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0AT8A1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameATP8A1
DescriptionPotential phospholipid-transporting atpase ia (ec 3.6.3.1) (chromaffin granule atpase ii) (atpase class i type 8a member 1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016021 integral to membrane (NAS)
0015247 aminophospholipid transporter activity (NAS)
0005524 ATP binding (NAS)
0019829 cation-transporting ATPase activity (NAS)
0015917 aminophospholipid transport (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
P-type (or E1-E2-type) ATPases constitute a superfamily of cation transport enzymes.resent both in prokaryota and eukaryota.hose members mediate membrane flux of all common biologically relevant cations . The enzymes.hat form an aspartyl phosphate intermediate in the course of ATP hydrolysis.an be divided into 4 major groups : (1) Ca2+-transporting ATPases; (2) Na+/K+- and gastric H+/K+-transporting ATPases; (3) plasma membrane H+-transporting ATPases (proton pumps) of plants.ungi and lower eukaryotes; and (4) all bacterial P-type ATPases.xcept the Mg2+-ATPase of Salmonella typhimurium.hich is more similar to the eukaryotic sequences. However.reat variety of sequence analysis methods results in diversity of classification.
  IPR008250:E1-E2 ATPase-associated region
This group of hydrolase enzymes is structurally different from the alpha/beta hydrolase family (abhydrolase). This group includes L-2-haloacid dehalogenase.poxide hydrolases and phosphatases. The structure consists of two domains. One is an inserted four helix bundle.hich is the least well conserved region of the alignment.etween residues 16 and 96 of HAD1_PSESP. The rest of the fold is composed of the core alpha/beta domain.
  IPR005834:Haloacid dehalogenase-like hydrolase
ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient.sing the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse.sing the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases.hich can differ in function (ATP synthesis and/or hydrolysis).tructure (F-.- and A-ATPases contain rotary motors) and in the type of ions they transport . F-ATPases (F1F0-ATPases) in mitochondria.hloroplasts and bacterial plasma membranes are the prime producers of ATP.sing the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).V-ATPases (V1V0-ATPases) are primarily found in eukaryotic vacuoles.atalysing ATP hydrolysis to transport solutes and lower pH in organelles.A-ATPases (A1A0-ATPases) are found in Archaea and function like F-ATPases.P-ATPases (E1E2-ATPases) are found in bacteria and in eukaryotic plasma membranes and organelles.nd function to transport a variety of different ions across membranes.E-ATPases are cell-surface enzymes that hydrolyse a range of NTPs.ncluding extracellular ATP.P-ATPases (sometime known as E1-E2 ATPases) () are found in bacteria and in a number of eukaryotic plasma membranes and organelles . P-ATPases function to transport a variety of different compounds.ncluding ions and phospholipids.cross a membrane using ATP hydrolysis for energy. There are many different classes of P-ATPases.ach of which transports a specific type of ion: H+.a+.+.g2+.a2+.g+ and Ag2+.n2+.o2+.b2+.i2+.d2+.u+ and Cu2+. P-ATPases can be composed of one or two polypeptides.nd can usually assume two main conformations called E1 and E2. This entry represents the several classes of P-type ATPases.ncluding those that transport K+ ().g2+ ().d2+ ().u 2+ ().n2+ ().a+ ().a2+ ().a+/K+ ().nd H+/K+ (). These P-ATPases are found in both prokaryotes and eukaryotes.More information about this protein can be found at Protein of the Month: ATP Synthases .
  IPR001757:ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter
These sequences represent the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other . These ATPases are found only in eukaryotes.
  IPR006539:Phospholipid-translocating P-type ATPase, flippase
IPR008250:E1-E2_ATPase 
Evalue:-3.53760194778442 
Location:132-170IPR005834:Hydrolase 
Evalue:-2.85387206077576 
Location:403-822
SequencesProtein: AT8A1_HUMAN (1164 aa)
mRNA: AB013452 NM_006095
Local Annotation
Synapse Ontology
the mechanism by which the restiong potential is held.
sdb:0288 maintain membrane potential  (Evidence:keywords)
KO assignmentK01530
  Level 3 annotation:
    phospholipid-translocating ATPase
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 133 residues, 42109391-42109787Exon2: 32 residues, 42111400-42111492Exon3: 33 residues, 42119580-42119673Exon4: 31 residues, 42120390-42120479Exon5: 38 residues, 42140338-42140446Exon6: 21 residues, 42141351-42141408Exon7: 22 residues, 42143356-42143418Exon8: 28 residues, 42148754-42148833Exon9: 43 residues, 42152070-42152193Exon10: 27 residues, 42152298-42152373Exon11: 39 residues, 42161463-42161574Exon12: 63 residues, 42161666-42161850Exon13: 59 residues, 42182269-42182442Exon14: 23 residues, 42200223-42200288Exon15: 48 residues, 42203789-42203928Exon16: 48 residues, 42218933-42219073Exon17: 30 residues, 42221536-42221621Exon18: 25 residues, 42240690-42240760Exon19: 18 residues, 42245786-42245836Exon20: 29 residues, 42247971-42248054Exon21: 37 residues, 42249278-42249384Exon22: 26 residues, 42252741-42252814Exon23: 17 residues, 42265934-42265979Exon24: 31 residues, 42271392-42271481Exon25: 28 residues, 42272395-42272473Exon26: 44 residues, 42275033-42275161Exon27: 57 residues, 42276586-42276752Exon28: 39 residues, 42278394-42278506Exon29: 44 residues, 42283122-42283250Exon30: 25 residues, 42285033-42285103Exon31: 26 residues, 42287584-42287658Exon32: 15 residues, 42297251-42297292Exon33: 17 residues, 42312806-42312852Exon34: 35 residues, 42321309-42321408Exon35: 35 residues, 42322387-42322487Exon36: 40 residues, 42323768-42323883Exon37: 17 residues, 42353598-42353645Exon38: 2 residues, -Jump to AT8A1_HUMANExon1: 133 residues, 42109391-42109787Exon2: 32 residues, 42111400-42111492Exon3: 33 residues, 42119580-42119673Exon4: 31 residues, 42120390-42120479Exon5: 38 residues, 42140338-42140446Exon6: 21 residues, 42141351-42141408Exon7: 22 residues, 42143356-42143418Exon8: 28 residues, 42148754-42148833Exon9: 43 residues, 42152070-42152193Exon10: 27 residues, 42152298-42152373Exon11: 39 residues, 42161463-42161574Exon12: 63 residues, 42161666-42161850Exon13: 59 residues, 42182269-42182442Exon14: 23 residues, 42200223-42200288Exon15: 48 residues, 42203789-42203928Exon16: 48 residues, 42218933-42219073Exon17: 30 residues, 42221536-42221621Exon18: 25 residues, 42240690-42240760Exon19: 18 residues, 42245786-42245836Exon20: 29 residues, 42247971-42248054Exon21: 37 residues, 42249278-42249384Exon22: 26 residues, 42252741-42252814Exon23: 17 residues, 42265934-42265979Exon24: 31 residues, 42271392-42271481Exon25: 28 residues, 42272395-42272473Exon26: 44 residues, 42275033-42275161Exon27: 57 residues, 42276586-42276752Exon28: 39 residues, 42278394-42278506Exon29: 44 residues, 42283122-42283250Exon30: 25 residues, 42285033-42285103Exon31: 26 residues, 42287584-42287658Exon32: 15 residues, 42297251-42297292Exon33: 17 residues, 42312806-42312852Exon34: 35 residues, 42321309-42321408Exon35: 35 residues, 42322387-42322487Exon36: 40 residues, 42323768-42323883Exon37: 18 residues, 42353598-42353647Exon38: 2 residues, -Jump to AT8A1_HUMAN  
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