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AT1B4_RAT
ID   AT1B4_RAT               Reviewed;         356 AA.
AC   Q9R193; Q9R192;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Protein ATP1B4;
DE   AltName: Full=X,K-ATPase subunit beta-m;
DE   AltName: Full=X/potassium-transporting ATPase subunit beta-m;
GN   Name=Atp1b4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC   STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
RX   PubMed=10456317; DOI=10.1016/s0014-5793(99)00954-0;
RA   Pestov N.B., Adams G., Shakhparonov M.I., Modyanov N.N.;
RT   "Identification of a novel gene of the X,K-ATPase beta-subunit family that
RT   is predominantly expressed in skeletal and heart muscles.";
RL   FEBS Lett. 456:243-248(1999).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=14656723; DOI=10.1152/ajpcell.00358.2003;
RA   Zhao H., Pestov N.B., Korneenko T.V., Shakhparonov M.I., Modyanov N.N.;
RT   "Accumulation of beta (m), a structural member of X,K-ATPase beta-subunit
RT   family, in nuclear envelopes of perinatal myocytes.";
RL   Am. J. Physiol. 286:C757-C767(2004).
RN   [3]
RP   INTERACTION WITH SNW1 AND TOR1AIP1.
RX   PubMed=17592128; DOI=10.1073/pnas.0704809104;
RA   Pestov N.B., Ahmad N., Korneenko T.V., Zhao H., Radkov R., Schaer D.,
RA   Roy S., Bibert S., Geering K., Modyanov N.N.;
RT   "Evolution of Na,K-ATPase betam-subunit into a coregulator of transcription
RT   in placental mammals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:11215-11220(2007).
CC   -!- FUNCTION: May act as a transcriptional coregulator during muscle
CC       development through its interaction with SNW1. Has lost its ancestral
CC       function as a Na,K-ATPase beta-subunit (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Does not associate with known Na,K-ATPase alpha-subunits (By
CC       similarity). Associates with a SMAD7-transcriptional complex. Interacts
CC       with SNW1 and TOR1AIP1. {ECO:0000250, ECO:0000269|PubMed:17592128}.
CC   -!- INTERACTION:
CC       Q9R193; D4A8G7: Snw1; NbExp=2; IntAct=EBI-15644324, EBI-15644341;
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250}; Single-pass
CC       type II membrane protein {ECO:0000250}. Note=Detected in nuclear
CC       envelops. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=Q9R193-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q9R193-2; Sequence=VSP_000354;
CC   -!- TISSUE SPECIFICITY: Expressed in perinatal myocytes (at protein level).
CC       Expressed during postnatal development in skeletal muscle and heart.
CC       {ECO:0000269|PubMed:14656723}.
CC   -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; AF158385; AAD49694.1; -; mRNA.
DR   EMBL; AF158386; AAD49695.1; -; mRNA.
DR   RefSeq; NP_445833.1; NM_053381.1. [Q9R193-1]
DR   AlphaFoldDB; Q9R193; -.
DR   SMR; Q9R193; -.
DR   DIP; DIP-60962N; -.
DR   IntAct; Q9R193; 2.
DR   STRING; 10116.ENSRNOP00000009329; -.
DR   PaxDb; Q9R193; -.
DR   GeneID; 84396; -.
DR   KEGG; rno:84396; -.
DR   UCSC; RGD:620994; rat. [Q9R193-1]
DR   CTD; 23439; -.
DR   RGD; 620994; Atp1b4.
DR   eggNOG; KOG3927; Eukaryota.
DR   InParanoid; Q9R193; -.
DR   OrthoDB; 998086at2759; -.
DR   PhylomeDB; Q9R193; -.
DR   Reactome; R-RNO-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   PRO; PR:Q9R193; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0000785; C:chromatin; IDA:RGD.
DR   GO; GO:0005637; C:nuclear inner membrane; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IEA:InterPro.
DR   GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
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.
DR   PROSITE; PS00391; ATPASE_NA_K_BETA_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Nucleus; Reference proteome; Signal-anchor;
KW   Transcription; Transcription regulation; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..356
FT                   /note="Protein ATP1B4"
FT                   /id="PRO_0000219125"
FT   TOPO_DOM        1..109
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        131..356
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255"
FT   REGION          32..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..71
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         106..109
FT                   /note="Missing (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:10456317"
FT                   /id="VSP_000354"
SQ   SEQUENCE   356 AA;  41518 MW;  C4B6A378B65BABFA CRC64;
     MRRQLRSRRA PAFPYGYRYR LDDQDEMNHN YLADEEEEAE EEAQVMMVPG LEEEEEEEEG
     KEEEEEREEE EGQGQSTGNA WWRKLQIVNE YLWDPEKRMS LARTGQSRSL ILVIYFFFYA
     SLAAVITLFI YMLFLAISPY MPTFTEQVKP PGVMIRPFAH SLNFNFNVSE PETWQRYVIS
     LNGFLQGYND SLQEEMNIDC PPGQYFIQDG DEDEDKKACQ FKRSFLKNCS GLEDPTFGYS
     TGQPCILLKM NRIVGFRPEF GDPVKVSCKV QKGDENDIRS INYYPESASF DLRYYPYYGK
     LTHVNYTSPL VAMHFTDVVK NQEVPVQCQL KGKGIVNDVI NDRFVGRIIF TLNIET
 
 
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