K1C25_RAT
ID K1C25_RAT Reviewed; 446 AA.
AC Q6IFX0;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Keratin, type I cytoskeletal 25;
DE AltName: Full=Cytokeratin-25;
DE Short=CK-25;
DE AltName: Full=Keratin-25;
DE Short=K25;
DE AltName: Full=Keratin-25A;
DE Short=K25A;
DE AltName: Full=Type I inner root sheath-specific keratin-K25irs1;
DE AltName: Full=Type I keratin KA38;
GN Name=Krt25 {ECO:0000250|UniProtKB:Q7Z3Z0};
GN Synonyms=Ka38 {ECO:0000312|EMBL:DAA04462.1},
GN Krt25a {ECO:0000312|RGD:1359097};
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:DAA04462.1}
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) (By similarity). Plays a role
CC in the cytoskeleton organization (By similarity).
CC {ECO:0000250|UniProtKB:Q7Z3Z0, ECO:0000250|UniProtKB:Q8VCW2}.
CC -!- SUBUNIT: Heterodimer of a type I and a type II keratin. Heterodimer
CC with type II keratin KRT5 leading to the formation of keratin
CC intermediate filament (KIF) network. Interacts with KRT6A to form
CC filaments. {ECO:0000250|UniProtKB:Q7Z3Z0, ECO:0000250|UniProtKB:Q8VCW2,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8VCW2}.
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; AABR03074128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK004028; DAA04462.1; -; mRNA.
DR RefSeq; NP_001008822.1; NM_001008822.1.
DR RefSeq; XP_017452807.1; XM_017597318.1.
DR RefSeq; XP_017452808.1; XM_017597319.1.
DR AlphaFoldDB; Q6IFX0; -.
DR SMR; Q6IFX0; -.
DR STRING; 10116.ENSRNOP00000015150; -.
DR iPTMnet; Q6IFX0; -.
DR PhosphoSitePlus; Q6IFX0; -.
DR jPOST; Q6IFX0; -.
DR PaxDb; Q6IFX0; -.
DR PRIDE; Q6IFX0; -.
DR Ensembl; ENSRNOT00000015150; ENSRNOP00000015150; ENSRNOG00000011196.
DR GeneID; 303519; -.
DR KEGG; rno:303519; -.
DR UCSC; RGD:1359097; rat.
DR CTD; 147183; -.
DR RGD; 1359097; Krt25.
DR eggNOG; ENOG502SKJN; Eukaryota.
DR GeneTree; ENSGT00940000161994; -.
DR HOGENOM; CLU_012560_8_3_1; -.
DR InParanoid; Q6IFX0; -.
DR OMA; KGWYEQF; -.
DR OrthoDB; 805081at2759; -.
DR PhylomeDB; Q6IFX0; -.
DR TreeFam; TF332742; -.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q6IFX0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000011196; Expressed in testis and 2 other tissues.
DR Genevisible; Q6IFX0; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0045095; C:keratin filament; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007568; P:aging; ISO:RGD.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0042633; P:hair cycle; ISO:RGD.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD.
DR GO; GO:0045109; P:intermediate filament organization; ISO:RGD.
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; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..446
FT /note="Keratin, type I cytoskeletal 25"
FT /id="PRO_0000312694"
FT DOMAIN 75..390
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..74
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..110
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 111..132
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 133..224
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 225..247
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 248..386
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 387..446
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 394..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3Z0"
SQ SEQUENCE 446 AA; 48943 MW; 3E78915CFA4C7CBD CRC64;
MSLRLSSGSK RSYARPSTGS LRGASFGAAN ACGVAGIGSG FSCAFGSSST GGNTGVANSC
AGFTVNEGGL LSGNEKVTMQ NLNDRLASYL DNVQALQEAN ADLEQKIKGW YEKFGPGSCR
GLDHDYSRYF PIIDDLKNQI ITSTTSNANA VLQIDNARLT ADDFRLKYEN ELALHQSVEA
DVNGLRRVLD EITLCRTDLE IQYETLSEEL TYLKKNHKEE MQALQCAAGG NVNVEMNAAP
GVDLTVLLNN MRAEYEALAE QNRRDAEAWF QEKSASLQQQ ITEDVGATTS ARNELTEMKR
TLQTLEIELQ SLLATKHSLE CSLTETEGNY CTQLAQIQAQ ISALEEQLHQ VRTETEGQKL
EYEQLLNVKA HLEKEIETYC LLIGGDEGAC KSSSYKSKDY TSGNAGNQSK DSPKAIVVKK
VLEEVDQRSK ILTTRLHSLE EKSQSN
