K1C12_MOUSE
ID K1C12_MOUSE Reviewed; 487 AA.
AC Q64291; A2A514; A2RRZ0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 25-MAY-2022, entry version 142.
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; Synonyms=Krt1-12, Krt1.12;
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 [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=FVB/N; TISSUE=Cornea;
RX PubMed=7508359; DOI=10.3109/02713689309029222;
RA Liu C.-Y., Zhu G., Westerhausen-Larson A., Converse R., Kao C.W.-C.,
RA Sun T.-T., Kao W.W.-Y.;
RT "Cornea-specific expression of K12 keratin during mouse development.";
RL Curr. Eye Res. 12:963-974(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Cornea;
RX PubMed=7523376; DOI=10.1016/s0021-9258(17)31438-2;
RA Liu C.-Y., Zhu G., Converse R., Kao C.W.-C., Nakamura H., Tseng S.C.-G.,
RA Mui M.-M., Seyer J., Justice M.J., Stech M.E., Hansen G.M., Kao W.W.-Y.;
RT "Characterization and chromosomal localization of the cornea-specific
RT murine keratin gene Krt1.12.";
RL J. Biol. Chem. 269:24627-24636(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP PROTEIN SEQUENCE OF 408-414, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=8977471;
RA Kao W.W., Liu C.Y., Converse R.L., Shiraishi A., Kao C.W., Ishizaki M.,
RA Doetschman T., Duffy J.;
RT "Keratin 12-deficient mice have fragile corneal epithelia.";
RL Invest. Ophthalmol. Vis. Sci. 37:2572-2584(1996).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=16431949; DOI=10.1167/iovs.05-1182;
RA Tanifuji-Terai N., Terai K., Hayashi Y., Chikama T., Kao W.W.;
RT "Expression of keratin 12 and maturation of corneal epithelium during
RT development and postnatal growth.";
RL Invest. Ophthalmol. Vis. Sci. 47:545-551(2006).
RN [8]
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).
CC -!- FUNCTION: Involved in corneal epithelium organization, integrity and
CC corneal keratin expression. {ECO:0000269|PubMed:8977471}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Keratin-3 associates with keratin-12.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q64291-1; Sequence=Displayed;
CC Name=2; Synonyms=K12-ALT9;
CC IsoId=Q64291-2; Sequence=VSP_002463, VSP_002464;
CC -!- TISSUE SPECIFICITY: Expressed in the corneal epithelium (at protein
CC level) (PubMed:7508359, PubMed:8977471, PubMed:26758872). Also
CC expressed in the suprabasal limbal epithelium of the cornea (at protein
CC level) (PubMed:7508359). {ECO:0000269|PubMed:26758872,
CC ECO:0000269|PubMed:7508359, ECO:0000269|PubMed:8977471}.
CC -!- DEVELOPMENTAL STAGE: Expression commences in corneal peridermal
CC epithelium in the embryo at 15.5 dpc (PubMed:16431949). Between 15.5
CC dpc and postnatal day 4 (P4), expression is restricted to the
CC suprabasal and/or superficial cells when the corneal epithelium begins
CC to stratify (PubMed:7508359, PubMed:16431949). At P30 expression is
CC sporadically detected in the basal corneal epithelium and the number of
CC positive basal cells increases as the mice grow older
CC (PubMed:16431949). {ECO:0000269|PubMed:16431949,
CC ECO:0000269|PubMed:7508359}.
CC -!- INDUCTION: Expression is retarded by epidermal growth factor (EGF).
CC {ECO:0000269|PubMed:7508359}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice are fertile and morphologically
CC normal with no defects in the skin or hair (PubMed:8977471). Corneal
CC epithelia show histological abnormalities and can be easily detached
CC from the corneal surface (PubMed:8977471). Reduced number of cell
CC layers in the corneal epithelium, with superficial epithelial cells
CC showing reduced adherence to underlying cell layers (PubMed:8977471).
CC Keratin intermediate filaments aggregate into dense bundles in the
CC corneal epithelium, with a reduced number of keratin filaments in basal
CC and suprabasal epithelial cells, and an absence of keratin filaments in
CC superficial epithelial cells (PubMed:8977471).
CC {ECO:0000269|PubMed:8977471}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA17792.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA52359.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U02880; AAA17792.1; ALT_FRAME; mRNA.
DR EMBL; U08095; AAA52359.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL591165; CAM21364.1; -; Genomic_DNA.
DR EMBL; BC131911; AAI31912.1; -; mRNA.
DR CCDS; CCDS36306.1; -. [Q64291-1]
DR PIR; A55033; A55033.
DR AlphaFoldDB; Q64291; -.
DR SMR; Q64291; -.
DR STRING; 10090.ENSMUSP00000017741; -.
DR PhosphoSitePlus; Q64291; -.
DR MaxQB; Q64291; -.
DR PaxDb; Q64291; -.
DR PeptideAtlas; Q64291; -.
DR PRIDE; Q64291; -.
DR ProteomicsDB; 269440; -. [Q64291-1]
DR ProteomicsDB; 269441; -. [Q64291-2]
DR MGI; MGI:96687; Krt12.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR InParanoid; Q64291; -.
DR PhylomeDB; Q64291; -.
DR TreeFam; TF332742; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR PRO; PR:Q64291; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q64291; protein.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
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:0060429; P:epithelium development; IMP:MGI.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:UniProtKB.
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 Alternative splicing; Coiled coil; Direct protein sequencing;
KW Intermediate filament; Keratin; Reference proteome.
FT CHAIN 1..487
FT /note="Keratin, type I cytoskeletal 12"
FT /id="PRO_0000063645"
FT DOMAIN 119..433
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..118
FT /note="Head"
FT REGION 119..154
FT /note="Coil 1A"
FT REGION 158..175
FT /note="Linker 1"
FT REGION 176..267
FT /note="Coil 1B"
FT REGION 268..290
FT /note="Linker 12"
FT REGION 291..428
FT /note="Coil 2"
FT REGION 428..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..487
FT /note="Tail"
FT COMPBIAS 433..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 211..212
FT /note="YE -> KL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002463"
FT VAR_SEQ 213..487
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002464"
FT CONFLICT 9
FT /note="A -> S (in Ref. 1; AAA17792 and 2; AAA52359)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="M -> I (in Ref. 1; AAA17792 and 2; AAA52359)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..101
FT /note="MGIAGSSGG -> IGDSWNAGV (in Ref. 1; AAA17792 and 2;
FT AAA52359)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="G -> R (in Ref. 3; CAM21364)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 487 AA; 52464 MW; 76FA2380822DCB94 CRC64;
MSLSVCTSAL SRRSSSQNGA AGRPWGASAS SVAGGYGGSA SGFGVGCGGL FSAASMFGSS
SGFSGGSAGC LPGLGSAYGG PLRGGAGGMG IGMGIAGSSG GGSLCIFSGN DGGLLSGSEK
ETMQNLNDRL ASYLGKVRSL EEANAELENK IREWYETRRT RDAGSQSDYS KYYPLIEDLK
NKIVSARVSN AQLLLQIDNA RLAAEDFRMK YENELALRQT VEADINGLRR VLDELTLTRA
DLEAQLETLT EELAYMKKNH EEELQSFQAG GPGEVNVEMD AAPGVDLTKV LNEMRAQYEA
MAEQNRKDAE AWFLEKSGEL RKEISSNTEQ LQSSKSEVTD LKRMVQNLEI ELQSQLAMKS
SLEGSLAETE GGYCCQLSQV QQLIGSLEEQ LQQVRADAER QNADHQRLLG VKARLEMEIE
TYRRLLEGDS QGDGFDESSS LSVSKPQTPS VDSSKDPNKT RKIKTVVQEI VNGEVVSSQV
QELEEEM
