K2C4_MOUSE
ID K2C4_MOUSE Reviewed; 525 AA.
AC P07744; A6H6D6; Q6P3F5;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Keratin, type II cytoskeletal 4;
DE AltName: Full=Cytokeratin-4;
DE Short=CK-4;
DE AltName: Full=Cytoskeletal 57 kDa keratin;
DE AltName: Full=Keratin-4;
DE Short=K4;
DE AltName: Full=Type-II keratin Kb4;
GN Name=Krt4; Synonyms=Krt2-4;
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], AND TISSUE SPECIFICITY.
RX PubMed=2418416; DOI=10.1093/nar/14.2.751;
RA Knapp B., Rentrop M., Schweizer J., Winter H.;
RT "Nonepidermal members of the keratin multigene family: cDNA sequences and
RT in situ localization of the mRNAs.";
RL Nucleic Acids Res. 14:751-763(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [3]
RP PROTEIN SEQUENCE OF 157-163; 410-421 AND 439-449, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-13, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Keratin-4 is generally associated with keratin-13.
CC -!- TISSUE SPECIFICITY: Expressed in the dorsal and ventral epithelium of
CC the tongue. Highest expression levels are detected in the suprabasal
CC layer with low levels detected in the basal cell layer. Within the
CC suprabasal layer expression is highest in the spinous cells, decreases
CC in the granular cells and is not detected in the stratum corneum.
CC {ECO:0000269|PubMed:2418416}.
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=AAH64008.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X03491; CAA27207.1; -; mRNA.
DR EMBL; BC064008; AAH64008.1; ALT_INIT; mRNA.
DR EMBL; BC145839; AAI45840.1; -; mRNA.
DR EMBL; BC145841; AAI45842.1; -; mRNA.
DR CCDS; CCDS37222.1; -.
DR PIR; A23518; A23518.
DR RefSeq; NP_032501.2; NM_008475.2.
DR AlphaFoldDB; P07744; -.
DR SMR; P07744; -.
DR BioGRID; 201034; 11.
DR IntAct; P07744; 2.
DR MINT; P07744; -.
DR STRING; 10090.ENSMUSP00000023797; -.
DR iPTMnet; P07744; -.
DR PhosphoSitePlus; P07744; -.
DR jPOST; P07744; -.
DR PaxDb; P07744; -.
DR PeptideAtlas; P07744; -.
DR PRIDE; P07744; -.
DR ProteomicsDB; 269055; -.
DR Antibodypedia; 3687; 494 antibodies from 38 providers.
DR DNASU; 16682; -.
DR Ensembl; ENSMUST00000023797; ENSMUSP00000023797; ENSMUSG00000059668.
DR GeneID; 16682; -.
DR KEGG; mmu:16682; -.
DR UCSC; uc007xuf.1; mouse.
DR CTD; 3851; -.
DR MGI; MGI:96701; Krt4.
DR VEuPathDB; HostDB:ENSMUSG00000059668; -.
DR eggNOG; ENOG502QURK; Eukaryota.
DR GeneTree; ENSGT00940000161550; -.
DR HOGENOM; CLU_012560_6_1_1; -.
DR InParanoid; P07744; -.
DR OMA; QYEDIIQ; -.
DR OrthoDB; 824246at2759; -.
DR PhylomeDB; P07744; -.
DR TreeFam; TF317854; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 16682; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Krt4; mouse.
DR PRO; PR:P07744; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P07744; protein.
DR Bgee; ENSMUSG00000059668; Expressed in superior surface of tongue and 89 other tissues.
DR Genevisible; P07744; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0045095; C:keratin filament; ISO:MGI.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IMP:UniProtKB.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP: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 Coiled coil; Direct protein sequencing; Intermediate filament; Keratin;
KW Methylation; Reference proteome.
FT CHAIN 1..525
FT /note="Keratin, type II cytoskeletal 4"
FT /id="PRO_0000063723"
FT DOMAIN 146..459
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..145
FT /note="Head"
FT REGION 146..181
FT /note="Coil 1A"
FT REGION 182..200
FT /note="Linker 1"
FT REGION 201..292
FT /note="Coil 1B"
FT REGION 293..316
FT /note="Linker 12"
FT REGION 317..455
FT /note="Coil 2"
FT REGION 456..524
FT /note="Tail"
FT SITE 397
FT /note="Stutter"
FT MOD_RES 13
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 13
FT /note="R -> P (in Ref. 1; CAA27207)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="S -> T (in Ref. 1; CAA27207)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="G -> D (in Ref. 2; AAH64008)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="L -> P (in Ref. 1; CAA27207)"
FT /evidence="ECO:0000305"
FT CONFLICT 476..480
FT /note="ASIGG -> QHWR (in Ref. 1; CAA27207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 56283 MW; 27A3A3DF7E87DF90 CRC64;
MIARQSSVRG ASRGFSSGSA IAGGVKRVAF SSGSMSGGAG RCSSGGFGSR SLYNLGGHKS
ISMSVAGSCQ GGGYGGAGGF GVGGYGAGFG AGGFGGGFGG SFNGRGGPGF PVCPAGGIQE
VTINQSLLTP LQVEIDPEIQ KIRTAEREQI KTLNNKFASF IDKVRFLEQQ NKVLETKWNL
LQQQTTTTSP KSLDPFFETY INALRKNLDT LSNDKGRLQS ELKMMQDSVE DFKTKYEEEI
NKRTAAENDF VVLKKDVDAA YMIKVELEAK MESLKDEINF TRVLYEAELA QMQTHVSDTS
VVLSMDNNRN LDLDGIIAEV RAQYEDIARK SKAEVESWYQ IKVQQLQMSA DQHGDSLKTT
KNEISELNRM IQRLRAEIEN IKKQSQTLQA SVADAEQRGE LALKDAYSKR AELETALQKA
KEDLARLLRD YQALMNVKLA LDVEIATYRK LLEGEECRMS GECKSAVSIS VVGGSASIGG
SGLGLGSGFC SGSGSGSGFG FGGGIYGGSG SKITSSATIT KRSPR
