ID Q6IG10_RAT Unreviewed; 517 AA.
AC Q6IG10;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 137.
DE SubName: Full=Keratin 86 {ECO:0000313|Ensembl:ENSRNOP00000068808.1};
DE SubName: Full=Type II keratin Kb26 {ECO:0000313|EMBL:DAA02220.1};
GN Name=Krt86 {ECO:0000313|Ensembl:ENSRNOP00000068808.1,
GN ECO:0000313|RGD:1303215}; Synonyms=Kb26 {ECO:0000313|RGD:1303215};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|EMBL:DAA02220.1};
RN [1] {ECO:0000313|EMBL:DAA02220.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15085952; DOI=10.1078/0171-9335-00354;
RA Hesse M., Zimek A., Weber K., Magin T.M.;
RT "Comprehensive analysis of keratin gene clusters in humans and rodents.";
RL Eur. J. Cell Biol. 83:19-26(2004).
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000068808.1, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068808.1,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000068808.1}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068808.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000256|RuleBase:RU000685}.
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DR EMBL; BK003975; DAA02220.1; -; mRNA.
DR RefSeq; NP_001008810.1; NM_001008810.1.
DR STRING; 10116.ENSRNOP00000068808; -.
DR Ensembl; ENSRNOT00000081386.2; ENSRNOP00000068808.1; ENSRNOG00000008367.9.
DR GeneID; 407760; -.
DR KEGG; rno:407760; -.
DR UCSC; RGD:1303215; rat.
DR AGR; RGD:1303215; -.
DR CTD; 3892; -.
DR RGD; 1303215; Krt86.
DR GeneTree; ENSGT00940000154026; -.
DR OrthoDB; 4640531at2759; -.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR Proteomes; UP000002494; Chromosome 7.
DR Genevisible; Q6IG10; RN.
DR GO; GO:0045095; C:keratin filament; ISO:RGD.
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 Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.500; Single helix bin; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR PANTHER; PTHR45616; GATA-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45616:SF52; KERATIN, TYPE II CUTICULAR HB6; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Intermediate filament {ECO:0000256|ARBA:ARBA00022754,
KW ECO:0000256|RuleBase:RU000685};
KW Keratin {ECO:0000256|ARBA:ARBA00022744, ECO:0000313|EMBL:DAA02220.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT DOMAIN 106..417
FT /note="IF rod"
FT /evidence="ECO:0000259|PROSITE:PS51842"
FT COILED 159..242
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 315..395
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 517 AA; 56654 MW; 15652D5E554AD44D CRC64;
MTCGSYCGGR AFSCASACGP RPGRCCITAA PYRGISCYRG LSGGFGSHSV CGAFRSGSCG
RSFGYRSGGI CGPSPPCITT VSVNESLLTP LNLEIDPNAQ CVKHEEKEQI KCLNSRFAAF
IDKVRFLEQQ NKLLETKWQF FQNRKCCESN VEPLFEGYIE TLRREAECVE ADSGRLAAEL
NHAQEAMEGY KKRYEEEVSL RATAENEFVA LKKDVDCAYL RKSDLEANTE ALTQEIDFLR
RLYEEETRIL HAHISDTSVI VKMDNSRDLN MDCVIAEIKA QYDDIASRSR AEAESWYRTK
CEEIKATVIR HGETLRRTRE EINELNRIIQ RLTAEIENAK CQNTKLEAAV TQSEQQGEAA
LTDARCKLAE LEAALQKAKQ DMACLLKEYQ EVMNSKLGLD IEIATYRRLL EGEEQRLCEG
VGSVNVCVSS SRGGVVCGDL CVSGTAPAVN TRVCSAPCSG NVVVGTPNAC GPCAGAGACS
GGCKKCEATK LQATAMGHPA RKDSTAGQWP RPLLLIL
//
