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Q6IMF1 (K2C80_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

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

Names and origin

Protein namesRecommended name:
Keratin, type II cytoskeletal 80
Alternative name(s):
Cytokeratin-80
Short name=CK-80
Keratin-80
Short name=K80
Type-II keratin Kb20
Gene names
Name:Krt80
Synonyms:Kb20
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Subunit structure

Heterotetramer of two type I and two type II keratins.

Miscellaneous

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

Sequence similarities

Belongs to the intermediate filament family.

Ontologies

Keywords
   Cellular componentIntermediate filament
Keratin
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentkeratin filament

Inferred from electronic annotation. Source: InterPro

   Molecular_functionstructural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452Keratin, type II cytoskeletal 80
PRO_0000314898

Regions

Region1 – 8282Head
Region82 – 11837Coil 1A
Region83 – 390308Rod
Region119 – 13517Linker 1
Region136 – 22792Coil 1B
Region228 – 25124Linker 12
Region252 – 390139Coil 2
Region391 – 45262Tail

Sites

Site3341Stutter

Amino acid modifications

Modified residue451Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6IMF1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: FEDBE9145CA03721

FASTA45250,550
        10         20         30         40         50         60 
MAYRSCVVGF SSHSGCEVTP AGSSQPGTSG WGSCGLPGPG FSSRSLTSCR PAGVIPKVTV 

        70         80         90        100        110        120 
NPSLLVPLDL KVDPAVQQQK NQEKEEMKVL NDKFASLIGK VQALEQRNQL LETRWGFLQG 

       130        140        150        160        170        180 
QGSATFDLSH HYETFQGRLQ EELRKVSQER GQLEASLLQV LEKVEEFRVR YEDEISKRTD 

       190        200        210        220        230        240 
LEFTFVQLKK DLDAECLRRT ELETKLKGLQ GFVELMRTVY EQELKDLTAQ VKDVSVTVGL 

       250        260        270        280        290        300 
DSRCHIDLSG IVEEVKAQYD AIAARSLEEA EAYSRSQLEE RAARSAEFGN SLQSSRCEIA 

       310        320        330        340        350        360 
DLNVRIQKLR SQIVSVKSHC LKLEENIKVA EEQGELAFQD AKDKMAQLEA ALQKAKQDMA 

       370        380        390        400        410        420 
RQLREYQDLM NTKLALDIEI ATYHKLMEGE ESRMDLPSTT VVSAVQSRCR TTASKSGLSK 

       430        440        450 
TPSRKKKNRG GPVIKITEMS EKYLSQESEA SE 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"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: IDENTIFICATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03055900 Genomic DNA. No translation available.
AABR03056151 Genomic DNA. No translation available.
BK001581 mRNA. Translation: DAA02056.1.
BK001582 mRNA. Translation: DAA02057.1.
RefSeqNP_001008815.1. NM_001008815.1.
UniGeneRn.103689.

3D structure databases

ProteinModelPortalQ6IMF1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000038848.

Proteomic databases

PaxDbQ6IMF1.
PRIDEQ6IMF1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000029697; ENSRNOP00000038848; ENSRNOG00000025994.
GeneID315318.
KEGGrno:315318.
UCSCRGD:1359177. rat.

Organism-specific databases

CTD144501.
RGD1359177. Krt80.

Phylogenomic databases

eggNOGNOG147372.
GeneTreeENSGT00730000110415.
HOGENOMHOG000230976.
HOVERGENHBG013015.
InParanoidQ6IMF1.
KOK07605.
OMASCEVTPV.
OrthoDBEOG7FV3Q8.
PhylomeDBQ6IMF1.
TreeFamTF317854.

Gene expression databases

GenevestigatorQ6IMF1.

Family and domain databases

InterProIPR001664. IF.
IPR003054. Keratin_II.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
[Graphical view]
PRINTSPR01276. TYPE2KERATIN.
ProtoNetSearch...

Other

NextBio669051.
PROQ6IMF1.

Entry information

Entry nameK2C80_RAT
AccessionPrimary (citable) accession number: Q6IMF1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 70 of the entry and version 1 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