Q6IG12 (K2C7_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Keratin, type II cytoskeletal 7

Alternative name(s):
Cytokeratin-7
Short name=CK-7
Keratin-7
Short name=K7
Type-II keratin Kb7

Gene names

Name:	Krt7
Synonyms:	Kb7, Krt2-7

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	457 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Blocks interferon-dependent interphase and stimulates DNA synthesis in cells By similarity. UniProtKB P08729
Subunit structure	Heterotetramer of two type I and two type II keratins. Interacts with eukaryotic translation initiator factor 3 (eIF3) subunit EIF3S10 By similarity. UniProtKB P08729
Post-translational modification	Arg-15 is dimethylated, probably to asymmetric dimethylarginine By similarity. UniProtKB P08729
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.

Ontologies

Keywords
Cellular component	Intermediate filament Keratin
Domain	Coiled coil
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of translation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	keratin filament Inferred from electronic annotation. Source: InterPro
Molecular_function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 457	456	Keratin, type II cytoskeletal 7		PRO_0000307638
Regions
	Region	2 – 84	83	Head
	Region	84 – 120	37	Coil 1A
	Region	85 – 393	309	Rod
	Region	121 – 138	18	Linker 1
	Region	139 – 230	92	Coil 1B
	Region	231 – 254	24	Linker 12
	Region	255 – 393	139	Coil 2
	Region	394 – 457	64	Tail
Sites
	Site	337	1	Stutter
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	2	1	Phosphoserine By similarity
	Modified residue	15	1	Dimethylated arginine; alternate By similarity UniProtKB P08729
	Modified residue	15	1	Omega-N-methylarginine; alternate By similarity
	Modified residue	173	1	N6-acetyllysine By similarity
	Modified residue	246	1	Phosphoserine By similarity
	Modified residue	248	1	Phosphoserine By similarity UniProtKB P08729

Sequences

	Sequence		Length	Mass (Da)
	Q6IG12 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: D6AD866E4949DEF8	FASTA	457	50,709
	10 20 30 40 50 60 MSIHFSSRST AYPGRGAQVR LSSGRASFGS RSLYGLGSSR PRVAVRSAYG GPVGAGIREI 70 80 90 100 110 120 TINQSLLAPL SVDIDPTIQQ VRQEEREQIK TLNNKFASFI DKVRFLEQQN KMLETKWALL 130 140 150 160 170 180 QEQKSAKSSQ LPRIFEAQIA GLRQQLETLQ LDGGRLEVEL RNMQDVVEDF KNKYEEEINR 190 200 210 220 230 240 RTAAENEFVL LKKDVDAAYT NKVELEAKAD SLQDEINFLK TLHETELAEL QSQISDTSVV 250 260 270 280 290 300 LSMDNSRSLD LDGIIADVKA QYEEMANHSR AEAEAWYQTK FETLQAQAGK HGDDLRNTRN 310 320 330 340 350 360 EIAEMNRSIQ RLQAEIDTLK NQRAKLESSI AEAEEQGELA IKDAHAKQGE LEAALQKAKQ 370 380 390 400 410 420 DVARQLREYQ ELLNTKLALD IEIATYRKLL EGEESRLSGD GMGPVNISVV NSTGGNGGKL 430 440 450 IFGGTMGSNA LSFSGGPGAL RAYSIKTTST TRRGTHN

References

	« Hide 'large scale' referencesShow '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. , 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AABR03058117 Genomic DNA. No translation available. AABR03059386 Genomic DNA. No translation available. BK003973 mRNA. Translation: DAA02218.1.
IPI	IPI00421788.
RefSeq	NP_001041335.1. NM_001047870.1.
UniGene	Rn.7913.
3D structure databases
HSSP	HSSP built from PDB template 1GK6 based on UniProtKB P03069.
ProteinModelPortal	Q6IG12.
SMR	Q6IG12. Positions 82-234, 250-392.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000010660.
PTM databases
PhosphoSite	Q6IG12.
Proteomic databases
PaxDb	Q6IG12.
PRIDE	Q6IG12.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	300242.
KEGG	rno:300242.
Organism-specific databases
CTD	3855.
RGD	1310865. Krt7.
Phylogenomic databases
eggNOG	NOG145985.
HOGENOM	HOG000230976.
HOVERGEN	HBG013015.
InParanoid	Q6IG12.
KO	K07605.
OrthoDB	EOG4TMR28.
Gene expression databases
Genevestigator	Q6IG12.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR003054. Keratin_II. IPR009053. Prefoldin. [Graphical view]
PANTHER	PTHR23239. PTHR23239. 1 hit. PTHR23239:SF18. PTHR23239:SF18. 1 hit.
Pfam	PF00038. Filament. 1 hit. [Graphical view]
PRINTS	PR01276. TYPE2KERATIN.
SUPFAM	SSF46579. Prefoldin. 1 hit.
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	646619.

Entry information

Entry name

K2C7_RAT

Accession

Primary (citable) accession number: Q6IG12

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program