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AT1B1_CHICK
ID   AT1B1_CHICK             Reviewed;         305 AA.
AC   P08251;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE   AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
GN   Name=ATP1B1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3038895; DOI=10.1016/s0021-9258(18)61025-7;
RA   Takeyasu K., Tamkun M.M., Siegel N.R., Fambrough D.M.;
RT   "Expression of hybrid (Na+ + K+)-ATPase molecules after transfection of
RT   mouse Ltk-cells with DNA encoding the beta-subunit of an avian brain sodium
RT   pump.";
RL   J. Biol. Chem. 262:10733-10740(1987).
CC   -!- FUNCTION: This is the non-catalytic component of the active enzyme,
CC       which catalyzes the hydrolysis of ATP coupled with the exchange of
CC       Na(+) and K(+) ions across the plasma membrane. The beta subunit
CC       regulates, through assembly of alpha/beta heterodimers, the number of
CC       sodium pumps transported to the plasma membrane.
CC   -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC       catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC       additional regulatory subunit. {ECO:0000305}.
CC   -!- INTERACTION:
CC       P08251; Q8AYS8: KCNMA1; NbExp=3; IntAct=EBI-7206371, EBI-1635766;
CC       P08251; Q08460: Kcnma1; Xeno; NbExp=5; IntAct=EBI-7206371, EBI-1633915;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; J02787; AAA48608.1; -; mRNA.
DR   PIR; A28491; A28491.
DR   RefSeq; NP_990851.1; NM_205520.4.
DR   AlphaFoldDB; P08251; -.
DR   SMR; P08251; -.
DR   DIP; DIP-29N; -.
DR   IntAct; P08251; 2.
DR   MINT; P08251; -.
DR   STRING; 9031.ENSGALP00000024537; -.
DR   PaxDb; P08251; -.
DR   GeneID; 396529; -.
DR   KEGG; gga:396529; -.
DR   CTD; 481; -.
DR   VEuPathDB; HostDB:geneid_396529; -.
DR   eggNOG; KOG3927; Eukaryota.
DR   InParanoid; P08251; -.
DR   OrthoDB; 998086at2759; -.
DR   PhylomeDB; P08251; -.
DR   PRO; PR:P08251; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IBA:GO_Central.
DR   GO; GO:0001671; F:ATPase activator activity; IBA:GO_Central.
DR   GO; GO:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0006883; P:cellular sodium ion homeostasis; IBA:GO_Central.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
DR   Gene3D; 2.60.40.1660; -; 1.
DR   InterPro; IPR000402; Na/K_ATPase_sub_beta.
DR   InterPro; IPR015565; Na/K_ATPase_sub_beta_chordates.
DR   InterPro; IPR038702; Na/K_ATPase_sub_beta_sf.
DR   PANTHER; PTHR11523; PTHR11523; 1.
DR   PANTHER; PTHR11523:SF10; PTHR11523:SF10; 1.
DR   Pfam; PF00287; Na_K-ATPase; 1.
DR   TIGRFAMs; TIGR01107; Na_K_ATPase_bet; 1.
DR   PROSITE; PS00390; ATPASE_NA_K_BETA_1; 1.
DR   PROSITE; PS00391; ATPASE_NA_K_BETA_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW   Potassium; Potassium transport; Reference proteome; Signal-anchor; Sodium;
KW   Sodium transport; Sodium/potassium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..305
FT                   /note="Sodium/potassium-transporting ATPase subunit beta-1"
FT                   /id="PRO_0000219102"
FT   TOPO_DOM        1..35
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..63
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..305
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        127..150
FT                   /evidence="ECO:0000250"
FT   DISULFID        160..176
FT                   /evidence="ECO:0000250"
FT   DISULFID        214..277
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  34941 MW;  E56E47E920769252 CRC64;
     MARGKANDGD GNWKKFIWNS EKKELLGRTG GSWFKILLFY VIFYGCLAGI FIGTIQVMLL
     TVSEFEPKYQ DRVAPPGLTQ VPQVQKTEIS FTVNDPKSYD PYVKNLEGFL NKYSAGEQTD
     NIVFQDCGDI PTDYKERGPY NDAQGQKKVC KFKREWLENC SGLQDNTFGY KDGKPCILVK
     LNRIIGFKPK APENESLPSD LAGKYNPYLI PVHCVAKRDE DADKIGMVEY YGMGGYPGFA
     LQYYPYYGRL LQPQYLQPLV AVQFTNLTYD VEVRVECKEY GQNIQYSDKD RFQGRFDIKF
     DIKSS
 
 
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