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Protein

Keratin, type I cytoskeletal 9

Gene

Krt9

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May serve an important special function either in the mature palmar and plantar skin tissue or in the morphogenetic program of the formation of these tissues. Plays a role in keratin filament assembly (By similarity). May be involved in spermatid nuclear shaping and sperm development.By similarity1 Publication

GO - Molecular functioni

  • structural constituent of cytoskeleton Source: RGD

GO - Biological processi

  • intermediate filament organization Source: UniProtKB
  • skin development Source: UniProtKB
  • spermatogenesis Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type I cytoskeletal 9
Alternative name(s):
Cytokeratin-9
Short name:
CK-9
Keratin-9
Short name:
K9
Spermatid perinuclear ring manchette protein K9
Gene namesi
Name:Krt9
Synonyms:Krt1-9Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628785. Krt9.

Subcellular locationi

GO - Cellular componenti

  • keratin filament Source: RGD
  • perinuclear region of cytoplasm Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 618618Keratin, type I cytoskeletal 9PRO_0000308373Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ8CIS9.

Expressioni

Tissue specificityi

Expressed in the perinuclear ring of spermatid manchettes within testis and in keratinocytes of the suprabasal layer of footpad epidermis (at protein level).1 Publication

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins.Curated

Structurei

3D structure databases

ProteinModelPortaliQ8CIS9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 137137HeadSequence analysisAdd
BLAST
Regioni138 – 446309RodSequence analysisAdd
BLAST
Regioni138 – 17336Coil 1ASequence analysisAdd
BLAST
Regioni174 – 19219Linker 1Sequence analysisAdd
BLAST
Regioni193 – 28492Coil 1BSequence analysisAdd
BLAST
Regioni285 – 30723Linker 12Sequence analysisAdd
BLAST
Regioni308 – 446139Coil 2Sequence analysisAdd
BLAST
Regioni447 – 609163TailSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi15 – 131117Gly-richSequence analysisAdd
BLAST
Compositional biasi470 – 612143Ser-richSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Sequence analysis

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiQ8CIS9.
KOiK07604.
PhylomeDBiQ8CIS9.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 3 hits.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CIS9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFRQISSSF RSSSGSSCGG GGGRGASRGS MRSSFGRSSR AGGESRFGSS
60 70 80 90 100
SGFGGGGFSA CGTGGGGSFG SSYGGGYGRG FSAGSSSGMF GGSSRGCFGG
110 120 130 140 150
GSGGGFGGGS GGGFGGGFGG GFGGGSGGGE GSILNTNEKV VMQNLNSRLA
160 170 180 190 200
SYMDKVQELE EDNANLEKQI QEWYSRKGNR VFQKDYSHYY NTIEDLKDRI
210 220 230 240 250
VDLTARNNKA LIDMDNTRMT LGDFRVKLEM EQSLPQGVDA DINGLQKVLD
260 270 280 290 300
DINMEKSDLE IQFDSLDDEL KALKKSHKEE MNQLTGLNDG DVNVEINVAP
310 320 330 340 350
STDLTQVLND MREEYEHLIS KNRQDIEQHY ESQMTQIEHQ LTNSGPEMET
360 370 380 390 400
NMKQVSQLQH SVQELNIELQ TQLTTKSALE KALEDTKNRY CGQLQQIREQ
410 420 430 440 450
ISEMEAQLAQ VRAETECQNQ EYGLLLSIKT RLEKEIETYR KLLEGGQQDF
460 470 480 490 500
ESSGAGQIGF GSGKGGQRGS GGSYGGGSGD SYEGESGGSY GGGSGGSHGG
510 520 530 540 550
KSGGSYGGGS SSGGGSGGSY GGGSGGSHGG KSGGSHGGGS GGSYGGGSGS
560 570 580 590 600
GGESGGSYGG GSGGSHGGQK GGSGGSYEGG SGGSYGGGSG SGGGSGGSYG
610
GGNTRPSQSQ SSQIPRLR
Length:618
Mass (Da):63,009
Last modified:March 1, 2003 - v1
Checksum:iB0140A0E34E2A28F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY128946 mRNA. Translation: AAN05455.1.
RefSeqiNP_703206.1. NM_153476.1.
UniGeneiRn.145135.

Genome annotation databases

GeneIDi266717.
KEGGirno:266717.
UCSCiRGD:628785. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY128946 mRNA. Translation: AAN05455.1.
RefSeqiNP_703206.1. NM_153476.1.
UniGeneiRn.145135.

3D structure databases

ProteinModelPortaliQ8CIS9.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ8CIS9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi266717.
KEGGirno:266717.
UCSCiRGD:628785. rat.

Organism-specific databases

CTDi3857.
RGDi628785. Krt9.

Phylogenomic databases

HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiQ8CIS9.
KOiK07604.
PhylomeDBiQ8CIS9.

Miscellaneous databases

NextBioi624558.
PROiQ8CIS9.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 3 hits.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Keratin 9 is a component of the perinuclear ring of the manchette of rat spermatids."
    Mochida K., Rivkin E., Gil M., Kierszenbaum A.L.
    Dev. Biol. 227:510-519(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: Sprague-DawleyImported.
    Tissue: Epidermis1 Publication and Testis1 Publication.

Entry informationi

Entry nameiK1C9_RAT
AccessioniPrimary (citable) accession number: Q8CIS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.