KRT85_MOUSE
ID KRT85_MOUSE Reviewed; 507 AA.
AC Q9Z2T6; Q8CE83; Q9D7M4;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Keratin, type II cuticular Hb5;
DE AltName: Full=Keratin-85;
DE Short=K85;
DE AltName: Full=Type II hair keratin Hb5;
DE AltName: Full=Type-II keratin Kb25;
GN Name=Krt85; Synonyms=Krt2-18, Krthb5;
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 [MRNA].
RC STRAIN=ICR; TISSUE=Hair follicle, and Skin;
RA Inoue T., Kizawa K.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin, and Tongue;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AF021836; AAD01692.1; -; mRNA.
DR EMBL; AK028825; BAC26139.1; -; mRNA.
DR EMBL; AK009099; BAB26069.1; -; mRNA.
DR RefSeq; NP_058575.2; NM_016879.2.
DR AlphaFoldDB; Q9Z2T6; -.
DR SMR; Q9Z2T6; -.
DR BioGRID; 207339; 1.
DR iPTMnet; Q9Z2T6; -.
DR PhosphoSitePlus; Q9Z2T6; -.
DR SwissPalm; Q9Z2T6; -.
DR jPOST; Q9Z2T6; -.
DR MaxQB; Q9Z2T6; -.
DR PeptideAtlas; Q9Z2T6; -.
DR PRIDE; Q9Z2T6; -.
DR ProteomicsDB; 264872; -.
DR Antibodypedia; 56660; 45 antibodies from 17 providers.
DR DNASU; 53622; -.
DR Ensembl; ENSMUST00000230067; ENSMUSP00000155398; ENSMUSG00000116336.
DR GeneID; 53622; -.
DR KEGG; mmu:53622; -.
DR UCSC; uc007xtf.3; mouse.
DR CTD; 3891; -.
DR MGI; MGI:1859268; Krt85.
DR GeneTree; ENSGT00940000162337; -.
DR InParanoid; Q9Z2T6; -.
DR OMA; CRSYRIN; -.
DR PhylomeDB; Q9Z2T6; -.
DR BioGRID-ORCS; 53622; 2 hits in 15 CRISPR screens.
DR PRO; PR:Q9Z2T6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9Z2T6; protein.
DR Bgee; ENSMUSG00000116336; Expressed in lip and 6 other tissues.
DR ExpressionAtlas; Q9Z2T6; baseline and differential.
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 1: Evidence at protein level;
KW Coiled coil; Intermediate filament; Isopeptide bond; Keratin;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..507
FT /note="Keratin, type II cuticular Hb5"
FT /id="PRO_0000063703"
FT DOMAIN 123..434
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..123
FT /note="Head"
FT REGION 124..158
FT /note="Coil 1A"
FT REGION 159..168
FT /note="Linker 1"
FT REGION 169..269
FT /note="Coil 1B"
FT REGION 270..286
FT /note="Linker 12"
FT REGION 287..430
FT /note="Coil 2"
FT REGION 431..507
FT /note="Tail"
FT CROSSLNK 229
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P78386"
FT CONFLICT 37
FT /note="A -> R (in Ref. 1; AAD01692)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="E -> G (in Ref. 1; AAD01692)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="L -> F (in Ref. 2; BAB26069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 55759 MW; 602A27B0D36C3334 CRC64;
MSCRSYRISP GCGVTRNFSS CSAVAPKTGN RCCISAAPFR GVSCYRGLTG FSSRSLCNPS
PCGPRMAVGG FRSGSCGRSF GYRSGGVCGP SPPCITTVSV NESLLTPLNL EIDPNAQCVK
YEEKEQIKCL NSKFAAFIDK VRFLEQQNKL LETKWQFYQN RKCCESNLEP LFGGYIEALR
REAECVEADS GRLAAELNHV QEAMEGYKKK YEEEVALRAT AENEFVVLKK DVDCAYLRKS
DLEANVEALV EESSFLKRLY EEEVCVLQAH ISDTSVIVKM DNSRDLNMDC VVAEIKAQYD
DVASRSRAEA ESWYRTKCEE MKATVIRHGE TLRRTKEEIN ELNRMIQRLT AEIENAKCQR
AKLEAAVAEA EQQGEAALAD ARCKLAELEG ALQKAKQDMA CLLKEYQEVM NSKLALDIEI
ATYRRLLEGE EQRLCEGVGS VNVCVSSSRG GVTCGGLTYG TTPGRQIVSG PSVTGGSITV
MAPDSCSPCQ PRASSFTCGS SRSVRFA
