K1C27_MOUSE
ID K1C27_MOUSE Reviewed; 448 AA.
AC Q9Z320;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Keratin, type I cytoskeletal 27;
DE AltName: Full=Cytokeratin-27;
DE Short=CK-27;
DE AltName: Full=Keratin complex-1, acidic, gene C29;
DE AltName: Full=Keratin-27;
DE Short=K27;
DE AltName: Full=Type I inner root sheath-specific keratin-K25irs3;
GN Name=Krt27 {ECO:0000312|MGI:MGI:1339999};
GN Synonyms=c29 {ECO:0000312|EMBL:BAA34228.1},
GN Krt1-c29 {ECO:0000312|MGI:MGI:1339999};
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:BAA34228.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/10J {ECO:0000312|EMBL:BAA34228.1};
RC TISSUE=Skin {ECO:0000312|EMBL:BAA34228.1};
RX PubMed=10087197; DOI=10.1006/geno.1998.5721;
RA Sato H., Koide T., Sagai T., Ishiguro S., Tamai M., Saitou N.,
RA Shiroishi T.;
RT "The genomic organization of type I keratin genes in mice.";
RL Genomics 56:303-309(1999).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF 315-LYS--SER-388.
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 [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, SUBUNIT, TISSUE SPECIFICITY, 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). {ECO:0000269|PubMed:14996088,
CC ECO:0000269|PubMed:17920809}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Interacts with KRT6A to form filaments. {ECO:0000269|PubMed:14996088,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14996088}.
CC -!- TISSUE SPECIFICITY: Expressed in skin. Expressed in the Henle layer and
CC cuticle of the irs in hair follicle bulb. In the hair follicle,
CC expression was observed in all layers of the irs but was stronger in
CC the Henle layer and cuticle than the Huxley layer until the Henle layer
CC differentiated (at protein level). {ECO:0000269|PubMed:10087197,
CC 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; AB013607; BAA34228.1; -; mRNA.
DR EMBL; AL590991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25379.1; -.
DR RefSeq; NP_034796.1; NM_010666.2.
DR AlphaFoldDB; Q9Z320; -.
DR SMR; Q9Z320; -.
DR BioGRID; 201029; 9.
DR IntAct; Q9Z320; 1.
DR MINT; Q9Z320; -.
DR STRING; 10090.ENSMUSP00000017732; -.
DR iPTMnet; Q9Z320; -.
DR PhosphoSitePlus; Q9Z320; -.
DR jPOST; Q9Z320; -.
DR MaxQB; Q9Z320; -.
DR PaxDb; Q9Z320; -.
DR PRIDE; Q9Z320; -.
DR ProteomicsDB; 269164; -.
DR Antibodypedia; 55223; 12 antibodies from 9 providers.
DR DNASU; 16675; -.
DR Ensembl; ENSMUST00000017732; ENSMUSP00000017732; ENSMUSG00000017588.
DR GeneID; 16675; -.
DR KEGG; mmu:16675; -.
DR UCSC; uc007lip.1; mouse.
DR CTD; 342574; -.
DR MGI; MGI:1339999; Krt27.
DR VEuPathDB; HostDB:ENSMUSG00000017588; -.
DR eggNOG; ENOG502SIHJ; Eukaryota.
DR GeneTree; ENSGT00940000161982; -.
DR HOGENOM; CLU_012560_8_3_1; -.
DR InParanoid; Q9Z320; -.
DR OMA; SRVHTME; -.
DR OrthoDB; 805081at2759; -.
DR PhylomeDB; Q9Z320; -.
DR TreeFam; TF332742; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 16675; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q9Z320; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9Z320; protein.
DR Bgee; ENSMUSG00000017588; Expressed in hair follicle and 52 other tissues.
DR Genevisible; Q9Z320; 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 GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
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..448
FT /note="Keratin, type I cytoskeletal 27"
FT /id="PRO_0000312702"
FT DOMAIN 74..389
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..73
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 74..109
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 110..131
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 132..223
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 224..246
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 247..385
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 386..448
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 427..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 315..388
FT /note="Missing: In Rex wavy coat; 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"
SQ SEQUENCE 448 AA; 49105 MW; 14CAF4EAC0828AEA CRC64;
MSVRFSSASR RLGSVRLSSA GAALGAGNAC GVPGIGSGFS CAFGGSSLAG GLGMGGASCG
AFTANEHGLL SGNEKVTMQN LNDRLASYLE NVQALEEANA DLEQKIKDWY EKFGPGSCRG
LDHDYSRYFP IIDDLRTQII SATAHNANII LQNDNARLTA DDFRMKYENE LALHQSVDAD
INGLRRVLDE LTLCRTDLEV QLETLSEELA YLKKNHEEEM QALQCAAGGN VNVEMNAAPG
VDLTVLLNNM RAEYEALAEQ NRRDAEAWFQ EKSASLQQQI SDDAGATTSA RNELTEMKRT
LQTLEIELQS LLAMKHSLEC SLTETEGNYC TQLAQIQAQI SALEEQLHQV RTETEGQKLE
YEQLLNVKAH LEKEIETYCR LIDGDEGSCV KAKGQGRPGN QTKDSPKTAI VKTVVEELDP
RGKVLSSRVH TLEEKSTKVN KTEQRIPS
