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P26460

- KCRB_SQUAC

UniProt

P26460 - KCRB_SQUAC

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Protein

Creatine kinase B-type

Gene
N/A
Organism
Squalus acanthias (Spiny dogfish)
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.
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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei13 – 131ATPPROSITE-ProRule annotation
Binding sitei47 – 471ATPPROSITE-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 B-type (EC:2.7.3.2)
Alternative name(s):
B-CK
Creatine kinase B chain
OrganismiSqualus acanthias (Spiny dogfish)
Taxonomic identifieri7797 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiSqualimorphiiSqualiformesSqualidaeSqualus

Subcellular locationi

Basal cell membrane
Note: Basal membrane of the sodium chloride-secreting epithelia.

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›52›52Creatine kinase B-typePRO_0000211972Add
BLAST

Expressioni

Tissue specificityi

Creatine kinase B is the major isoform present in the rectal gland.

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.

Structurei

3D structure databases

ProteinModelPortaliP26460.
SMRiP26460. Positions 1-28.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5252Phosphagen kinase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini1 – 5252Phosphagen kinase N-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

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: Fragments.

P26460-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
AKVLTLDLYK KLRDKSTPSG FTLDDIIQNE HLGYVLTCPS NLGTXLRAXV

HV
Length:52
Mass (Da):5,778
Last modified:August 1, 1992 - v1
Checksum:i3BC2C989F21CFF30
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-adjacent residuesi28 – 292Curated
Sequence uncertaintyi38 – 381
Non-terminal residuei52 – 521

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31V → I.
Natural varianti5 – 51T → S.
Natural varianti10 – 101K → S.
Natural varianti13 – 131R → K.
Natural varianti16 – 161S → Q.

Sequence databases

PIRiA42272.
B42272.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

PIRi A42272.
B42272.

3D structure databases

ProteinModelPortali P26460.
SMRi P26460. Positions 1-28.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "Purification and localization of brain-type creatine kinase in sodium chloride transporting epithelia of the spiny dogfish, Squalus acanthias."
    Friedman D.L., Roberts R.
    J. Biol. Chem. 267:4270-4276(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Rectal gland.

Entry informationi

Entry nameiKCRB_SQUAC
AccessioniPrimary (citable) accession number: P26460
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 29, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3