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Q29577

- KCRU_PIG

UniProt

Q29577 - KCRU_PIG

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Protein

Creatine kinase U-type, mitochondrial

Gene

CKMT1

Organism
Sus scrofa (Pig)
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 sitei224 – 2241ATPPROSITE-ProRule annotation
Binding sitei269 – 2691ATPPROSITE-ProRule annotation
Binding sitei325 – 3251ATPPROSITE-ProRule annotation
Binding sitei368 – 3681ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi161 – 1655ATPPROSITE-ProRule annotation
Nucleotide bindingi353 – 3586ATPPROSITE-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 U-type, mitochondrial (EC:2.7.3.2)
Alternative name(s):
Acidic-type mitochondrial creatine kinase
Short name:
Mia-CK
Ubiquitous mitochondrial creatine kinase
Short name:
U-MtCK
Gene namesi
Name:CKMT1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: 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 – 3939MitochondrionBy similarityAdd
BLAST
Chaini40 – 416377Creatine kinase U-type, mitochondrialPRO_0000211983Add
BLAST

Proteomic databases

PaxDbiQ29577.
PRIDEiQ29577.

Interactioni

Subunit structurei

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 13188Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini158 – 400243Phosphagen kinase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 6324Cardiolipin-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.
InParanoidiQ29577.

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.

Q29577-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGPFSRLLS ARPGLRLLAL AGAGSLAAGF LLRPEPIRAA SERRRQYPPS
60 70 80 90 100
AEYPDLRKHN NCMASHLTPA VYARLCDKTT PTGWTLDQCI QTGVDNPGHP
110 120 130 140 150
FIKTVGMVAG DEETYEVFAE LFDPVIQERH NGYDPRTMKH TTDLDASKIR
160 170 180 190 200
SGFFDERYVL SSRVRTGRSI RGLSLPPACT RAERREVERV VVDALSGLKG
210 220 230 240 250
DLAGRYYRLS EMTEAEQQQL IDDHFLFDKP VSPLLTAAGM ARDWPDARGI
260 270 280 290 300
WHNNEKSFLI WVNEEDHTRV ISMEKGGNMK KVFERFCRGL KEVERLIQER
310 320 330 340 350
GWEFMWNERL GYILTCPSNL GTGLRAGVHI KLPLLSKDSR FPKILENLRL
360 370 380 390 400
QKRGTGGVDT AATGSIFDIS NLDRLGKSEV ELVQLVIDGV NYLIDCERRL
410
ERGQDIRIPP PLPNKH
Length:416
Mass (Da):46,950
Last modified:September 22, 2009 - v2
Checksum:i113919BF6571CF08
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti365 – 3662SI → ES in CAA23265. (PubMed:8672129)Curated
Sequence conflicti396 – 3983CER → LANG in CAA23265. (PubMed:8672129)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU650786 mRNA. Translation: ACD02423.1.
F14801 mRNA. Translation: CAA23265.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU650786 mRNA. Translation: ACD02423.1 .
F14801 mRNA. Translation: CAA23265.1 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q29577.
PRIDEi Q29577.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG3869.
HOGENOMi HOG000232165.
HOVERGENi HBG001339.
InParanoidi Q29577.

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. Liu G.Y.
    Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
    Winteroe A.K., Fredholm M., Davies W.
    Mamm. Genome 7:509-517(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 333-409.
    Tissue: Small intestine.

Entry informationi

Entry nameiKCRU_PIG
AccessioniPrimary (citable) accession number: Q29577
Secondary accession number(s): B2ZF48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: September 22, 2009
Last modified: October 29, 2014
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Mitochondrial creatine kinase binds cardiolipin.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3