KRT86_MOUSE
ID KRT86_MOUSE Reviewed; 486 AA.
AC P97861; Q3TTV9;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Keratin, type II cuticular Hb6;
DE AltName: Full=Keratin-86;
DE Short=K86;
DE AltName: Full=Type II hair keratin Hb6;
DE AltName: Full=Type-II keratin Kb26;
GN Name=Krt86; Synonyms=Krt2-10, Krthb6;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-486.
RX PubMed=9084137; DOI=10.1046/j.1432-0436.1997.6130187.x;
RA Rogers M.A., Langbein L., Praetzel S., Krieg T., Winter H., Schweizer J.;
RT "Sequences and differential expression of three novel human type-II hair
RT keratins.";
RL Differentiation 61:187-194(1997).
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC -!- MISCELLANEOUS: There are two types of hair/microfibrillar keratin, I
CC (acidic) and II (neutral to basic).
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AK161149; BAE36215.1; -; mRNA.
DR EMBL; X99143; CAA67580.1; -; mRNA.
DR CCDS; CCDS37218.1; -.
DR RefSeq; NP_034797.1; NM_010667.2.
DR AlphaFoldDB; P97861; -.
DR SMR; P97861; -.
DR BioGRID; 201031; 2.
DR ComplexPortal; CPX-5870; Keratin-36 - Keratin-86 dimer complex.
DR STRING; 10090.ENSMUSP00000085365; -.
DR iPTMnet; P97861; -.
DR PhosphoSitePlus; P97861; -.
DR jPOST; P97861; -.
DR MaxQB; P97861; -.
DR PaxDb; P97861; -.
DR PRIDE; P97861; -.
DR ProteomicsDB; 264873; -.
DR DNASU; 16679; -.
DR Ensembl; ENSMUST00000088049; ENSMUSP00000085365; ENSMUSG00000067614.
DR GeneID; 16679; -.
DR KEGG; mmu:16679; -.
DR UCSC; uc007xti.1; mouse.
DR CTD; 3892; -.
DR MGI; MGI:109362; Krt86.
DR VEuPathDB; HostDB:ENSMUSG00000067614; -.
DR eggNOG; ENOG502RTZU; Eukaryota.
DR GeneTree; ENSGT00940000154026; -.
DR HOGENOM; CLU_012560_5_0_1; -.
DR InParanoid; P97861; -.
DR OMA; VNACAPC; -.
DR OrthoDB; 557821at2759; -.
DR PhylomeDB; P97861; -.
DR TreeFam; TF317854; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 16679; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Krt1; mouse.
DR PRO; PR:P97861; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P97861; protein.
DR Bgee; ENSMUSG00000067614; Expressed in lip and 19 other tissues.
DR ExpressionAtlas; P97861; baseline and differential.
DR Genevisible; P97861; MM.
DR GO; GO:0045095; C:keratin filament; ISO:MGI.
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; IPR009030; Growth_fac_rcpt_cys_sf.
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 SUPFAM; SSF57184; SSF57184; 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..486
FT /note="Keratin, type II cuticular Hb6"
FT /id="PRO_0000063705"
FT DOMAIN 106..417
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..106
FT /note="Head"
FT REGION 107..141
FT /note="Coil 1A"
FT REGION 142..151
FT /note="Linker 1"
FT REGION 152..252
FT /note="Coil 1B"
FT REGION 253..269
FT /note="Linker 12"
FT REGION 270..413
FT /note="Coil 2"
FT REGION 414..486
FT /note="Tail"
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 486 AA; 53251 MW; 8EABB193B38C8F2A CRC64;
MTCGSYCGGR 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
VGSVNVCVSS SRGGVVCGDL CVSGTAPAVN TRVCSAPCSG NVVVGTPNAC APCAGAGACS
GGCKKC
