Q64291 · K1C12_MOUSE
- ProteinKeratin, type I cytoskeletal 12
- GeneKrt12
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids487 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in corneal epithelium organization, integrity and corneal keratin expression.
Miscellaneous
There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoskeleton | |
Cellular Component | intermediate filament | |
Molecular Function | structural molecule activity | |
Biological Process | cornea development in camera-type eye | |
Biological Process | epithelial cell differentiation | |
Biological Process | epithelium development | |
Biological Process | intermediate filament organization | |
Biological Process | morphogenesis of an epithelium |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKeratin, type I cytoskeletal 12
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ64291
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Knockout mice are fertile and morphologically normal with no defects in the skin or hair (PubMed:8977471).
Corneal epithelia show histological abnormalities and can be easily detached from the corneal surface (PubMed:8977471).
Reduced number of cell layers in the corneal epithelium, with superficial epithelial cells showing reduced adherence to underlying cell layers (PubMed:8977471).
Keratin intermediate filaments aggregate into dense bundles in the corneal epithelium, with a reduced number of keratin filaments in basal and suprabasal epithelial cells, and an absence of keratin filaments in superficial epithelial cells (PubMed:8977471).
Corneal epithelia show histological abnormalities and can be easily detached from the corneal surface (PubMed:8977471).
Reduced number of cell layers in the corneal epithelium, with superficial epithelial cells showing reduced adherence to underlying cell layers (PubMed:8977471).
Keratin intermediate filaments aggregate into dense bundles in the corneal epithelium, with a reduced number of keratin filaments in basal and suprabasal epithelial cells, and an absence of keratin filaments in superficial epithelial cells (PubMed:8977471).
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000063645 | 1-487 | Keratin, type I cytoskeletal 12 | |||
Sequence: MSLSVCTSALSRRSSSQNGAAGRPWGASASSVAGGYGGSASGFGVGCGGLFSAASMFGSSSGFSGGSAGCLPGLGSAYGGPLRGGAGGMGIGMGIAGSSGGGSLCIFSGNDGGLLSGSEKETMQNLNDRLASYLGKVRSLEEANAELENKIREWYETRRTRDAGSQSDYSKYYPLIEDLKNKIVSARVSNAQLLLQIDNARLAAEDFRMKYENELALRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHEEELQSFQAGGPGEVNVEMDAAPGVDLTKVLNEMRAQYEAMAEQNRKDAEAWFLEKSGELRKEISSNTEQLQSSKSEVTDLKRMVQNLEIELQSQLAMKSSLEGSLAETEGGYCCQLSQVQQLIGSLEEQLQQVRADAERQNADHQRLLGVKARLEMEIETYRRLLEGDSQGDGFDESSSLSVSKPQTPSVDSSKDPNKTRKIKTVVQEIVNGEVVSSQVQELEEEM |
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the corneal epithelium (at protein level) (PubMed:26758872, PubMed:7508359, PubMed:8977471).
Also expressed in the suprabasal limbal epithelium of the cornea (at protein level) (PubMed:7508359).
Also expressed in the suprabasal limbal epithelium of the cornea (at protein level) (PubMed:7508359).
Induction
Expression is retarded by epidermal growth factor (EGF).
Developmental stage
Expression commences in corneal peridermal epithelium in the embryo at 15.5 dpc (PubMed:16431949).
Between 15.5 dpc and postnatal day 4 (P4), expression is restricted to the suprabasal and/or superficial cells when the corneal epithelium begins to stratify (PubMed:16431949, PubMed:7508359).
At P30 expression is sporadically detected in the basal corneal epithelium and the number of positive basal cells increases as the mice grow older (PubMed:16431949).
Between 15.5 dpc and postnatal day 4 (P4), expression is restricted to the suprabasal and/or superficial cells when the corneal epithelium begins to stratify (PubMed:16431949, PubMed:7508359).
At P30 expression is sporadically detected in the basal corneal epithelium and the number of positive basal cells increases as the mice grow older (PubMed:16431949).
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-118 | Head | ||||
Sequence: MSLSVCTSALSRRSSSQNGAAGRPWGASASSVAGGYGGSASGFGVGCGGLFSAASMFGSSSGFSGGSAGCLPGLGSAYGGPLRGGAGGMGIGMGIAGSSGGGSLCIFSGNDGGLLSGS | ||||||
Region | 119-154 | Coil 1A | ||||
Sequence: EKETMQNLNDRLASYLGKVRSLEEANAELENKIREW | ||||||
Domain | 119-433 | IF rod | ||||
Sequence: EKETMQNLNDRLASYLGKVRSLEEANAELENKIREWYETRRTRDAGSQSDYSKYYPLIEDLKNKIVSARVSNAQLLLQIDNARLAAEDFRMKYENELALRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHEEELQSFQAGGPGEVNVEMDAAPGVDLTKVLNEMRAQYEAMAEQNRKDAEAWFLEKSGELRKEISSNTEQLQSSKSEVTDLKRMVQNLEIELQSQLAMKSSLEGSLAETEGGYCCQLSQVQQLIGSLEEQLQQVRADAERQNADHQRLLGVKARLEMEIETYRRLLEGDSQGD | ||||||
Region | 158-175 | Linker 1 | ||||
Sequence: RRTRDAGSQSDYSKYYPL | ||||||
Region | 176-267 | Coil 1B | ||||
Sequence: IEDLKNKIVSARVSNAQLLLQIDNARLAAEDFRMKYENELALRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHEEELQSF | ||||||
Region | 268-290 | Linker 12 | ||||
Sequence: QAGGPGEVNVEMDAAPGVDLTKV | ||||||
Region | 291-428 | Coil 2 | ||||
Sequence: LNEMRAQYEAMAEQNRKDAEAWFLEKSGELRKEISSNTEQLQSSKSEVTDLKRMVQNLEIELQSQLAMKSSLEGSLAETEGGYCCQLSQVQQLIGSLEEQLQQVRADAERQNADHQRLLGVKARLEMEIETYRRLLEG | ||||||
Region | 428-461 | Disordered | ||||
Sequence: GDSQGDGFDESSSLSVSKPQTPSVDSSKDPNKTR | ||||||
Region | 429-487 | Tail | ||||
Sequence: DSQGDGFDESSSLSVSKPQTPSVDSSKDPNKTRKIKTVVQEIVNGEVVSSQVQELEEEM | ||||||
Compositional bias | 433-454 | Polar residues | ||||
Sequence: DGFDESSSLSVSKPQTPSVDSS |
Sequence similarities
Belongs to the intermediate filament family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q64291-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length487
- Mass (Da)52,464
- Last updated2007-04-03 v2
- Checksum76FA2380822DCB94
Q64291-2
- Name2
- SynonymsK12-ALT9
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Z4YJD9 | Z4YJD9_MOUSE | Krt12 | 487 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 9 | in Ref. 1; AAA17792 and 2; AAA52359 | ||||
Sequence: A → S | ||||||
Sequence conflict | 89 | in Ref. 1; AAA17792 and 2; AAA52359 | ||||
Sequence: M → I | ||||||
Sequence conflict | 93-101 | in Ref. 1; AAA17792 and 2; AAA52359 | ||||
Sequence: MGIAGSSGG → IGDSWNAGV | ||||||
Alternative sequence | VSP_002463 | 211-212 | in isoform 2 | |||
Sequence: YE → KL | ||||||
Alternative sequence | VSP_002464 | 213-487 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 318 | in Ref. 3; CAM21364 | ||||
Sequence: G → R | ||||||
Compositional bias | 433-454 | Polar residues | ||||
Sequence: DGFDESSSLSVSKPQTPSVDSS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U02880 EMBL· GenBank· DDBJ | AAA17792.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
U08095 EMBL· GenBank· DDBJ | AAA52359.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
AL591165 EMBL· GenBank· DDBJ | CAM21364.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC131911 EMBL· GenBank· DDBJ | AAI31912.1 EMBL· GenBank· DDBJ | mRNA |