Skip Header

Contribute Send feedback
Read comments (?) or add your own

P11009 (KCRS_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Creatine kinase S-type, mitochondrial
EC=2.7.3.2
Alternative name(s):
Basic-type mitochondrial creatine kinase
Short name=Mib-CK
Sarcomeric mitochondrial creatine kinase
Short name=S-MtCK
Gene names
Name:CKMT2
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.

Catalytic activity

ATP + creatine = ADP + phosphocreatine.

Subunit structure

Exists as an octamer composed of four MTCK homodimers. Ref.4

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.

Tissue specificity

Expressed in the leg muscle and heart.

Miscellaneous

Mitochondrial creatine kinase binds cardiolipin.

Sequence similarities

Belongs to the ATP:guanido phosphotransferase family.

Contains 1 phosphagen kinase C-terminal domain.

Contains 1 phosphagen kinase N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Mitochondrion Ref.2 Ref.3
Chain40 – 419380Creatine kinase S-type, mitochondrial
PRO_0000016599

Regions

Domain46 – 13287Phosphagen kinase N-terminal
Domain159 – 401243Phosphagen kinase C-terminal
Nucleotide binding162 – 1665ATP By similarity
Nucleotide binding354 – 3596ATP By similarity

Sites

Binding site2251ATP By similarity
Binding site2701ATP By similarity
Binding site3261ATP By similarity
Binding site3691ATP By similarity

Experimental info

Sequence conflict20 – 234AAGS → CSRQ in AAA48688. Ref.2

Secondary structure

1 .............................................................. 419
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11009 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 9ACC60D709B9283F

FASTA41947,084
        10         20         30         40         50         60 
MAGTFGRLLA GRVTAALFAA AGSGVLTTGY LLNQQNVKAT VHEKRKLFPP SADYPDLRKH 

        70         80         90        100        110        120 
NNCMAECLTP AIYAKLRDKL TPNGYSLDQC IQTGVDNPGH PFIKTVGMVA GDEESYEVFA 

       130        140        150        160        170        180 
EIFDPVIKAR HNGYDPRTMK HHTDLDASKI THGQFDERYV LSSRVRTGRS IRGLSLPPAC 

       190        200        210        220        230        240 
SRAERREVEN VVVTALAGLK GDLSGKYYSL TNMSERDQQQ LIDDHFLFDK PVSPLLTCAG 

       250        260        270        280        290        300 
MARDWPDARG IWHNNDKTFL VWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIKE 

       310        320        330        340        350        360 
RGWEFMWNER LGYVLTCPSN LGTGLRAGVH VKLPRLSKDP RFPKILENLR LQKRGTGGVD 

       370        380        390        400        410 
TAAVADVYDI SNLDRMGRSE VELVQIVIDG VNYLVDCEKK LEKGQDIKVP PPLPQFGRK

« Hide

References

[1]"Evolution of the creative kinases. The chicken acidic type mitochondrial creatine kinase gene as the first nonmammalian gene."
Muehlebach S.M., Wirz T., Braendle U., Perriard J.-C.
J. Biol. Chem. 271:11920-11929(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-39.
Strain: White leghorn.
[2]"Distinct tissue specific mitochondrial creatine kinases from chicken brain and striated muscle with a conserved CK framework."
Hossle J.P., Schlegel J., Wegmann G., Wyss M., Boehlen P., Eppenberger H.M., Wallimann T., Perriard J.-C.
Biochem. Biophys. Res. Commun. 151:408-416(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-419, PROTEIN SEQUENCE OF 40-69.
Tissue: Heart and Skeletal muscle.
[3]"The N-terminal heptapeptide of mitochondrial creatine kinase is important for octamerization."
Kaldis P., Furter R., Wallimann T.
Biochemistry 33:952-959(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 40-48.
[4]"Structure of mitochondrial creatine kinase."
Fritz-Wolf K., Schnyder T., Wallimann T., Kabsch W.
Nature 381:341-345(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M18866 mRNA. Translation: AAA48688.1.
IPIIPI00585452.
PIRA27708.
RefSeqNP_001161216.1. NM_001167744.1.
UniGeneGga.869.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CRKX-ray3.00A/B/C/D40-419[»]
ProteinModelPortalP11009.
SMRP11009. Positions 40-419.
ModBaseSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000032149.

Proteomic databases

PaxDbP11009.
PRIDEP11009.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396508.
KEGGgga:396508.

Organism-specific databases

CTD1160.

Phylogenomic databases

eggNOGCOG3869.
HOGENOMHOG000232165.
HOVERGENHBG001339.
InParanoidP11009.
KOK00933.
OrthoDBEOG40VVPN.

Enzyme and pathway databases

SABIO-RKP11009.

Family and domain databases

Gene3D1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProIPR000749. ATP-guanido_PTrfase.
IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PANTHERPTHR11547. PTHR11547. 1 hit.
PfamPF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]
SUPFAMSSF48034. ATP-gua_Ptrans. 1 hit.
PROSITEPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11009.
NextBio20816547.

Entry information

Entry nameKCRS_CHICK
AccessionPrimary (citable) accession number: P11009
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 15, 1998
Last modified: April 3, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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