K1C25_MOUSE
ID K1C25_MOUSE Reviewed; 446 AA.
AC Q8VCW2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Keratin, type I cytoskeletal 25;
DE AltName: Full=Cytokeratin-25;
DE Short=CK-25;
DE AltName: Full=Keratin-25;
DE Short=K25;
DE AltName: Full=Type I inner root sheath-specific keratin-K25irs1;
DE Short=mIRSa1;
GN Name=Krt25 {ECO:0000312|EMBL:AAH18391.1, ECO:0000312|MGI:MGI:1918060};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF TYR-379 AND
RP LEU-381.
RC STRAIN=C57BL/6J {ECO:0000269|PubMed:17920809};
RC TISSUE=Skin {ECO:0000269|PubMed:17920809};
RX PubMed=17920809; DOI=10.1016/j.ygeno.2007.07.013;
RA Tanaka S., Miura I., Yoshiki A., Kato Y., Yokoyama H., Shinogi A.,
RA Masuya H., Wakana S., Tamura M., Shiroishi T.;
RT "Mutations in the helix termination motif of mouse type I IRS keratin genes
RT impair the assembly of keratin intermediate filament.";
RL Genomics 90:703-711(2007).
RN [2]
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 [3] {ECO:0000312|EMBL:AAH18391.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH18391.1};
RC TISSUE=Salivary gland {ECO:0000312|EMBL:AAH18391.1};
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] {ECO:0000305}
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=14996088; DOI=10.1111/j.1365-2133.2004.05720.x;
RA Porter R.M., Gandhi M., Wilson N.J., Wood P., McLean W.H.I., Lane E.B.;
RT "Functional analysis of keratin components in the mouse hair follicle inner
RT root sheath.";
RL Br. J. Dermatol. 150:195-204(2004).
CC -!- FUNCTION: Essential for the proper assembly of type I and type II
CC keratin protein complexes and formation of keratin intermediate
CC filaments in the inner root sheath (irs) (PubMed:14996088,
CC PubMed:17920809). Plays a role in the cytoskeleton organization (By
CC similarity). {ECO:0000250|UniProtKB:Q7Z3Z0,
CC ECO:0000269|PubMed:14996088, ECO:0000269|PubMed:17920809}.
CC -!- SUBUNIT: Heterodimer of a type I and a type II keratin
CC (PubMed:14996088). Heterodimer with type II keratin KRT5 leading to the
CC formation of keratin intermediate filament (KIF) network. Interacts
CC with KRT6A to form filaments (By similarity).
CC {ECO:0000250|UniProtKB:Q7Z3Z0, ECO:0000269|PubMed:14996088,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14996088}.
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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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; AL590991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018391; AAH18391.1; -; mRNA.
DR CCDS; CCDS25377.1; -.
DR RefSeq; NP_598491.1; NM_133730.1.
DR AlphaFoldDB; Q8VCW2; -.
DR SMR; Q8VCW2; -.
DR BioGRID; 214269; 1.
DR ComplexPortal; CPX-5869; Keratin-25 - Keratin-71 dimer complex.
DR STRING; 10090.ENSMUSP00000048439; -.
DR PhosphoSitePlus; Q8VCW2; -.
DR jPOST; Q8VCW2; -.
DR PaxDb; Q8VCW2; -.
DR PeptideAtlas; Q8VCW2; -.
DR PRIDE; Q8VCW2; -.
DR ProteomicsDB; 268937; -.
DR Antibodypedia; 57604; 105 antibodies from 19 providers.
DR DNASU; 70810; -.
DR Ensembl; ENSMUST00000038004; ENSMUSP00000048439; ENSMUSG00000035831.
DR GeneID; 70810; -.
DR KEGG; mmu:70810; -.
DR UCSC; uc007lin.1; mouse.
DR CTD; 147183; -.
DR MGI; MGI:1918060; Krt25.
DR VEuPathDB; HostDB:ENSMUSG00000035831; -.
DR eggNOG; ENOG502SKJN; Eukaryota.
DR GeneTree; ENSGT00940000161994; -.
DR HOGENOM; CLU_012560_8_3_1; -.
DR InParanoid; Q8VCW2; -.
DR OMA; KGWYEQF; -.
DR OrthoDB; 805081at2759; -.
DR PhylomeDB; Q8VCW2; -.
DR TreeFam; TF332742; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 70810; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Krt25; mouse.
DR PRO; PR:Q8VCW2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VCW2; protein.
DR Bgee; ENSMUSG00000035831; Expressed in hair follicle and 53 other tissues.
DR Genevisible; Q8VCW2; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0045095; C:keratin filament; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0042633; P:hair cycle; ISO:MGI.
DR GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR GO; GO:0045109; P:intermediate filament organization; IMP:MGI.
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; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Intermediate filament; Keratin; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..446
FT /note="Keratin, type I cytoskeletal 25"
FT /id="PRO_0000312692"
FT DOMAIN 75..390
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..74
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 75..110
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 111..132
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 133..224
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 225..247
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 248..386
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 387..446
FT /note="Tail"
FT /evidence="ECO:0000255"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3Z0"
FT MUTAGEN 379
FT /note="Y->N: In Rex mutant M100573; mice exhibit curly hair
FT and vibrissae. The diameter of the hair shaft is irregular
FT due to morphological abnormalities in all three layers of
FT the irs."
FT /evidence="ECO:0000269|PubMed:17920809"
FT MUTAGEN 381
FT /note="L->P: In Rex mutant Re; mice exhibit curly hair and
FT vibrissae. The diameter of the hair shaft is irregular due
FT to morphological abnormalities in all three layers of the
FT irs."
FT /evidence="ECO:0000269|PubMed:17920809"
SQ SEQUENCE 446 AA; 48921 MW; 6B502F612AC4BE28 CRC64;
MSLRLSSGSR RSYARPSTGS LRGASFGAGN ACGVAGIGSG FSCAFGGSST GGNTGVANSC
AGFTVNEGGL LSGNEKVTMQ NLNDRLASYL DNVQALQEAN ADLEQKIKGW YEKFGPGSCR
GLDHDYSRYF PIIDDLKNQI ITSTTSNANA VLQIDNARLT ADDFRLKYEN ELALHQSVEA
DVNGLRRVLD EITLCRTDLE IQYETLSEEL TYLKKNHKEE MQALQCAAGG NVNVEMNAAP
GVDLTVLLNN MRAEYEALAE QNRRDAEAWF QEKSASLQQQ ITEDVGATTS ARNELTEMKR
TLQTLEIELQ SLLATKHSLE CSLTETEGNY CTQLAQIQAQ ISALEEQLHQ VRTETEGQKL
EYEQLLNVKA HLEKEIETYC LLIGGDEGAC KSSSYKSKDY GSGNAGNQIK DPVKAIVVKK
VLEEVDQRSK ILTTRLHSLE EKSQSN
