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P04414

- KCRM_TORCA

UniProt

P04414 - KCRM_TORCA

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Protein

Creatine kinase M-type

Gene
N/A
Organism
Torpedo californica (Pacific electric ray)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein 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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei191 – 1911ATPPROSITE-ProRule annotation
Binding sitei236 – 2361ATPPROSITE-ProRule annotation
Binding sitei292 – 2921ATP
Binding sitei335 – 3351ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi128 – 1325ATP
Nucleotide bindingi320 – 3256ATP

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 M-type (EC:2.7.3.2)
Alternative name(s):
Creatine kinase M chain
M-CK
OrganismiTorpedo californica (Pacific electric ray)
Taxonomic identifieri7787 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiBatoideaTorpediniformesTorpedinidaeTorpedo

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381Creatine kinase M-typePRO_0000211981Add
BLAST

Miscellaneous databases

PMAP-CutDBP04414.

Interactioni

Subunit structurei

Dimer of identical or non-identical chains. With MM being the major form in skeletal muscle and myocardium, MB existing in myocardium, and BB existing in many tissues, especially brain.1 Publication

Structurei

Secondary structure

1
381
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 194
Helixi29 – 335
Helixi36 – 427
Helixi53 – 6210
Beta strandi67 – 693
Helixi81 – 844
Helixi86 – 9611
Helixi112 – 1143
Turni123 – 1253
Beta strandi126 – 13510
Turni143 – 1453
Helixi148 – 16215
Helixi167 – 1693
Beta strandi171 – 1755
Helixi176 – 1783
Helixi181 – 1899
Helixi200 – 2034
Turni204 – 21411
Beta strandi216 – 2205
Beta strandi223 – 24422
Helixi246 – 26621
Turni275 – 2773
Helixi284 – 2863
Beta strandi292 – 2987
Helixi302 – 3043
Helixi308 – 3158
Beta strandi317 – 3215
Beta strandi324 – 3296
Beta strandi333 – 3386
Beta strandi342 – 3443
Helixi346 – 36823
Helixi374 – 3763

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VRPX-ray2.10A/B1-381[»]
ProteinModelPortaliP04414.
SMRiP04414. Positions 8-381.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04414.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 9888Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini125 – 367243Phosphagen kinase C-terminalPROSITE-ProRule annotationAdd
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

Phylogenomic databases

HOVERGENiHBG001339.

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.

P04414-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPFGNTHNKW KLNYSAAEEF PDLSKHNNHM AKALTLDIYK KLRDKETPSG
60 70 80 90 100
FTLDDIIQTG VDNPGHPFIM TVGCVAGDEE CYEVFKDLFD PVIEDRHGGY
110 120 130 140 150
KPTDKHKTDL NQENLKGGDD LDPNYVLSSR VRTGRSIKGI ALPPHCSRGE
160 170 180 190 200
RRLVEKLCID GLATLTGEFQ GKYYPLSSMS DAEQQQLIDD HFLFDKPISP
210 220 230 240 250
LLLASGMARD WPDGRGIWHN NDKTFLVWVN EEDHLRVISM QKGGNMKEVF
260 270 280 290 300
RRFCVGLKKI EDIFVKAGRG FMWNEHLGYV LTCPSNLGTG LRGGVHVKIP
310 320 330 340 350
HLCKHEKFSE VLKRTRLQKR GTGGVDTAAV GSIYDISNAD RLGFSEVEQV
360 370 380
QMVVDGVKLM VEMEKRLENG KSIDDLMPAQ K
Length:381
Mass (Da):42,934
Last modified:August 13, 1987 - v1
Checksum:iDF4A54FDDF3BD570
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M36427 mRNA. Translation: AAA49278.1.
PIRiA00677. KIRYCT.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M36427 mRNA. Translation: AAA49278.1 .
PIRi A00677. KIRYCT.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1VRP X-ray 2.10 A/B 1-381 [» ]
ProteinModelPortali P04414.
SMRi P04414. Positions 8-381.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG001339.

Miscellaneous databases

EvolutionaryTracei P04414.
PMAP-CutDB P04414.

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. "Creatine kinase protein sequence encoded by a cDNA made from Torpedo californica electric organ mRNA."
    West B.L., Babbitt P.C., Mendez B., Baxter J.D.
    Proc. Natl. Acad. Sci. U.S.A. 81:7007-7011(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Electric organ.
  2. "The 2.1 A structure of Torpedo californica creatine kinase complexed with the ADP-Mg(2+)-NO(3)(-)-creatine transition-state analogue complex."
    Lahiri S.D., Wang P.-F., Babbitt P.C., McLeish M.J., Kenyon G.L., Allen K.N.
    Biochemistry 41:13861-13867(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP ANALOG, SUBUNIT.

Entry informationi

Entry nameiKCRM_TORCA
AccessioniPrimary (citable) accession number: P04414
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: October 29, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This electric ray muscle-specific creatine kinase (MM isozyme) is isolated from the electric organ, which derives embryologically from skeletal muscle. It may be involved in the electrical discharge process.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3