P51165 (AT1B1_ANGAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sodium/potassium-transporting ATPase subunit beta-1

Alternative name(s):
Sodium/potassium-dependent ATPase subunit beta-1

Gene names

Name:

atp1b1

Organism

Anguilla anguilla (European freshwater eel) (Muraena anguilla)

Taxonomic identifier

7936 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Anguilliformes › Anguillidae › Anguilla

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na+ and K+ ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane.
Subunit structure	Composed of three subunits: alpha (catalytic), beta and gamma.
Subcellular location	Membrane; Single-pass type II membrane protein.
Tissue specificity	Detected in all tissues except liver and cardiac muscle. Highest levels found in intestine, ovary and kidney with marginally lower levels in brain, spleen, esophagus, eye and pancreas, intermediate levels in gill and low levels in white and red skeletal muscle. Ref.2
Sequence similarities	Belongs to the X(+)/potassium ATPases subunit beta family.

Ontologies

Keywords
Biological process	Ion transport Potassium transport Sodium transport Sodium/potassium transport Transport
Cellular component	Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Potassium Sodium
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	sodium:potassium-exchanging ATPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 303	303	Sodium/potassium-transporting ATPase subunit beta-1		PRO_0000219114
Regions
	Topological domain	1 – 34	34	Cytoplasmic Potential
	Transmembrane	35 – 55	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	56 – 303	248	Extracellular Potential
Amino acid modifications
	Glycosylation	113	1	N-linked (GlcNAc...) Potential
	Glycosylation	194	1	N-linked (GlcNAc...) Potential
	Glycosylation	264	1	N-linked (GlcNAc...) Potential
	Disulfide bond	126 ↔ 149		By similarity
	Disulfide bond	159 ↔ 175		By similarity
	Disulfide bond	214 ↔ 275		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P51165 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 3117CF841542321C	FASTA	303	34,901
	10 20 30 40 50 60 MPAATKDSDG GWKKFLWNSE KKEFLGRTGG SWAKILLFYV IFYGCLAGIF IGTIQALLLT 70 80 90 100 110 120 INDFKPVYQD RVAPPGLSHT PRSEKSEMSF KVGDPSTYQK YVKAMHDFLQ AYNDSKQENM 130 140 150 160 170 180 MKYEDCGDTP KSYINRGELD NNQGIKKACI FRRSWLDKCS GLEDPTFGFS EGKPCLIVKL 190 200 210 220 230 240 NRIVNFRPRP PTSNDSIPEE AQSKVQPDVI PIYCTNKREE DAAKVREIKY YGIQEGFPLQ 250 260 270 280 290 300 YYPYYGKQLH PQYLQPLVAV HFTNLTMATE LRIECRVYGQ NIAYSDKDRY RGRFDVKFTI NES

References

[1]	"Primary sequence, tissue specificity and expression of the Na+,K(+)-ATPase alpha 1 subunit in the European eel (Anguilla anguilla)." Cutler C., Sanders I.L., Hazon N., Cramb G. Comp. Biochem. Physiol. 111B:567-573(1995) [PubMed: 8574922] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Gill.
[2]	"Primary sequence, tissue specificity and expression of the Na+,K(+)-ATPase beta 1 subunit in the European eel (Anguilla anguilla)." Cutler C., Sanders I.L., Hazon N., Cramb G. Fish Physiol. Biochem. 14:423-429(1995) Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Gill.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X76109 mRNA. Translation: CAA53715.1.
PIR	S45093.
3D structure databases
ProteinModelPortal	P51165.
SMR	P51165. Positions 28-73.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG050603.
Family and domain databases
InterPro	IPR000402. ATPase_P-typ_cation-exchng_bsu. IPR015565. ATPase_P-typ_Na/K-dep_b1su. [Graphical view]
PANTHER	PTHR11523. ATPase_H_Na/K_b. 1 hit. PTHR11523:SF10. Na/K_ATPaseBeta1. 1 hit.
Pfam	PF00287. Na_K-ATPase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01107. Na_K_ATPase_bet. 1 hit.
PROSITE	PS00390. ATPASE_NA_K_BETA_1. 1 hit. PS00391. ATPASE_NA_K_BETA_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AT1B1_ANGAN

Accession

Primary (citable) accession number: P51165

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	August 10, 2010
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program