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AT1B1_CAEEL
ID   AT1B1_CAEEL             Reviewed;         320 AA.
AC   Q93235;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE   AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
GN   Name=nkb-1; ORFNames=C17E4.9;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=12754521; DOI=10.1038/nbt829;
RA   Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA   Kasai K., Takahashi N., Isobe T.;
RT   "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT   identify N-linked glycoproteins.";
RL   Nat. Biotechnol. 21:667-672(2003).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RA   Doi M., Iwasaki K.;
RT   "A novel function of the Na+/K+ ATPase subunit in vesicle transport for the
RT   retrograde synaptic transmission pathway.";
RL   (In) Proceedings of the 14th international C. elegans meeting, pp.231-231,
RL   Los Angeles (2003).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA   Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT   "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT   elegans.";
RL   Glycobiology 15:952-964(2005).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
CC   -!- FUNCTION: Non-catalytic component of the active enzyme, which catalyzes
CC       the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions
CC       across the plasma membrane. The beta subunit regulates, through
CC       assembly of alpha/beta heterodimers, the number of sodium pumps
CC       transported to the plasma membrane (By similarity). May also may
CC       function in the peptidic vesicle transport pathway from the endoplasmic
CC       reticulum for the defecation behaviors. {ECO:0000250,
CC       ECO:0000269|Ref.3}.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Defecation defects. {ECO:0000269|Ref.3}.
CC   -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; Z81037; CAB02752.1; -; Genomic_DNA.
DR   PIR; T19358; T19358.
DR   RefSeq; NP_492506.1; NM_060105.5.
DR   AlphaFoldDB; Q93235; -.
DR   SMR; Q93235; -.
DR   BioGRID; 47573; 9.
DR   STRING; 6239.C17E4.9.1; -.
DR   iPTMnet; Q93235; -.
DR   EPD; Q93235; -.
DR   PaxDb; Q93235; -.
DR   PeptideAtlas; Q93235; -.
DR   EnsemblMetazoa; C17E4.9a.1; C17E4.9a.1; WBGene00007646.
DR   GeneID; 182726; -.
DR   KEGG; cel:CELE_C17E4.9; -.
DR   UCSC; C17E4.9; c. elegans.
DR   CTD; 182726; -.
DR   WormBase; C17E4.9a; CE08258; WBGene00007646; nkb-1.
DR   eggNOG; KOG3927; Eukaryota.
DR   GeneTree; ENSGT01030000234579; -.
DR   HOGENOM; CLU_057702_0_0_1; -.
DR   InParanoid; Q93235; -.
DR   OMA; QKNDECT; -.
DR   OrthoDB; 998086at2759; -.
DR   PhylomeDB; Q93235; -.
DR   Reactome; R-CEL-210991; Basigin interactions.
DR   Reactome; R-CEL-936837; Ion transport by P-type ATPases.
DR   PRO; PR:Q93235; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00007646; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
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; IPR038702; Na/K_ATPase_sub_beta_sf.
DR   PANTHER; PTHR11523; PTHR11523; 1.
DR   Pfam; PF00287; Na_K-ATPase; 1.
DR   PROSITE; PS00390; ATPASE_NA_K_BETA_1; 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..320
FT                   /note="Sodium/potassium-transporting ATPase subunit beta-1"
FT                   /id="PRO_0000250558"
FT   TOPO_DOM        1..51
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..320
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754521,
FT                   ECO:0000269|PubMed:15888633, ECO:0000269|PubMed:17761667"
FT   DISULFID        176..190
FT                   /evidence="ECO:0000250"
FT   DISULFID        228..285
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   320 AA;  36672 MW;  BB1CDDCBCD070B8E CRC64;
     MEKKVDENAT LMNGVETTGP ARDDVPETFR EFLYNKKNGT VMGRTGKSWF QIIVFYIIFY
     AFLAAFWLTC LTIFMKTLDP KVPRFYGKGT IIGVNPGVGY QPWLKERPDS TLIKYNLRDQ
     KSYKAYLEQM KTYLTKYDSN ATETRECGAG DSNDDLEKNP DALPCRFDLS VFDKGCSEKS
     DFGYKSGKPC VIISLNRLIG WRPTDYQENS VPEEVKDRYK AGSIAINCRG ATNVDQEHIG
     KVTYMPSNGI DGRYYPYVFT KGYQQPIAMV KFDTIPRNKL VIVECRAYAL NIEHDISSRL
     GMVYFEVMVE DKPVEEKKEL
 
 
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