K1C27_RAT
ID K1C27_RAT Reviewed; 449 AA.
AC Q6IFW8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Keratin, type I cytoskeletal 27;
DE AltName: Full=Cytokeratin-27;
DE Short=CK-27;
DE AltName: Full=Keratin-27;
DE Short=K27;
DE AltName: Full=Type I inner root sheath-specific keratin-K25irs3;
DE AltName: Full=Type I keratin KA40;
GN Name=Krt27 {ECO:0000250|UniProtKB:Q7Z3Y8};
GN Synonyms=Ka40 {ECO:0000312|EMBL:DAA04464.1};
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;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
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 [2] {ECO:0000305, ECO:0000312|EMBL:DAA04464.1}
RP IDENTIFICATION.
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).
CC -!- FUNCTION: Essential for the proper assembly of type I and type II
CC keratin protein complexes and formation of keratin intermediate
CC filaments in the inner root sheath (irs).
CC {ECO:0000250|UniProtKB:Q9Z320}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Interacts with KRT6A to form filaments (By similarity).
CC {ECO:0000250|UniProtKB:Q9Z320, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z320}.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AABR03073900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK004030; DAA04464.1; -; mRNA.
DR RefSeq; NP_001008824.1; NM_001008824.1.
DR AlphaFoldDB; Q6IFW8; -.
DR SMR; Q6IFW8; -.
DR STRING; 10116.ENSRNOP00000015740; -.
DR iPTMnet; Q6IFW8; -.
DR PhosphoSitePlus; Q6IFW8; -.
DR jPOST; Q6IFW8; -.
DR PaxDb; Q6IFW8; -.
DR PRIDE; Q6IFW8; -.
DR Ensembl; ENSRNOT00000015740; ENSRNOP00000015740; ENSRNOG00000011628.
DR GeneID; 450229; -.
DR KEGG; rno:450229; -.
DR UCSC; RGD:1359115; rat.
DR CTD; 342574; -.
DR RGD; 1359115; Krt27.
DR eggNOG; ENOG502SIHJ; Eukaryota.
DR GeneTree; ENSGT00940000161982; -.
DR HOGENOM; CLU_012560_8_3_1; -.
DR InParanoid; Q6IFW8; -.
DR OMA; SRVHTME; -.
DR OrthoDB; 805081at2759; -.
DR PhylomeDB; Q6IFW8; -.
DR TreeFam; TF332742; -.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q6IFW8; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000011628; Expressed in ovary and 1 other tissue.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Intermediate filament; Keratin; Reference proteome.
FT CHAIN 1..449
FT /note="Keratin, type I cytoskeletal 27"
FT /id="PRO_0000312703"
FT DOMAIN 74..389
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..73
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 74..109
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 110..131
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 132..223
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 224..246
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 247..385
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 386..449
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 425..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 449 AA; 49109 MW; FD863F380DDBAD1B CRC64;
MSVRFSSASR RLGSVRLSSP GAALGAGNTC GVPGIGSGFS CAFGGSSLAG GLGMGGASCG
AFTVNEHGLL SGNEKVTMQN LNDRLASYLE NVQALEEANA DLEQKIKDWY EKFGPGSCRG
LDHDYSRYFP IIDDLRTQII SATAQNANIV LQNDNARLTA DDFRMKYENE LALHQSVDAD
INGLRRVLDE LTLCRTDLEV QLETLSEELA YLKKNHEEEM QALQCAAGGN VNVEMNAAPG
VDLTVLLNNM RAEYEALAEQ NRRDAEAWFQ EKSASLQQQI SDDAGATTSA RNELTEMKRT
LQTLEIELQS LLAMKHSLEC SLTETEGNYC TQLAQIQAQI SALEEQLHQV RTETEGQKLE
YEQLLNVKAH LEKEIETYCL LIGGDEGSCV KSKGQGGPGN QTKDSPKTAI VKTVVEELDP
RGKVLSSRVH TLEEKSTKVN NKNEQRIPS
