ID D3ZSY5_RAT Unreviewed; 557 AA.
AC D3ZSY5; Q6IG07;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 2.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Keratin 84 {ECO:0000313|Ensembl:ENSRNOP00000011733.2};
DE SubName: Full=Type II keratin Kb24 {ECO:0000313|EMBL:DAA02223.1};
GN Name=Krt84 {ECO:0000313|Ensembl:ENSRNOP00000011733.2,
GN ECO:0000313|RGD:1359402};
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|Ensembl:ENSRNOP00000011733.2, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|EMBL:DAA02223.1}
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:ENSRNOP00000011733.2, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000011733.2,
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:ENSRNOP00000011733.2}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000011733.2};
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; BK003978; DAA02223.1; -; mRNA.
DR RefSeq; NP_001008812.1; NM_001008812.1.
DR PaxDb; 10116-ENSRNOP00000011733; -.
DR Ensembl; ENSRNOT00000011732.4; ENSRNOP00000011733.2; ENSRNOG00000008819.6.
DR GeneID; 315320; -.
DR KEGG; rno:315320; -.
DR AGR; RGD:1359402; -.
DR CTD; 3890; -.
DR RGD; 1359402; Krt84.
DR eggNOG; ENOG502QWIE; Eukaryota.
DR GeneTree; ENSGT00940000162040; -.
DR OMA; EQKCARS; -.
DR OrthoDB; 4640531at2759; -.
DR TreeFam; TF317854; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000008819; Expressed in thymus and 1 other cell type or tissue.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:RGD.
DR GO; GO:0045095; C:keratin filament; ISO:RGD.
DR GO; GO:0030280; F:structural constituent of skin epidermis; ISO:RGD.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; ISO:RGD.
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:SF17; KERATIN, TYPE II CUTICULAR HB4; 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:DAA02223.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT DOMAIN 177..488
FT /note="IF rod"
FT /evidence="ECO:0000259|PROSITE:PS51842"
FT COILED 174..201
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 286..313
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 386..466
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 557 AA; 61201 MW; B1B45168EC8DA1C0 CRC64;
MSCRSYRVSS GRRVGNFSSC SAMTPQHLNR FRASSVSCRS GPGFRGLGGF GSRSVINFGS
SSPRIAVGCS RPIRYGVGFG AGNGIAFGSG DGSGICLGYR AGSGVGLGFG AGSCLGYGFG
GPGFGGPGFG GPGFGYRIGG IGGPSAPAIT AVTVNQSLLT PLNLEIDPNA QRVKKDEKEQ
IKTLNNKFAS FIDKVRFLEQ QNKLLETKWS FLQDQKCARS NLEPLFDNYI TSLRRQLDVL
VSDQARLQAE RNHMQDILEG FKKKYEEEVV FRANAENEFV ALKKDVDAAF LNKSDLEANV
DALAQEIEFL KALYLEEIQL LQSHISETSV IVKMDNSRDL NLDGIIAEVK AQYEEVARRS
RADVESWYQT KYEEMRVTAG QHCDNLRNTR DEINELTRLI QRLKTEIEHT KAQCAKLEAA
VAEAEQQGEA ALNDAKCKLT DLEGALQQAK QDMARQLREY QELMNAKLAL DIEIVTYRKL
LEGEEIRICE GVGPVNICKY LPLSQTVSSL PIKFPFGTCG DQEAPKIADL AKTYSHGRRA
ISVPRLCVLS RGSQNKE
//
