K1C10_RAT
ID K1C10_RAT Reviewed; 526 AA.
AC Q6IFW6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Keratin, type I cytoskeletal 10;
DE AltName: Full=Cytokeratin-10;
DE Short=CK-10;
DE AltName: Full=Keratin-10;
DE Short=K10;
DE AltName: Full=Type I keratin Ka10;
GN Name=Krt10 {ECO:0000250|UniProtKB:P13645};
GN Synonyms=Ka10 {ECO:0000312|EMBL:DAA04466.1};
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:DAA04466.1}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000312|EMBL:DAA04466.1};
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: Plays a role in the establishment of the epidermal barrier on
CC plantar skin (By similarity). Involved in the maintenance of cell layer
CC development and keratin filament bundles in suprabasal cells of the
CC epithelium (By similarity). {ECO:0000250|UniProtKB:P02535}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Heterodimer with KRT1 (By similarity). Two heterodimers of KRT1 and
CC KRT10 form a heterotetramer (By similarity). The KRT10 subunit in the
CC heterotetramer is probably disulfide-linked (By similarity).
CC {ECO:0000250|UniProtKB:P02535, ECO:0000250|UniProtKB:P13645}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000250|UniProtKB:P13645}. Cell surface
CC {ECO:0000250|UniProtKB:P13645}. Cytoplasm
CC {ECO:0000250|UniProtKB:P02535}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR03074182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK004032; DAA04466.1; -; mRNA.
DR RefSeq; NP_001008804.1; NM_001008804.1.
DR AlphaFoldDB; Q6IFW6; -.
DR SMR; Q6IFW6; -.
DR BioGRID; 268782; 2.
DR STRING; 10116.ENSRNOP00000029821; -.
DR iPTMnet; Q6IFW6; -.
DR PhosphoSitePlus; Q6IFW6; -.
DR jPOST; Q6IFW6; -.
DR PaxDb; Q6IFW6; -.
DR PRIDE; Q6IFW6; -.
DR Ensembl; ENSRNOT00000036023; ENSRNOP00000029821; ENSRNOG00000030170.
DR GeneID; 450225; -.
DR KEGG; rno:450225; -.
DR UCSC; RGD:1359092; rat.
DR CTD; 3858; -.
DR RGD; 1359092; Krt10.
DR eggNOG; ENOG502QV0B; Eukaryota.
DR GeneTree; ENSGT00940000160849; -.
DR InParanoid; Q6IFW6; -.
DR OMA; QGQPRDY; -.
DR OrthoDB; 798081at2759; -.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q6IFW6; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000030170; Expressed in stomach and 20 other tissues.
DR ExpressionAtlas; Q6IFW6; baseline and differential.
DR Genevisible; Q6IFW6; RN.
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:0045095; C:keratin filament; ISO:RGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0030280; F:structural constituent of skin epidermis; ISO:RGD.
DR GO; GO:0071277; P:cellular response to calcium ion; ISO:RGD.
DR GO; GO:0008544; P:epidermis development; ISO:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0045109; P:intermediate filament organization; ISO:RGD.
DR GO; GO:0003334; P:keratinocyte development; ISO:RGD.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IBA:GO_Central.
DR GO; GO:0018149; P:peptide cross-linking; ISO:RGD.
DR GO; GO:0045684; P:positive regulation of epidermis development; ISS:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
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 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Disulfide bond; Intermediate filament; Keratin;
KW Phosphoprotein; Reference proteome; Secreted.
FT CHAIN 1..526
FT /note="Keratin, type I cytoskeletal 10"
FT /id="PRO_0000257991"
FT DOMAIN 145..459
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..144
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..180
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 181..201
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 202..293
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 294..316
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 317..455
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 456..526
FT /note="Tail"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT DISULFID 400
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P13645"
SQ SEQUENCE 526 AA; 56505 MW; 0B0AB97DAADEA9EC CRC64;
MSVRFSSNSR QYSSARSGGG GGGGGGGSSI RVSSTKSSLG GGYSSGGFSG GSFSRGSSSG
GCFGGSSGGY GGFGGGSFGG GYGGGSFGGG YGGGSFGGGY GGGSFGGGYG GGSFGGGSFG
GGSFGGGSFG GGLGGDGGGL LSGNEKVTMQ NLNDRLASYM NKVRDLEESN YELEGKIKEW
YEKHGNSSQR EPRDYSKYYK TIEDLKGQIV NLTTDNANVL LQIDNARLAA DDFRLKYENE
VALRQSVEAD INGLRRVLDE LTLSKADLEM QIESLTEELA YLKKNHEEEM KDLQNVSTGD
VNVEMNAAPG VDLTQLLNNM RNQYEQLAEK NRKDAEAWFN EKSKELTTEI DSNIEQMSSH
KSEITELRRT VQGLEIELQS QLALKQSLEA SLAETEGRYC VQLSQIQSQI SALEEQLQQI
RAETECQNAE YQQLLDIKTR LENEIQTYRS LLEGEGGYVG NLQITLNCFP SEFHLAKLTQ
TQGKTRGWKG SNTNKTRVIK TIIEEVTPEG RVLSSMIESE TKKHFY
