SMART: Pfam domain IRK

The domain within your query sequence starts at position 22 and ends at position 361; the E-value for the IRK domain shown below is 2.1e-155.

VKKNGQCNVYFANLSNKSQRYMADIFTTCVDTRWRYMLMIFSAAFLVSWLFFGLLFWCIA
FFHGDLEASPSVPAAGGPGGNGGASPNAPKPCIMHVNGFLGAFLFSVETQTTIGYGFRCV
TEECPLAVIAVVVQSIVGCVIDSFMIGTIMAKMARPKKRAQTLLFSHHAVISVRDGKLCL
MWRVGNLRKSHIVEAHVRAQLIKPYMTQEGEYLPLDQRDLNVGYDIGLDRIFLVSPIIIV
HEIDEDSPLYGMGKEELESEDFEIVVILEGMVEATAMTTQARSSYLASEILWGHRFEPVV
FEEKSHYKVDYSRFHKTYEVAGTPCCSARELQESKITVLP

IRK

PFAM accession number:	PF01007
Interpro abstract (IPR040445):	Inwardly-rectifying potassium channels (Kir) are the principal class of two-TM domain potassium channels. They are characterised by the property of inward-rectification, which is described as the ability to allow large inward currents and smaller outward currents. Inwardly rectifying potassium channels (Kir) are responsible for regulating diverse processes including: cellular excitability, vascular tone, heart rate, renal salt flow, and insulin release [ (PUBMED:10102275) ]. To date, around twenty members of this superfamily have been cloned, which can be grouped into six families by sequence similarity, and these are designated Kir1.x-6.x [ (PUBMED:7580148) (PUBMED:10449331) ]. Cloned Kir channel cDNAs encode proteins of between ~370-500 residues, both N- and C-termini are thought to be cytoplasmic, and the N terminus lacks a signal sequence. Kir channel alpha subunits possess only 2TM domains linked with a P-domain. The two 'transmembrane passes' place the C-terminal tail on the cytoplasmic side of the membrane [ (PUBMED:7580148) ]. It is thought that four Kir subunits assemble to form a tetrameric channel complex, which may be hetero- or homomeric [ (PUBMED:10102275) ].

PFAM accession number:

PF01007

Interpro abstract (IPR040445):

Inwardly-rectifying potassium channels (Kir) are the principal class of two-TM domain potassium channels. They are characterised by the property of inward-rectification, which is described as the ability to allow large inward currents and smaller outward currents. Inwardly rectifying potassium channels (Kir) are responsible for regulating diverse processes including: cellular excitability, vascular tone, heart rate, renal salt flow, and insulin release [ (PUBMED:10102275) ]. To date, around twenty members of this superfamily have been cloned, which can be grouped into six families by sequence similarity, and these are designated Kir1.x-6.x [ (PUBMED:7580148) (PUBMED:10449331) ].

Cloned Kir channel cDNAs encode proteins of between ~370-500 residues, both N- and C-termini are thought to be cytoplasmic, and the N terminus lacks a signal sequence. Kir channel alpha subunits possess only 2TM domains linked with a P-domain. The two 'transmembrane passes' place the C-terminal tail on the cytoplasmic side of the membrane [ (PUBMED:7580148) ]. It is thought that four Kir subunits assemble to form a tetrameric channel complex, which may be hetero- or homomeric [ (PUBMED:10102275) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry IRK