GenomeNet

Database: UniProt
Entry: A0A3Q7RVH4_VULVU
LinkDB: A0A3Q7RVH4_VULVU
Original site: A0A3Q7RVH4_VULVU 
ID   A0A3Q7RVH4_VULVU        Unreviewed;      1021 AA.
AC   A0A3Q7RVH4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
GN   Name=ATP1A1 {ECO:0000313|RefSeq:XP_025850417.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025850417.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025850417.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025850417.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025850417.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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       {ECO:0000256|ARBA:ARBA00037422}.
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; Evidence={ECO:0000256|ARBA:ARBA00035887};
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC       {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004554}. Cell membrane, sarcolemma
CC       {ECO:0000256|ARBA:ARBA00004415}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004415}. Cell membrane
CC       {ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU362084}. Cell projection, axon
CC       {ECO:0000256|ARBA:ARBA00004489}. Lateral cell membrane
CC       {ECO:0000256|ARBA:ARBA00034693}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00034693}. Melanosome
CC       {ECO:0000256|ARBA:ARBA00004223}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIC subfamily. {ECO:0000256|ARBA:ARBA00006934,
CC       ECO:0000256|RuleBase:RU362084}.
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   RefSeq; XP_025850417.1; XM_025994632.1.
DR   AlphaFoldDB; A0A3Q7RVH4; -.
DR   SMR; A0A3Q7RVH4; -.
DR   STRING; 9627.ENSVVUP00000014105; -.
DR   Ensembl; ENSVVUT00000018523; ENSVVUP00000014115; ENSVVUG00000010340.
DR   KEGG; vvp:112916773; -.
DR   OMA; QQPPIFN; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   CDD; cd02608; P-type_ATPase_Na-K_like; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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   NCBIfam; TIGR01106; ATPase-IIC_X-K; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43294:SF9; SODIUM_POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA-1; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362084};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU362084};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362084};
KW   Metal-binding {ECO:0000256|RuleBase:RU362084};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362084};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|RuleBase:RU362084};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538,
KW   ECO:0000256|RuleBase:RU362084};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053};
KW   Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW   Sodium/potassium transport {ECO:0000256|ARBA:ARBA00022607};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362084};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362084}; Transport {ECO:0000256|RuleBase:RU362084}.
FT   TRANSMEM        94..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        128..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        289..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        319..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        851..872
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        911..930
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        951..978
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        984..1002
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   DOMAIN          40..114
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1021 AA;  112810 MW;  572572EB4508A706 CRC64;
     MAFKVGRDKY EPAAVSEHGD KKKAKKERDM DELKKEVSMD DHKLSLDELH RKYGTDLSRG
     LTTARAAEIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSM LLWIGAILCF LAYGIQAATE
     EEPQNDNLYL GVVLSAVVII TGCFSYYQEA KSSKIMESFK NMVPQQALVI RNGEKMSINA
     EEVVVGDLVE VKGGDRIPAD LRIISANGCK VDNSSLTGES EPQTRSPDFT NENPLETRNI
     AFFSTNCVEG TARGIVVYTG DRTVMGRIAT LASGLEGGQT PIAAEIEHFI HIITGVAVFL
     GVSFFILSLI LEYTWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE
     AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT TENQSGVSFD KSSATWLALS
     RIAGLCNRAV FQANQENLPI LKRAVAGDAS ESALLKCIEL CCGSVKEMRD RYAKIVEIPF
     NSTNKYQLSI HKNPNTSEPR HLLVMKGAPE RILDRCSSIL LHGKEQPLDE ELKDAFQNAY
     LELGGLGERV LGFCHLFLPD EQFPEGFQFD TDDVNFPVEN LCFVGLISMI DPPRAAVPDA
     VGKCRSAGIK VIMVTGDHPI TAKAIAKGVG IISEGNETVE DIAARLNIPV SQVNPRDAKA
     CVVHGSDLKD MTSEQLDDIL KYHTEIVFAR TSPQQKLIIV EGCQRQGAIV AVTGDGVNDS
     PALKKADIGV AMGIAGSDVS KQAADMILLD DNFASIVTGV EEGRLIFDNL KKSIAYTLTS
     NIPEITPFLI FIIANIPLPL GTVTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPKTD
     KLVNERLISM AYGQIGMIQA LGGFFTYFVI LAENGFLPTH LLGLRVDWDD RWINDVEDSY
     GQQWTYEQRK IVEFTCHTAF FVSIVVVQWA DLVICKTRRN SVFQQGMKNK ILIFGLFEET
     ALAAFLSYCP GMGVALRMYP LKPTWWFCAF PYSLLIFVYD EVRKLIIRRR PGGWVEKETY
     Y
//
DBGET integrated database retrieval system