KRT81_MOUSE
ID KRT81_MOUSE Reviewed; 481 AA.
AC Q9ERE2; E9QLY5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Keratin, type II cuticular Hb1 {ECO:0000250|UniProtKB:Q14533};
DE AltName: Full=Keratin-81 {ECO:0000303|PubMed:12399393};
DE Short=K81;
DE AltName: Full=Type II hair keratin Hb1;
GN Name=Krt81 {ECO:0000312|MGI:MGI:1928858};
GN Synonyms=Krt2-19 {ECO:0000312|MGI:MGI:1928858};
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:AAG34120.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 92-481, AND TISSUE SPECIFICITY.
RC STRAIN=C3H/HeN {ECO:0000312|EMBL:AAG34120.1};
RC TISSUE=Dorsal skin {ECO:0000269|PubMed:12399393};
RX PubMed=12399393; DOI=10.1093/genetics/162.2.831;
RA Poirier C., Yoshiki A., Fujiwara K., Guenet J.-L., Kusakabe M.;
RT "Hague (Hag): a new mouse hair mutation with an unstable semidominant
RT allele.";
RL Genetics 162:831-840(2002).
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in dorsal skin.
CC {ECO:0000269|PubMed:12399393}.
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}.
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DR EMBL; AC103674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC157583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF312018; AAG34120.1; -; mRNA.
DR CCDS; CCDS49734.1; -.
DR RefSeq; NP_001159629.1; NM_001166157.1.
DR AlphaFoldDB; Q9ERE2; -.
DR SMR; Q9ERE2; -.
DR BioGRID; 211105; 5.
DR STRING; 10090.ENSMUSP00000056525; -.
DR iPTMnet; Q9ERE2; -.
DR PhosphoSitePlus; Q9ERE2; -.
DR jPOST; Q9ERE2; -.
DR MaxQB; Q9ERE2; -.
DR PaxDb; Q9ERE2; -.
DR PeptideAtlas; Q9ERE2; -.
DR PRIDE; Q9ERE2; -.
DR ProteomicsDB; 263678; -.
DR DNASU; 64818; -.
DR Ensembl; ENSMUST00000061185; ENSMUSP00000056525; ENSMUSG00000067615.
DR GeneID; 64818; -.
DR KEGG; mmu:64818; -.
DR UCSC; uc007xth.2; mouse.
DR CTD; 3887; -.
DR MGI; MGI:1928858; Krt81.
DR VEuPathDB; HostDB:ENSMUSG00000067615; -.
DR eggNOG; ENOG502SKJW; Eukaryota.
DR GeneTree; ENSGT00940000154026; -.
DR HOGENOM; CLU_012560_5_0_1; -.
DR InParanoid; Q9ERE2; -.
DR OMA; CCESHLE; -.
DR OrthoDB; 557821at2759; -.
DR PhylomeDB; Q9ERE2; -.
DR TreeFam; TF317854; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 64818; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Krt81; mouse.
DR PRO; PR:Q9ERE2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9ERE2; protein.
DR Bgee; ENSMUSG00000067615; Expressed in lip and 43 other tissues.
DR Genevisible; Q9ERE2; MM.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Intermediate filament; Isopeptide bond; Keratin;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..481
FT /note="Keratin, type II cuticular Hb1"
FT /id="PRO_0000361690"
FT DOMAIN 106..417
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..106
FT /note="Head"
FT /evidence="ECO:0000250"
FT REGION 107..141
FT /note="Coil 1A"
FT /evidence="ECO:0000250"
FT REGION 142..151
FT /note="Linker 1"
FT /evidence="ECO:0000250"
FT REGION 152..252
FT /note="Coil 1B"
FT /evidence="ECO:0000250"
FT REGION 253..269
FT /note="Linker 12"
FT /evidence="ECO:0000250"
FT REGION 270..413
FT /note="Coil 2"
FT /evidence="ECO:0000250"
FT REGION 414..481
FT /note="Tail"
FT /evidence="ECO:0000250"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P78386"
SQ SEQUENCE 481 AA; 52863 MW; DEF13B624C76C80A CRC64;
MTCGSGFCGR AFSCASACGP RPGRCCISAA PYRGISCYRG LSGGFGSQSV CGAFRSGSCG
RSFGYRSGGI CGPSPPCITT VSVNESLLTP LNLEIDPNAQ CVKHEEKEQI KCLNSKFAAF
IDKVRFLEQQ NKLLETKWQF YQNRKCCESN MEPLFEGYIE ALRREAECVE ADSGRLAAEL
NHAQESMEGY KKRYEEEVSL RATAENEFVA LKKDVDCAYL RKSDLEANAE ALTQETDFLR
RMYDEETRIL HSHISDTSIV VKMDNSRDLN MDCVVAEIKA QYDDIASRSR AEAESWYRTK
CEEIKATVIR HGETLRRTRE EINELNRMIQ RLTAEIENAK CQNTKLEAAV TQSEQQGEAA
LADARCKLAE LEGALQKAKQ DMACLLKEYQ EVMNSKLGLD VEITTYRRLL EGEEQRLCEG
VGAVNVCVSS SRGGVVCGDL CVSGSRPVIG SACSAPCSGN LAVNTGLCAP CGSAVSCGRK
C