KRT36_MOUSE
ID KRT36_MOUSE Reviewed; 473 AA.
AC B1AQ75; Q61861;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Keratin, type I cuticular Ha6 {ECO:0000250|UniProtKB:O76013};
DE AltName: Full=Keratin-36 {ECO:0000312|EMBL:CAM17771.1};
DE Short=K36;
DE AltName: Full=Keratin-5 {ECO:0000312|MGI:MGI:109364};
DE AltName: Full=MHRa-1 {ECO:0000312|EMBL:CAA46480.1};
DE AltName: Full=Type I keratin 48 kDa {ECO:0000303|PubMed:1385239};
GN Name=Krt36 {ECO:0000312|EMBL:CAM17771.1};
GN Synonyms=Hra-1 {ECO:0000312|MGI:MGI:109364},
GN Krt1-22 {ECO:0000312|MGI:MGI:109364}, Krt1-5 {ECO:0000312|MGI:MGI:109364};
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] {ECO:0000305, ECO:0000312|EMBL:CAA46480.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 283-473, SUBUNIT, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=NMRI; TISSUE=Tail epidermis {ECO:0000269|PubMed:1385239};
RX PubMed=1385239; DOI=10.1111/j.1432-0436.1992.tb00671.x;
RA Tobiasch E., Winter H., Schweizer J.;
RT "Structural features and sites of expression of a new murine 65 kD and 48
RT kD hair-related keratin pair, associated with a special type of
RT parakeratotic epithelial differentiation.";
RL Differentiation 50:163-178(1992).
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC {ECO:0000269|PubMed:1385239}.
CC -!- TISSUE SPECIFICITY: In skin, only expressed in the suprabasal cells of
CC tail scale epidermis. Suprabasally expressed in stratified squamous
CC epithelia and also in the posterior unit of the complex filiform
CC papillae of tongue. Expressed in rare anatomical sites in which an
CC orthokeratinized stratum corneum would be too soft and a hard
CC keratinized structure would be too rigid to meet the functional
CC requirement of the respective epithelia. {ECO:0000269|PubMed:1385239}.
CC -!- INDUCTION: mRNA synthesis is suppressed during retinoic acid-mediated
CC orthokeratotic conversion of tail scale epidermis.
CC {ECO:0000269|PubMed:1385239}.
CC -!- MISCELLANEOUS: There are two types of hair/microfibrillar keratin, I
CC (acidic) and II (neutral to basic). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA46480.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL590873; CAM17771.1; -; Genomic_DNA.
DR EMBL; AL662808; CAM17771.1; JOINED; Genomic_DNA.
DR EMBL; AL662808; CAM15791.1; -; Genomic_DNA.
DR EMBL; AL590873; CAM15791.1; JOINED; Genomic_DNA.
DR EMBL; X65506; CAA46480.1; ALT_FRAME; mRNA.
DR CCDS; CCDS48929.1; -.
DR PIR; I48660; S21388.
DR RefSeq; NP_001167570.1; NM_001174099.1.
DR RefSeq; XP_017169791.1; XM_017314302.1.
DR AlphaFoldDB; B1AQ75; -.
DR SMR; B1AQ75; -.
DR BioGRID; 201028; 4.
DR ComplexPortal; CPX-5870; Keratin-36 - Keratin-86 dimer complex.
DR STRING; 10090.ENSMUSP00000103039; -.
DR iPTMnet; B1AQ75; -.
DR PhosphoSitePlus; B1AQ75; -.
DR jPOST; B1AQ75; -.
DR MaxQB; B1AQ75; -.
DR PaxDb; B1AQ75; -.
DR PeptideAtlas; B1AQ75; -.
DR PRIDE; B1AQ75; -.
DR ProteomicsDB; 263677; -.
DR Antibodypedia; 16678; 139 antibodies from 26 providers.
DR DNASU; 16673; -.
DR Ensembl; ENSMUST00000107416; ENSMUSP00000103039; ENSMUSG00000020916.
DR GeneID; 16673; -.
DR KEGG; mmu:16673; -.
DR UCSC; uc011yey.1; mouse.
DR CTD; 8689; -.
DR MGI; MGI:109364; Krt36.
DR VEuPathDB; HostDB:ENSMUSG00000020916; -.
DR eggNOG; ENOG502QQY9; Eukaryota.
DR GeneTree; ENSGT00940000161311; -.
DR HOGENOM; CLU_012560_8_0_1; -.
DR InParanoid; B1AQ75; -.
DR OMA; AHPCSTE; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; B1AQ75; -.
DR TreeFam; TF332742; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 16673; 3 hits in 69 CRISPR screens.
DR PRO; PR:B1AQ75; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; B1AQ75; protein.
DR Bgee; ENSMUSG00000020916; Expressed in tail skin and 27 other tissues.
DR Genevisible; B1AQ75; MM.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:UniProtKB.
DR GO; GO:0045095; C:keratin filament; ISO:MGI.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IDA:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; IDA:UniProtKB.
DR InterPro; IPR018039; IF_conserved.
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; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Intermediate filament; Keratin; Reference proteome.
FT CHAIN 1..473
FT /note="Keratin, type I cuticular Ha6"
FT /id="PRO_0000363989"
FT DOMAIN 93..404
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..93
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 94..128
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 129..139
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 140..240
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 241..256
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 257..400
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 401..473
FT /note="Tail"
FT /evidence="ECO:0000255"
FT SITE 342
FT /note="Stutter"
FT /evidence="ECO:0000255"
FT CONFLICT 285..286
FT /note="NT -> IA (in Ref. 2; CAA46480)"
FT /evidence="ECO:0000305"
FT CONFLICT 316..318
FT /note="VNS -> SQL (in Ref. 2; CAA46480)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="Q -> R (in Ref. 2; CAA46480)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="N -> H (in Ref. 2; CAA46480)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="N -> K (in Ref. 2; CAA46480)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 52790 MW; A492B6686024FCA8 CRC64;
MATQICTPTF SAGSAKGLCG TSGSFSRISS IHSMGSCRAP SLVGTVGSVS SFRTGFSGPG
SCLPGSYLSS GCHSSGFAGS GGWFCEGAFN GNEKATMQIL NDRLANYLEK VRQLEQENTQ
LECRIREWYE CQIPYICPDY QSYFKTAEEL QQKILLTKSE NARLILQIDN AKLAADDFRT
KYETELSLRQ LVEADINGLR RILDELTLCK ADLEAQVESL KEELLCLKRN HEEEVNALRS
QLGDRLNVEV DAAPPVDLNK ILDDMRCQYE TLVENNRRDV EAWFNTQTEE LNQQVVSSSE
QLQCCQTEII ELRRTVNSLE IELQAQQSMR NSLESTLAET EARYSSQLGQ MQCLITNVES
QLAEIRCDLE RQNHEYQVLL DVKARLESEI ATYRRLLDGE DCKLPAHPCS TECKPAVRVP
YIPSTTCTPA GPCTPAGPCT PAPQVSTQIR TITEEIRDGR VISSREHVVP RAM
