K1C19_RAT
ID K1C19_RAT Reviewed; 403 AA.
AC Q63279; A0JN08; Q5M7V2; Q6S6J4; Q9Z253;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Keratin, type I cytoskeletal 19;
DE AltName: Full=Cytokeratin-19;
DE Short=CK-19;
DE AltName: Full=Keratin-19;
DE Short=K19;
DE AltName: Full=Type I keratin Ka19;
GN Name=Krt19; Synonyms=Ka19, Krt1-19;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DMD, AND TISSUE SPECIFICITY.
RC TISSUE=Heart muscle;
RX PubMed=15247274; DOI=10.1074/jbc.m400128200;
RA Ursitti J.A., Lee P.C., Resneck W.G., McNally M.M., Bowman A.L.,
RA O'Neill A., Stone M.R., Bloch R.J.;
RT "Cloning and characterization of cytokeratins 8 and 19 in adult rat
RT striated muscle. Interaction with the dystrophin glycoprotein complex.";
RL J. Biol. Chem. 279:41830-41838(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-123.
RC STRAIN=Wistar;
RA Appert A., Perlman S., Cate R., Laverriere J.N., Vigier B., Magre S.;
RT "Sex-dependent expression of keratin 19 in differentiating fetal rat
RT gonads. Repressive effect of anti-Mullerian hormone on K19 gene
RT transcription.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 114-368, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Wistar;
RX PubMed=8541209; DOI=10.1016/0925-4773(95)00401-l;
RA Fridmacher V., le Bert M., Guillou F., Magre S.;
RT "Switch in the expression of the K19/K18 keratin genes as a very early
RT evidence of testicular differentiation in the rat.";
RL Mech. Dev. 52:199-207(1995).
RN [6]
RP PROTEIN SEQUENCE OF 94-100 AND 163-169, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP GENE MODEL.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-35; SER-40; SER-57
RP AND SER-67, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in the organization of myofibers. Together with
CC KRT8, helps to link the contractile apparatus to dystrophin at the
CC costameres of striated muscle (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Interacts with PNN (By similarity). Interacts with the actin-binding
CC domain of DMD. {ECO:0000250, ECO:0000269|PubMed:15247274}.
CC -!- INTERACTION:
CC Q63279; P11530: Dmd; NbExp=3; IntAct=EBI-876985, EBI-706166;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, skin and in costameres
CC of myoplasm at the sarcolemmal membrane in skeletal and cardiac muscle
CC fibers. Undifferentiated gonads and somatic cells of ovarian cords
CC throughout the fetal ovary development. {ECO:0000269|PubMed:15247274,
CC ECO:0000269|PubMed:8541209}.
CC -!- DEVELOPMENTAL STAGE: Found in somatic cells of ovarian cords throughout
CC the fetal ovary development. {ECO:0000269|PubMed:8541209}.
CC -!- DOMAIN: This keratin differs from all other IF proteins in lacking the
CC C-terminal tail domain.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAH88424.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AY464140; AAR36876.1; -; mRNA.
DR EMBL; AABR03073341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC088424; AAH88424.1; ALT_INIT; mRNA.
DR EMBL; BC126075; AAI26076.1; -; mRNA.
DR EMBL; AH006934; AAC64402.1; -; Genomic_DNA.
DR EMBL; X81449; CAA57205.1; -; mRNA.
DR EMBL; BK004046; DAA04480.1; -; mRNA.
DR RefSeq; NP_955792.1; NM_199498.2.
DR AlphaFoldDB; Q63279; -.
DR SMR; Q63279; -.
DR BioGRID; 262079; 1.
DR IntAct; Q63279; 3.
DR STRING; 10116.ENSRNOP00000019133; -.
DR iPTMnet; Q63279; -.
DR PhosphoSitePlus; Q63279; -.
DR jPOST; Q63279; -.
DR PaxDb; Q63279; -.
DR PRIDE; Q63279; -.
DR Ensembl; ENSRNOT00000019133; ENSRNOP00000019133; ENSRNOG00000003899.
DR GeneID; 360626; -.
DR KEGG; rno:360626; -.
DR UCSC; RGD:619936; rat.
DR CTD; 3880; -.
DR RGD; 619936; Krt19.
DR eggNOG; ENOG502QV0B; Eukaryota.
DR GeneTree; ENSGT00940000154602; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; Q63279; -.
DR OMA; QEYLLLM; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; Q63279; -.
DR TreeFam; TF332742; -.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q63279; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000014233; Expressed in colon and 18 other tissues.
DR Genevisible; Q63279; RN.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISO:RGD.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0043034; C:costamere; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:RGD.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR GO; GO:1990357; C:terminal web; ISO:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0008307; F:structural constituent of muscle; ISO:RGD.
DR GO; GO:0060706; P:cell differentiation involved in embryonic placenta development; ISO: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:0007219; P:Notch signaling pathway; ISO:RGD.
DR GO; GO:0043627; P:response to estrogen; ISO:RGD.
DR GO; GO:0045214; P:sarcomere organization; ISO: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; Keratin;
KW Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..403
FT /note="Keratin, type I cytoskeletal 19"
FT /id="PRO_0000063674"
FT DOMAIN 83..394
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..82
FT /note="Head"
FT REGION 83..118
FT /note="Coil 1A"
FT REGION 119..136
FT /note="Linker 1"
FT REGION 137..228
FT /note="Coil 1B"
FT REGION 229..251
FT /note="Linker 12"
FT REGION 247..393
FT /note="Necessary for interaction with PNN"
FT /evidence="ECO:0000250"
FT REGION 252..390
FT /note="Coil 2"
FT REGION 391..403
FT /note="Rod-like helical tail"
FT SITE 270
FT /note="Stutter"
FT SITE 330
FT /note="Stutter"
FT MOD_RES 7
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 24
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 24
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 43
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 51
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 394
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT CONFLICT 143
FT /note="K -> N (in Ref. 5; CAA57205)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="F -> L (in Ref. 5; CAA57205)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="A -> G (in Ref. 5; CAA57205)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="L -> H (in Ref. 5; CAA57205)"
FT /evidence="ECO:0000305"
FT CONFLICT 265..266
FT /note="KN -> MD (in Ref. 5; CAA57205)"
FT /evidence="ECO:0000305"
FT CONFLICT 274..280
FT /note="YLTQIDE -> LLKIDET (in Ref. 5; CAA57205)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="R -> E (in Ref. 5; CAA57205)"
FT /evidence="ECO:0000305"
FT CONFLICT 364..365
FT /note="QE -> HQ (in Ref. 5; CAA57205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 44636 MW; 8D8E4ED8109EE158 CRC64;
MTSYSYRQSS AMSSYGGMGG GPVRFGSGGV FRAPSIHGGS GGRGVSVSST RIVSSSSGGY
VGGRGGSFSG ALTVTDGLLG GNEKITMQNL NDRLASYLDK VRALEQANGE LEVKIRDWYQ
KQGPGPFRDY SQYFKTIEDL RDKILGATIE NSKIVLQIDN ARLAADDFRT KFETEQALRM
SVEADINGLR RVLDELTLAR TDLEMQIENL KEELAYLKKN HEEEISALRS QVGGQVSVEV
DSTPGIDLAK ILSEMRSQYE AMAEKNRKDA EAWYLTQIDE LNTQVAVHTT QIQINKTEVT
ELRRKVQDLE IELQSQLSMK AALEGTVAEI EARYGAQLSH IQGVISSIEV QLSNVRADTE
RQNQEYQQLM DIKSRLEQEI ATYRSLLEGQ EAHYNSLSIA KAL
