophy phenotype due to a missense
RT mutation in the helix-initiation motif of keratin 12.";
RL Eye 27:367-373(2013).
RN [21]
RP VARIANT MECD1 GLN-140.
RX PubMed=24099278; DOI=10.1016/j.ajo.2013.08.008;
RA Ogasawara M., Matsumoto Y., Hayashi T., Ohno K., Yamada H., Kawakita T.,
RA Dogru M., Shimazaki J., Tsubota K., Tsuneoka H.;
RT "KRT12 mutations and in vivo confocal microscopy in two Japanese families
RT with Meesmann corneal dystrophy.";
RL Am. J. Ophthalmol. 157:93-102(2014).
RN [22]
RP VARIANTS MECD1 VAL-132 AND ASN-248.
RX PubMed=30535821; DOI=10.1007/s10384-018-00643-6;
RA Nishino T., Kobayashi A., Mori N., Masaki T., Yokogawa H., Fujiki K.,
RA Yanagawa A., Murakami A., Sugiyama K.;
RT "In vivo histology and p.L132V mutation in KRT12 gene in Japanese patients
RT with Meesmann corneal dystrophy.";
RL Jpn. J. Ophthalmol. 63:46-55(2019).
CC -!- FUNCTION: Involved in corneal epithelium organization, integrity and
CC corneal keratin expression. {ECO:0000269|PubMed:26758872}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Keratin-3 associates with keratin-12.
CC -!- TISSUE SPECIFICITY: Expressed in the corneal epithelium (at protein
CC level). {ECO:0000269|PubMed:26758872, ECO:0000269|PubMed:8759347}.
CC -!- DISEASE: Corneal dystrophy, Meesmann 1 (MECD1) [MIM:122100]: A form of
CC Meesmann corneal dystrophy, a corneal disease characterized by
CC fragility of the anterior corneal epithelium. Histological examination
CC shows a disorganized and thickened epithelium with widespread
CC cytoplasmic vacuolation and numerous small, round, debris-laden
CC intraepithelial cysts. Patients are usually asymptomatic until
CC adulthood when rupture of the corneal microcysts may cause erosions,
CC producing clinical symptoms such as photophobia, contact lens
CC intolerance and intermittent diminution of visual acuity. Rarely,
CC subepithelial scarring causes irregular corneal astigmatism and
CC permanent visual impairment. MECD1 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:10612503, ECO:0000269|PubMed:10644419,
CC ECO:0000269|PubMed:10781519, ECO:0000269|PubMed:12543196,
CC ECO:0000269|PubMed:15148206, ECO:0000269|PubMed:16227835,
CC ECO:0000269|PubMed:16352477, ECO:0000269|PubMed:17653038,
CC ECO:0000269|PubMed:18245975, ECO:0000269|PubMed:18661274,
CC ECO:0000269|PubMed:20577595, ECO:0000269|PubMed:23222558,
CC ECO:0000269|PubMed:24099278, ECO:0000269|PubMed:26758872,
CC ECO:0000269|PubMed:30535821, ECO:0000269|PubMed:9171831,
CC ECO:0000269|PubMed:9399908}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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}.
CC -!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
CC URL="http://www.interfil.org";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Keratin-12 entry;
CC URL="https://en.wikipedia.org/wiki/Keratin_12";
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DR EMBL; D78367; BAA11376.1; -; mRNA.
DR EMBL; AB007119; BAA25063.1; -; Genomic_DNA.
DR EMBL; AF137286; AAF61432.1; -; Genomic_DNA.
DR EMBL; AK313747; BAG36487.1; -; mRNA.
DR EMBL; CH471152; EAW60685.1; -; Genomic_DNA.
DR CCDS; CCDS11378.1; -.
DR RefSeq; NP_000214.1; NM_000223.3.
DR AlphaFoldDB; Q99456; -.
DR SMR; Q99456; -.
DR BioGRID; 110057; 5.
DR STRING; 9606.ENSP00000251643; -.
DR DrugBank; DB11157; Anthralin.
DR DrugBank; DB00400; Griseofulvin.
DR GlyGen; Q99456; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99456; -.
DR PhosphoSitePlus; Q99456; -.
DR SwissPalm; Q99456; -.
DR BioMuta; KRT12; -.
DR DMDM; 2497269; -.
DR jPOST; Q99456; -.
DR MassIVE; Q99456; -.
DR PaxDb; Q99456; -.
DR PeptideAtlas; Q99456; -.
DR PRIDE; Q99456; -.
DR ProteomicsDB; 78275; -.
DR Antibodypedia; 55294; 242 antibodies from 33 providers.
DR DNASU; 3859; -.
DR Ensembl; ENST00000251643.5; ENSP00000251643.4; ENSG00000187242.6.
DR Ensembl; ENST00000572470.2; ENSP00000459559.2; ENSG00000263243.2.
DR GeneID; 3859; -.
DR KEGG; hsa:3859; -.
DR MANE-Select; ENST00000251643.5; ENSP00000251643.4; NM_000223.4; NP_000214.1.
DR UCSC; uc002hvk.3; human.
DR CTD; 3859; -.
DR DisGeNET; 3859; -.
DR GeneCards; KRT12; -.
DR HGNC; HGNC:6414; KRT12.
DR HPA; ENSG00000187242; Not detected.
DR MalaCards; KRT12; -.
DR MIM; 122100; phenotype.
DR MIM; 601687; gene.
DR neXtProt; NX_Q99456; -.
DR OpenTargets; ENSG00000187242; -.
DR Orphanet; 98954; Meesmann corneal dystrophy.
DR PharmGKB; PA30201; -.
DR VEuPathDB; HostDB:ENSG00000187242; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR GeneTree; ENSGT00940000159382; -.
DR HOGENOM; CLU_012560_8_3_1; -.
DR InParanoid; Q99456; -.
DR OMA; EVEGDYC; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; Q99456; -.
DR TreeFam; TF332742; -.
DR PathwayCommons; Q99456; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 3859; 10 hits in 1075 CRISPR screens.
DR ChiTaRS; KRT12; human.
DR GeneWiki; Keratin_12; -.
DR GenomeRNAi; 3859; -.
DR Pharos; Q99456; Tbio.
DR PRO; PR:Q99456; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q99456; protein.
DR Bgee; ENSG00000187242; Expressed in mucosa of transverse colon and 57 other tissues.
DR ExpressionAtlas; Q99456; baseline and differential.
DR Genevisible; Q99456; HS.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc.
DR GO; GO:0061303; P:cornea development in camera-type eye; IMP:UniProtKB.
DR GO; GO:0008544; P:epidermis development; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:UniProtKB.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
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 1: Evidence at protein level;
KW Coiled coil; Corneal dystrophy; Direct protein sequencing; Disease variant;
KW Intermediate filament; Keratin; Reference proteome.
FT CHAIN 1..494
FT /note="Keratin, type I cytoskeletal 12"
FT /id="PRO_0000063644"
FT DOMAIN 125..440
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..124
FT /note="Head"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..160
FT /note="Coil 1A"
FT REGION 164..182
FT /note="Linker 1"
FT REGION 183..274
FT /note="Coil 1B"
FT REGION 275..297
FT /note="Linker 12"
FT REGION 298..435
FT /note="Coil 2"
FT REGION 436..494
FT /note="Tail"
FT REGION 446..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 15
FT /note="P -> S (in dbSNP:rs11650915)"
FT /evidence="ECO:0000269|PubMed:18245975,
FT ECO:0000269|PubMed:20577595"
FT /id="VAR_049783"
FT VARIANT 20
FT /note="R -> W (in dbSNP:rs17566772)"
FT /evidence="ECO:0000269|PubMed:10644419,
FT ECO:0000269|PubMed:18245975"
FT /id="VAR_009547"
FT VARIANT 129
FT /note="M -> T (in MECD1; dbSNP:rs28936695)"
FT /evidence="ECO:0000269|PubMed:10644419,
FT ECO:0000269|PubMed:16352477"
FT /id="VAR_013126"
FT VARIANT 129
FT /note="M -> V (in MECD1; dbSNP:rs267607387)"
FT /evidence="ECO:0000269|PubMed:20577595"
FT /id="VAR_072069"
FT VARIANT 130
FT /note="Q -> P (in MECD1; dbSNP:rs58864803)"
FT /evidence="ECO:0000269|PubMed:10781519"
FT /id="VAR_013127"
FT VARIANT 132
FT /note="L -> P (in MECD1; increased expression of keratins
FT KRT5, KRT6, KRT14 and KRT16 and decreased expression of
FT KRT12 in the corneal epithelium; increased expression of
FT DDIT3/CHOP and CASP12 in the corneal epithelium indicative
FT of up-regulation of the unfolded protein response.;
FT dbSNP:rs886038212)"
FT /evidence="ECO:0000269|PubMed:23222558,
FT ECO:0000269|PubMed:26758872"
FT /id="VAR_072070"
FT VARIANT 132
FT /note="L -> V (in MECD1)"
FT /evidence="ECO:0000269|PubMed:30535821"
FT /id="VAR_083313"
FT VARIANT 135
FT /note="R -> G (in MECD1; dbSNP:rs58410481)"
FT /evidence="ECO:0000269|PubMed:9399908"
FT /id="VAR_008526"
FT VARIANT 135
FT /note="R -> I (in MECD1; dbSNP:rs57218384)"
FT /evidence="ECO:0000269|PubMed:9399908"
FT /id="VAR_008525"
FT VARIANT 135
FT /note="R -> S (in MECD1; dbSNP:rs61282718)"
FT /evidence="ECO:0000269|PubMed:15148206"
FT /id="VAR_031394"
FT VARIANT 135
FT /note="R -> T (in MECD1; dbSNP:rs57218384)"
FT /evidence="ECO:0000269|PubMed:10644419,
FT ECO:0000269|PubMed:9171831"
FT /id="VAR_003834"
FT VARIANT 137
FT /note="A -> P (in MECD1; dbSNP:rs58038639)"
FT /evidence="ECO:0000269|PubMed:12543196"
FT /id="VAR_031395"
FT VARIANT 140
FT /note="L -> Q (in MECD1)"
FT /evidence="ECO:0000269|PubMed:24099278"
FT /id="VAR_072071"
FT VARIANT 140
FT /note="L -> R (in MECD1; dbSNP:rs58918655)"
FT /evidence="ECO:0000269|PubMed:9399908"
FT /id="VAR_008527"
FT VARIANT 143
FT /note="V -> L (in MECD1; dbSNP:rs58343600)"
FT /evidence="ECO:0000269|PubMed:18245975,
FT ECO:0000269|PubMed:9171831"
FT /id="VAR_003835"
FT VARIANT 248
FT /note="D -> N (in MECD1; unknown pathological significance;
FT dbSNP:rs150674571)"
FT /evidence="ECO:0000269|PubMed:30535821"
FT /id="VAR_083314"
FT VARIANT 399
FT /note="L -> LISNLEAQLL (in MECD1)"
FT /id="VAR_031396"
FT VARIANT 426
FT /note="I -> S (in MECD1; dbSNP:rs59350319)"
FT /evidence="ECO:0000269|PubMed:16352477"
FT /id="VAR_031397"
FT VARIANT 426
FT /note="I -> V (in MECD1; unknown pathological significance;
FT dbSNP:rs59465138)"
FT /evidence="ECO:0000269|PubMed:10612503"
FT /id="VAR_083315"
FT VARIANT 429
FT /note="Y -> C (in MECD1; dbSNP:rs59202432)"
FT /evidence="ECO:0000269|PubMed:16227835"
FT /id="VAR_031398"
FT VARIANT 429
FT /note="Y -> D (in MECD1; dbSNP:rs58162394)"
FT /evidence="ECO:0000269|PubMed:9399908"
FT /id="VAR_008528"
FT VARIANT 430
FT /note="R -> P (in MECD1; dbSNP:rs62635290)"
FT /evidence="ECO:0000269|PubMed:17653038"
FT /id="VAR_072072"
FT VARIANT 433
FT /note="L -> R (in MECD1; dbSNP:rs267607386)"
FT /evidence="ECO:0000269|PubMed:18661274"
FT /id="VAR_072073"
SQ SEQUENCE 494 AA; 53511 MW; 75C981380532B682 CRC64;
MDLSNNTMSL SVRTPGLSRR LSSQSVIGRP RGMSASSVGS GYGGSAFGFG ASCGGGFSAA
SMFGSSSGFG GGSGSSMAGG LGAGYGRALG GGSFGGLGMG FGGSPGGGSL GILSGNDGGL
LSGSEKETMQ NLNDRLASYL DKVRALEEAN TELENKIREW YETRGTGTAD ASQSDYSKYY
PLIEDLRNKI ISASIGNAQL LLQIDNARLA AEDFRMKYEN ELALRQGVEA DINGLRRVLD
ELTLTRTDLE MQIESLNEEL AYMKKNHEDE LQSFRVGGPG EVSVEMDAAP GVDLTRLLND
MRAQYETIAE QNRKDAEAWF IEKSGELRKE ISTNTEQLQS SKSEVTDLRR AFQNLEIELQ
SQLAMKKSLE DSLAEAEGDY CAQLSQVQQL ISNLEAQLLQ VRADAERQNV DHQRLLNVKA
RLELEIETYR RLLDGEAQGD GLEESLFVTD SKSQAQSTDS SKDPTKTRKI KTVVQEMVNG
EVVSSQVQEI EELM
