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O77814

- KCRS_RABIT

UniProt

O77814 - KCRS_RABIT

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Protein

Creatine kinase S-type, mitochondrial

Gene

CKMT2

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

ATP + creatine = ADP + phosphocreatine.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei225 – 2251ATPPROSITE-ProRule annotation
Binding sitei270 – 2701ATPPROSITE-ProRule annotation
Binding sitei326 – 3261ATPPROSITE-ProRule annotation
Binding sitei369 – 3691ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi162 – 1665ATPPROSITE-ProRule annotation
Nucleotide bindingi354 – 3596ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. creatine kinase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Creatine kinase S-type, mitochondrial (EC:2.7.3.2)
Alternative name(s):
Basic-type mitochondrial creatine kinase
Short name:
Mib-CK
RSMTCK
Sarcomeric mitochondrial creatine kinase
Short name:
S-MtCK
Gene namesi
Name:CKMT2
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3939MitochondrionAdd
BLAST
Chaini40 – 419380Creatine kinase S-type, mitochondrialPRO_0000016597Add
BLAST

Proteomic databases

PRIDEiO77814.

Interactioni

Subunit structurei

Exists as an octamer composed of four CKMT2 homodimers.By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000009646.

Structurei

3D structure databases

ProteinModelPortaliO77814.
SMRiO77814. Positions 47-413.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 13287Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini159 – 401243Phosphagen kinase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 6425Cardiolipin-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the ATP:guanido phosphotransferase family.PROSITE-ProRule annotation
Contains 1 phosphagen kinase C-terminal domain.PROSITE-ProRule annotation
Contains 1 phosphagen kinase N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG3869.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiO77814.

Family and domain databases

Gene3Di1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PfamiPF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]
SUPFAMiSSF48034. SSF48034. 1 hit.
PROSITEiPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O77814-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASTFSKLLT GRNASLLFAT LGTSALTTGY LVNRQKVCAE ARDQHKLFPP
60 70 80 90 100
SADYPDLRKH NNCMAECLTP SIYAKLRNKV TANGYTLDQC IQTGVDNPGH
110 120 130 140 150
PFIKTVGMVA GDEESYEVFA DLFDPVIKLR HNGYDPRVMK HPTDLDASKI
160 170 180 190 200
TQGQFDERYV LSSRVRTGRS IRGLSLPPAC SRAEAREVEN VAITALEGLK
210 220 230 240 250
GDLAGRYYRL SEMTEQDQQR LIDDHFLFDK PVSPLLTCAG MARDWPDARG
260 270 280 290 300
IWHNYDNTFL IWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIQE
310 320 330 340 350
RGWEFMWNER LGYILTCPSN LGTGLRAGVH VRIPKLSKDP RFSKILENLR
360 370 380 390 400
LQKRGTGGVD TRAVADVYDI SNIDRIGRSE VELVQIVIDG VNYLVDCEKK
410
LERGQDIKVP PPLPQFGKK
Length:419
Mass (Da):47,407
Last modified:November 1, 1998 - v1
Checksum:iC26469B25730CC6F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ011334 mRNA. Translation: CAA09597.1.
RefSeqiNP_001156542.1. NM_001163070.1.
UniGeneiOcu.3234.

Genome annotation databases

GeneIDi100302412.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ011334 mRNA. Translation: CAA09597.1 .
RefSeqi NP_001156542.1. NM_001163070.1.
UniGenei Ocu.3234.

3D structure databases

ProteinModelPortali O77814.
SMRi O77814. Positions 47-413.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000009646.

Proteomic databases

PRIDEi O77814.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100302412.

Organism-specific databases

CTDi 1160.

Phylogenomic databases

eggNOGi COG3869.
HOGENOMi HOG000232165.
HOVERGENi HBG001339.
InParanoidi O77814.

Family and domain databases

Gene3Di 1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProi IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view ]
Pfami PF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view ]
SUPFAMi SSF48034. SSF48034. 1 hit.
PROSITEi PS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning, Escherichia coli expression, and phase-transition chromatography-based purification of recombinant rabbit heart mitochondrial creatine kinase."
    Marcillat O., Perraut C., Granjon T., Vial C., Vacheron M.J.
    Protein Expr. Purif. 17:163-168(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.

Entry informationi

Entry nameiKCRS_RABIT
AccessioniPrimary (citable) accession number: O77814
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: October 29, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Mitochondrial creatine kinase binds cardiolipin.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3