K1C15_RAT
ID K1C15_RAT Reviewed; 447 AA.
AC Q6IFV3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Keratin, type I cytoskeletal 15;
DE AltName: Full=Cytokeratin-15;
DE Short=CK-15;
DE AltName: Full=Keratin-15;
DE Short=K15;
DE AltName: Full=Type I keratin Ka15;
GN Name=Krt15 {ECO:0000250|UniProtKB:P19012};
GN Synonyms=Ka15 {ECO:0000312|EMBL:DAA04479.1};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAI01869.1}
RP PROTEIN SEQUENCE OF 96-104 AND 175-181, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4] {ECO:0000305, ECO:0000312|EMBL:DAA04479.1}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000312|EMBL:DAA04479.1};
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-290 AND THR-312, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins (By
CC similarity). Forms a heterodimer with KRT14 (By similarity). Interacts
CC with NOD2 (By similarity). {ECO:0000250|UniProtKB:P19012,
CC ECO:0000250|UniProtKB:Q61414}.
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; AABR03073341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101868; AAI01869.1; -; mRNA.
DR EMBL; BK004045; DAA04479.1; -; mRNA.
DR RefSeq; NP_001004022.1; NM_001004022.2.
DR AlphaFoldDB; Q6IFV3; -.
DR SMR; Q6IFV3; -.
DR STRING; 10116.ENSRNOP00000019037; -.
DR iPTMnet; Q6IFV3; -.
DR PhosphoSitePlus; Q6IFV3; -.
DR jPOST; Q6IFV3; -.
DR PaxDb; Q6IFV3; -.
DR PRIDE; Q6IFV3; -.
DR GeneID; 287700; -.
DR KEGG; rno:287700; -.
DR UCSC; RGD:1303044; rat.
DR CTD; 3866; -.
DR RGD; 1303044; Krt15.
DR VEuPathDB; HostDB:ENSRNOG00000003899; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; Q6IFV3; -.
DR OMA; IECRYAT; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; Q6IFV3; -.
DR TreeFam; TF332742; -.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q6IFV3; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000014099; Expressed in esophagus and 12 other tissues.
DR Genevisible; Q6IFV3; RN.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; TAS:RGD.
DR GO; GO:0045095; C:keratin filament; TAS:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0045103; P:intermediate filament-based process; TAS:RGD.
DR InterPro; IPR018039; IF_conserved.
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; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Intermediate filament;
KW Isopeptide bond; Keratin; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..447
FT /note="Keratin, type I cytoskeletal 15"
FT /id="PRO_0000063659"
FT DOMAIN 94..406
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..93
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 94..129
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 130..148
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 149..240
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 241..260
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 261..402
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 403..447
FT /note="Tail"
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61414"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61414"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 290
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT CROSSLNK 289
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
SQ SEQUENCE 447 AA; 48870 MW; CD16F2D55F193671 CRC64;
MATTFLQTSS TFGSGSTRGG SLRVGGGSFG GGSLYGGGGS RSISASSARF VSSGAGVGFG
GGMSCGFGGG FGGGFGGGFG DFGGGDGGLL SGNEKVTMQN LNDRLASYLD KVRALEEANT
ELEVKIRDWY QKQSPASPDR DYSHYFKTME EIRDKILAAT IDNSRVILEI DNARLAADDF
RLKYENELAL RQGVEADING LRRVLDELTL ARTDLEMQIE QLNEELAYLK KNHEEEMKEF
SSQLAGQVNV EMDAAPGVDL TRMLAEMREQ YEAIAEKNRR DVEAWFFSKT EELNKEVASN
TEMIQTSKTE ITDLRRTLQG LEIELQSQLS MKAGLENSLA EVECRYATQL QQIQGLITGL
ETQLSELRCE MEAQNQEYNM LLDIKTRLEQ EISTYRNLLE GQDAKMAAIG VREASLRGGS
SGGGSNFHIS VEESVDGKVV SSRKRES
