K1C24_MOUSE
ID K1C24_MOUSE Reviewed; 512 AA.
AC A1L317; A1L316; Q8BKC6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Keratin, type I cytoskeletal 24;
DE AltName: Full=Cytokeratin-24;
DE Short=CK-24;
DE AltName: Full=Keratin-24;
DE Short=K24;
DE AltName: Full=Type I keratin-24;
GN Name=Krt24; Synonyms=Ka24;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-512.
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin, I (acidic) and II (neutral to basic) (40-55 and 56-70 kDa,
CC respectively).
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AL590991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC129847; AAI29848.1; -; mRNA.
DR EMBL; BC129848; AAI29849.1; -; mRNA.
DR EMBL; AK053678; BAC35470.1; -; mRNA.
DR CCDS; CCDS36305.1; -.
DR RefSeq; NP_083669.1; NM_029393.1.
DR AlphaFoldDB; A1L317; -.
DR SMR; A1L317; -.
DR BioGRID; 217685; 3.
DR STRING; 10090.ENSMUSP00000017255; -.
DR iPTMnet; A1L317; -.
DR PhosphoSitePlus; A1L317; -.
DR jPOST; A1L317; -.
DR MaxQB; A1L317; -.
DR PaxDb; A1L317; -.
DR PeptideAtlas; A1L317; -.
DR PRIDE; A1L317; -.
DR ProteomicsDB; 269163; -.
DR Antibodypedia; 16540; 218 antibodies from 15 providers.
DR DNASU; 75706; -.
DR Ensembl; ENSMUST00000017255; ENSMUSP00000017255; ENSMUSG00000020913.
DR GeneID; 75706; -.
DR KEGG; mmu:75706; -.
DR UCSC; uc007lim.1; mouse.
DR CTD; 192666; -.
DR MGI; MGI:1922956; Krt24.
DR VEuPathDB; HostDB:ENSMUSG00000020913; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR GeneTree; ENSGT00940000161783; -.
DR HOGENOM; CLU_012560_8_3_1; -.
DR InParanoid; A1L317; -.
DR OMA; SGSTNMG; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; A1L317; -.
DR TreeFam; TF332742; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 75706; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Krt24; mouse.
DR PRO; PR:A1L317; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; A1L317; protein.
DR Bgee; ENSMUSG00000020913; Expressed in tail skin and 38 other tissues.
DR Genevisible; A1L317; MM.
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 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 2: Evidence at transcript level;
KW Coiled coil; Intermediate filament; Keratin; Reference proteome.
FT CHAIN 1..512
FT /note="Keratin, type I cytoskeletal 24"
FT /id="PRO_0000314851"
FT DOMAIN 141..455
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..140
FT /note="Head"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..176
FT /note="Coil 1A"
FT REGION 177..197
FT /note="Linker 1"
FT REGION 198..289
FT /note="Coil 1B"
FT REGION 290..312
FT /note="Linker 12"
FT REGION 313..451
FT /note="Coil 2"
FT REGION 452..512
FT /note="Tail"
FT CONFLICT 70
FT /note="S -> N (in Ref. 2; AAI29849)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="Y -> F (in Ref. 2; AAI29849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 54041 MW; F4CBEFC441D2D91E CRC64;
MFCSAQKGSC SSRVSSSGAV GSRGCTGGSS FGGGSSCGLG GGSAWGFQGS SNSWSLSGGS
KGSMGGGFGS CSVRGGFGAA SSYGGGSGFG GSSGFGGGSG FGGGSGFGGG SSGGFSSYGG
SMGCGLGGVS GYDGGLLSGS EKQTMQDLND RLANYLDKVR ALEEANTDLE CKIKDWYGKH
GSVKGGSGRD YSQYYSIIED LKKQILSATC ENARMTLQID NARLAADDFR MKYEHELCLR
ECLEADINGL RKVLDEMTMT RCDLEMQIEG LTEELVFLRK NHEEEMKCMQ GSSGGDVTVE
MNAAPGVDLT KLLNDMRAQY EAMAEQNRQE AERQFNERSA SLQAQISSDA GEANCARSEV
MELKRTVQTL EIELQSQLAL KCSLEGTLAD TEAGYVAQLS GIQAQISSLE EQLSQIRAET
QCQSAEYECL LNIKTRLEQE IETYRRLLNG DGGGCDYRNL VSKNVVLSDS GSCAGQGKDP
SKTRVTKTII EEVVDGRVVS SQVSNISEVK IK
