K1C14_RAT
ID K1C14_RAT Reviewed; 485 AA.
AC Q6IFV1; O35813;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Keratin, type I cytoskeletal 14;
DE AltName: Full=Cytokeratin-14;
DE Short=CK-14;
DE AltName: Full=Keratin-14;
DE Short=K14;
DE AltName: Full=Type I keratin Ka14;
GN Name=Krt14; Synonyms=Ka14 {ECO:0000312|EMBL:DAA04481.1}, Krt1-14;
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:BAA22371.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 67-317, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar {ECO:0000269|PubMed:8950218}; TISSUE=Esophagus;
RX PubMed=8950218; DOI=10.1016/s0304-3835(96)04403-5;
RA Wang D.-Y., Xiang Y.-Y., Tanaka M., Shen Q., Sugimura H.;
RT "Identification of cytokeratin subspecies altered in rat experimental
RT esophageal tumors by subtractive cloning.";
RL Cancer Lett. 108:119-127(1996).
RN [3] {ECO:0000305, ECO:0000312|EMBL:DAA04481.1}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000312|EMBL:DAA04481.1};
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: The nonhelical tail domain is involved in promoting KRT5-
CC KRT14 filaments to self-organize into large bundles and enhances the
CC mechanical properties involved in resilience of keratin intermediate
CC filaments in vitro. {ECO:0000250|UniProtKB:P02533}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins (By
CC similarity). Forms a disulfide-linked heterodimer (via 2B domains) with
CC KRT5 (via 2B domains) (By similarity). Forms a heterodimer with KRT1;
CC the interaction is more abundant in the absence of KRT5 (By
CC similarity). Interacts with TRADD and with keratin filaments (By
CC similarity). Associates with other type I keratins (By similarity).
CC Interacts with EPPK1 (By similarity). Interacts with KLHL24 (By
CC similarity). {ECO:0000250|UniProtKB:P02533,
CC ECO:0000250|UniProtKB:Q61781}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P02533}. Nucleus
CC {ECO:0000250|UniProtKB:P02533}. Note=Expressed in both as a filamentous
CC pattern. {ECO:0000250|UniProtKB:P02533}.
CC -!- TISSUE SPECIFICITY: Expressed in most cells of squamous cell
CC carcinomas, in spinous and suprabasal cells around the branching
CC papillary region of papillomas, and weakly in a few proliferative cells
CC of hyperplastic tissue. {ECO:0000269|PubMed:8950218}.
CC -!- PTM: A disulfide bond is formed between rather than within filaments
CC and promotes the formation of a keratin filament cage around the
CC nucleus. {ECO:0000250|UniProtKB:Q61781}.
CC -!- PTM: Ubiquitinated by the BCR(KLHL24) E3 ubiquitin ligase complex.
CC {ECO:0000250|UniProtKB:P02533}.
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 -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AABR03073469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D63774; BAA22371.1; -; mRNA.
DR EMBL; BK004047; DAA04481.1; -; mRNA.
DR RefSeq; NP_001008751.1; NM_001008751.1.
DR AlphaFoldDB; Q6IFV1; -.
DR SMR; Q6IFV1; -.
DR IntAct; Q6IFV1; 1.
DR STRING; 10116.ENSRNOP00000005285; -.
DR iPTMnet; Q6IFV1; -.
DR PhosphoSitePlus; Q6IFV1; -.
DR jPOST; Q6IFV1; -.
DR PaxDb; Q6IFV1; -.
DR PRIDE; Q6IFV1; -.
DR Ensembl; ENSRNOT00000005285; ENSRNOP00000005285; ENSRNOG00000003899.
DR GeneID; 287701; -.
DR KEGG; rno:287701; -.
DR UCSC; RGD:1307463; rat.
DR CTD; 3861; -.
DR RGD; 1307463; Krt14.
DR eggNOG; ENOG502R8V7; Eukaryota.
DR GeneTree; ENSGT00940000154602; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; Q6IFV1; -.
DR OMA; YWATIND; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; Q6IFV1; -.
DR TreeFam; TF332742; -.
DR Reactome; R-RNO-446107; Type I hemidesmosome assembly.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q6IFV1; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003899; Expressed in esophagus and 12 other tissues.
DR ExpressionAtlas; Q6IFV1; baseline and differential.
DR Genevisible; Q6IFV1; RN.
DR GO; GO:0045178; C:basal part of cell; ISO:RGD.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; ISO:RGD.
DR GO; GO:0045095; C:keratin filament; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990254; F:keratin filament binding; ISO:RGD.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007568; P:aging; ISO:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; IDA:UniProtKB.
DR GO; GO:0042633; P:hair cycle; ISO:RGD.
DR GO; GO:0045110; P:intermediate filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0010212; P:response to ionizing radiation; IEP:RGD.
DR GO; GO:0010043; P:response to zinc ion; IEP:RGD.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 2.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Disulfide bond; Intermediate filament; Keratin;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..485
FT /note="Keratin, type I cytoskeletal 14"
FT /id="PRO_0000063655"
FT DOMAIN 122..433
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..121
FT /note="Head"
FT /evidence="ECO:0000250|UniProtKB:P02533"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..157
FT /note="Coil 1A"
FT /evidence="ECO:0000250|UniProtKB:P02533"
FT REGION 158..175
FT /note="Linker 1"
FT /evidence="ECO:0000250|UniProtKB:P02533"
FT REGION 176..267
FT /note="Coil 1B"
FT /evidence="ECO:0000250|UniProtKB:P02533"
FT REGION 268..290
FT /note="Linker 12"
FT /evidence="ECO:0000250|UniProtKB:P02533"
FT REGION 291..429
FT /note="Coil 2"
FT /evidence="ECO:0000250|UniProtKB:P02533"
FT REGION 430..485
FT /note="Tail"
FT /evidence="ECO:0000250|UniProtKB:P02533"
FT REGION 432..485
FT /note="Interaction with Type I keratins and keratin
FT filaments"
FT /evidence="ECO:0000250"
FT REGION 437..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 371
FT /note="Stutter"
FT /evidence="ECO:0000250|UniProtKB:P02533"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61781"
FT DISULFID 374
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 77
FT /note="I -> L (in Ref. 2; BAA22371)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="I -> F (in Ref. 2; BAA22371)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="G -> R (in Ref. 2; BAA22371)"
FT /evidence="ECO:0000305"
FT CONFLICT 88..107
FT /note="Missing (in Ref. 2; BAA22371)"
FT /evidence="ECO:0000305"
FT CONFLICT 205..207
FT /note="DDF -> NDL (in Ref. 2; BAA22371)"
FT /evidence="ECO:0000305"
FT CONFLICT 211..215
FT /note="FETEQ -> YDNET (in Ref. 2; BAA22371)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..220
FT /note="IN -> QL (in Ref. 2; BAA22371)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="G -> N (in Ref. 2; BAA22371)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="R -> C (in Ref. 2; BAA22371)"
FT /evidence="ECO:0000305"
FT CONFLICT 237..238
FT /note="LA -> MS (in Ref. 2; BAA22371)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="K -> T (in Ref. 2; BAA22371)"
FT /evidence="ECO:0000305"
FT CONFLICT 265..271
FT /note="ASMRGQV -> LALRVRL (in Ref. 2; BAA22371)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="K -> Q (in Ref. 2; BAA22371)"
FT /evidence="ECO:0000305"
FT CONFLICT 309..317
FT /note="AEDWFFTKT -> VEAWLEATS (in Ref. 2; BAA22371)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 52684 MW; C12CC69E59CD8DBE CRC64;
MATCSRQFTS SSSMKGSCGI GGGSSRMSSV LAGGSCRAPS TYGGMSRFSS AGAYAVGSGY
GGGFSSSSFG GGFGGGIGGG IGGGLGGGIG GGFGGGIGGG FGGGIGSGFG GGLGDGLLVG
SEKVTMQNLN DRLATYLDKV RALEEANSDL EVKIRDWYQR QRPTEIKDYS PYFKTIEDLK
SKILAATVDN ANVLLQIDNA RLAADDFRTK FETEQSLRIN VESDINGLRR VLDELTLARA
DLEMQIESLK EELAYLKKNH EEEMASMRGQ VGGDVNVEMD AAPGVDLSRI LNEMRDQYEK
MAEKNRKDAE DWFFTKTEEL NREVATNSEL VQSGKSEISE LRRTMQNLEI ELQSQLSMKA
SLENNLEETK GRYCMQLAQI QEMIGSVEEQ LAQLRCEMEQ QNQEYKILLD VKTRLEQEIA
TYRRLLEGED AHLSSAQFSS SSQFSSGSQS SRDVTSTNRQ IRTKVMDVHD GKVVSTHEQV
LRTKN
