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Q63279 (K1C19_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Keratin, type I cytoskeletal 19
Alternative name(s):
Cytokeratin-19
Short name=CK-19
Keratin-19
Short name=K19
Type I keratin Ka19
Gene names
Name:Krt19
Synonyms:Ka19, Krt1-19
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the organization of myofibers. Together with KRT8, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle By similarity.

Subunit structure

Heterotetramer of two type I and two type II keratins. Interacts with PNN By similarity. Interacts with the actin-binding domain of DMD. Ref.1

Tissue specificity

Expressed in brain, heart, skin and in costameres of myoplasm at the sarcolemmal membrane in skeletal and cardiac muscle fibers. Undifferentiated gonads and somatic cells of ovarian cords throughout the fetal ovary development. Ref.1 Ref.5

Developmental stage

Found in somatic cells of ovarian cords throughout the fetal ovary development. Ref.5

Domain

This keratin differs from all other IF proteins in lacking the C-terminal tail domain.

Miscellaneous

There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).

Sequence similarities

Belongs to the intermediate filament family.

Sequence caution

The sequence AAH88424.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DmdP115303EBI-876985,EBI-706166

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 403403Keratin, type I cytoskeletal 19
PRO_0000063674

Regions

Region1 – 8282Head
Region83 – 390308Rod
Region83 – 11836Coil 1A
Region119 – 13618Linker 1
Region137 – 22892Coil 1B
Region229 – 25123Linker 12
Region247 – 393147Necessary for interaction with PNN By similarity
Region252 – 390139Coil 2
Region391 – 40313Rod-like helical tail

Sites

Site2701Stutter
Site3301Stutter

Amino acid modifications

Modified residue91Phosphoserine Ref.8
Modified residue131Phosphoserine Ref.8
Modified residue351Phosphoserine By similarity
Modified residue551Phosphoserine Ref.8
Modified residue571Phosphoserine Ref.8
Modified residue3941Phosphotyrosine By similarity
Modified residue3961Phosphoserine Ref.8

Experimental info

Sequence conflict1431K → N in CAA57205. Ref.5
Sequence conflict1681F → L in CAA57205. Ref.5
Sequence conflict1771A → G in CAA57205. Ref.5
Sequence conflict2481L → H in CAA57205. Ref.5
Sequence conflict265 – 2662KN → MD in CAA57205. Ref.5
Sequence conflict274 – 2807YLTQIDE → LLKIDET in CAA57205. Ref.5
Sequence conflict3031R → E in CAA57205. Ref.5
Sequence conflict364 – 3652QE → HQ in CAA57205. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q63279 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 8D8E4ED8109EE158

FASTA40344,636
        10         20         30         40         50         60 
MTSYSYRQSS AMSSYGGMGG GPVRFGSGGV FRAPSIHGGS GGRGVSVSST RIVSSSSGGY 

        70         80         90        100        110        120 
VGGRGGSFSG ALTVTDGLLG GNEKITMQNL NDRLASYLDK VRALEQANGE LEVKIRDWYQ 

       130        140        150        160        170        180 
KQGPGPFRDY SQYFKTIEDL RDKILGATIE NSKIVLQIDN ARLAADDFRT KFETEQALRM 

       190        200        210        220        230        240 
SVEADINGLR RVLDELTLAR TDLEMQIENL KEELAYLKKN HEEEISALRS QVGGQVSVEV 

       250        260        270        280        290        300 
DSTPGIDLAK ILSEMRSQYE AMAEKNRKDA EAWYLTQIDE LNTQVAVHTT QIQINKTEVT 

       310        320        330        340        350        360 
ELRRKVQDLE IELQSQLSMK AALEGTVAEI EARYGAQLSH IQGVISSIEV QLSNVRADTE 

       370        380        390        400 
RQNQEYQQLM DIKSRLEQEI ATYRSLLEGQ EAHYNSLSIA KAL

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of cytokeratins 8 and 19 in adult rat striated muscle. Interaction with the dystrophin glycoprotein complex."
Ursitti J.A., Lee P.C., Resneck W.G., McNally M.M., Bowman A.L., O'Neill A., Stone M.R., Bloch R.J.
J. Biol. Chem. 279:41830-41838(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DMD, TISSUE SPECIFICITY.
Tissue: Heart muscle.
[2]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Placenta.
[4]"Sex-dependent expression of keratin 19 in differentiating fetal rat gonads. Repressive effect of anti-Mullerian hormone on K19 gene transcription."
Appert A., Perlman S., Cate R., Laverriere J.N., Vigier B., Magre S.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-123.
Strain: Wistar.
[5]"Switch in the expression of the K19/K18 keratin genes as a very early evidence of testicular differentiation in the rat."
Fridmacher V., le Bert M., Guillou F., Magre S.
Mech. Dev. 52:199-207(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 114-368, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: Wistar.
[6]Lubec G., Diao W., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 94-100 AND 163-169, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
[7]"Comprehensive analysis of keratin gene clusters in humans and rodents."
Hesse M., Zimek A., Weber K., Magin T.M.
Eur. J. Cell Biol. 83:19-26(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE MODEL.
[8]"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-13; SER-55; SER-57 AND SER-396, MASS SPECTROMETRY.
Tissue: Renal collecting duct.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY464140 mRNA. Translation: AAR36876.1.
AABR03073341 Genomic DNA. No translation available.
BC088424 mRNA. Translation: AAH88424.1. Different initiation.
BC126075 mRNA. Translation: AAI26076.1.
AH006934 Genomic DNA. Translation: AAC64402.1.
X81449 mRNA. Translation: CAA57205.1.
BK004046 mRNA. Translation: DAA04480.1.
IPIIPI00207014.
RefSeqNP_955792.1. NM_199498.1.
UniGeneRn.9359.

3D structure databases

ProteinModelPortalQ63279.
SMRQ63279. Positions 80-117.
ModBaseSearch...

Protein-protein interaction databases

IntActQ63279. 1 interaction.
STRING10116.ENSRNOP00000019133.

PTM databases

PhosphoSiteQ63279.

Proteomic databases

PaxDbQ63279.
PRIDEQ63279.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000019133; ENSRNOP00000019133; ENSRNOG00000014233.
GeneID360626.
KEGGrno:360626.
UCSCRGD:619936. rat.

Organism-specific databases

CTD3880.
RGD619936. Krt19.

Phylogenomic databases

eggNOGNOG148784.
GeneTreeENSGT00610000085921.
HOGENOMHOG000230975.
HOVERGENHBG013015.
InParanoidQ63279.
KOK07604.
OMATEQLQIS.
OrthoDBEOG4RR6HT.

Gene expression databases

GenevestigatorQ63279.
GermOnlineENSRNOG00000014233. Rattus norvegicus.

Family and domain databases

InterProIPR016044. F.
IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
[Graphical view]
PRINTSPR01248. TYPE1KERATIN.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio673509.

Entry information

Entry nameK1C19_RAT
AccessionPrimary (citable) accession number: Q63279
Secondary accession number(s): A0JN08 expand/collapse secondary AC list , Q5M7V2, Q6S6J4, Q9Z253
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: August 30, 2005
Last modified: April 3, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents