ATP8B3

Identifiers

ATP8B3, ATPIK, ATPase phospholipid transporting 8B3

External IDs

MGI: 1914581 HomoloGene: 19034 GeneCards: ATP8B3

Genetically Related Diseases

Gene ontology
Molecular function	• nucleotide binding • metal ion binding • phospholipid-translocating ATPase activity • hydrolase activity • ATP binding • magnesium ion binding
Cellular component	• integral component of membrane • Golgi apparatus • endoplasmic reticulum membrane • membrane • plasma membrane • acrosomal membrane • acrosomal vesicle • endoplasmic reticulum • cytoplasmic vesicle
Biological process	• lipid transport • Golgi organization • phospholipid transport • phospholipid translocation • binding of sperm to zona pellucida • transport
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


148229


67331

Ensembl


ENSG00000130270


ENSMUSG00000003341

UniProt


O60423


Q6UQ17

RefSeq (mRNA)


NM_001178002 NM_138813


NM_026094

RefSeq (protein)


NP_001171473.1 NP_620168.1


NP_080370.2

Location (UCSC)

Chr 19: 1.78 – 1.81 Mb

Chr 10: 80.52 – 80.54 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

The human gene ATP8B3 encodes the protein ATPase, aminophospholipid transporter, class I, type 8B, member 3.^[4]

The protein encoded by this gene belongs to the family of P-type cation transport ATPases, and to the subfamily of aminophospholipid-transporting ATPases. The aminophospholipid translocases transport phosphatidylserine and phosphatidylethanolamine from one side of a bilayer to another. This gene encodes the member 3 of the phospholipid-transporting ATPase 8B.

Alternatively spliced transcript variants encoding different isoforms have been found for this gene.^[4]

References

Halleck, M. S.; Lawler Jr., J. F.; Blackshaw, S.; Gao, L.; Nagarajan, P.; Hacker, C.; Pyle, S.; Newman, J. T.; Nakanishi, Y.; Ando, H.; Weinstock, D.; Williamson, P.; Schlegel, R. A. (1999). "Differential expression of putative transbilayer amphipath transporters". Physiological genomics. 1 (3): 139–150. PMID 11015572.
Harris, M. J.; Arias, I. M. (2003). "FIC1, a P-type ATPase linked to cholestatic liver disease, has homologues (ATP8B2 and ATP8B3) expressed throughout the body". Biochimica et Biophysica Acta. 1633 (2): 127–131. doi:10.1016/S1388-1981(03)00107-0. PMID 12880872.
Fries, A. S.; Svendsen, O. (1978). "Studies on Tyzzer's disease in rats". Laboratory animals. 12 (1): 1–4. PMID 146761.
Scott, L. J.; Muglia, P.; Kong, X. Q.; Guan, W.; Flickinger, M.; Upmanyu, R.; Tozzi, F.; Li, J. Z.; Burmeister, M.; Absher, D.; Thompson, R. C.; Francks, C.; Meng, F.; Antoniades, A.; Southwick, A. M.; Schatzberg, A. F.; Bunney, W. E.; Barchas, J. D.; Jones, E. G.; Day, R.; Matthews, K.; McGuffin, P.; Strauss, J. S.; Kennedy, J. L.; Middleton, L.; Roses, A. D.; Watson, S. J.; Vincent, J. B.; Myers, R. M.; Farmer, A. E. (2009). "Genome-wide association and meta-analysis of bipolar disorder in individuals of European ancestry". Proceedings of the National Academy of Sciences. 106 (18): 7501–7506. doi:10.1073/pnas.0813386106. PMC 2678639. PMID 19416921.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Membrane transport protein: ion pumps, ATPases / ATP synthase (TC 3A2-3A3)

F-, V-, and A-type ATPase (3.A.2)

H⁺ (F-type)	H⁺ transporting, mitochondrial: ATP5A1 ATP5B ATP5C1 ATP5C2 ATP5D ATP5E ATP5F1 ATP5G1 ATP5G2 ATP5G3 ATP5H ATP5I ATP5J ATP5J2 ATP5L ATP5L2 ATP5O ATP5S

H⁺ (V-type)	H⁺ transporting, lysosomal: ATP6AP1 ATP6AP2 ATP6V1A ATP6V1B1 ATP6V1B2 ATP6V1C1 ATP6V1C2 ATP6V1D ATP6V1E1 ATP6V1E2 ATP6V1F ATP6V1G1 ATP6V1G2 ATP6V1G3 ATP6V1H ATP6V0A1 ATP6V0A2 ATP6V0A4 ATP6V0B ATP6V0C ATP6V0D1 ATP6V0D2 ATP6V0E ATP6V0E1 TCIRG1

A-ATPase	found in Archea

P-type ATPase (3.A.3)

3.A.3.1.1: Na⁺/K⁺ transporting: ATP1A1
ATP1A2
ATP1A3
ATP1A4
ATP1B1
ATP1B2
ATP1B3
ATP1B4
ATP1G1

3.A.3.1.2: H⁺/K⁺
H⁺/K⁺ exchanging: ATP4A
ATP4B

3.A.3.1.4: H⁺/K⁺ transporting, nongastric: ATP12A

3.A.3.2: Ca²⁺ (SERCA, PMCA, SPCA) / Ca²⁺ transporting: ATP2A1
ATP2A2
ATP2A3
ATP2B1
ATP2B2
ATP2B3
ATP2B4
ATP2C1

3.A.3.5: Cu²⁺ transporting: ATP7A
ATP7B

3.A.3.8.8: flippase: ATP8A2

Other/ungrouped:

Na⁺/K⁺ – H⁺

Mg²⁺ transporting: ATP3
Class I, type 8: ATP8A1
ATP8B1
ATP8B2
ATP8B3
ATP8B4
Class II, type 9: ATP9A
ATP9B
Class V, type 10: ATP10A
ATP10B
ATP10D
Class VI, type 11: ATP11A
ATP11B
ATP11C
type 13: ATP13A1
ATP13A2
ATP13A3
ATP13A4
ATP13A5

see also ATPase disorders

Hydrolases: acid anhydride hydrolases (EC 3.6)

3.6.1

3.6.2

3.6.3-4: ATPase

3.6.3

Cu++ (3.6.3.4)	Menkes/ATP7A Wilson/ATP7B

Ca+ (3.6.3.8)	SERCA ATP2A1 ATP2A2 ATP2A3 Plasma membrane ATP2B1 ATP2B2 ATP2B3 ATP2B4 SPCA ATP2C1 ATP2C2

Na+/K+ (3.6.3.9)	ATP1A1 ATP1A2 ATP1A3 ATP1A4 ATP1B1 ATP1B2 ATP1B3 ATP1B4

H+/K+ (3.6.3.10)	ATP4A

Other P-type ATPase	ATP8B1 ATP10A ATP11B ATP12A ATP13A2 ATP13A3

3.6.4

3.6.5: GTPase

3.6.5.1: Heterotrimeric G protein	G_αs G_αi GNAI1 GNAI2 GNAI3 G_αq/11 GNAQ GNA11 G_α12/13 GNA12 GNA13 Transducin GNAT1 GNAT2 Gustducin GNAT3

3.6.5.2: Small GTPase > Ras superfamily	Rho family of GTPases: Cdc42 CDC42 TC10 TCL RhoUV RhoU RhoV Rac Rac1 2 3 RhoG RhoBTB 1 2 RhoH Rho A B C Rnd 1 2 3 RhoDF RhoF RhoD other: Ras HRAS KRAS NRAS Rab RAB23 RAB27 Arf ARF6 SAR1B ARL13B ARL6 Ran Rheb Rap RGK

3.6.5.3: Protein-synthesizing GTPase	Prokaryotic IF-2 EF-Tu EF-G Eukaryotic

3.6.5.5-6: Polymerization motors	Dynamin Tubulin

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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ATP8B3

References

Further reading