位置:首页 > 蛋白库 > AT1A3_CHICK
AT1A3_CHICK
ID   AT1A3_CHICK             Reviewed;        1010 AA.
AC   P24798;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-3;
DE            Short=Na(+)/K(+) ATPase alpha-3 subunit;
DE            EC=7.2.2.13;
DE   AltName: Full=Na(+)/K(+) ATPase alpha(III) subunit;
DE   AltName: Full=Sodium pump subunit alpha-3;
GN   Name=ATP1A3;
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=2171348; DOI=10.1152/ajpcell.1990.259.4.c619;
RA   Takeyasu K., Lemas V., Fambrough D.M.;
RT   "Stability of Na(+)-K(+)-ATPase alpha-subunit isoforms in evolution.";
RL   Am. J. Physiol. 259:C619-C630(1990).
CC   -!- FUNCTION: This is the catalytic component of the active enzyme, which
CC       catalyzes the hydrolysis of ATP coupled with the exchange of sodium and
CC       potassium ions across the plasma membrane. This action creates the
CC       electrochemical gradient of sodium and potassium ions, providing the
CC       energy for active transport of various nutrients.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) +
CC         Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         EC=7.2.2.13;
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:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIC subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M59960; AAA48982.1; -; mRNA.
DR   PIR; B37227; B37227.
DR   RefSeq; NP_990806.1; NM_205475.1.
DR   AlphaFoldDB; P24798; -.
DR   SMR; P24798; -.
DR   PRIDE; P24798; -.
DR   GeneID; 396467; -.
DR   CTD; 478; -.
DR   VEuPathDB; HostDB:geneid_396530; -.
DR   InParanoid; P24798; -.
DR   OrthoDB; 388324at2759; -.
DR   PhylomeDB; P24798; -.
DR   PRO; PR:P24798; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; ISS:UniProtKB.
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:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR   GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
DR   CDD; cd02608; P-type_ATPase_Na-K_like; 1.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR005775; P-type_ATPase_IIC.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81660; SSF81660; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Ion transport; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW   Potassium transport; Reference proteome; Sodium; Sodium transport;
KW   Sodium/potassium transport; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1010
FT                   /note="Sodium/potassium-transporting ATPase subunit alpha-
FT                   3"
FT                   /id="PRO_0000046301"
FT   TOPO_DOM        1..74
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        96..118
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        140..275
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..307
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        326..759
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        760..779
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        780..789
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        790..810
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        811..830
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        831..853
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        854..905
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        906..925
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        926..938
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        939..957
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        958..972
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        973..993
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        994..1010
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          69..71
FT                   /note="Interaction with phosphoinositide-3 kinase"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        363
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         704
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         708
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         930
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1010 AA;  111284 MW;  71526BC25633BFA6 CRC64;
     MGDKGEKESP KKGKGKRDLD DLKKEVAMTE HKMSIEEVCR KYNTDCVQGL THSKAQEILA
     RDGPNALTPP PTTPEWVKFC RQLFGGFSIL LWIGAILCFL AYGIQAGTED EPSNDNLYLG
     IVLAAVVIIT GCFSYYQEAK SSKIMESFKN MVPQQALVIR EGEKMQLNAE EVVVGDLVEV
     KGGDRVPADL RIISAHGCKV DNSSLTGESE PQTRSPDCTH DNPLETRNIT FFSTNCVEGT
     ARGVVIATGD RTVMGRIATL ASGLEVGKTP IAVEIEHFIQ LITGVAVFLG ISFFVLSLIL
     GYTWLEAVIF LIGIIVANVP EGLLATVTVC LTLTAKRMAR KNCLVKNLEA VETLGSTSTI
     CSDKTGTLTQ NRMTVAHMWF DNQIHEADTT EDQSGTSFDK SSATWVALSH IAGLCNRAVF
     KGGQENVPIL KRDVAGDASE SALLKCIELS SGSVKVMRER NKKVAEIPFN STNKYQLSIH
     ETEDPNDNRY LLVMKGAPER ILDRCSTILL QGKEQPLDEE MKEAFQNAYL ELGGLGERVL
     GFCHFYLPEE QYPKGFAFDC DDVNFATDNL CFVGLMSMID PPRAAVPDAV GKCRSAGIKV
     IMVTGDHPIT AKAIAKGVGI ISEGNETVED IAARLNIPVS QVNPRDAKAC VIHGTDLKDM
     SSEQIDEILQ NHTEIVFART SPQQKLIIVE GCQRQGAIVA VTGDGVNDSP ALKKADIGVA
     MGIRGSDVSK QAADMILLDD NFASIVTGVE EGRLIFDNLK KSIAYTLTSN IPEITPFLLF
     IMANIPLPLG TITILCIDLG TDMVPAISLA YEAAESDIMK RQPRNPRSDK LVNERLISMA
     YGQIGMIQAL GGFFSYFVIL AENGFLPSCL VGIRLSWDDR TINDLEDSYG QQWTYEQRKV
     VEFTCHTAFF VSIVVVQWAD LIICKTRRNS VFQQGMKNKI LIFGLFEETA LAAFLSYCPG
     MDVALRMYPL KPSWWFCAFP YSFLIFVYDE IRKLILRRNP GGWVEKETYY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024