[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Skeletal muscle; Xu D.Q., Xiong Y.Z., Ling X.F., Lang J.; "Molecular cloning and characterization of porcine CKM."; Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Ling X.F., Xiong Y.Z., Xu D.Q.; "Cloning and sequence analysis of genomic structure and the proximal promoter region of porcine CKM gene."; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.

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 (By similarity).
CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
SUBUNIT: 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 (By similarity).
SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AY754869; AAV28621.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ153192; AAZ66747.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q5XLD3; 2-381.

ModBase

Q5XLD3.

Family and domain databases

InterPro

IPR000749; ATP-gua_Ptrans.
IPR014746; Gln_synth/guanido_kin_cat.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.135.10; ATP-gua_Ptrans; 1.
G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.

PANTHER

PTHR11547; ATP-gua_Ptrans; 1.

Pfam

PF00217; ATP-gua_Ptrans; 1.
PF02807; ATP-gua_PtransN; 1.
Pfam graphical view of domain structure.

PROSITE

PS00112; GUANIDO_KINASE; 1.

BLOCKS

Q5XLD3.

Phylogenomic databases

HOVERGEN

Q5XLD3; -.

Other

ProtoNet

Q5XLD3.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Kinase; Nucleotide-binding; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 381`	`381`	`Creatine kinase M-type.`	`PRO_0000211977`
`NP_BIND`	`128 132`	`5`	`ATP (By similarity).`
`NP_BIND`	`320 325`	`6`	`ATP (By similarity).`
`ACT_SITE`	`283 283`		`By similarity.`
`BINDING`	`191 191`		`ATP (By similarity).`
`BINDING`	`292 292`		`ATP (By similarity).`
`BINDING`	`335 335`		`ATP (By similarity).`

Sequence information

Length: 381 AA [This is the length of the unprocessed precursor]

Molecular weight: 43059 Da [This is the MW of the unprocessed precursor]

CRC64: DF768FBFAF4E636D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPFGNTHNKY KLNFKAEEEY PDLSKHNNHM AKALTLEIYK KLRDKETPSG FTLDDVIQTG 

        70         80         90        100        110        120 
VDNPGHPFIM TVGCVAGDEE SYVVFKDLFD PIIQDRHGGY KPTDKHKTDL NHENLKGGDD 

       130        140        150        160        170        180 
LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT 

       190        200        210        220        230        240 
EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM 

       250        260        270        280        290        300 
EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA 

       310        320        330        340        350        360 
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM 

       370        380 
VEMEKKLEKG QSIDDMIPAQ K

Q5XLD3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools