PROTEIN SEQUENCE.
TISSUE=Rectal gland;
PubMed=1310991 [NCBI, ExPASy, EBI, Israel, Japan]
Friedman D.L., Roberts R.;
"Purification and localization of brain-type creatine kinase in sodium chloride transporting epithelia of the spiny dogfish, Squalus acanthias.";
J. Biol. Chem. 267:4270-4276(1992).

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.
FUNCTION: The isoform-specific function of B creatine kinase may be to provide a system for the rapid regeneration of metabolic energy for sodium transport.
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.
SUBCELLULAR LOCATION: Basal cell membrane. Note=Basal membrane of the sodium chloride-secreting epithelia.
TISSUE SPECIFICITY: Creatine kinase B is the major isoform present in the rectal gland.
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

PIR

A42272; A42272.
B42272; B42272.

3D structure databases

HSSP

P11009; 1CRK. [HSSP ENTRY / PDB]

ModBase

P26460.

Ontologies

GO:0009925;	Cellular component: basal plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004111;	Molecular function: creatine kinase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR000749; ATP-gua_Ptrans.
Graphical view of domain structure.

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.

Phylogenomic databases

HOVERGEN

P26460; -.

Other

UniRef

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

Keywords

ATP-binding; Cell membrane; Direct protein sequencing; Kinase; Membrane; Nucleotide-binding; Polymorphism; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 >52`	`>52`	`Creatine kinase B-type.`	`PRO_0000211972`
`BINDING`	`13 13`		`ATP (By similarity).`
`BINDING`	`47 47`		`ATP (By similarity).`
`VARIANT`	`3 3`	`1`	`V -> I.`
`VARIANT`	`5 5`	`1`	`T -> S.`
`VARIANT`	`10 10`	`1`	`K -> S.`
`VARIANT`	`13 13`	`1`	`R -> K.`
`VARIANT`	`16 16`	`1`	`S -> Q.`
`UNSURE`	`38 38`
`NON_CONS`	`28 29`
`NON_TER`	`1 1`
`NON_TER`	`52 52`

Sequence information

Length: 52 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 5778 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 3BC2C989F21CFF30 [This is a checksum on the sequence]

        10         20         30         40         50 
AKVLTLDLYK KLRDKSTPSG FTLDDIIQNE HLGYVLTCPS NLGTXLRAXV HV

P26460 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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