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AT1B3_RABIT
ID   AT1B3_RABIT             Reviewed;         279 AA.
AC   Q9GLC3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-3;
DE   AltName: Full=Sodium/potassium-dependent ATPase subunit beta-3;
DE            Short=ATPB-3;
DE   AltName: CD_antigen=CD298;
GN   Name=ATP1B3;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Renal medulla;
RA   Gumz M.L., Otto T.C., Cain B.D.;
RT   "Identification of the rabbit Na+/K+ ATPase beta 3 subunit.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
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 exact function of
CC       the beta-3 subunit is not known (By similarity). {ECO:0000250}.
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. Interacts with catalytic alpha subunit
CC       ATP12A. {ECO:0000250|UniProtKB:Q63377}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q63377}; Single-pass type II membrane protein
CC       {ECO:0000255}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q63377}; Single-pass type II membrane protein
CC       {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:P54709}.
CC       Note=Identified by mass spectrometry in melanosome fractions from stage
CC       I to stage IV. {ECO:0000250|UniProtKB:P54709}.
CC   -!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain
CC       and may mediate cell adhesion properties. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; AF302929; AAG21398.1; -; mRNA.
DR   RefSeq; NP_001075560.1; NM_001082091.1.
DR   AlphaFoldDB; Q9GLC3; -.
DR   SMR; Q9GLC3; -.
DR   STRING; 9986.ENSOCUP00000020337; -.
DR   PRIDE; Q9GLC3; -.
DR   GeneID; 100008788; -.
DR   KEGG; ocu:100008788; -.
DR   CTD; 483; -.
DR   InParanoid; Q9GLC3; -.
DR   OrthoDB; 998086at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IEA:InterPro.
DR   GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1660; -; 1.
DR   InterPro; IPR000402; Na/K_ATPase_sub_beta.
DR   InterPro; IPR038702; Na/K_ATPase_sub_beta_sf.
DR   PANTHER; PTHR11523; PTHR11523; 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.
PE   2: Evidence at transcript 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..279
FT                   /note="Sodium/potassium-transporting ATPase subunit beta-3"
FT                   /id="PRO_0000265961"
FT   TOPO_DOM        1..35
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..56
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..279
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          186..279
FT                   /note="immunoglobulin-like"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        128..144
FT                   /evidence="ECO:0000250"
FT   DISULFID        154..170
FT                   /evidence="ECO:0000250"
FT   DISULFID        191..250
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   279 AA;  31593 MW;  C0E66712B5EDAB99 CRC64;
     MTKKEKKSFN QSLAEWKRFI YNPTSGEFLG RTAKSWGLIL LFYLVFYGFL AALFTFTMWV
     MLQTLNDEVP KYRDQIPSPG LMVFPKPLSA LEYTFSASDP SSYRGYIEDL RKFLKPYTLE
     EQKNLTVCPD GILSEQKGPV YVACQFPIFL LQACSGMSDP DFGYSQGSPC VLVKMNRIIG
     LKPEGTPRIE CIPKDENVAS ISTYPNNGII DLKYFPYYGK KLHVGYLQPL VAAQVIFSAN
     STKKEVTVEC KIDGSPNLKN QDDRDKFLGR VAFKIIARA
 
 
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