K1C28_MOUSE
ID K1C28_MOUSE Reviewed; 462 AA.
AC A6BLY7; Q9D637;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Keratin, type I cytoskeletal 28;
DE AltName: Full=Cytokeratin-28;
DE Short=CK-28;
DE AltName: Full=Keratin-25D;
DE Short=K25D;
DE AltName: Full=Keratin-28;
DE Short=K28;
DE AltName: Full=Type I inner root sheath-specific keratin-K25irs4;
GN Name=Krt28 {ECO:0000312|EMBL:BAF64536.1};
GN Synonyms=Krt25d {ECO:0000312|MGI:MGI:1918093};
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, ECO:0000312|EMBL:BAF64536.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAF64536.1};
RC TISSUE=Skin {ECO:0000312|EMBL:BAF64536.1};
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] {ECO:0000312|EMBL:BAB29485.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB29485.1};
RC TISSUE=Skin {ECO:0000312|EMBL:BAB29485.1};
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).
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 types I and II keratin
CC protein complexes and the formation of keratin intermediate filaments
CC in the inner root sheath (irs). {ECO:0000269|PubMed:14996088,
CC ECO:0000269|PubMed:17920809}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14996088}.
CC -!- TISSUE SPECIFICITY: In the hair follicle and bulb, uniformly expressed
CC in all three layers of the inner root sheath (the Henle layer, the
CC Huxley layer and the cuticle) and observed in matrix cells (at protein
CC level). {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}.
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DR EMBL; AB288231; BAF64536.1; -; mRNA.
DR EMBL; AK014642; BAB29485.1; -; mRNA.
DR EMBL; AL591165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS48906.1; -.
DR RefSeq; NP_081850.1; NM_027574.1.
DR AlphaFoldDB; A6BLY7; -.
DR SMR; A6BLY7; -.
DR BioGRID; 214288; 1.
DR STRING; 10090.ENSMUSP00000006963; -.
DR iPTMnet; A6BLY7; -.
DR PhosphoSitePlus; A6BLY7; -.
DR EPD; A6BLY7; -.
DR jPOST; A6BLY7; -.
DR MaxQB; A6BLY7; -.
DR PaxDb; A6BLY7; -.
DR PeptideAtlas; A6BLY7; -.
DR PRIDE; A6BLY7; -.
DR ProteomicsDB; 269165; -.
DR Antibodypedia; 28714; 88 antibodies from 19 providers.
DR DNASU; 70843; -.
DR Ensembl; ENSMUST00000006963; ENSMUSP00000006963; ENSMUSG00000055937.
DR GeneID; 70843; -.
DR KEGG; mmu:70843; -.
DR UCSC; uc007liq.2; mouse.
DR CTD; 162605; -.
DR MGI; MGI:1918093; Krt28.
DR VEuPathDB; HostDB:ENSMUSG00000055937; -.
DR eggNOG; ENOG502SHRG; Eukaryota.
DR GeneTree; ENSGT00940000162192; -.
DR HOGENOM; CLU_012560_8_3_1; -.
DR InParanoid; A6BLY7; -.
DR OMA; KGWYDKY; -.
DR OrthoDB; 805081at2759; -.
DR PhylomeDB; A6BLY7; -.
DR TreeFam; TF332742; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 70843; 4 hits in 72 CRISPR screens.
DR PRO; PR:A6BLY7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; A6BLY7; protein.
DR Bgee; ENSMUSG00000055937; Expressed in hair follicle and 26 other tissues.
DR Genevisible; A6BLY7; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Intermediate filament; Keratin; Reference proteome.
FT CHAIN 1..462
FT /note="Keratin, type I cytoskeletal 28"
FT /id="PRO_0000312706"
FT DOMAIN 84..399
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..83
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..119
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 120..141
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 142..233
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 234..256
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 257..395
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 396..462
FT /note="Tail"
FT /evidence="ECO:0000255"
SQ SEQUENCE 462 AA; 50346 MW; 8021DAC2A1E91423 CRC64;
MSLRFSGGSR HVGIQSGSLR PPSGGAGFAG SSVAGGSVAG SGFSWALGGT LGSAPGGSHA
TGALGNVSGV CFIGSEGGLL SGNEKVTMQN LNNRLASYLD NVKALEEANS ELERKIKTWH
EKYGPGSCRG LDRDYSKYHL TIEDLKSKII SSTAANANII LQIDNARLAA DDFRLKYENE
LTLHQNVEAD INGLRRVLDE LTLCRTDQEL QYESLSEEMT YLKKNHEEEM KVLQCAAGGN
VNVEMNAAPG VDLTVLLNNM RAEYEALAEQ NRRDAEAWFQ EKSATLQQQI SNDLGAATSA
RTELTELKRS LQTLEIELQS LSATKHSLEC SLAETEGNYC SQLAQIQAQI SALEEQLHQV
RTETEGQKLE HEQLLDIKAH LEKEIETYCR LIDGDENSCS VSKGFESGTS GNSPKDVSKT
TLVKTVVEEI DQRGKVLSSR IHSIEEKMSK MSNGKAEQRV PF
