Q5XLD3 (KCRM_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Creatine kinase M-type
EC=2.7.3.2

Alternative name(s):
Creatine kinase M chain
M-CK

Gene names

Name:

CKM

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity.
Catalytic activity	ATP + creatine = ADP + phosphocreatine.
Subunit structure	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.
Sequence similarities	Belongs to the ATP:guanido phosphotransferase family. Contains 1 phosphagen kinase C-terminal domain. Contains 1 phosphagen kinase N-terminal domain.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 381	380	Creatine kinase M-type		PRO_0000211977
Regions
	Domain	11 – 98	88	Phosphagen kinase N-terminal
	Domain	125 – 367	243	Phosphagen kinase C-terminal
	Nucleotide binding	128 – 132	5	ATP By similarity
	Nucleotide binding	320 – 325	6	ATP By similarity
Sites
	Binding site	191	1	ATP By similarity
	Binding site	236	1	ATP By similarity
	Binding site	292	1	ATP By similarity
	Binding site	335	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5XLD3 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: DF768FBFAF4E636D	FASTA	381	43,059
	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

References

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

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY754869 mRNA. Translation: AAV28621.1. DQ153192 Genomic DNA. Translation: AAZ66747.1.
RefSeq	NP_001123421.1. NM_001129949.1.
UniGene	Ssc.415.
3D structure databases
ProteinModelPortal	Q5XLD3.
SMR	Q5XLD3. Positions 2-381.
ModBase	Search...
Proteomic databases
PRIDE	Q5XLD3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	397264.
KEGG	ssc:397264.
Organism-specific databases
CTD	1158.
Phylogenomic databases
HOVERGEN	HBG001339.
KO	K00933.
Family and domain databases
Gene3D	1.10.135.10. 1 hit. 3.30.590.10. 1 hit.
InterPro	IPR000749. 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]
PANTHER	PTHR11547. PTHR11547. 1 hit.
Pfam	PF00217. ATP-gua_Ptrans. 1 hit. PF02807. ATP-gua_PtransN. 1 hit. [Graphical view]
SUPFAM	SSF48034. ATP-gua_Ptrans. 1 hit.
PROSITE	PS00112. PHOSPHAGEN_KINASE. 1 hit. PS51510. PHOSPHAGEN_KINASE_C. 1 hit. PS51509. PHOSPHAGEN_KINASE_N. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KCRM_PIG

Accession

Primary (citable) accession number: Q5XLD3
Secondary accession number(s): Q45EW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	November 23, 2004
Last modified:	March 6, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program